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