ID 143E_DROME STANDARD; PRT; 260 AA. AC P92177; Q9VEA8; DT 15-JUL-1998 (Rel. 36, Created) DT 15-JUL-1998 (Rel. 36, Last sequence update) DT 16-OCT-2001 (Rel. 40, 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; Tracheata; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND MUTAGENESIS OF GLU-183; PHE-199 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., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: 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 -!- 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; AAF55519.1; -. DR HSSP; P29312; 1A38. DR FlyBase; FBgn0020238; 14-3-3-epsilon. 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. 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 260 AA; 29570 MW; 1282192917E3A7A4 CRC64; MTERENNVYK AKLAEQAERY DEMVEAMKKV ASMDVELTVE ERNLLSVAYK NVIGARRASW RIITSIEQKE ENKGAEEKLE MIKTYRGQVE KELRDICSDI LNVLEKHLIP CATSGESKVF YYKMKGDYHR YLAEFATGSD RKDAAENSLI AYKAASDIAM NDLPPTHPIR LGLALNFSVF YYEILNSPDR ACRLAKAAFD DAIAELDTLS EESYKDSTLI MQLLRDNLTL WTSDMQAEDP NAGDGEPKEQ IQDVEDQDVS // 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 16-OCT-2001 (Rel. 40, 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; Tracheata; Hexapoda; Insecta; OC Pterygota; 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 activator RT 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 photoreceptor RT 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., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: REQUIRED IN RAF-DEPENDENT CELL PROLIFERATION AND CC PHOTORECEPTOR DIFFERENTIAITON DURING EYE DEVELOPMENT. ACTS CC UPSTREAM OF RAF AND DOWNSTREAM OF RAS, AND IS ESSENTIAL FOR CC VIABILITY. CC -!- ALTERNATIVE PRODUCTS: 2 ISOFORMS; VI (SHOWN HERE) AND VI'; ARE CC PRODUCED BY ALTERNATIVE SPLICING. 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; AAF58843.2; -. DR PIR; JC1122; JC1122. DR HSSP; P29312; 1A38. DR FlyBase; FBgn0004907; 14-3-3-zeta. 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'). 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 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 16-OCT-2001 (Rel. 40, 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; Tracheata; Hexapoda; Insecta; OC Pterygota; 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 encoding RT 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., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA 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 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 HSSP; P00349; 2PGD. DR FlyBase; FBgn0004654; Pgd. DR InterPro; IPR001744; 6PGD. 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 A4_DROME STANDARD; PRT; 886 AA. AC P14599; DT 01-APR-1990 (Rel. 14, Created) DT 01-APR-1990 (Rel. 14, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE BETA-AMYLOID-LIKE PROTEIN PRECURSOR. GN APPL OR VND. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Tracheata; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=89184650; PubMed=2494667; RA Rosen D.R., Martin-Morris L., Luo L., White K.; RT "A Drosophila gene encoding a protein resembling the human beta- RT amyloid protein precursor."; RL Proc. Natl. Acad. Sci. U.S.A. 86:2478-2482(1989). RN [2] RP SEQUENCE OF 1-83 FROM N.A. RX MEDLINE=91184006; PubMed=2127912; RA Martin-Morris L.E., White K.; RT "The Drosophila transcript encoded by the beta-amyloid protein RT precursor-like gene is restricted to the nervous system."; RL Development 110:185-195(1990). CC -!- FUNCTION: PROBABLY CORRESPONDS TO THE PROTEIN ENCODED BY THE CC ESSENTIAL LOCUS VND, A GENE REQUIRED FOR EMBRYONIC NERVOUS SYSTEM CC DEVELOPMENT. CC -!- SUBCELLULAR LOCATION: TYPE I MEMBRANE PROTEIN. CC -!- TISSUE SPECIFICITY: APPL TRANSCRIPTS ARE FOUND IN THE CENTRAL AND CC PERIPHERAL NERVOUS SYSTEMS. WITHIN THE NERVOUS SYSTEM TRANSCRIPTS CC ARE NOT OBSERVED IN NEUROBLASTS, NEWLY GENERATED NEURONS AND AT CC LEAST ONE CLASS OF PRESUMED GLIAL CELLS. CC -!- DEVELOPMENTAL STAGE: APPL TRANSCRIPTS ARE FOUND IN POST-MITOTIC CC NEURONS IN THE CENTRAL AND PERIPHERAL NERVOUS SYSTEMS IN ALL CC DEVELOPMENTAL STAGES. CC -!- SIMILARITY: BELONGS TO THE APP FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; J04516; AAA28874.1; -. DR EMBL; X55774; CAA39294.1; -. DR EMBL; X55775; CAA39294.1; JOINED. DR PIR; A32758; A32758. DR HSSP; P05067; 1MWP. DR FlyBase; FBgn0000108; Appl. DR InterPro; IPR001868; A4_APP. DR Pfam; PF02177; A4_EXTRA; 1. DR SMART; SM00006; A4_EXTRA; 1. DR PROSITE; PS00319; A4_EXTRA; 1. DR PROSITE; PS00320; A4_INTRA; 1. KW Signal; Transmembrane; Amyloid; Neurogenesis. FT SIGNAL 1 27 POTENTIAL. FT CHAIN 28 886 BETA-AMYLOID-LIKE PROTEIN. FT DOMAIN 28 810 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 811 833 POTENTIAL. FT DOMAIN 834 886 CYTOPLASMIC (POTENTIAL). FT DOMAIN 876 879 CLATHRIN-BINDING (POTENTIAL). FT CARBOHYD 150 150 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 161 161 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 236 236 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 239 239 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 573 573 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 886 AA; 98261 MW; C5C1EA4194DB5A8D CRC64; MCAALRRNLL LRSLWVVLAI GTAQVQAASP RWEPQIAVLC EAGQIYQPQY LSEEGRWVTD LSKKTTGPTC LRDKMDLLDY CKKAYPNRDI TNIVESSHYQ KIGGWCRQGA LNAAKCKGSH RWIKPFRCLG PFQSDALLVP EGCLFDHIHN ASRCWPFVRW NQTGAAACQE RGMQMRTFAM LLPCGISVFS GVEFVCCPKH FKTDEIHVKK TDLPVMPAAQ INSANDELMN DEDDSNDSNY SKDANEDDLD DEDDLMGDDE EDDMVADEAA TAGGSPNTGS SGDSNSGSLD DINAEYDSGE EGDNYEEDGA GSESEAEVEA SWDQSGGAKV VSLKSDSSSP SSAPVAPAPE KAPVKSESVT STPQLSASAA AFVAANSGNS GTGAGAPPST AQPTSDPYFT HFDPHYEHQS YKVSQKRLEE SHREKVTRVM KDWSDLEEKY QDMRLADPKA AQSFKQRMTA RFQTSVQALE EEGNAEKHQL AAMHQQRVLA HINQRKREAM TCYTQALTEQ PPNAHHVEKC LQKLLRALHK DRAHALAHYR HLLNSGGPGG LEAAASERPR TLERLIDIDR AVNQSMTMLK RYPELSAKIA QLMNDYILAL RSKDDIPGSS LGMSEEAEAG ILDKYRVEIE RKVAEKERLR LAEKQRKEQR AAEREKLREE KLRLEAKKVD DMLKSQVAEQ QSQPTQSSTQ SQAQQQQQEK SLPGKELGPD AALVTAANPN LETTKSEKDL SDTEYGEATV STTKVQTVLP TVDDDAVQRA VEDVAAAVAH QEAEPQVQHF MTHDLGHRES SFSLRREFAQ HAHAAKEGRN VYFTLSFAGI ALMAAVFVGV AVAKWRTSRS PHAQGFIEVD QNVTTHHPIV REEKIVPNMQ INGYENPTYK YFEVKE // ID NSF1_DROME STANDARD; PRT; 745 AA. AC P46461; Q9VYF4; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 15-JUN-2002 (Rel. 41, Last annotation update) DE VESICULAR-FUSION PROTEIN NSF1 (N-ETHYLMALEIMIDE-SENSITIVE FUSION DE PROTEIN 1) (NEM-SENSITIVE FUSION PROTEIN 1) (DNSF-1) (COMATOSE DE PROTEIN). GN NSF1 OR NSF-1 OR NSF OR COMT OR CG1618. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Tracheata; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=HEAD; RX MEDLINE=94261657; PubMed=8202553; RA Ordway R.W., Pallanck L., Ganetzky B.; RT "Neurally expressed Drosophila genes encoding homologs of the NSF and RT SNAP secretory proteins."; RL Proc. Natl. Acad. Sci. U.S.A. 91:5715-5719(1994). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=BERKELEY; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: REQUIRED FOR VESICLE-MEDIATED TRANSPORT. CATALYZES THE CC FUSION OF TRANSPORT VESICLES WITHIN THE GOLGI CISTERNAE. IS ALSO CC REQUIRED FOR TRANSPORT FROM THE ENDOPLASMIC RETICLUM TO THE GOLGI CC STACK. SEEM TO FUNCTION AS A FUSION PROTEIN REQUIRED FOR THE CC DELIVERY OF CARGO PROTEINS TO ALL COMPARTMENTS OF THE GOLGI STACK CC INDEPENDENT OF VESICLE ORIGIN. CC -!- SUBUNIT: HOMOHEXAMER (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- TISSUE SPECIFICITY: NERVOUS SYSTEM. CC -!- SIMILARITY: BELONGS TO THE AAA FAMILY OF ATPASES. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U09373; AAA83413.1; -. DR EMBL; AE003492; AAF48244.1; ALT_SEQ. DR HSSP; P18708; 1NSF. DR FlyBase; FBgn0000346; comt. DR InterPro; IPR003593; AAA_ATPase. DR InterPro; IPR003959; AAA_ATPase_centr. DR InterPro; IPR003960; AAA_sub. DR InterPro; IPR003338; ATPaseVAT_N. DR InterPro; IPR004201; Cdc48_2. DR Pfam; PF00004; AAA; 4. DR Pfam; PF02359; cdc48_N; 1. DR Pfam; PF02933; cdc48_2; 2. DR SMART; SM00382; AAA; 2. DR PROSITE; PS00674; AAA; 1. KW Transport; Protein transport; Endoplasmic reticulum; Golgi stack; KW ATP-binding; Repeat; Multigene family. FT NP_BIND 260 267 ATP (POTENTIAL). FT NP_BIND 543 550 ATP (POTENTIAL). SQ SEQUENCE 745 AA; 82555 MW; A34E7B037E91769F CRC64; MAYILKATKC PTDELSLTNR AIVNVGDFPE EIKYADISPA PGQHFIFALE KTVEVPSGYV GFSLVQRKWA MVSINQELEV RPYRFDASSD VITCVSFETD FLQKKTVSQE PYDSDQMAKE FIMQFAGMAL TVGQSLVFNF KDKKLLGLAV KSLEAIDPKS LGEGKDTAMR NVRFGRILGN TVVQFEKAEN SSLNLQGKSK GKVVRQSIIN PDWDFGKMGI GGLDKEFNSI FRRAFASRVF PPELVEQLGC KHVKGILLYG PPGTGKTLMA RQIGTMLNAR EPKIVNGPQI LDKYVGESEA NVRRLFAEAE EEEKRLGPNS GLHIIIFDEI DAICKQRGSV AGNSGVHDTV VNQLLTKIDG VDQLNNILVI GMTNRRDMID EALLRPGRLE VQMEISLPNE QGRVQILNIH TKRMREFNKI NDDVDNKEIA ALTKNFSGAE LEGLVRAAQS SAMNRLIKAD AKVTVDPEAM EKLKVNRDDF LHSLEHDIKP AFGTAQEILD NMLARGVINW GAPVSNLLED GMLYVQQAKA PESSGLVSVL VAGAPNSGKT ALAAQLAKMS DFPFVKVCSP EDMVGYTESA KCLHIRKIFD DAYRSMLSCI VVDNVERLLD YGSIGPRYSN MTLQALLVLL KKQPPKGRKL LILCTSSRRE VLEEMEMLTA FTSVLHVPNL SKPDHVLAVL ENTDIFSKGE IQAIGKKMAG KRVFIGIKKL LGLIDMARQT EQSQRAIKFL SKMEEEGGLD MVARQ // ID NSF2_DROME STANDARD; PRT; 752 AA. AC P54351; Q9VFQ5; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE VESICULAR-FUSION PROTEIN NSF2 (N-ETHYLMALEIMIDE-SENSITIVE FUSION DE PROTEIN 2) (NEM-SENSITIVE FUSION PROTEIN 2) (DNSF-2). GN NSF2 OR NSF-2 OR CG9931. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Tracheata; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=CANTON-S; RX MEDLINE=95370175; PubMed=7642522; RA Pallanck L., Ordway R.W., Ramaswami M., Chi W.Y., Krishnan K.S., RA Ganetzky B.; RT "Distinct roles for N-ethylmaleimide-sensitive fusion protein (NSF) RT suggested by the identification of a second Drosophila NSF homolog."; RL J. Biol. Chem. 270:18742-18744(1995). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=BERKELEY; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA 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 SEQUENCE OF 9-752 FROM N.A. RC TISSUE=HEAD; RX MEDLINE=95350218; PubMed=7624376; RA Boulianne G.L., Trimble W.S.; RT "Identification of a second homolog of N-ethylmaleimide-sensitive RT fusion protein that is expressed in the nervous system and secretory RT tissues of Drosophila."; RL Proc. Natl. Acad. Sci. U.S.A. 92:7095-7099(1995). CC -!- FUNCTION: REQUIRED FOR VESICLE-MEDIATED TRANSPORT. CATALYZES THE CC FUSION OF TRANSPORT VESICLES WITHIN THE GOLGI CISTERNAE. IS ALSO CC REQUIRED FOR TRANSPORT FROM THE ENDOPLASMIC RETICLUM TO THE GOLGI CC STACK. SEEM TO FUNCTION AS A FUSION PROTEIN REQUIRED FOR THE CC DELIVERY OF CARGO PROTEINS TO ALL COMPARTMENTS OF THE GOLGI STACK CC INDEPENDENT OF VESICLE ORIGIN (BY SIMILARITY). CC -!- SUBUNIT: HOMOHEXAMER (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- TISSUE SPECIFICITY: NERVOUS SYSTEM AND SECRETORY TISSUES. CC -!- DEVELOPMENTAL STAGE: THE HIGHEST LEVELS ARE DETECTED IN EMBRYOS CC BEFORE AND DURING CELLULARIZATION. AFTER ONSET OF GASTRULATION THE CC HIGHEST LEVELS OF EXPRESSION APPEAR IN EMBRYONIC REGIONS THAT GIVE CC RISE TO ENDODERMAL AND ECTODERMAL TISSUES INCLUDING THE MIDGUT AND CC HINDGUT. CC -!- SIMILARITY: BELONGS TO THE AAA FAMILY OF ATPASES. CC -!- CAUTION: IT IS UNCERTAIN WHETHER MET-1 OR MET-9 IS THE INITIATOR. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U30502; AAA75044.1; -. DR EMBL; AE003702; AAF54995.1; ALT_SEQ. DR EMBL; U28836; AAC46844.1; -. DR HSSP; P18708; 1NSF. DR FlyBase; FBgn0013998; Nsf2. DR InterPro; IPR003593; AAA_ATPase. DR InterPro; IPR003959; AAA_ATPase_centr. DR InterPro; IPR003960; AAA_sub. DR InterPro; IPR003338; ATPaseVAT_N. DR InterPro; IPR004201; Cdc48_2. DR Pfam; PF00004; AAA; 2. DR Pfam; PF02933; cdc48_2; 1. DR Pfam; PF02359; cdc48_N; 1. DR SMART; SM00382; AAA; 2. DR PROSITE; PS00674; AAA; 1. KW Transport; Protein transport; Endoplasmic reticulum; Golgi stack; KW ATP-binding; Repeat; Multigene family. FT NP_BIND 265 272 ATP (POTENTIAL). FT NP_BIND 548 555 ATP (POTENTIAL). FT CONFLICT 680 680 H -> N (IN REF. 2). SQ SEQUENCE 752 AA; 83457 MW; 0D76008F65A318AF CRC64; MSIEKAHRMR AIKCPTDELS LTNKAIVNVS DFTEEVKYVD ISPGPGLHYI FALEKISGPE LPLGHVGFSL VQRKWATLSI NQEIDVRPYR FDASADIITL VSFETDFLQK KTTTQEPYDS DEMAKEFLMQ FAGMPLTVGQ TLVFQFKDKK FLGLAVKTLE AVDPRTVGDS LPKTRNVRFG RILGNTVVQF EKAENSVLNL QGRSKGKIVR QSIINPDWDF GKMGIGGLDK EFNAIFRRAF ASRVFPPELV EQLGIKHVKG ILLYGPPGTG KTLMARQIGT MLNAREPKIV NGPQILDKYV GESEANIRRL FAEAEEEEKR LGPNSGLHII IFDEIDAICK ARGSVAGNSG VHDTVVNQLL AKIDGVEQLN NILVIGMTNR RDMIDEALLR PGRLEVQMEI SLPNEQGRVQ ILNIHTKRMR DFNKIASDVD NNEIAAKTKN FSGAELEGLV RAAQSTAMNR LIKADSKVHV DPEAMEKLRV TRADFLHALD NDIKPAFGAA QEMLENLLAR GIINWGPPVT ELLEDGMLSV QQAKATESSG LVSVLIEGAP NSGKSALAAN LAQLSDFPFV KVCSPEDMVG FTESAKCLHI RKIFDDAYRS TLSCIVVDNV ERLLDYGPIG PRYSNLTLQA LLVLLKKQPP KGRKLLILCT SSRRDVLEEM EMLSAFTSVL HVSNLSTPEH VLAVLDDSDL FSPEELQSIA RKMAGKRLCI GIKKLLALID MIRQSEPHQR VIKFLSKMEE EGGLEMDRVQ GH // ID PRS4_DROME STANDARD; PRT; 439 AA. AC P48601; DT 01-FEB-1996 (Rel. 33, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 01-OCT-1996 (Rel. 34, Last annotation update) DE 26S PROTEASE REGULATORY SUBUNIT 4 (P26S4). GN PROS26.4 OR P26S4. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Tracheata; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=96404010; PubMed=8808288; RA Hoyle J., Fisher E.M.C.; RT "Genomic organization and mapping of the mouse P26s4 ATPase gene: a RT member of the remarkably conserved AAA gene family."; RL Genomics 31:115-118(1996). CC -!- FUNCTION: THE 26S PROTEASE IS INVOLVED IN THE ATP-DEPENDENT CC DEGRADATION OF UBIQUITINATED PROTEINS. THE REGULATORY (OR ATPASE) CC COMPLEX CONFERS ATP DEPENDENCY AND SUBSTRATE SPECIFICITY TO THE CC 26S COMPLEX (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC AND NUCLEAR (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE AAA FAMILY OF ATPASES. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U39303; AAB34134.1; -. DR FlyBase; FBgn0015282; Pros26.4. DR InterPro; IPR003593; AAA_ATPase. DR InterPro; IPR003959; AAA_ATPase_centr. DR InterPro; IPR003960; AAA_sub. DR Pfam; PF00004; AAA; 1. DR SMART; SM00382; AAA; 1. DR TIGRFAMs; TIGR01242; 26Sp45; 1. DR PROSITE; PS00674; AAA; 1. KW Proteasome; ATP-binding; Nuclear protein. FT NP_BIND 225 232 ATP (POTENTIAL). SQ SEQUENCE 439 AA; 49323 MW; D4B31073756A293C CRC64; MGQNQSAQGG AGEKKDDKDK KKKYEPPIPT RVGKKKRRAK GPDAAMKLPQ VTPHTRARLK LLKLERIKDY LMMEDEFIRN QERLKPQDEK NEEERSKVDD LRGTPMSVGN LEEIIDDNHA IVSTSVGSEH YVSILSFVDK DQLEPGCSVL LNHKVHAVVG VLSDDTDPMV TMMKLEKAPQ ETYADIGGLD TQIQEIKESV ELPLTHPEYY EEMGIKPPKG VILYGPPGTG KTLLAKAVAN QTSATFLRVV GSELIQKYLG DGPKLVRELF RVAEEHAPSI VFIDEIDAVG TKRYDSNSGG EREIQRTMLE LLNQLDGFDS RGDVKVIMAT NRIETLDPAL IRPGRIDRKI EFPLPDEKTK RRIFTIHTSR MTLAEDVNLS ELIMAKDDLS GADIKAICTE AGLMALRERR MKVTNEDFKK SKESVLYRKK EGTPEGLYL // ID PRS8_DROME STANDARD; PRT; 405 AA. AC O18413; O45023; DT 15-JUL-1998 (Rel. 36, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE 26S PROTEASE REGULATORY SUBUNIT 8. GN PROS45 OR UG OR DUG OR CG1489. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Tracheata; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=TESTIS; RX MEDLINE=98137788; PubMed=9469929; RA Mounkes L.C., Fuller M.T.; RT "The DUG gene of Drosophila melanogaster encodes a structural and RT functional homolog of the S. cerevisiae SUG1 predicted ATPase RT associated with the 26S proteasome."; RL Gene 206:165-174(1998). RN [2] RP SEQUENCE FROM N.A. RA Cheng L., Roemer N., Smyth K.-A., Belote J., Nambu J., Schwartz L.M.; RL Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A. RC STRAIN=BERKELEY; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: THE 26S PROTEASE IS INVOLVED IN THE ATP-DEPENDENT CC DEGRADATION OF UBIQUITINATED PROTEINS. THE REGULATORY (OR ATPASE) CC COMPLEX CONFERS ATP DEPENDENCY AND SUBSTRATE SPECIFICITY TO THE CC 26S COMPLEX (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC AND NUCLEAR (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE AAA FAMILY OF ATPASES. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U97538; AAC48284.1; -. DR EMBL; AF043734; AAC63219.1; -. DR EMBL; AE003568; AAF50835.1; -. DR FlyBase; FBgn0020369; Pros45. DR InterPro; IPR003593; AAA_ATPase. DR InterPro; IPR003959; AAA_ATPase_centr. DR InterPro; IPR003960; AAA_sub. DR Pfam; PF00004; AAA; 1. DR SMART; SM00382; AAA; 1. DR TIGRFAMs; TIGR01242; 26Sp45; 1. DR PROSITE; PS00674; AAA; 1. KW Proteasome; ATP-binding; Nuclear protein. FT NP_BIND 189 196 ATP (POTENTIAL). FT CONFLICT 94 94 F -> S (IN REF. 1). SQ SEQUENCE 405 AA; 45857 MW; C098EEE56B348211 CRC64; MTVTNRMEIE SAYHKGEGFR SYYIQKIEEL QLVVAEKHQN LRRLQAQRNE LNAKVRMLRE ELQLLQEQGS YVGEVVKPMD KKKVLVKVHP EGKFVVDLDK NIDINDVTPN CRVALRNESY TLHKILPNKV DPLVSLMMVE KVPDSTYEMV GGLDKQIKEI KEVIELPVKH PELFDALGIA QPKGVLLYGP PGTGKTLLAR AVAHHTECTF IRVSGSELVQ KFIGEGSRMV RELFVMAREH APSIIFMDEI DSIGSSRIES GSGGDSEVQR TMLELLNQLD GFEATKNIKV IMATNRIDIL DPALLRPGRI DRKIEFPPPN EEARLDILKI HSRKMNLTRG INLRKIAELM PGASGAEVKG VCTEAGMYAL RERRVHVTQE DFEMAVAKVM QKDSEKNMSI KKLWK // ID MDR4_DROME STANDARD; PRT; 1302 AA. AC Q00449; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE MULTIDRUG RESISTANCE PROTEIN HOMOLOG 49 (P-GLYCOPROTEIN 49). GN MDR49. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Tracheata; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=HEAD; RX MEDLINE=91304385; PubMed=2072901; RA Wu C.-T., Budding M., Griffin M.S., Croop J.M.; RT "Isolation and characterization of Drosophila multidrug resistance RT gene homologs."; RL Mol. Cell. Biol. 11:3940-3948(1991). CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- SIMILARITY: BELONGS TO THE ABC TRANSPORTER FAMILY. MDR SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M59076; AAA28679.1; -. DR PIR; A41249; A41249. DR FlyBase; FBgn0004512; Mdr49. DR InterPro; IPR003593; AAA_ATPase. DR InterPro; IPR003439; ABC_transportr. DR InterPro; IPR001140; ABCtranprtrTM. DR Pfam; PF00005; ABC_tran; 2. DR Pfam; PF00664; ABC_membrane; 2. DR ProDom; PD000006; ABC_transportr; 2. DR SMART; SM00382; AAA; 2. DR PROSITE; PS00211; ABC_TRANSPORTER; 2. KW ATP-binding; Glycoprotein; Transmembrane; Transport; Repeat; KW Multigene family. FT DOMAIN 1 46 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 47 67 POTENTIAL. FT TRANSMEM 117 145 POTENTIAL. FT TRANSMEM 193 213 POTENTIAL. FT TRANSMEM 221 240 POTENTIAL. FT TRANSMEM 301 322 POTENTIAL. FT TRANSMEM 340 360 POTENTIAL. FT DOMAIN 361 734 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 735 756 POTENTIAL. FT TRANSMEM 780 801 POTENTIAL. FT TRANSMEM 856 876 POTENTIAL. FT TRANSMEM 878 897 POTENTIAL. FT TRANSMEM 960 980 POTENTIAL. FT TRANSMEM 997 1017 POTENTIAL. FT DOMAIN 1018 1302 CYTOPLASMIC (POTENTIAL). FT NP_BIND 437 444 ATP (POTENTIAL). FT NP_BIND 1094 1101 ATP (POTENTIAL). FT REPEAT 1 670 FT REPEAT 671 1302 FT CARBOHYD 101 101 N-LINKED (GLCNAC...) (POTENTIAL). FT VARIANT 697 697 S -> N. FT VARIANT 712 712 D -> N. FT VARIANT 952 952 V -> I. SQ SEQUENCE 1302 AA; 142724 MW; 4720C169455C28CD CRC64; MVKKEESRLP QAGDFQLKEG SVVDATRKYS YFDLFRYSTR CERFLLVVSL LVATAASAFI PYFMIIYGEF TSLLVDRTVG VGTSSPAFAL PMFGGGQQLT NASKEENNQA IIDDATAFGI GSLVGSVAMF LLITLAIDLA NRIALNQIDR IRKLFLEAML RQDIAWYDTS SGSNFASKMT EDLDKLKEGI GEKIVIVVFL IMTFVIGIVS AFVYGWKLTL VVLSCVPFII AATSVVARLQ GSLAEKELKS YSDAANVVEE VFSGIRTVFA FSGQEKEKER FGKLLIPAEN TGRKKGLYSG MGNALSWLII YLCMALAIWY GVTLILDERD LPDRVYTPAV LVIVLFAVIM GAQNLGFASP HVEAIAVATA AGQTLFNIID RPSQVDPMDE KGNRPENTAG HIRFEGIRFR YPARPDVEIL KGLTVDVLPG QTVAFVGASG CGKSTLIQLM QRFYDPEAGS VKLDGRDLRT LNVGWLRSQI GVVGQEPVLF ATTIGENIRY GRPSATQADI EKAARAANCH DFITRLPKGY DTQVGEKGAQ ISGGQKQRIA IARALVRQPQ VLLLDEATSA LDPTSEKRVQ SALELASQGP TTLVVAHRLS TITNADKIVF LKDGVVAEQG THEELMERRG LYCELVSITQ RKEATEADEG AVAGRPLQKS QNLSDEETDD DEEDEEEDEE PELQTSGSSR DSGFRASTRR KRRSQRRKKK KDKEVVSKVS FTQLMKLNSP EWRFIVVGGI ASVMHGATFP LWGLFFGDFF GILSDGDDDV VRAEVLKISM IFVGIGLMAG LGNMLQTYMF TTAGVKMTTR LRKRAFGTII GQDIAYFDDE RNSVGALCSR LASDCSNVQG ATGARVGTML QAVATLVVGM VVGFVFSWQQ TLLTLVTLPL VCLSVYLEGR FIMKSAQKAK ASIEEASQVA VEAITNIRTV NGLCLERQVL DQYVQQIDRV DVACRRKVRF RGLVFALGQA APFLAYGISM YYGGILVAEE RMNYEDIIKV AEALIFGSWM LGQALAYAPN VNDAILSAGR LMDLFKRTST QPNPPQSPYN TVEKSEGDIV YENVGFEYPT RKGTPILQGL NLTIKKSTTV ALVGPSGSGK STCVQLLLRY YDPVSGSVNL SGVPSTEFPL DTLRSKLGLV SQEPVLFDRT IAENIAYGNN FRDDVSMQEI IEAAKKSNIH NFISALPQGY DTRLGKTSQL SGGQKQRIAI ARALVRNPKI LILDEATSAL DLESEKVVQQ ALDEARSGRT CLTIAHRLTT VRNADLICVL KRGVVVEHGT HDELMALNKI YANLYLMQQV SG // ID MDR5_DROME STANDARD; PRT; 1302 AA. AC Q00748; Q9VRW3; DT 01-APR-1993 (Rel. 25, Created) DT 15-JUN-2002 (Rel. 41, Last sequence update) DT 15-JUN-2002 (Rel. 41, Last annotation update) DE MULTIDRUG RESISTANCE PROTEIN HOMOLOG 65 (P-GLYCOPROTEIN 65). GN MDR65 OR CG10181. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Tracheata; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=HEAD; RX MEDLINE=91304385; PubMed=2072901; RA Wu C.-T., Budding M., Griffin M.S., Croop J.M.; RT "Isolation and characterization of Drosophila multidrug resistance RT gene homologs."; RL Mol. Cell. Biol. 11:3940-3948(1991). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=WSIII27, AND WSIII25; RX MEDLINE=20467314; PubMed=11012721; RA Begun D.J., Whitley P.; RT "Genetics of alpha-amanitin resistance in a natural population of RT Drosophila melanogaster."; RL Heredity 85:184-190(2000). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=BERKELEY; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- SIMILARITY: BELONGS TO THE ABC TRANSPORTER FAMILY. MDR SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M59077; AAA28680.1; -. DR EMBL; AF251287; AAF69147.1; -. DR EMBL; AF251286; AAF69146.1; -. DR EMBL; AE003563; AAF50669.1; -. DR PIR; B41249; B41249. DR FlyBase; FBgn0004513; Mdr65. DR InterPro; IPR003593; AAA_ATPase. DR InterPro; IPR003439; ABC_transportr. DR InterPro; IPR001140; ABCtranprtrTM. DR Pfam; PF00005; ABC_tran; 2. DR Pfam; PF00664; ABC_membrane; 2. DR ProDom; PD000006; ABC_transportr; 2. DR SMART; SM00382; AAA; 2. DR PROSITE; PS00211; ABC_TRANSPORTER; 2. KW ATP-binding; Glycoprotein; Transmembrane; Transport; Repeat; KW Multigene family. FT DOMAIN 1 48 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 49 69 1 (POTENTIAL). FT DOMAIN 70 118 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 119 147 2 (POTENTIAL). FT DOMAIN 148 194 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 195 215 3 (POTENTIAL). FT DOMAIN 216 223 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 224 242 4 (POTENTIAL). FT DOMAIN 243 302 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 303 323 5 (POTENTIAL). FT DOMAIN 324 341 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 342 362 6 (POTENTIAL). FT DOMAIN 363 731 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 732 753 7 (POTENTIAL). FT DOMAIN 754 776 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 777 798 8 (POTENTIAL). FT DOMAIN 799 852 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 853 873 9 (POTENTIAL). FT DOMAIN 874 874 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 875 894 10 (POTENTIAL). FT DOMAIN 895 956 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 957 977 11 (POTENTIAL). FT DOMAIN 978 993 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 994 1014 12 (POTENTIAL). FT DOMAIN 1015 1302 CYTOPLASMIC (POTENTIAL). FT NP_BIND 440 447 ATP (POTENTIAL). FT NP_BIND 1094 1101 ATP (POTENTIAL). FT REPEAT 1 673 1. FT REPEAT 674 1302 2. FT CARBOHYD 103 103 N-LINKED (GLCNAC...) (POTENTIAL). FT CONFLICT 369 369 T -> S (IN REF. 1). FT CONFLICT 678 678 F -> L (IN REF. 1). SQ SEQUENCE 1302 AA; 143784 MW; 39A7BCABFA31924A CRC64; MERDEVSTSS SEGKSQEEAP MAEGLEPTEP IAFLKLFRFS TYGEIGWLFF GFIMCCIKAL TLPAVVIIYS EFTSMLVDRA MQFGTSSNVH ALPLFGGGKT LTNASREENN EALYDDSISY GILLTIASVV MFISGIFSVD VFNMVALRQV TRMRIKLFSS VIRQDIGWHD LASKQNFTQS MVDDVEKIRD GISEKVGHFV YLVVGFIITV AISFSYGWKL TLAVSSYIPL VILLNYYVAK FQGKLTAREQ ESYAGAGNLA EEILSSIRTV VSFGGEKSEV QRYENFLVPA RKASQWKGAF SGLSDAVLKS MLYLSCAGAF WYGVNLIIDD RNVENKEYTP AILMIAFFGI IVGADNIART APFLESFATA RGCATNLFKV IDLTSKIDPL STDGKLLNYG LRGDVEFQDV FFRYPSRPEV IVHRGLNIRI RAGQTVALVG SSGCGKSTCV QLLQRFYDPV FGSVLLDDLD IRKYNIQWLR SNIAVVGQEP VLFLGTIAQN ISYGKPGATQ KEIEAAATQA GAHEFITNLP ESYRSMIGER GSQLSGGQKQ RIAIARALIQ NPKILLLDEA TSALDYQSEK QVQQALDLAS KGRTTIVVSH RLSAIRGADK IVFIHDGKVL EEGSHDDLMA LEGAYYNMVR AGDINMPDEV EKEDSIEDTK QKSLALFEKS FETSPLNFEK GQKNSVQFEE PIIKALIKDT NAQSAEAPPE KPNFFRTFSR ILQLAKQEWC YLILGTISAV AVGFLYPAFA VIFGEFYAAL AEKDPEDALR RTAVLSWACL GLAFLTGLVC FLQTYLFNYA GIWLTTRMRA MTFNAMVNQE VGWFDDENNS VGALSARLSG EAVDIQGAIG YPLSGMIQAL SNFISSVSVA MYYNWKLALL CLANCPIIVG SVILEAKMMS NAVVREKQVI EEACRIATES ITNIRTVAGL RREADVIREY TEEIQRVEVL IRQKLRWRGV LNSTMQASAF FAYAVALCYG GVLVSEGQLP FQDIIKVSET LLYGSMMLAQ SLAFTPAFSA ALIAGHRLFQ ILDRKPKIQS PMGTIKNTLA KQLNLFEGVR YRGIQFRYPT RPDAKILNGL DLEVLKGQTV ALVGHSGCGK STCVQLLQRY YDPDEGTIHI DHDDIQHDLT LDGVRTKLGI VSQEPTLFER SIAENIAYGD NRRSVSMVEI IAAAKSANAH SFIISLPNGY DTRMGARGTQ LSGGQKQRIA IARALVRNPK ILLLDEATSA LDLQSEQLVQ QALDTACSGR TCIVIAHRLS TVQNADVICV IQNGQVVEQG NHMQLISQGG IYAKLHKTQK DH // ID BROW_DROME STANDARD; PRT; 675 AA. AC P12428; Q24264; DT 01-OCT-1989 (Rel. 12, Created) DT 01-OCT-1989 (Rel. 12, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE BROWN PROTEIN. GN BW. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Tracheata; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=89218981; PubMed=3149712; RA Dreesen T.D., Johnson D.H., Henikoff S.; RT "The brown protein of Drosophila melanogaster is similar to the white RT protein and to components of active transport complexes."; RL Mol. Cell. Biol. 8:5206-5215(1988). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=95044127; PubMed=7956072; RA Martin-Morris L.E., Loughney K., Kershisnik E.O., Poortinga G., RA Henikoff S.; RT "Characterization of sequences responsible for trans-inactivation of RT the Drosophila brown gene."; RL Cold Spring Harb. Symp. Quant. Biol. 58:577-584(1993). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=IG281; RA Nitasaka E., Green M.M., Yamazaki T.; RL Submitted (NOV-1992) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: PART OF A MEMBRANE-SPANNING PERMEASE SYSTEM NECESSARY CC FOR THE TRANSPORT OF PIGMENT PRECURSORS INTO PIGMENT CELLS CC RESPONSIBLE FOR EYE COLOR. BROWN AND WHITE DIMERIZE FOR THE CC TRANSPORT OF GUANINE. CC -!- SUBUNIT: HETERODIMER OF BROWN WITH WHITE. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- SIMILARITY: BELONGS TO THE ABC TRANSPORTER FAMILY. MDR SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M20630; AAA28397.1; -. DR EMBL; L23543; AAC37214.1; -. DR EMBL; L05635; AAA28398.1; -. DR PIR; A31399; FYFFB. DR FlyBase; FBgn0000241; bw. DR InterPro; IPR003439; ABC_transportr. DR Pfam; PF00005; ABC_tran; 1. DR ProDom; PD000006; ABC_transportr; 1. DR PROSITE; PS00211; ABC_TRANSPORTER; 1. KW Pigment; ATP-binding; Transmembrane; Transport. FT NP_BIND 66 73 ATP (BY SIMILARITY). FT TRANSMEM 423 441 POTENTIAL. FT TRANSMEM 454 474 POTENTIAL. FT TRANSMEM 504 522 POTENTIAL. FT TRANSMEM 531 552 POTENTIAL. FT TRANSMEM 565 583 POTENTIAL. FT TRANSMEM 645 665 POTENTIAL. FT VARIANT 28 28 D -> A. FT VARIANT 274 274 L -> I. FT VARIANT 331 331 E -> Q. FT VARIANT 407 407 R -> P. FT VARIANT 638 638 N -> T. FT CONFLICT 44 44 R -> P (IN REF. 3). SQ SEQUENCE 675 AA; 75943 MW; 81DEBDF856F4F174 CRC64; MQESGGSSGQ GGPSLCLEWK QLNYYVPDQE QSNYSFWNEC RKKRELRILQ DASGHMKTGD LIAILGGSGA GKTTLLAAIS QRLRGNLTGD VVLNGMAMER HQMTRISSFL PQFEINVKTF TAYEHLYFMS HFKMHRRTTK AEKRQRVADL LLAVGLRDAA HTRIQQLSGG ERKRLSLAEE LITDPIFLFC DEPTTGLDSF SAYSVIKTLR HLCTRRRIAK HSLNQVYGED SFETPSGESS ASGSGSKSIE MEVVAESHES LLQTMRELPA LGVLSNSPNG THKKAAICSI HQPTSDIFEL FTHIILMDGG RIVYQGRTEQ AAKFFTDLGY ELPLNCNPAD FYLKTLADKE GKENAGAVLR AKYEHETDGL YSGSWLLARS YSGDYLKHVQ NFKKIRWIYQ VYLLMVRFMT EDLRNIRSGL IAFGFFMITA VTLSLMYSGI GGLTQRTVQD VGGSIFMLSN EMIFTFSYGV TYIFPAALPI IRREVGEGTY SLSAYYVALV LSFVPVAFFK GYVFLSVIYA SIYYTRGFLL YLSMGFLMSL SAVAAVGYGV FLSSLFESDK MASECAAPFD LIFLIFGGTY MNVDTVPGLK YLSLFFYSNE ALMYKFWIDI DNIDCPVNED HPCIKTGVEV LQQGSYRNAD YTYWLDCFSL VVVAVIFHIV SFGLVRRYIH RSGYY // ID SCRT_DROME STANDARD; PRT; 666 AA. AC P45843; DT 01-NOV-1995 (Rel. 32, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE SCARLET PROTEIN. GN ST. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Tracheata; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=CANTON-S; RA Garcia R.L., Perkins H.D., Howells A.J.; RL Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE OF 200-306 FROM N.A. RX MEDLINE=89339145; PubMed=2503416; RA Tearle R.G., Belote J.M., McKeown M., Baker B.S., Howells A.J.; RT "Cloning and characterization of the scarlet gene of Drosophila RT melanogaster."; RL Genetics 122:595-606(1989). CC -!- FUNCTION: PART OF A MEMBRANE-SPANNING PERMEASE SYSTEM NECESSARY CC FOR THE TRANSPORT OF PIGMENT PRECURSORS INTO PIGMENT CELLS CC RESPONSIBLE FOR EYE COLOR. SCARLET AND WHITE DIMERIZE FOR THE CC TRANSPORT OF TRYPTOPHAN. CC -!- SUBUNIT: HETERODIMER OF SCARLET WITH WHITE. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- SIMILARITY: BELONGS TO THE ABC TRANSPORTER FAMILY. MDR SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U39739; AAA82056.1; -. DR EMBL; X76201; CAA53794.1; -. DR FlyBase; FBgn0003515; st. DR InterPro; IPR003593; AAA_ATPase. DR InterPro; IPR003439; ABC_transportr. DR InterPro; IPR005284; Pigment_permease. DR Pfam; PF00005; ABC_tran; 1. DR ProDom; PD000006; ABC_transportr; 1. DR SMART; SM00382; AAA; 1. DR TIGRFAMs; TIGR00955; 3a01204; 1. DR PROSITE; PS00211; ABC_TRANSPORTER; 1. KW Pigment; ATP-binding; Transmembrane; Transport. FT NP_BIND 108 115 ATP (POTENTIAL). FT TRANSMEM 418 438 POTENTIAL. FT TRANSMEM 445 465 POTENTIAL. FT TRANSMEM 491 511 POTENTIAL. FT TRANSMEM 519 539 POTENTIAL. FT TRANSMEM 552 572 POTENTIAL. FT TRANSMEM 577 597 POTENTIAL. FT TRANSMEM 640 660 POTENTIAL. SQ SEQUENCE 666 AA; 74506 MW; 6796ED4084B59CE4 CRC64; MSDSDSKRID VEAPERVEQH ELQVMPVGST IEVPSLDSTP KLSKRNSSER SLPLRSYSKW SPTEQGATLV WRDLCVYTNV GGSGQRMKRI INNSTGAIQP GTLMALMGSS GSGKTTLMST LAFRQPAGTV VQGDILINGR RIGPFMHRNH GYVYQDDLFL GSVSVLEHLN FMAHLRLDRR VSKEERRLII KELLERTGLL SAAQTRIGSG DDKKVLSGGE RKRLAFAVEL LNNPVILFCD EPTTGLDSYS AQQLVATLYE LAQKGTTILC TIHQPSSQLF DNFNNVMLLA DGRVAFTGSP QHALSFFANH GYYCPEAYNP ADFLIGVLAT DPGYEQASQR SAQHLCDQFA VSSAAKQRDM LVNLEIHMAQ SGNFPFDTEV ESFRGVAWYK RFHVVWLRAI VTLLRDPTIQ WLRFIQKIAM AFIIGACFAG TTEPSQLGVQ AVQGALFIMI SENTYHPMYS VLNLFPQGFP LFMRETRSGL YSTGQYYAAN ILALLPGMII EPLIFVIICY WLTGLRSTFY AFGVTAMCVV LVMNVATACG CFFSTAFNSV PLAMAYLVPL DYIFMITSGI FIQVNSLPVA FWWTQFLSWM LYANEAMTAA QWSGVQNITC FQESADLPCF HTGQDVLDKY TFNESNVYRN LLAMVGLYFG FHLLGYYCLW RRARKL // ID WHIT_DROME STANDARD; PRT; 687 AA. AC P10090; Q9V3A2; Q9XY33; DT 01-MAR-1989 (Rel. 10, Created) DT 01-NOV-1991 (Rel. 20, Last sequence update) DT 15-JUN-2002 (Rel. 41, Last annotation update) DE WHITE PROTEIN. GN W OR EG:BACN33B1.1 OR CG2759. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Tracheata; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=HEAD; RX MEDLINE=90221897; PubMed=2109311; RA Pepling M., Mount S.M.; RT "Sequence of a cDNA from the Drosophila melanogaster white gene."; RL Nucleic Acids Res. 18:1633-1633(1990). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=85134865; PubMed=6084717; RA O'Hare K., Murphy C., Levis R., Rubin G.M.; RT "DNA sequence of the white locus of Drosophila melanogaster."; RL J. Mol. Biol. 180:437-455(1984). RN [3] RP SEQUENCE FROM N.A. RX MEDLINE=21100348; PubMed=11156992; RA Lukacsovich T., Asztalos Z., Awano W., Baba K., Kondo S., Niwa S., RA Yamamoto D.; RT "Dual-tagging gene trap of novel genes in Drosophila melanogaster."; RL Genetics 157:727-742(2001). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=BERKELEY; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA 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 [5] RP SEQUENCE FROM N.A. RC STRAIN=OREGON-R; RX MEDLINE=20196011; PubMed=10731137; RA Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., RA Barrell B.G., Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., RA Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Borkova D., RA Minana B., Kafatos F.C., Louis C., Siden-Kiamos I., Bolshakov S., RA Papagiannakis G., Spanos L., Cox S., Madueno E., de Pablos B., RA Modolell J., Peter A., Schoettler P., Werner M., Mourkioti F., RA Beinert N., Dowe G., Schaefer U., Jaeckle H., Bucheton A., RA Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S., RA McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C., RA Glover D.M.; RT "From sequence to chromosome: the tip of the X chromosome of D. RT melanogaster."; RL Science 287:2220-2222(2000). RN [6] RP SEQUENCE OF 224-331 FROM N.A. RX MEDLINE=89339145; PubMed=2503416; RA Tearle R.G., Belote J.M., McKeown M., Baker B.S., Howells A.J.; RT "Cloning and characterization of the scarlet gene of Drosophila RT melanogaster."; RL Genetics 122:595-606(1989). CC -!- FUNCTION: PART OF A MEMBRANE-SPANNING PERMEASE SYSTEM NECESSARY CC FOR THE TRANSPORT OF PIGMENT PRECURSORS INTO PIGMENT CELLS CC RESPONSIBLE FOR EYE COLOR. WHITE DIMERIZE WITH BROWN FOR THE CC TRANSPORT OF GUANINE AND WITH SCARLET FOR THE TRANSPORT OF CC TRYPTOPHAN. CC -!- SUBUNIT: HETERODIMER OF WHITE WITH EITHER BROWN OR SCARLET. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- SIMILARITY: BELONGS TO THE ABC TRANSPORTER FAMILY. MDR SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X51749; CAA36038.1; -. DR EMBL; X02974; CAA26716.1; -. DR EMBL; AB028139; BAA78210.1; -. DR EMBL; AE003425; AAF45826.1; -. DR EMBL; AL133506; CAB65847.1; -. DR EMBL; X76202; CAA53795.1; -. DR PIR; S07263; FYFFW. DR PIR; S08635; S08635. DR FlyBase; FBgn0003996; w. DR InterPro; IPR003593; AAA_ATPase. DR InterPro; IPR003439; ABC_transportr. DR InterPro; IPR005284; Pigment_permease. DR Pfam; PF00005; ABC_tran; 2. DR ProDom; PD000006; ABC_transportr; 1. DR SMART; SM00382; AAA; 1. DR TIGRFAMs; TIGR00955; 3a01204; 1. DR PROSITE; PS00211; ABC_TRANSPORTER; 1. KW Pigment; ATP-binding; Transmembrane; Transport. FT NP_BIND 130 137 ATP (BY SIMILARITY). FT TRANSMEM 435 453 POTENTIAL. FT TRANSMEM 465 485 POTENTIAL. FT TRANSMEM 515 533 POTENTIAL. FT TRANSMEM 542 563 POTENTIAL. FT TRANSMEM 576 594 POTENTIAL. FT TRANSMEM 659 678 POTENTIAL. FT CONFLICT 25 29 GDSGA -> LIFEIPYHCRVTAD (IN REF. 2 AND FT 3). FT CONFLICT 49 49 L -> R (IN REF. 4 AND 5). FT CONFLICT 335 371 VGAQCPTNYNPADFYVQVLAVVPGREIESRDRIAKIC -> FT ITLHLNSYPAWVPSVLPTTIRRTFTYRCWPLCPDGRSSPVI FT GSPRYG (IN REF. 3). SQ SEQUENCE 687 AA; 75672 MW; 24AFAD799DE0D396 CRC64; MGQEDQELLI RGGSKHPSAE HLNNGDSGAA SQSCINQGFG QAKNYGTLLP PSPPEDSGSG SGQLAENLTY AWHNMDIFGA VNQPGSGWRQ LVNRTRGLFC NERHIPAPRK HLLKNVCGVA YPGELLAVMG SSGAGKTTLL NALAFRSPQG IQVSPSGMRL LNGQPVDAKE MQARCAYVQQ DDLFIGSLTA REHLIFQAMV RMPRHLTYRQ RVARVDQVIQ ELSLSKCQHT IIGVPGRVKG LSGGERKRLA FASEALTDPP LLICDEPTSG LDSFTAHSVV QVLKKLSQKG KTVILTIHQP SSELFELFDK ILLMAEGRVA FLGTPSEAVD FFSYVGAQCP TNYNPADFYV QVLAVVPGRE IESRDRIAKI CDNFAISKVA RDMEQLLATK NLEKPLEQPE NGYTYKATWF MQFRAVLWRS WLSVLKEPLL VKVRLIQTTM VAILIGLIFL GQQLTQVGVM NINGAIFLFL TNMTFQNVFA TINVFTSELP VFMREARSRL YRCDTYFLGK TIAELPLFLT VPLVFTAIAY PMIGLRAGVL HFFNCLALVT LVANVSTSFG YLISCASSST SMALSVGPPV IIPFLLFGGF FLNSGSVPVY LKWLSYLSWF RYANEGLLIN QWADVEPGEI SCTSSNTTCP SSGKVILETL NFSAADLPLD YVGLAILIVS FRVLAYLALR LRARRKE // ID ACBP_DROME STANDARD; PRT; 86 AA. AC P42281; Q9VS23; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE ACYL-COA-BINDING PROTEIN HOMOLOG (ACBP) (DIAZEPAM BINDING INHIBITOR DE HOMOLOG) (DBI). GN DBI OR CG8627. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Tracheata; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=OREGON-R; RX MEDLINE=95021227; PubMed=7935415; RA Kolmer M., Roos C., Tirronen M., Myoehaenen S., Alho H.; RT "Tissue-specific expression of the diazepam-binding inhibitor in RT Drosophila melanogaster: cloning, structure, and localization of the RT gene."; RL Mol. Cell. Biol. 14:6983-6995(1994). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=OREGON-R; RA Lagueux M., Bulet P., Hetru C.; RL Submitted (NOV-1993) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A. RC STRAIN=BERKELEY; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: BINDS MEDIUM- AND LONG-CHAIN ACYL-COA ESTERS WITH VERY CC HIGH AFFINITY AND MAY FUNCTION AS AN INTRACELLULAR CARRIER OF CC ACYL-COA ESTERS (BY SIMILARITY). MAY BE INVOLVED IN ENERGY CC METABOLISM IN A MANNER THAT DEPENDS ON THE SUBSTRATE USED FOR CC ENERGY PRODUCTION. DBI AND ITS METABOLITES ARE INVOLVED IN THE CC REGULATION OF MULTIPLE BIOLOGICAL PROCESSES. CC -!- TISSUE SPECIFICITY: CARDIA, PART OF THE MALPIGHIAN TUBULES, FAT CC BODY, AND GAMETES OF BOTH SEXES. CC -!- DEVELOPMENTAL STAGE: EXPRESSED FROM THE LARVAL STAGE ONWARDS CC THROUGHOUT THE ADULT STAGE. CC -!- SIMILARITY: BELONGS TO THE ACBP FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U04822; AAA21649.1; -. DR EMBL; U04823; AAA21650.1; -. DR EMBL; X75596; CAA53268.1; -. DR EMBL; AE003560; AAF50607.1; -. DR HSSP; P07107; 1ACA. DR FlyBase; FBgn0010387; Dbi. DR InterPro; IPR000582; Ac_coA_bind_prot. DR Pfam; PF00887; ACBP; 1. DR PRINTS; PR00689; ACOABINDINGP. DR PROSITE; PS00880; ACBP; 1. KW Transport; Lipid-binding. FT CONFLICT 55 55 K -> S (IN REF. 2). SQ SEQUENCE 86 AA; 9557 MW; 623986B5566228E1 CRC64; MVSEQFNAAA EKVKSLTKRP SDDEFLQLYA LFKQASVGDN DTAKPGLLDL KGKAKWEAWN KQKGKSSEAA QQEYITFVEG LVAKYA // ID ACH1_DROME STANDARD; PRT; 567 AA. AC P09478; DT 01-MAR-1989 (Rel. 10, Created) DT 01-MAR-1989 (Rel. 10, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE ACETYLCHOLINE RECEPTOR PROTEIN, ALPHA-LIKE CHAIN 1 PRECURSOR. GN ACRB OR ALS OR ACR96AA. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Tracheata; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=OREGON-R; RX MEDLINE=88283626; PubMed=2840281; RA Bossy B., Ballivet M., Spierer P.; RT "Conservation of neural nicotinic acetylcholine receptors from RT Drosophila to vertebrate central nervous systems."; RL EMBO J. 7:611-618(1988). CC -!- FUNCTION: AFTER BINDING ACETYLCHOLINE, THE ACHR RESPONDS BY AN CC EXTENSIVE CHANGE IN CONFORMATION THAT AFFECTS ALL SUBUNITS AND CC LEADS TO OPENING OF AN ION-CONDUCTING CHANNEL ACROSS THE PLASMA CC MEMBRANE. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- TISSUE SPECIFICITY: CNS IN EMBRYOS. CC -!- DEVELOPMENTAL STAGE: LATE EMBRYONIC, LATE PUPAL AND SECOND INSTAR CC LARVAE STAGES. CC -!- SIMILARITY: BELONGS TO THE LIGAND-GATED IONIC CHANNELS FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X07194; CAA30172.1; -. DR PIR; S00381; ACFFA1. DR FlyBase; FBgn0000036; nAcR-alpha-96Aa. DR InterPro; IPR000188; GABAA_receptor. DR InterPro; IPR001175; Neur_channel. DR Pfam; PF02931; Neur_chan_LBD; 1. DR Pfam; PF02932; Neur_chan_memb; 1. DR PRINTS; PR00252; NRIONCHANNEL. DR TIGRFAMs; TIGR00860; LIC; 1. DR PROSITE; PS00236; NEUROTR_ION_CHANNEL; 1. KW Receptor; Postsynaptic membrane; Ionic channel; Glycoprotein; Signal; KW Transmembrane; Multigene family; Polymorphism. FT SIGNAL 1 21 FT CHAIN 22 567 ACETYLCHOLINE RECEPTOR PROTEIN, ALPHA- FT LIKE CHAIN 1. FT DOMAIN 22 240 EXTRACELLULAR. FT TRANSMEM 241 264 FT TRANSMEM 272 290 FT TRANSMEM 306 325 FT DOMAIN 326 513 CYTOPLASMIC. FT TRANSMEM 514 532 FT DISULFID 149 163 BY SIMILARITY. FT DISULFID 222 223 ASSOCIATED WITH RECEPTOR ACTIVATION FT (BY SIMILARITY). FT CARBOHYD 45 45 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 233 233 N-LINKED (GLCNAC...) (POTENTIAL). FT VARIANT 538 538 H -> Y. SQ SEQUENCE 567 AA; 64016 MW; 35C84F67E907D4AE CRC64; MGSVLFAAVF IALHFATGGL ANPDAKRLYD DLLSNYNRLI RPVGNNSDRL TVKMGLRLSQ LIDVNLKNQI MTTNVWVEQE WNDYKLKWNP DDYGGVDTLH VPSEHIWHPD IVLYNNADGN YEVTIMTKAI LHHTGKVVWK PPAIYKSFCE IDVEYFPFDE QTCFMKFGSW TYDGYMVDLR HLKQTADSDN IEVGIDLQDY YISVEWDIMR VPAVRNEKFY SCCEEPYLDI VFNLTLRRKT LFYTVNLIIP CVGISFLSVL VFYLPSDSGE KISLCISILL SLTVFFLLLA EIIPPTSLTV PLLGKYLLFT MMLVTLSVVV TIAVLNVNFR SPVTHRMAPW VQRLFIQILP KLLCIERPKK EEPEEDQPPE VLTDVYHLPP DVDKFVNYDS KRFSGDYGIP ALPASHRFDL AAAGGISAHC FAEPPLPSSL PLPGADDDLF SPSGLNGDIS PGCCPAAAAA AAADLSPTFE KPYAREMEKT IEGSRFIAQH VKNKDKFESV EEDWKYVAMV LDRMFLWIFA IACVVGTALI ILQAPSLHDQ SQPIDILYSK IAKKKFELLK MGSENTL // ID ACH2_DROME STANDARD; PRT; 576 AA. AC P17644; Q9VC73; DT 01-AUG-1990 (Rel. 15, Created) DT 01-AUG-1990 (Rel. 15, Last sequence update) DT 15-JUN-2002 (Rel. 41, Last annotation update) DE ACETYLCHOLINE RECEPTOR PROTEIN, ALPHA-LIKE CHAIN 2 PRECURSOR. GN NACR-ALPHA-96AB OR ACRE OR SAD OR ACR96AB OR CG6844. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Tracheata; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=HEAD; RX MEDLINE=90301489; PubMed=2114015; RA Baumann A., Jonas P., Gundelfinger E.D.; RT "Sequence of D alpha 2, a novel alpha-like subunit of Drosophila RT nicotinic acetylcholine receptors."; RL Nucleic Acids Res. 18:3640-3640(1990). RN [2] RP SEQUENCE FROM N.A. RC TISSUE=HEAD; RX MEDLINE=90353591; PubMed=2117557; RA Jonas P., Baumann A., Merz B., Gundelfinger E.D.; RT "Structure and developmental expression of the D alpha 2 gene encoding RT a novel nicotinic acetylcholine receptor protein of Drosophila RT melanogaster."; RL FEBS Lett. 269:264-268(1990). RN [3] RP SEQUENCE FROM N.A. RX MEDLINE=90360975; PubMed=1697262; RA Sawruk E., Schloss P., Betz H., Schmitt B.; RT "Heterogeneity of Drosophila nicotinic acetylcholine receptors: SAD, a RT novel developmentally regulated alpha-subunit."; RL EMBO J. 9:2671-2677(1990). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=BERKELEY; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: AFTER BINDING ACETYLCHOLINE, THE ACHR RESPONDS BY AN CC EXTENSIVE CHANGE IN CONFORMATION THAT AFFECTS ALL SUBUNITS AND CC LEADS TO OPENING OF AN ION-CONDUCTING CHANNEL ACROSS THE PLASMA CC MEMBRANE. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- TISSUE SPECIFICITY: CNS IN EMBRYOS. CC -!- DEVELOPMENTAL STAGE: LATE EMBRYONIC AND LATE PUPAL STAGES. CC -!- SIMILARITY: BELONGS TO THE LIGAND-GATED IONIC CHANNELS FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X52274; CAA36517.1; -. DR EMBL; X53583; CAA37652.1; -. DR EMBL; AE003748; AAF56303.1; -. DR PIR; S11679; ACFFA2. DR FlyBase; FBgn0000039; nAcR-alpha-96Ab. DR InterPro; IPR000188; GABAA_receptor. DR InterPro; IPR001175; Neur_channel. DR Pfam; PF02931; Neur_chan_LBD; 1. DR Pfam; PF02932; Neur_chan_memb; 1. DR PRINTS; PR00252; NRIONCHANNEL. DR TIGRFAMs; TIGR00860; LIC; 1. DR PROSITE; PS00236; NEUROTR_ION_CHANNEL; 1. KW Receptor; Postsynaptic membrane; Ionic channel; Glycoprotein; Signal; KW Transmembrane; Multigene family. FT SIGNAL 1 21 PROBABLE. FT CHAIN 22 576 ACETYLCHOLINE RECEPTOR PROTEIN, ALPHA- FT LIKE CHAIN 2. FT DOMAIN 22 261 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 262 285 POTENTIAL. FT TRANSMEM 293 311 POTENTIAL. FT TRANSMEM 327 346 POTENTIAL. FT DOMAIN 347 526 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 527 545 POTENTIAL. FT DISULFID 169 183 BY SIMILARITY. FT DISULFID 243 244 ASSOCIATED WITH RECEPTOR ACTIVATION FT (BY SIMILARITY). FT CARBOHYD 65 65 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 254 254 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 570 570 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 576 AA; 65506 MW; 97D6A46CADC3F42F CRC64; MAPGCCTTRP RPIALLAHIW RHCKPLCLLL VLLLLCETVQ ANPDAKRLYD DLLSNYNRLI RPVSNNTDTV LVKLGLRLSQ LIDLNLKDQI LTTNVWLEHE WQDHKFKWDP SEYGGVTELY VPSEHIWLPD IVLYNNADGE YVVTTMTKAI LHYTGKVVWT PPAIFKSSCE IDVRYFPFDQ QTCFMKFGSW TYDGDQIDLK HISQKNDKDN KVEIGIDLRE YYPSVEWDIL GVPAERHEKY YPCCAEPYPD IFFNITLRRK TLFYTVNLII PCVGISYLSV LVFYLPADSG EKIALCISIL LSQTMFFLLI SEIIPSTSLA LPLLGKYLLF TMLLVGLSVV ITIIILNIHY RKPSTHKMRP WIRSFFIKRL PKLLLMRVPK DLLRDLAANK INYGLKFSKT KFGQALMDEM QMNSGGSSPD SLRRMQGRVG AGGCNGMHVT TATNRFSGLV GALGGGLSTL SGYNGLPSVL SGLDDSLSDV AARKKYPFEL EKAIHNVMFI QHHMQRQDEF NAEDQDWGFV AMVMDRLFLW LFMIASLVGT FVILGEAPSL YDDTKAIDVQ LSDVAKQIYN LTEKKN // ID ACH3_DROME STANDARD; PRT; 521 AA. AC P04755; Q9VZC3; DT 13-AUG-1987 (Rel. 05, Created) DT 13-AUG-1987 (Rel. 05, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE ACETYLCHOLINE RECEPTOR PROTEIN, BETA-LIKE CHAIN 1 PRECURSOR. GN NACR-BETA-64B OR ACRD OR ARD OR ACR64B OR CG11348 OR CG12606. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Tracheata; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RA Hermans-Borgmeyer I., Zopf D., Ryseck R.-P., Hovemann B., Betz H., RA Gundelfinger E.D.; RT "Primary structure of a developmentally regulated nicotinic RT acetylcholine receptor protein from Drosophila."; RL EMBO J. 5:1503-1508(1986). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=88296842; PubMed=3136037; RA Sawruk E., Hermans-Borgmeyer I., Betz H., Gundelfinger E.D.; RT "Characterization of an invertebrate nicotinic acetylcholine receptor RT gene: the ard gene of Drosophila melanogaster."; RL FEBS Lett. 235:40-46(1988). RN [3] RP SEQUENCE FROM N.A. RX MEDLINE=88174720; PubMed=2832736; RA Wadsworth S.C., Rosenthal L.S., Kammermeyer K.L., Potter M.B., RA Nelson D.J.; RT "Expression of a Drosophila melanogaster acetylcholine receptor- RT related gene in the central nervous system."; RL Mol. Cell. Biol. 8:778-785(1988). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=BERKELEY; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: AFTER BINDING ACETYLCHOLINE, THE ACHR RESPONDS BY AN CC EXTENSIVE CHANGE IN CONFORMATION THAT AFFECTS ALL SUBUNITS AND CC LEADS TO OPENING OF AN ION-CONDUCTING CHANNEL ACROSS THE PLASMA CC MEMBRANE. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- TISSUE SPECIFICITY: CNS IN EMBRYOS. CC -!- DEVELOPMENTAL STAGE: LATE EMBRYONIC AND LATE PUPAL STAGES. CC -!- SIMILARITY: BELONGS TO THE LIGAND-GATED IONIC CHANNELS FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X04016; CAA27641.1; -. DR EMBL; X07956; CAA30778.1; -. DR EMBL; X07957; CAA30778.1; JOINED. DR EMBL; X07958; CAA30778.1; JOINED. DR EMBL; M20316; AAA28311.1; -. DR EMBL; AE003481; AAF47900.1; -. DR PIR; S03012; ACFFNN. DR FlyBase; FBgn0000038; nAcR-beta-64B. DR InterPro; IPR000188; GABAA_receptor. DR InterPro; IPR001175; Neur_channel. DR Pfam; PF02931; Neur_chan_LBD; 1. DR Pfam; PF02932; Neur_chan_memb; 1. DR PRINTS; PR00252; NRIONCHANNEL. DR TIGRFAMs; TIGR00860; LIC; 1. DR PROSITE; PS00236; NEUROTR_ION_CHANNEL; 1. KW Receptor; Postsynaptic membrane; Ionic channel; Glycoprotein; Signal; KW Transmembrane; Multigene family. FT SIGNAL 1 24 POTENTIAL. FT CHAIN 25 521 ACETYLCHOLINE RECEPTOR PROTEIN, BETA-LIKE FT CHAIN 1. FT DOMAIN 25 235 EXTRACELLULAR. FT TRANSMEM 236 260 FT TRANSMEM 268 286 FT TRANSMEM 302 323 FT DOMAIN 324 481 CYTOPLASMIC. FT TRANSMEM 482 500 FT DISULFID 152 166 BY SIMILARITY. FT CARBOHYD 48 48 N-LINKED (GLCNAC...) (POTENTIAL). FT VARIANT 73 73 V -> I. FT CONFLICT 383 384 EL -> DV (IN REF. 3). SQ SEQUENCE 521 AA; 59901 MW; FF9BA2ABC0C3AA62 CRC64; MESSCKSWLL CSILVLVAFS LVSASEDEER LVRDLFRGYN KLIRPVQNMT QKVGVRFGLA FVQLINVNEK NQVMKSNVWL RLVWYDYQLQ WDEADYGGIG VLRLPPDKVW KPDIVLFNNA DGNYEVRYKS NVLIYPTGEV LWVPPAIYQS SCTIDVTYFP FDQQTCIMKF GSWTFNGDQV SLALYNNKNF VDLSDYWKSG TWDIIEVPAY LNVYEGDSNH PTETDITFYI IIRRKTLFYT VNLILPTVLI SFLCVLVFYL PAEAGEKVTL GISILLSLVV FLLLVSKILP PTSLVLPLIA KYLLFTFIMN TVSILVTVII INWNFRGPRT HRMPMYIRSI FLHYLPAFLF MKRPRKTRLR WMMEMPGMSM PAHPHPSYGS PAELPKHISA IGGKQSKMEV MELSDLHHPN CKINRKVNSG GELGLGDGCR RESESSDSIL LSPEASKATE AVEFIAEHLR NEDLYIQTRE DWKYVAMVID RLQLYIFFIV TTAGTVGILM DAPHIFEYVD QDRIIEIYRG K // ID ACH4_DROME STANDARD; PRT; 519 AA. AC P25162; O18403; Q9VC71; DT 01-MAY-1992 (Rel. 22, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE ACETYLCHOLINE RECEPTOR PROTEIN, BETA-LIKE CHAIN 2 PRECURSOR. GN ACRF OR SBD OR ACR96AC OR NACR-BETA-96A OR CG6798. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Tracheata; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE OF 20-519 FROM N.A. RC STRAIN=CANTON-S; RX MEDLINE=91032173; PubMed=2121539; RA Sawruk E., Udri C., Betz H., Schmitt B.; RT "SBD, a novel structural subunit of the Drosophila nicotinic RT acetylcholine receptor, shares its genomic localization with two RT alpha-subunits."; RL FEBS Lett. 273:177-181(1990). RN [2] RP SEQUENCE OF 1-65 FROM N.A. RA Millar N.S.; RT "Temperature-sensitive expression of Drosophila neuronal nicotinic RT acetylcholine receptors."; RL Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A. RC STRAIN=BERKELEY; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: AFTER BINDING ACETYLCHOLINE, THE ACHR RESPONDS BY AN CC EXTENSIVE CHANGE IN CONFORMATION THAT AFFECTS ALL SUBUNITS AND CC LEADS TO OPENING OF AN ION-CONDUCTING CHANNEL ACROSS THE PLASMA CC MEMBRANE. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- TISSUE SPECIFICITY: CNS IN EMBRYOS. CC -!- DEVELOPMENTAL STAGE: LATE EMBRYONIC AND LATE PUPAL STAGES. CC -!- SIMILARITY: BELONGS TO THE LIGAND-GATED IONIC CHANNELS FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X55676; CAA39211.1; -. DR EMBL; Y14678; CAA74994.1; -. DR EMBL; AE003748; AAF56304.1; -. DR PIR; S12899; S12899. DR FlyBase; FBgn0004118; nAcR-beta-96A. DR InterPro; IPR000188; GABAA_receptor. DR InterPro; IPR001175; Neur_channel. DR Pfam; PF02931; Neur_chan_LBD; 1. DR Pfam; PF02932; Neur_chan_memb; 1. DR TIGRFAMs; TIGR00860; LIC; 1. DR PROSITE; PS00236; NEUROTR_ION_CHANNEL; 1. KW Receptor; Postsynaptic membrane; Ionic channel; Glycoprotein; Signal; KW Transmembrane; Multigene family. FT SIGNAL 1 18 POTENTIAL. FT CHAIN 19 519 ACETYLCHOLINE RECEPTOR PROTEIN, BETA-LIKE FT CHAIN 2. FT DOMAIN 19 244 EXTRACELLULAR. FT TRANSMEM 245 269 POTENTIAL. FT TRANSMEM 277 295 POTENTIAL. FT TRANSMEM 311 332 POTENTIAL. FT DOMAIN 333 462 CYTOPLASMIC. FT TRANSMEM 463 481 POTENTIAL. FT CARBOHYD 50 50 N-LINKED (GLCNAC...) (POTENTIAL). FT DISULFID 154 168 BY SIMILARITY. FT CONFLICT 344 344 P -> R (IN REF. 1). SQ SEQUENCE 519 AA; 60140 MW; DDE67674529D2FCB CRC64; MWHWSLLCVF LLVPLANSTA PISFEANPDT KRLYDDLLSN YNRLIRPVVN NTETLTVWLG LKLSQLIEVN LKNQVMTTNL WVKQRWFDYK LRWDPEEYGG VEQLYVPSEH IWVPDIVLYN NWDGNYEVTL MTKATLKYTG EVFWEPPAIY KSSCEMNVEY FPYDEQICFM KFGSWTYNGA QVDLKHLDQI PGSNLVQVGI DLTEFYLSVE WDILEVPATK NEEYYPDTLE PFSDITFKLT MRRKTLFYTV NLIVPCVALT FLTVLVFYLP SDSGEKVTLC ISILVSLTVF FLLLAEIIPP TSLAVPLLGK YLLFTMILVS LSVWTTVCVL NIHFRSPSTH NMSPLVRKLF LHFMPKLMMM RRTQYTLPDY DDSTPSNGYT NEIDVRDSIS DFPSEFKDSQ DGAYDNGMQN SVDSDNVIPR NLTPEVLQAL RAVRFIAQHI KDADKDNEIV EDWKFVSMVL DRFFLWLFTL SCVFGTLAII CQSPSLYDTR SPIDRQLSEI PLRKNNFMLP PDIVRQVLT // ID GAB_DROME STANDARD; PRT; 606 AA. AC P25123; Q26302; DT 01-MAY-1992 (Rel. 22, Created) DT 01-MAY-1992 (Rel. 22, Last sequence update) DT 15-JUL-1998 (Rel. 36, Last annotation update) DE GAMMA-AMINOBUTYRIC-ACID RECEPTOR BETA SUBUNIT PRECURSOR (GABA(A) DE RECEPTOR) (CYCLODIENE RESISTANCE PROTEIN). GN RDL. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Tracheata; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=91334435; PubMed=1651498; RA Ffrench-Constant R.H., Mortlock D.P., Shaffer C.D., Macintyre R.J., RA Roush R.T.; RT "Molecular cloning and transformation of cyclodiene resistance in RT Drosophila: an invertebrate gamma-aminobutyric acid subtype A receptor RT locus."; RL Proc. Natl. Acad. Sci. U.S.A. 88:7209-7213(1991). RN [2] RP SEQUENCE OF 70-113 FROM N.A. RX MEDLINE=93260477; PubMed=7684073; RA Ffrench-Constant R.H., Rocheleau T.A.; RT "Drosophila gamma-aminobutyric acid receptor gene Rdl shows extensive RT alternative splicing."; RL J. Neurochem. 60:2323-2326(1993). CC -!- FUNCTION: GABA, AN INHIBITORY NEUROTRANSMITTER, MEDIATES NEURONAL CC INHIBITION BY BINDING TO THE GABA RECEPTOR AND OPENING AN INTEGRAL CC CHLORIDE CHANNEL. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- MISCELLANEOUS: RESISTANCE IS THOUGHT TO BE DUE TO INSENSITIVITY OF CC THE CYCLODIENE/PICROTOXININ BINDING SITE ON THE GABA(A) RECEPTOR- CC CHLORIDE IONOPHORE COMPLEX. CC -!- SIMILARITY: BELONGS TO THE LIGAND-GATED IONIC CHANNELS FAMILY. CC -!- CAUTION: IT IS UNCERTAIN WHETHER MET-1, MET-6 OR MET-12 IS THE CC INITIATOR. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M69057; AAA28556.1; -. DR EMBL; S61113; AAB26669.1; -. DR PIR; A41145; A41145. DR FlyBase; FBgn0004244; Rdl. DR InterPro; IPR000188; GABAA_receptor. DR InterPro; IPR001175; Neur_channel. DR Pfam; PF02931; Neur_chan_LBD; 1. DR Pfam; PF02932; Neur_chan_memb; 1. DR PRINTS; PR00252; NRIONCHANNEL. DR TIGRFAMs; TIGR00860; LIC; 1. DR PROSITE; PS00236; NEUROTR_ION_CHANNEL; 1. KW Postsynaptic membrane; Ionic channel; Glycoprotein; Signal; KW Transmembrane. FT SIGNAL 1 44 POTENTIAL. FT CHAIN 45 606 GAMMA-AMINOBUTYRIC-ACID RECEPTOR BETA FT SUBUNIT. FT DOMAIN 45 268 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 269 291 POTENTIAL. FT TRANSMEM 297 316 POTENTIAL. FT TRANSMEM 333 356 POTENTIAL. FT DOMAIN 357 568 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 569 590 POTENTIAL. FT CARBOHYD 58 58 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 248 248 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 253 253 N-LINKED (GLCNAC...) (POTENTIAL). FT DISULFID 185 199 BY SIMILARITY. FT DOMAIN 499 535 GLY-RICH. FT CONFLICT 97 97 V -> L (IN REF. 2). FT CONFLICT 101 101 L -> K (IN REF. 2). SQ SEQUENCE 606 AA; 65748 MW; 81B9DB08E1906EF1 CRC64; MSDSKMDKLA RMAPLPRTPL LTIWLAINMA LIAQETGHKR IHTVQAATGG GSMLGDVNIS AILDSFSVSY DKRVRPNYGG PPVEVGVTMY VLSISSVSEV LMDFTLDFYF RQFWTDPRLA YRKRPGVETL SVGSEFIKNI WVPDTFFVNE KQSYFHIATT SNEFIRVHHS GSITRSIRLT ITASCPMNLQ YFPMDRQLCH IEIESFGYTM RDIRYFWRDG LSSVGMSSEV ELPQFRVLGH RQRATEINLT TGNYSRLACE IQFVRSMGYY LIQIYIPSGL IVVISWVSFW LNRNATPARV ALGVTTVLTM TTLMSSTNAA LPKISYVKSI DVYLGTCFVM VFASLLEYAT VGYMAKRIQM RKQRFMAIQK IAEQKKQQLD GANQQQANPN PNANVGGPGG VGVGPGGPGG PGGGVNVGVG MGMGPEHGHG HGHHAHSHGH PHAPKQTVSN RPIGFSNIQQ NVGTRGCSIV GPLFQEVRFK VHDPKAHSKG GTLENTVNGG RGGPQSHGPG PGQGGGPPGG GGGGGGGGGP PEGGGDPEAA VPAHLLHPGK VKKDINKLLG ITPSDIDKYS RIVFPVCFVC FNLMYWIIYL HVSDVVADDL VLLGEE // ID GAB3_DROME STANDARD; PRT; 496 AA. AC Q08832; Q9VXL8; DT 01-FEB-1995 (Rel. 31, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE GAMMA-AMINOBUTYRIC-ACID RECEPTOR BETA-LIKE SUBUNIT PRECURSOR (GABA(A) DE RECEPTOR). GN LCCH3 OR CG17336. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Tracheata; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=CANTON-S; RX MEDLINE=93290631; PubMed=7685594; RA Henderson J.E., Soderlund D.M., Knipple D.C.; RT "Characterization of a putative gamma-aminobutyric acid (GABA) RT receptor beta subunit gene from Drosophila melanogaster."; RL Biochem. Biophys. Res. Commun. 193:474-482(1993). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=BERKELEY; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: GABA, AN INHIBITORY NEUROTRANSMITTER, MEDIATES NEURONAL CC INHIBITION BY BINDING TO THE GABA RECEPTOR AND OPENING AN INTEGRAL CC CHLORIDE CHANNEL (BY SIMILARITY). CC -!- SUBUNIT: GENERALLY PENTAMERIC. THERE ARE FIVE TYPES OF GABA(A) CC RECEPTOR CHAINS: ALPHA, BETA, GAMMA, DELTA, AND RHO. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- SIMILARITY: BELONGS TO THE LIGAND-GATED IONIC CHANNELS FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L17436; AAA28559.1; -. DR EMBL; S62717; AAB27090.1; -. DR EMBL; AE003500; AAF48540.1; -. DR PIR; JN0603; JN0603. DR FlyBase; FBgn0010240; Lcch3. DR InterPro; IPR000188; GABAA_receptor. DR InterPro; IPR001175; Neur_channel. DR Pfam; PF02931; Neur_chan_LBD; 1. DR Pfam; PF02932; Neur_chan_memb; 1. DR PRINTS; PR00252; NRIONCHANNEL. DR TIGRFAMs; TIGR00860; LIC; 1. DR PROSITE; PS00236; NEUROTR_ION_CHANNEL; 1. KW Postsynaptic membrane; Ionic channel; Glycoprotein; Signal; KW Transmembrane. FT SIGNAL 1 20 OR 27 (POTENTIAL). FT CHAIN 21 496 GAMMA-AMINOBUTYRIC-ACID RECEPTOR BETA- FT LIKE SUBUNIT. FT DOMAIN 21 258 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 259 280 POTENTIAL. FT TRANSMEM 285 306 POTENTIAL. FT TRANSMEM 318 342 POTENTIAL. FT DOMAIN 343 472 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 473 494 POTENTIAL. FT CARBOHYD 39 39 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 189 189 N-LINKED (GLCNAC...) (POTENTIAL). FT DISULFID 176 190 BY SIMILARITY. FT CONFLICT 12 12 G -> S (IN REF. 1). SQ SEQUENCE 496 AA; 56597 MW; 62C9A9E97E8DF681 CRC64; MTCFTRVGVS CGLFFFLLGA QLQLIRCIRK DVLAGRLENV TQTISNILQG YDIRLRPNFG GEPLHVGMDL TIASFDAISE VNMDYTITMY LNQYWRDERL AFNIFGQYFD DENDDGISDV LTLSGDFAEK IWVPDTFFAN DKNSFLHDVT ERNKLVRLGG DGAVTYGMRF TTTLACMMDL HYYPLDSQNC TVEIESYGYT VSDVVMYWKP TPVRGVEDAE LPQFTIIGYE TNDRKERLAT GVYQRLSLSF KLQRNIGYFV FQTYLPSILI VMLSWVSFWI NHEATSARVA LGITTVLTMT TISTGVRSSL PRISYVKAID IYLVMCFVFV FAALLEYAAV NYTYWGKRAK KKIKKVKECC PGKIGKSERS ETCSTTEDII ELQDVRMSPI PSLRRGTYNA TLDSIGTETM NLGKFPPSFR ITRNYGTGHS QLRRRAQRGI STRPRMLHAL KRGASAIKAT IPKIKDVNII DKYSRMIFPI SFLAFNLGYW LFYILE // ID GLK1_DROME STANDARD; PRT; 991 AA. AC Q03445; DT 15-JUL-1998 (Rel. 36, Created) DT 15-JUL-1998 (Rel. 36, Last sequence update) DT 15-JUL-1998 (Rel. 36, Last annotation update) DE GLUTAMATE RECEPTOR I PRECURSOR (DGLUR-I) (KAINATE-SELECTIVE DE GLUTAMATE RECEPTOR). GN GLU-RI. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Tracheata; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=93066263; PubMed=1359540; RA Ultsch A., Schuster C.M., Laube B., Schloss P., Schmitt B., Betz H.; RT "Glutamate receptors of Drosophila melanogaster: cloning of a kainate- RT selective subunit expressed in the central nervous system."; RL Proc. Natl. Acad. Sci. U.S.A. 89:10484-10488(1992). CC -!- FUNCTION: L-GLUTAMATE ACTS AS AN EXCITATORY NEUROTRANSMITTER AT CC MANY SYNAPSES IN THE CENTRAL NERVOUS SYSTEM. THE POSTSYNAPTIC CC ACTIONS OF GLU ARE MEDIATED BY A VARIETY OF RECEPTORS THAT ARE CC NAMED ACCORDING TO THEIR SELECTIVE AGONISTS (BY SIMILARITY). CC -!- SUBUNIT: FORMS HOMOOLIGOMERIC CHANNELS WHICH ARE ACTIVATED BY CC KAINATE. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. CC -!- TISSUE SPECIFICITY: CENTRAL NERVOUS SYSTEM. CC -!- DEVELOPMENTAL STAGE: NO EXPRESSION IS SEEN IN EARLY EMBRYOGENESIS, CC WHEREAS HIGH EXPRESSION OCCURS IN LATE EMBRYOS. DURING LARVAL CC DEVELOPMENT, EXPRESSION DECREASES TO UNDETECTABLE LEVELS IN LATE CC LARVAE, RESUMES AT THE EARLY PUPAL STAGE AND GRADUALLY INCREASES CC IN LATE PUPAE AND EARLY ADULT FLIES. HIGH LEVELS OF EXPRESSION CC COINCIDE WITH MAJOR STAGES OF NEUROGENESIS. CC -!- SIMILARITY: BELONGS TO THE LIGAND-GATED IONIC CHANNELS FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M97192; AAA28575.1; -. DR HSSP; P19491; 1GR2. DR FlyBase; FBgn0004619; Glu-RI. DR InterPro; IPR001828; ANF_receptor. DR InterPro; IPR001320; Ion_glu_receptor. DR InterPro; IPR001311; SBP/glu_receptor. DR Pfam; PF00060; lig_chan; 1. DR Pfam; PF01094; ANF_receptor; 1. DR ProDom; PD000500; Ion_glu_receptor; 1. DR SMART; SM00079; PBPe; 1. KW Receptor; Postsynaptic membrane; Ionic channel; Transmembrane; KW Signal; Glycoprotein. FT SIGNAL 1 27 POTENTIAL. FT CHAIN 28 991 GLUTAMATE RECEPTOR I. FT DOMAIN 28 611 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 612 632 POTENTIAL. FT TRANSMEM 711 731 POTENTIAL. FT TRANSMEM 896 916 POTENTIAL. FT DOMAIN 28 32 POLY-GLN. FT DOMAIN 367 371 POLY-SER. FT CARBOHYD 67 67 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 195 195 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 208 208 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 281 281 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 376 376 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 385 385 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 426 426 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 437 437 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 477 477 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 991 AA; 111655 MW; F81D5D6D614D0D2C CRC64; MHSRLKFLAY LHFICASSIF WPEFSSAQQQ QQTVSLTEKI PLGAIFEQGT DDVQSAFKYA LLNHNLNVSS RRFELQAYVD VINTADAFKL SRLICNQFSR GVYSMLGAVS PDSFDTLHSY SNTFQMPFVT PWFPEKVLAP SSGLLDFAIS MRPDYHQAII DTIQYYGWQS IIYLYDSHDG LLRLQQIYQE LKPGNETFRV QMVKRIANVT MAIEFLHTLE DLGRFSKKRI VLDCPAEMAK EIIVQHVRDI KLGRRTYHYL LSGLVMDNHW PSDVVEFGAI NITGFRIVDS NRRAVRDFHD NRKRLEPSAK AKARTQGGPN SLPPISAQAA LMYDAVFVLV EAFNRILRKK PDQFRSNHLQ RRSHGGSSSS SATGTNESSA LLDCNTSKGW VTPWEQGEKI SRVLRKVEID GLSGEIRFDE DGRRINYTLH VVEMSVNSTL QQVAEWRDDA GLLPLHSHNY ASSSRSASAS TGDYDRNHTY IVSSLLEEPY LSLKQYTYGE SLVGNDRFEG YCKDLADMLA AQLGIKYEIR LVQDGNYGAE NQYAPGGWDG MVGELIRKEA DIAISAMTIT AERERVIDFS KPFMTLGISI MIKKPVKQTP GVFSFLNPLS QEIWISVILS YVGVSFVLYF VTRFPPYEWR IVRRPQADST AQQPPGIIGG ATLSEPQAHV PPVPPNEFTM LNSFWYSLAA FMQQGCDITP PSIAGRIAAA VWWFFTIILI SSYTANLAAF LTVERMVAPI KTPEDLAMQT DVNYGTLLHG STWEFFRRSQ IGLHNKMWEY MNANQHHSVH TYDEGIRRVR QSKGKYALLV ESPKNEYVNA RPPCDTMKVG RNIDTKGFGV ATPIGSPLRK RLNEAVLTLK ENGELLRIRN KWWFDKTECN LDQETSTPNE LSLSNVAGIY YILIGGLLLA VIVAIVEFFC RNKTPQLKSP GSNGSAGGVP GMLGSSTYQR DSLSDAIMHS QAKLAMQASS EYDERLVGVE LASNVRYQYS M // ID ACPM_DROME STANDARD; PRT; 152 AA. AC Q94519; Q94520; Q9W0G8; Q9W0G9; DT 30-MAY-2000 (Rel. 39, Created) DT 30-MAY-2000 (Rel. 39, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE ACYL CARRIER PROTEIN, MITOCHONDRIAL PRECURSOR (ACP) (NADH-UBIQUINONE DE OXIDOREDUCTASE 9.6 KDA SUBUNIT) (NADH-UBIQUINONE OXIDOREDUCTASE ACYL- DE CARRIER SUBUNIT). GN MTACP1 OR ND-ACC OR MTACP OR CG9160. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Tracheata; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=OVARY; RX MEDLINE=99168769; PubMed=10071211; RA Caggese C., Ragone G., Perrini B., Moschetti R., de Pinto V., RA Caizzi R., Barsanti P.; RT "Identification of nuclear genes encoding mitochondrial proteins: RT isolation of a collection of D. melanogaster cDNAs homologous to RT sequences in the Human Gene Index database."; RL Mol. Gen. Genet. 261:64-70(1999). RN [2] RP SEQUENCE FROM N.A. RA Ragone G., Caizzi R., Caggese C.; RT "Two forms of cDNA and the sequence of Drosophila melanogaster gene RT for acyl-carrier subunit of NADH:ubiquinone oxidoreductase show RT evidence of alternatively spliced forms."; RL Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A. RC STRAIN=BERKELEY; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- SUBUNIT: COMPLEX I IS COMPOSED OF ABOUT 30 DIFFERENT SUBUNITS. CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL. CC -!- ALTERNATIVE PRODUCTS: 2 ISOFORMS; A LONG FORM (SHOWN HERE) AND CC A SHORT FORM; ARE PRODUCED BY ALTERNATIVE SPLICING. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AJ000879; CAA04368.1; -. DR EMBL; AJ000879; CAA04369.1; -. DR EMBL; Y09068; CAA70289.1; -. DR EMBL; Y09069; CAA70290.1; -. DR EMBL; AE003471; AAF47479.1; -. DR EMBL; AE003471; AAF47480.1; -. DR HSSP; P80643; 1HY8. DR FlyBase; FBgn0011361; mtacp1. DR InterPro; IPR003231; Acyl_carrier. DR InterPro; IPR003880; Ppantne_attach. DR Pfam; PF00550; pp-binding; 1. DR ProDom; PD000887; Acyl_carrier; 1. DR PROSITE; PS00012; PHOSPHOPANTETHEINE; FALSE_NEG. DR PROSITE; PS50075; ACP_DOMAIN; 1. KW Fatty acid biosynthesis; Phosphopantetheine; Mitochondrion; KW Transit peptide; Oxidoreductase; Alternative splicing. FT TRANSIT 1 ? MITOCHONDRION (POTENTIAL). FT CHAIN ? 152 ACYL CARRIER PROTEIN. FT BINDING 108 108 PHOSPHOPANTETHEINE (POTENTIAL). FT VARSPLIC 51 92 ECRGRWQTQLVRKYSAKPPLSLKLINERVLLVLKLYDKIDP FT S -> KFGVRSYSAKSTIEDIKFRVLKVVSAYDKVTAE FT (IN SHORT ISOFORM). FT CONFLICT 63 63 K -> R (IN REF. 3). SQ SEQUENCE 152 AA; 17235 MW; 79C79A8BE1512A54 CRC64; MSFTQIARSC SRLAATLAPR RVASGILIQS QASRMMHRIA VPSMTSQLSQ ECRGRWQTQL VRKYSAKPPL SLKLINERVL LVLKLYDKID PSKLNVESHF INDLGLDSLD HVEVIMAMED EFGFEIPDSD AEKLLKPADI IKYVADKEDV YE // ID ACT1_DROME STANDARD; PRT; 376 AA. AC P10987; Q24227; Q9W460; Q9U5X7; DT 01-JUL-1989 (Rel. 11, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE ACTIN-5C. GN ACT5C OR CG4027. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Tracheata; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RA Fyrberg E.A., Bond B.J., Hershey N.D., Mixter K.S., Davidson N.; RL Submitted (DEC-1987) to the EMBL/GenBank/DDBJ databases. RN [2] R