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Database: UniProt
Entry: Q8UVG6_DANRE
LinkDB: Q8UVG6_DANRE
Original site: Q8UVG6_DANRE 
ID   Q8UVG6_DANRE            Unreviewed;       135 AA.
AC   Q8UVG6; A7E2P5;
DT   01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2002, sequence version 1.
DT   27-MAR-2024, entry version 165.
DE   SubName: Full=Cellular retinol-binding protein type II {ECO:0000313|EMBL:AAM95336.1};
DE   SubName: Full=Putative cellular retinol-binding protein {ECO:0000313|EMBL:AAL38648.1};
DE   SubName: Full=Rbp2a protein {ECO:0000313|EMBL:AAI50458.1};
DE   SubName: Full=Retinol-binding protein 2 {ECO:0000313|EMBL:AAH62286.1, ECO:0000313|Ensembl:ENSDARP00000093236, ECO:0000313|RefSeq:NP_694549.1};
GN   Name=rbp2a {ECO:0000313|EMBL:AAI50458.1,
GN   ECO:0000313|Ensembl:ENSDARP00000093236,
GN   ECO:0000313|RefSeq:NP_694549.1, ECO:0000313|ZFIN:ZDB-GENE-020320-2};
GN   Synonyms=CRBPII {ECO:0000313|RefSeq:NP_694549.1}, rbp2
GN   {ECO:0000313|RefSeq:NP_694549.1}, wu:fb69e02
GN   {ECO:0000313|RefSeq:NP_694549.1};
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955 {ECO:0000313|EMBL:AAI50458.1};
RN   [1] {ECO:0000313|EMBL:AAM95336.1, ECO:0000313|RefSeq:NP_694549.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=12230582; DOI=10.1046/j.1432-1033.2002.03170.x;
RA   Cameron M.C., Denovan-Wright E.M., Sharma M.K., Wright J.M.;
RT   "Cellular retinol-binding protein type II (CRBPII) in adult zebrafish
RT   (Danio rerio). cDNA sequence, tissue-specific expression and gene linkage
RT   analysis.";
RL   Eur. J. Biochem. 269:4685-4692(2002).
RN   [2] {ECO:0000313|EMBL:AAL38648.1, ECO:0007829|PDB:1KQW}
RP   X-RAY CRYSTALLOGRAPHY (1.38 ANGSTROMS) OF 2-135.
RX   PubMed=12162964; DOI=10.1016/s0022-2836(02)00628-9;
RA   Calderone V., Folli C., Marchesani A., Berni R., Zanotti G.;
RT   "Identification and structural analysis of a zebrafish apo and holo
RT   cellular retinol-binding protein.";
RL   J. Mol. Biol. 321:527-535(2002).
RN   [3] {ECO:0000313|RefSeq:NP_694549.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=14717701;
RA   Liu R.Z., Denovan-Wright E.M., Degrave A., Thisse C., Thisse B.,
RA   Wright J.M.;
RT   "Spatio-temporal distribution of cellular retinol-binding protein gene
RT   transcripts (CRBPI and CRBPII) in the developing and adult zebrafish (Danio
RT   rerio).";
RL   Eur. J. Biochem. 271:339-348(2004).
RN   [4] {ECO:0000313|RefSeq:NP_694549.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=16109975;
RA   Woods I.G., Wilson C., Friedlander B., Chang P., Reyes D.K., Nix R.,
RA   Kelly P.D., Chu F., Postlethwait J.H., Talbot W.S.;
RT   "The zebrafish gene map defines ancestral vertebrate chromosomes.";
RL   Genome Res. 15:1307-1314(2005).
RN   [5] {ECO:0000313|RefSeq:NP_694549.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=15509725; DOI=10.1093/molbev/msi030;
RA   Liu R.Z., Sun Q., Thisse C., Thisse B., Wright J.M., Denovan-Wright E.M.;
RT   "The cellular retinol-binding protein genes are duplicated and
RT   differentially transcribed in the developing and adult zebrafish (Danio
RT   rerio).";
RL   Mol. Biol. Evol. 22:469-477(2005).
RN   [6] {ECO:0000313|EMBL:AAI50458.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Liver {ECO:0000313|EMBL:AAI50458.1}, and Whole
RC   {ECO:0000313|EMBL:AAH62286.1};
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
RN   [7] {ECO:0000313|Ensembl:ENSDARP00000093236}
RP   IDENTIFICATION.
RC   STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000093236};
RG   Ensembl;
RL   Submitted (FEB-2012) to UniProtKB.
RN   [8] {ECO:0000313|Ensembl:ENSDARP00000093236, ECO:0000313|Proteomes:UP000000437}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000093236};
RX   PubMed=23594743; DOI=10.1038/nature12111;
RG   Genome Reference Consortium Zebrafish;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA   Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA   Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA   White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA   Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA   Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA   Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Elliot D., Eliott D.,
RA   Threadgold G., Harden G., Ware D., Begum S., Mortimore B., Mortimer B.,
RA   Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M.,
RA   Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M.,
RA   Glithero R., Howden P., Barker N., Lloyd C., Stevens C., Harley J.,
RA   Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D.,
RA   Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K.,
RA   Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R.,
RA   Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M.,
RA   Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D.,
RA   Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M.,
RA   Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M.,
RA   Woodmansey R., Clark G., Cooper J., Cooper J., Tromans A., Grafham D.,
RA   Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J.,
RA   Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I.,
RA   Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M.,
RA   Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M.,
RA   Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G., Osoegawa K., Zhu B.,
RA   Rapp A., Widaa S., Langford C., Yang F., Schuster S.C., Carter N.P.,
RA   Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R.,
RA   Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I.,
RA   Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H.,
RA   Rogers J., Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the human
RT   genome.";
RL   Nature 496:498-503(2013).
RN   [9] {ECO:0000313|RefSeq:NP_694549.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=28437725;
RA   Zhang Q., Ma X., Dzakpasu M., Wang X.C.;
RT   "Evaluation of ecotoxicological effects of benzophenone UV filters:
RT   Luminescent bacteria toxicity, genotoxicity and hormonal activity.";
RL   Ecotoxicol. Environ. Saf. 142:338-347(2017).
RN   [10] {ECO:0000313|RefSeq:NP_694549.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=29246861;
RA   He J., Yang Y., Zhang J., Chen J., Wei X., He J., Luo L.;
RT   "Ribosome biogenesis protein Urb1 acts downstream of mTOR complex 1 to
RT   modulate digestive organ development in zebrafish.";
RL   J. Genet. Genomics 44:567-576(2017).
RN   [11] {ECO:0000313|RefSeq:NP_694549.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=28850571;
RA   Lickwar C.R., Camp J.G., Weiser M., Cocchiaro J.L., Kingsley D.M.,
RA   Furey T.S., Sheikh S.Z., Rawls J.F.;
RT   "Genomic dissection of conserved transcriptional regulation in intestinal
RT   epithelial cells.";
RL   PLoS Biol. 15:e2002054-e2002054(2017).
RN   [12] {ECO:0000313|RefSeq:NP_694549.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=28096348;
RA   Rabinowitz J.S., Robitaille A.M., Wang Y., Ray C.A., Thummel R., Gu H.,
RA   Djukovic D., Raftery D., Berndt J.D., Moon R.T.;
RT   "Transcriptomic, proteomic, and metabolomic landscape of positional memory
RT   in the caudal fin of zebrafish.";
RL   Proc. Natl. Acad. Sci. U.S.A. 114:E717-E726(2017).
RN   [13] {ECO:0000313|RefSeq:NP_694549.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=27898262;
RA   Lebedeva S., de Jesus Domingues A.M., Butter F., Ketting R.F.;
RT   "Characterization of genetic loss-of-function of Fus in zebrafish.";
RL   RNA Biol. 14:29-35(2017).
RN   [14] {ECO:0000313|Ensembl:ENSDARP00000153700}
RP   IDENTIFICATION.
RC   STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000153700};
RG   Ensembl;
RL   Submitted (APR-2018) to UniProtKB.
RN   [15] {ECO:0000313|RefSeq:NP_694549.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the calycin superfamily. Fatty-acid binding
CC       protein (FABP) family. {ECO:0000256|ARBA:ARBA00008390,
CC       ECO:0000256|RuleBase:RU003696}.
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DR   EMBL; BX000987; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BX088654; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC062286; AAH62286.1; -; mRNA.
DR   EMBL; BC150457; AAI50458.1; -; mRNA.
DR   EMBL; AF448140; AAL38648.1; -; mRNA.
DR   EMBL; AF363957; AAM95336.1; -; mRNA.
DR   RefSeq; NP_694549.1; NM_153004.1.
DR   PDB; 1KQW; X-ray; 1.38 A; A=2-135.
DR   PDB; 1KQX; X-ray; 1.70 A; A=2-135.
DR   PDBsum; 1KQW; -.
DR   PDBsum; 1KQX; -.
DR   STRING; 7955.ENSDARP00000093236; -.
DR   PaxDb; 7955-ENSDARP00000093236; -.
DR   Ensembl; ENSDART00000102459.5; ENSDARP00000093236.3; ENSDARG00000070038.5.
DR   Ensembl; ENSDART00000180859.1; ENSDARP00000153700.1; ENSDARG00000115141.1.
DR   GeneID; 568032; -.
DR   KEGG; dre:568032; -.
DR   AGR; ZFIN:ZDB-GENE-020320-2; -.
DR   CTD; 568032; -.
DR   ZFIN; ZDB-GENE-020320-2; rbp2a.
DR   eggNOG; KOG4015; Eukaryota.
DR   HOGENOM; CLU_113772_5_1_1; -.
DR   OMA; EFEECTK; -.
DR   OrthoDB; 46617at2759; -.
DR   TreeFam; TF316894; -.
DR   Reactome; R-DRE-975634; Retinoid metabolism and transport.
DR   Proteomes; UP000000437; Alternate scaffold 15.
DR   Proteomes; UP000000437; Chromosome 15.
DR   Bgee; ENSDARG00000070038; Expressed in intestine and 20 other cell types or tissues.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005504; F:fatty acid binding; IBA:GO_Central.
DR   GO; GO:0015908; P:fatty acid transport; IBA:GO_Central.
DR   CDD; cd19463; CRBP2; 1.
DR   Gene3D; 2.40.128.20; -; 1.
DR   InterPro; IPR012674; Calycin.
DR   InterPro; IPR000463; Fatty_acid-bd.
DR   InterPro; IPR031259; ILBP.
DR   InterPro; IPR000566; Lipocln_cytosolic_FA-bd_dom.
DR   PANTHER; PTHR11955; FATTY ACID BINDING PROTEIN; 1.
DR   PANTHER; PTHR11955:SF59; RETINOL-BINDING PROTEIN 2; 1.
DR   Pfam; PF00061; Lipocalin; 1.
DR   PRINTS; PR00178; FATTYACIDBP.
DR   SUPFAM; SSF50814; Lipocalins; 1.
DR   PROSITE; PS00214; FABP; 1.
PE   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:1KQW, ECO:0007829|PDB:1KQX};
KW   Proteomics identification {ECO:0007829|PeptideAtlas:Q8UVG6};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000437};
KW   Transport {ECO:0000256|RuleBase:RU003696}.
FT   DOMAIN          7..24
FT                   /note="Cytosolic fatty-acid binding proteins"
FT                   /evidence="ECO:0000259|PROSITE:PS00214"
SQ   SEQUENCE   135 AA;  15806 MW;  451F80A5C2F3EDA3 CRC64;
     MPADFNGTWE MLSNDNFEDV MKALDIDFAT RKIAVHLKQT KVIVQNGDKF ETKTLSTFRN
     YEVNFVIGEE FDEQTKGLDN RTVKTLVKWD GDKLVCVQKG EKENRGWKQW IEGDLLHLEI
     HCQDKVCHQV FKKKN
//
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