ID RDGB_DROME Reviewed; 1259 AA. AC P43125; A4V4E8; O02434; Q6NP01; Q961R2; Q9VY88; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2005, sequence version 2. DT 16-JAN-2019, entry version 144. DE RecName: Full=Protein retinal degeneration B; DE AltName: Full=Probable calcium transporter rdgB; GN Name=rdgB; ORFNames=CG11111; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=7227; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), FUNCTION, TISSUE SPECIFICITY, RP AND DISRUPTION PHENOTYPE. RC STRAIN=Oregon-R; TISSUE=Head; RX PubMed=1903119; RA Vihtelic T.S., Hyde D.R., O'Tousa J.E.; RT "Isolation and characterization of the Drosophila retinal degeneration RT B (rdgB) gene."; RL Genetics 127:761-768(1991). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B). RX PubMed=9680295; RA Rubboli F., Bulfone A., Bogni S., Marchitiello A., Zollo M., RA Borsani G., Ballabio A., Banfi S.; RT "A mammalian homologue of the Drosophila retinal degeneration B gene: RT implications for the evolution of phototransduction mechanisms."; RL Genes Funct. 1:205-213(1997). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley; RX PubMed=10731132; DOI=10.1126/science.287.5461.2185; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., RA Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING. RC STRAIN=Berkeley; RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A). RC STRAIN=Berkeley; TISSUE=Head; RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 513-1241. RC STRAIN=Berkeley; TISSUE=Head; RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., RA Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., RA George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., RA Miranda A., Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., RA Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., RA Celniker S.E.; RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases. RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-274; SER-277; SER-401; RP SER-403 AND SER-434, AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Embryo; RX PubMed=18327897; DOI=10.1021/pr700696a; RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.; RT "Phosphoproteome analysis of Drosophila melanogaster embryos."; RL J. Proteome Res. 7:1675-1682(2008). CC -!- FUNCTION: May control phosphatidylinositol concentration in CC transport vesicles from the subrhabdomeric cisternae (SRC) to the CC rhabdomere. May function as a calcium transporter. CC {ECO:0000269|PubMed:1903119}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=A; Synonyms=C, D; CC IsoId=P43125-1; Sequence=Displayed; CC Note=No experimental confirmation available.; CC Name=B; CC IsoId=P43125-2; Sequence=VSP_014533; CC -!- TISSUE SPECIFICITY: Expressed in adult heads, not detected in CC bodies. {ECO:0000269|PubMed:1903119}. CC -!- DISRUPTION PHENOTYPE: Flies exhibit rapid light-induced retinal CC degeneration. {ECO:0000269|PubMed:1903119}. CC -!- SIMILARITY: Belongs to the PtdIns transfer protein family. PI CC transfer class IIA subfamily. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAR82797.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305}; CC Sequence=CAA41044.1; Type=Frameshift; Positions=1054, 1158; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X57978; CAA41044.1; ALT_FRAME; mRNA. DR EMBL; Y08035; CAA69291.1; -; mRNA. DR EMBL; AE014298; AAF48315.1; -; Genomic_DNA. DR EMBL; AE014298; AAF48316.2; -; Genomic_DNA. DR EMBL; AE014298; AAX52494.1; -; Genomic_DNA. DR EMBL; AE014298; AAX52495.1; -; Genomic_DNA. DR EMBL; AY051422; AAK92846.1; -; mRNA. DR EMBL; BT011130; AAR82797.1; ALT_SEQ; mRNA. DR PIR; A61221; A61221. DR RefSeq; NP_001014740.1; NM_001014740.2. [P43125-1] DR RefSeq; NP_001014741.1; NM_001014741.3. [P43125-1] DR RefSeq; NP_001162749.1; NM_001169278.3. [P43125-2] DR RefSeq; NP_511149.2; NM_078594.3. [P43125-2] DR RefSeq; NP_727733.1; NM_167382.3. [P43125-1] DR UniGene; Dm.7839; -. DR ProteinModelPortal; P43125; -. DR SMR; P43125; -. DR BioGrid; 58713; 28. DR STRING; 7227.FBpp0304106; -. DR SwissLipids; SLP:000000468; -. DR iPTMnet; P43125; -. DR PaxDb; P43125; -. DR PRIDE; P43125; -. DR EnsemblMetazoa; FBtr0073822; FBpp0073653; FBgn0003218. [P43125-1] DR EnsemblMetazoa; FBtr0073823; FBpp0073654; FBgn0003218. [P43125-2] DR EnsemblMetazoa; FBtr0100194; FBpp0099560; FBgn0003218. [P43125-1] DR EnsemblMetazoa; FBtr0100195; FBpp0099561; FBgn0003218. [P43125-1] DR EnsemblMetazoa; FBtr0301533; FBpp0290748; FBgn0003218. [P43125-2] DR GeneID; 32340; -. DR KEGG; dme:Dmel_CG11111; -. DR CTD; 32340; -. DR FlyBase; FBgn0003218; rdgB. DR eggNOG; KOG3668; Eukaryota. DR eggNOG; COG5083; LUCA. DR GeneTree; ENSGT00940000164860; -. DR InParanoid; P43125; -. DR PhylomeDB; P43125; -. DR Reactome; R-DME-1483226; Synthesis of PI. DR GenomeRNAi; 32340; -. DR PRO; PR:P43125; -. DR Proteomes; UP000000803; Chromosome X. DR Bgee; FBgn0003218; Expressed in 23 organ(s), highest expression level in head. DR ExpressionAtlas; P43125; baseline and differential. DR Genevisible; P43125; DM. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0016021; C:integral component of membrane; TAS:FlyBase. DR GO; GO:0005887; C:integral component of plasma membrane; ISS:FlyBase. DR GO; GO:0005886; C:plasma membrane; ISS:FlyBase. DR GO; GO:0016029; C:subrhabdomeral cisterna; TAS:FlyBase. DR GO; GO:0005388; F:calcium-transporting ATPase activity; ISS:FlyBase. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0070300; F:phosphatidic acid binding; IDA:FlyBase. DR GO; GO:1990050; F:phosphatidic acid transporter activity; IDA:FlyBase. DR GO; GO:0031210; F:phosphatidylcholine binding; IBA:GO_Central. DR GO; GO:0008525; F:phosphatidylcholine transporter activity; IDA:FlyBase. DR GO; GO:0035091; F:phosphatidylinositol binding; IDA:FlyBase. DR GO; GO:0008526; F:phosphatidylinositol transporter activity; IDA:BHF-UCL. DR GO; GO:0071482; P:cellular response to light stimulus; IMP:FlyBase. DR GO; GO:0016059; P:deactivation of rhodopsin mediated signaling; IMP:FlyBase. DR GO; GO:0046488; P:phosphatidylinositol metabolic process; IMP:FlyBase. DR GO; GO:0015914; P:phospholipid transport; IDA:BHF-UCL. DR GO; GO:0007602; P:phototransduction; IMP:FlyBase. DR GO; GO:0007603; P:phototransduction, visible light; IMP:FlyBase. DR GO; GO:0016056; P:rhodopsin mediated signaling pathway; IMP:FlyBase. DR GO; GO:0007608; P:sensory perception of smell; IMP:FlyBase. DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW. DR Gene3D; 3.30.530.20; -; 1. DR InterPro; IPR004177; DDHD_dom. DR InterPro; IPR036412; HAD-like_sf. DR InterPro; IPR031315; LNS2/PITP. DR InterPro; IPR001666; PI_transfer. DR InterPro; IPR023393; START-like_dom_sf. DR PANTHER; PTHR10658; PTHR10658; 1. DR Pfam; PF02862; DDHD; 2. DR Pfam; PF02121; IP_trans; 1. DR PRINTS; PR00391; PITRANSFER. DR SMART; SM01127; DDHD; 1. DR SMART; SM00775; LNS2; 1. DR SUPFAM; SSF56784; SSF56784; 1. DR PROSITE; PS51043; DDHD; 1. PE 1: Evidence at protein level; KW Alternative splicing; Calcium; Calcium transport; Complete proteome; KW Ion transport; Phosphoprotein; Reference proteome; KW Sensory transduction; Transport; Vision. FT CHAIN 1 1259 Protein retinal degeneration B. FT /FTId=PRO_0000097209. FT DOMAIN 730 913 DDHD. {ECO:0000255|PROSITE- FT ProRule:PRU00378}. FT COMPBIAS 321 332 Asp/Glu-rich (highly acidic). FT MOD_RES 274 274 Phosphoserine. FT {ECO:0000269|PubMed:18327897}. FT MOD_RES 277 277 Phosphoserine. FT {ECO:0000269|PubMed:18327897}. FT MOD_RES 401 401 Phosphoserine. FT {ECO:0000269|PubMed:18327897}. FT MOD_RES 403 403 Phosphoserine. FT {ECO:0000269|PubMed:18327897}. FT MOD_RES 434 434 Phosphoserine. FT {ECO:0000269|PubMed:18327897}. FT VAR_SEQ 1242 1259 YLERKTVSSCCLMVFQTT -> LHEQATNEN (in FT isoform B). {ECO:0000303|PubMed:1903119, FT ECO:0000303|PubMed:9680295}. FT /FTId=VSP_014533. FT CONFLICT 89 91 WNA -> MEC (in Ref. 1; CAA41044/ FT CAA69291). {ECO:0000305}. FT CONFLICT 542 543 QH -> HD (in Ref. 1; CAA41044/CAA69291). FT {ECO:0000305}. FT CONFLICT 622 622 Y -> C (in Ref. 1; CAA41044/CAA69291). FT {ECO:0000305}. FT CONFLICT 824 824 H -> R (in Ref. 1; CAA41044/CAA69291). FT {ECO:0000305}. FT CONFLICT 1002 1002 E -> Q (in Ref. 1; CAA41044/CAA69291). FT {ECO:0000305}. SQ SEQUENCE 1259 AA; 138895 MW; 9DD40B76EB1079F7 CRC64; MLIKEYRIPL PLTVEEYRIA QLYMIAKKSR EESHGEGSGV EIIINEPYKD GPGGNGQYTK KIYHVGNHLP GWIKSLLPKS ALTVEEEAWN AYPYTRTRYT CPFVEKFSLD IETYYYPDNG YQDNVFQLSG SDLRNRIVDV IDIVKDQLWG GDYVKEEDPK HFVSDKTGRG PLAEDWLEEY WREVKGKKQP TPRNMSLMTA YKICRVEFRY WGMQTKLEKF IHDVALRKMM LRAHRQAWAW QDEWFGLTIE DIRELERQTQ LALAKKMGGG EECSDDSVSE PYVSTAATAA STTGSERKKS APAVPPIVTQ QPPSAEASSD EEGEEEEDDD EDENDAIGTG VDLSANQGGS AQRSRSQSIQ MAQKGKFGSK GALHSPVGSA HSFDLQVANW RMERLEVDSK SNSDEEFFDC LDTNETNSLA KWSSLELLGE GDDSPPPHGG PSSAASVGGR GNSRQEDSIF NQDFLMRVAS ERGNKRQLRS SASVDRSHDS SPPGSPSTPS CPTTILILVV HAGSVLDAAS ELTAKKSDVT TFRGSFEAVM RQHYPSLLTH VTIKMVPCPS ICTDALGILS SLSPYSFDAS PSAADIPNIA DVPIGAIPLL SVASPEFHET VNKTVAAANI VYHEFLKSEE GHGFSGQIVM LGDSMGSLLA YEALCRSNGS QPGTASGASN SGGDAATNIN THNPLSPRNS RLDDDERFIE ADLDAKRLLV APSPRRRRSS SSSDSRATKL DFEVCDFFMF GSPLSVVLAA RKLHDAKAAL PRPNCHQVYN LFHPTDPIAS RLEPLLSARF SILAPVNVPR YAKYPLGNGQ PLHLLEVIQS HPQHFNDGNN LLAGRRLSDA SMQSTISGLI ENVSLSTIHA LQNKWWGTKR LDYALYCPEG LSNFPAHALP HLFHASYWES PDVIAFILRQ IGKFEGIPFV GSNDDKDNAS FHPGQPREKW IKKRTSVKLK NVAANHRAND VIVQEGREQR LNARFMYGPL DMITLHGEKV DVHIMKDPPA GEWTFLSTEV TDKNGRISYS IPDQVSLGYG IYPVKMVVRG DHTSVDCYMA VVPPLTECVV FSIDGSFTAS MSVTGRDPKV RAGAVDVCRH WQELGYLLIY ITGRPDMQQQ RVVSWLSQHN FPHGLISFAD GLSTDPLGHK TAYLNNLVQN HGISITAAYG SSKDISVYTN VGMRTDQIFI VGKVGKKLQS NATVLSDGYA AHLAGLQAVG GSRPAKGNAR MVIPRGCFNL PGQTANPRRR RYLERKTVSS CCLMVFQTT //