RABP1_HUMAN
ID RABP1_HUMAN Reviewed; 137 AA.
AC P29762; Q6IAY7; Q8WTV5;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Cellular retinoic acid-binding protein 1;
DE AltName: Full=Cellular retinoic acid-binding protein I;
DE Short=CRABP-I;
GN Name=CRABP1; Synonyms=RBP5;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1309505; DOI=10.1016/0014-4827(92)90387-n;
RA Eller M.S., Oleksiak M.F., McQuaid T.J., McAfee S.G., Gilchrest B.A.;
RT "The molecular cloning and expression of two CRABP cDNAs from human skin.";
RL Exp. Cell Res. 198:328-336(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1654334; DOI=10.1016/s0021-9258(19)47422-x;
RA Astroem A., Tavakkol A., Pettersson U., Cromie M., Elder J.T.,
RA Voorhees J.J.;
RT "Molecular cloning of two human cellular retinoic acid-binding proteins
RT (CRABP). Retinoic acid-induced expression of CRABP-II but not CRABP-I in
RT adult human skin in vivo and in skin fibroblasts in vitro.";
RL J. Biol. Chem. 266:17662-17666(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=11909957; DOI=10.1128/mcb.22.8.2632-2641.2002;
RA Budhu A.S., Noy N.;
RT "Direct channeling of retinoic acid between cellular retinoic acid-binding
RT protein II and retinoic acid receptor sensitizes mammary carcinoma cells to
RT retinoic acid-induced growth arrest.";
RL Mol. Cell. Biol. 22:2632-2641(2002).
CC -!- FUNCTION: Cytosolic CRABPs may regulate the access of retinoic acid to
CC the nuclear retinoic acid receptors.
CC -!- INTERACTION:
CC P29762; O14745: SLC9A3R1; NbExp=3; IntAct=EBI-725950, EBI-349787;
CC P29762; P07101-3: TH; NbExp=3; IntAct=EBI-725950, EBI-12001016;
CC P29762; PRO_0000037576 [P27958]; Xeno; NbExp=3; IntAct=EBI-725950, EBI-8753518;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11909957}.
CC -!- DOMAIN: Forms a beta-barrel structure that accommodates hydrophobic
CC ligands in its interior. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the calycin superfamily. Fatty-acid binding
CC protein (FABP) family. {ECO:0000305}.
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DR EMBL; S74445; AAB20773.1; -; mRNA.
DR EMBL; CR457017; CAG33298.1; -; mRNA.
DR EMBL; BC022069; AAH22069.1; -; mRNA.
DR CCDS; CCDS10301.1; -.
DR PIR; JH0548; RJHU1.
DR RefSeq; NP_004369.1; NM_004378.2.
DR PDB; 7A9Y; X-ray; 1.64 A; AAA/BBB=1-137.
DR PDB; 7A9Z; X-ray; 2.41 A; AAA/BBB=1-137.
DR PDBsum; 7A9Y; -.
DR PDBsum; 7A9Z; -.
DR AlphaFoldDB; P29762; -.
DR BMRB; P29762; -.
DR SMR; P29762; -.
DR BioGRID; 107772; 8.
DR IntAct; P29762; 8.
DR MINT; P29762; -.
DR STRING; 9606.ENSP00000299529; -.
DR ChEMBL; CHEMBL2079; -.
DR DrugBank; DB00523; Alitretinoin.
DR DrugBank; DB00926; Etretinate.
DR DrugBank; DB04942; Tamibarotene.
DR DrugBank; DB00755; Tretinoin.
DR iPTMnet; P29762; -.
DR PhosphoSitePlus; P29762; -.
DR BioMuta; CRABP1; -.
DR DMDM; 266904; -.
DR EPD; P29762; -.
DR jPOST; P29762; -.
DR MassIVE; P29762; -.
DR MaxQB; P29762; -.
DR PaxDb; P29762; -.
DR PeptideAtlas; P29762; -.
DR PRIDE; P29762; -.
DR ProteomicsDB; 54609; -.
DR Antibodypedia; 1541; 258 antibodies from 30 providers.
DR DNASU; 1381; -.
DR Ensembl; ENST00000299529.7; ENSP00000299529.6; ENSG00000166426.8.
DR GeneID; 1381; -.
DR KEGG; hsa:1381; -.
DR MANE-Select; ENST00000299529.7; ENSP00000299529.6; NM_004378.3; NP_004369.1.
DR UCSC; uc002bdp.2; human.
DR CTD; 1381; -.
DR DisGeNET; 1381; -.
DR GeneCards; CRABP1; -.
DR HGNC; HGNC:2338; CRABP1.
DR HPA; ENSG00000166426; Tissue enhanced (retina, thyroid gland).
DR MIM; 180230; gene.
DR neXtProt; NX_P29762; -.
DR OpenTargets; ENSG00000166426; -.
DR PharmGKB; PA26858; -.
DR VEuPathDB; HostDB:ENSG00000166426; -.
DR eggNOG; KOG4015; Eukaryota.
DR GeneTree; ENSGT00940000159422; -.
DR HOGENOM; CLU_113772_0_2_1; -.
DR InParanoid; P29762; -.
DR OMA; EINFRIG; -.
DR OrthoDB; 1443155at2759; -.
DR PhylomeDB; P29762; -.
DR TreeFam; TF316894; -.
DR PathwayCommons; P29762; -.
DR Reactome; R-HSA-5365859; RA biosynthesis pathway.
DR SignaLink; P29762; -.
DR BioGRID-ORCS; 1381; 5 hits in 1065 CRISPR screens.
DR GeneWiki; CRABP1; -.
DR GenomeRNAi; 1381; -.
DR Pharos; P29762; Tbio.
DR PRO; PR:P29762; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; P29762; protein.
DR Bgee; ENSG00000166426; Expressed in left lobe of thyroid gland and 140 other tissues.
DR ExpressionAtlas; P29762; baseline and differential.
DR Genevisible; P29762; HS.
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:0016918; F:retinal binding; IEA:UniProtKB-KW.
DR GO; GO:0001972; F:retinoic acid binding; IBA:GO_Central.
DR GO; GO:0005501; F:retinoid binding; TAS:ProtInc.
DR GO; GO:0019841; F:retinol binding; IEA:UniProtKB-KW.
DR GO; GO:0015908; P:fatty acid transport; IBA:GO_Central.
DR GO; GO:0034653; P:retinoic acid catabolic process; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR Gene3D; 2.40.128.20; -; 1.
DR InterPro; IPR012674; Calycin.
DR InterPro; IPR031279; CRABP1.
DR InterPro; IPR000463; Fatty_acid-bd.
DR InterPro; IPR031259; ILBP.
DR InterPro; IPR000566; Lipocln_cytosolic_FA-bd_dom.
DR PANTHER; PTHR11955; PTHR11955; 1.
DR PANTHER; PTHR11955:SF62; PTHR11955:SF62; 1.
DR Pfam; PF00061; Lipocalin; 1.
DR PRINTS; PR00178; FATTYACIDBP.
DR SUPFAM; SSF50814; SSF50814; 1.
DR PROSITE; PS00214; FABP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Reference proteome; Retinol-binding; Transport;
KW Vitamin A.
FT CHAIN 1..137
FT /note="Cellular retinoic acid-binding protein 1"
FT /id="PRO_0000067406"
FT MOTIF 21..31
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT BINDING 132..134
FT /ligand="all-trans-retinoate"
FT /ligand_id="ChEBI:CHEBI:35291"
FT /evidence="ECO:0000250"
FT CONFLICT 112
FT /note="R -> S (in Ref. 4; AAH22069)"
FT /evidence="ECO:0000305"
FT CONFLICT 137
FT /note="E -> D (in Ref. 3; CAG33298)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 137 AA; 15566 MW; A3DB048973E4E8C4 CRC64;
MPNFAGTWKM RSSENFDELL KALGVNAMLR KVAVAAASKP HVEIRQDGDQ FYIKTSTTVR
TTEINFKVGE GFEEETVDGR KCRSLATWEN ENKIHCTQTL LEGDGPKTYW TRELANDELI
LTFGADDVVC TRIYVRE
