RDGB_DROME
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 03-AUG-2022, entry version 162.
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};
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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; 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 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 tissues.
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: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: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; 2.
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; 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
