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-OCT-2019, entry version 150.
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; DOI=10.1046/j.1365-4624.1997.00015.x;
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; 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   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; 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 transmembrane transporter activity, phosphorylative mechanism; 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 transfer 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 transfer 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
//