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 27-NOV-2024, entry version 170. 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; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea; OC Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=7227; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), FUNCTION, TISSUE SPECIFICITY, AND RP DISRUPTION PHENOTYPE. RC STRAIN=Oregon-R; TISSUE=Head; RX PubMed=1903119; DOI=10.1093/genetics/127.4.761; RA Vihtelic T.S., Hyde D.R., O'Tousa J.E.; RT "Isolation and characterization of the Drosophila retinal degeneration B RT (rdgB) gene."; RL Genetics 127:761-768(1991). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B). RX PubMed=9680295; DOI=10.1046/j.1365-4624.1997.00015.x; RA Rubboli F., Bulfone A., Bogni S., Marchitiello A., Zollo M., Borsani G., RA 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., Brandon R.C., RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., RA Shen H., 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., Svirskas R., RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., RA 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., Stapleton M., RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic RT 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., George R.A., RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., RA 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., Champe M., RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A., RA Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A., RA Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S., RA Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., 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). RN [8] RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF THR-95. RX PubMed=22822086; DOI=10.1074/jbc.m112.375840; RA Garner K., Hunt A.N., Koster G., Somerharju P., Groves E., Li M., Raghu P., RA Holic R., Cockcroft S.; RT "Phosphatidylinositol transfer protein, cytoplasmic 1 (PITPNC1) binds and RT transfers phosphatidic acid."; RL J. Biol. Chem. 287:32263-32276(2012). CC -!- FUNCTION: Catalyzes the transfer of phosphatidylinositol (PI) and CC phosphatidic acid (PA) between membranes (PubMed:22822086). May control CC phosphatidylinositol concentration in transport vesicles from the CC subrhabdomeric cisternae (SRC) to the rhabdomere (PubMed:1903119). May CC function as a calcium transporter (PubMed:1903119). CC {ECO:0000269|PubMed:1903119, ECO:0000269|PubMed:22822086}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol)(in) = a CC 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol)(out); CC Xref=Rhea:RHEA:38691, ChEBI:CHEBI:57880; CC Evidence={ECO:0000269|PubMed:22822086}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38692; CC Evidence={ECO:0000305|PubMed:22822086}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphate(in) = a 1,2-diacyl-sn- CC glycero-3-phosphate(out); Xref=Rhea:RHEA:36435, ChEBI:CHEBI:58608; CC Evidence={ECO:0000269|PubMed:22822086}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36436; CC Evidence={ECO:0000305|PubMed:22822086}; CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=A; Synonyms=C, D; CC IsoId=P43125-1; Sequence=Displayed; CC Name=B; CC IsoId=P43125-2; Sequence=VSP_014533; CC -!- TISSUE SPECIFICITY: Expressed in adult heads, not detected in bodies. CC {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 transfer CC 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; 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 AlphaFoldDB; P43125; -. DR SMR; P43125; -. DR BioGRID; 58713; 28. DR STRING; 7227.FBpp0304106; -. DR SwissLipids; SLP:000000468; -. DR TCDB; 9.A.78.1.2; the retinal degeneration b protein (rdgb) family. DR iPTMnet; P43125; -. DR PaxDb; 7227-FBpp0304106; -. 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 AGR; FB:FBgn0003218; -. DR CTD; 32340; -. DR FlyBase; FBgn0003218; rdgB. DR VEuPathDB; VectorBase:FBgn0003218; -. DR eggNOG; KOG3668; Eukaryota. DR GeneTree; ENSGT00940000164860; -. DR InParanoid; P43125; -. DR PhylomeDB; P43125; -. DR Reactome; R-DME-1483226; Synthesis of PI. DR BioGRID-ORCS; 32340; 0 hits in 3 CRISPR screens. DR GenomeRNAi; 32340; -. DR PRO; PR:P43125; -. DR Proteomes; UP000000803; Chromosome X. DR Bgee; FBgn0003218; Expressed in brain and 20 other cell types or tissues. DR ExpressionAtlas; P43125; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0016020; C:membrane; TAS:FlyBase. DR GO; GO:0005886; C:plasma membrane; ISS:FlyBase. DR GO; GO:0016029; C:subrhabdomeral cisterna; TAS:FlyBase. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0070300; F:phosphatidic acid binding; IDA:UniProtKB. DR GO; GO:1990050; F:phosphatidic acid transfer activity; IDA:UniProtKB. 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:UniProtKB. DR GO; GO:0008526; F:phosphatidylinositol transfer activity; IDA:BHF-UCL. DR GO; GO:0006816; P:calcium ion transport; IEA:UniProtKB-KW. DR GO; GO:0071482; P:cellular response to light stimulus; IMP:FlyBase. DR GO; GO:0016056; P:G protein-coupled opsin signaling pathway; IMP:FlyBase. DR GO; GO:0016059; P:negative regulation of opsin-mediated signaling pathway; 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:0007608; P:sensory perception of smell; IMP:FlyBase. DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW. DR CDD; cd08889; SRPBCC_PITPNM1-2_like; 1. DR FunFam; 3.40.50.1000:FF:000173; Membrane-associated phosphatidylinositol transfer protein 2; 1. DR FunFam; 3.30.530.20:FF:000001; Phosphatidylinositol transfer protein membrane associated 2; 1. 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; PHOSPHATIDYLINOSITOL TRANSFER PROTEIN; 1. DR PANTHER; PTHR10658:SF81; PROTEIN RETINAL DEGENERATION B; 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; SSF55961; Bet v1-like; 1. DR SUPFAM; SSF56784; HAD-like; 1. DR PROSITE; PS51043; DDHD; 1. PE 1: Evidence at protein level; KW Alternative splicing; Calcium; Calcium transport; Ion transport; KW Phosphoprotein; Reference proteome; Sensory transduction; Transport; KW Vision. FT CHAIN 1..1259 FT /note="Protein retinal degeneration B" FT /id="PRO_0000097209" FT DOMAIN 730..913 FT /note="DDHD" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00378" FT REGION 268..378 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 427..454 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 472..500 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 660..692 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 278..298 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 318..337 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 340..364 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 484..500 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 660..687 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 274 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:18327897" FT MOD_RES 277 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:18327897" FT MOD_RES 401 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:18327897" FT MOD_RES 403 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:18327897" FT MOD_RES 434 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:18327897" FT VAR_SEQ 1242..1259 FT /note="YLERKTVSSCCLMVFQTT -> LHEQATNEN (in isoform B)" FT /evidence="ECO:0000303|PubMed:1903119, FT ECO:0000303|PubMed:9680295" FT /id="VSP_014533" FT MUTAGEN 95 FT /note="T->C: Increased phosphatidic acid binding but no FT effect on phosphatidylinositol binding or transfer FT activity." FT /evidence="ECO:0000269|PubMed:22822086" FT CONFLICT 89..91 FT /note="WNA -> MEC (in Ref. 1; CAA41044/CAA69291)" FT /evidence="ECO:0000305" FT CONFLICT 542..543 FT /note="QH -> HD (in Ref. 1; CAA41044/CAA69291)" FT /evidence="ECO:0000305" FT CONFLICT 622 FT /note="Y -> C (in Ref. 1; CAA41044/CAA69291)" FT /evidence="ECO:0000305" FT CONFLICT 824 FT /note="H -> R (in Ref. 1; CAA41044/CAA69291)" FT /evidence="ECO:0000305" FT CONFLICT 1002 FT /note="E -> Q (in Ref. 1; CAA41044/CAA69291)" FT /evidence="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 //