PINTA_DROME
ID PINTA_DROME Reviewed; 273 AA.
AC Q9VD09;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Retinol-binding protein pinta {ECO:0000305};
DE AltName: Full=Prolonged depolarization afterpotential is not apparent {ECO:0000303|PubMed:15917458};
GN Name=pinta {ECO:0000303|PubMed:15917458};
GN ORFNames=CG13848 {ECO:0000312|FlyBase:FBgn0038966};
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 {ECO:0000312|Proteomes:UP000000803};
RN [1] {ECO:0000312|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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 [2] {ECO:0000312|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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 [3] {ECO:0000312|EMBL:AAO62632.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAO62632.1};
RC TISSUE=Head {ECO:0000312|EMBL:AAO62632.1};
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K., Yu C., Lewis S.E., Rubin G.M., Celniker S.;
RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000305}
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=15917458; DOI=10.1523/jneurosci.0995-05.2005;
RA Wang T., Montell C.;
RT "Rhodopsin formation in Drosophila is dependent on the PINTA retinoid-
RT binding protein.";
RL J. Neurosci. 25:5187-5194(2005).
CC -!- FUNCTION: Retinoid-binding protein which shows highest affinity for
CC all-trans retinol. Can also bind all-trans forms of retinoic acid and
CC retinal, but has lower affinity for cis form retinoids. Required in
CC retinal pigment cells for rhodopsin biosynthesis.
CC {ECO:0000269|PubMed:15917458}.
CC -!- TISSUE SPECIFICITY: Strongly expressed in retina, where it may localize
CC to pigment cells. Also detected in lamina, medulla, and optic lobes.
CC {ECO:0000269|PubMed:15917458}.
CC -!- DEVELOPMENTAL STAGE: Detected from the third larval instar onwards,
CC with maximal expression levels in adult flies.
CC {ECO:0000269|PubMed:15917458}.
CC -!- DISRUPTION PHENOTYPE: Visual response is impaired, characterized by
CC abnormal electroretinogram (ERG) recordings which show loss of the
CC prolonged depolarization afterpotential which normally occurs in
CC response to blue light. Expression levels of the opsins Rh1 and Rh4 are
CC severely decreased. {ECO:0000269|PubMed:15917458}.
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DR EMBL; AE014297; AAF55994.1; -; Genomic_DNA.
DR EMBL; AE014297; AHN57465.1; -; Genomic_DNA.
DR EMBL; BT005203; AAO62632.1; -; mRNA.
DR RefSeq; NP_001287466.1; NM_001300537.1.
DR RefSeq; NP_651042.1; NM_142785.2.
DR AlphaFoldDB; Q9VD09; -.
DR SMR; Q9VD09; -.
DR STRING; 7227.FBpp0083690; -.
DR PaxDb; Q9VD09; -.
DR PRIDE; Q9VD09; -.
DR DNASU; 42635; -.
DR EnsemblMetazoa; FBtr0084297; FBpp0083690; FBgn0038966.
DR EnsemblMetazoa; FBtr0346142; FBpp0311970; FBgn0038966.
DR GeneID; 42635; -.
DR KEGG; dme:Dmel_CG13848; -.
DR UCSC; CG13848-RA; d. melanogaster.
DR CTD; 42635; -.
DR FlyBase; FBgn0038966; pinta.
DR VEuPathDB; VectorBase:FBgn0038966; -.
DR eggNOG; KOG1471; Eukaryota.
DR HOGENOM; CLU_046597_3_1_1; -.
DR InParanoid; Q9VD09; -.
DR OMA; NADFYVE; -.
DR OrthoDB; 1053004at2759; -.
DR PhylomeDB; Q9VD09; -.
DR BioCyc; MetaCyc:MON-17367; -.
DR Reactome; R-DME-8877627; Vitamin E.
DR BioGRID-ORCS; 42635; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 42635; -.
DR PRO; PR:Q9VD09; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0038966; Expressed in midgut and 26 other tissues.
DR ExpressionAtlas; Q9VD09; baseline and differential.
DR GO; GO:1902936; F:phosphatidylinositol bisphosphate binding; IBA:GO_Central.
DR GO; GO:0016918; F:retinal binding; IEA:UniProtKB-KW.
DR GO; GO:0005501; F:retinoid binding; IDA:FlyBase.
DR GO; GO:0019841; F:retinol binding; IEA:UniProtKB-KW.
DR GO; GO:0007602; P:phototransduction; IMP:FlyBase.
DR GO; GO:0016063; P:rhodopsin biosynthetic process; IMP:FlyBase.
DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR CDD; cd00170; SEC14; 1.
DR Gene3D; 3.40.525.10; -; 1.
DR InterPro; IPR001251; CRAL-TRIO_dom.
DR InterPro; IPR036865; CRAL-TRIO_dom_sf.
DR InterPro; IPR036273; CRAL/TRIO_N_dom_sf.
DR Pfam; PF00650; CRAL_TRIO; 1.
DR SMART; SM00516; SEC14; 1.
DR SUPFAM; SSF46938; SSF46938; 1.
DR SUPFAM; SSF52087; SSF52087; 1.
DR PROSITE; PS50191; CRAL_TRIO; 1.
PE 2: Evidence at transcript level;
KW Reference proteome; Retinol-binding; Sensory transduction; Vision;
KW Vitamin A.
FT CHAIN 1..273
FT /note="Retinol-binding protein pinta"
FT /id="PRO_0000438114"
FT DOMAIN 86..245
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00056"
SQ SEQUENCE 273 AA; 31626 MW; 24E2B075A996A051 CRC64;
MWSRSSSSKR QVATTDGDPE RVLAQVQDLS DWLVANPQIN GCNTFENLHF FLRTSKFDVE
RAKKKLKTFY QMRAERTEWF DNRDPQLPEI QDLLKLGVFL PIGPDAEQRM VVVIRTAAHD
PKLHSQNNVF KTSKMILDLL LKLDPETCAR GMVAILDMQG VQLGHALQMN PKLIKRSVES
WTAYPCQPKL LEFTNAPRHV NFFLNTFRIF MTPKIRSRLF VRREGTSVSC DQLPKELGGQ
GLSYMELSVK WKQLVEENAD FYVEQDKYKS KLK
