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   27-MAR-2024, entry version 186.
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; P13569: CFTR; NbExp=4; IntAct=EBI-725950, EBI-349854;
CC       P29762; O14745: NHERF1; 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; 9.
DR   IntAct; P29762; 9.
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; 9606-ENSP00000299529; -.
DR   PeptideAtlas; P29762; -.
DR   ProteomicsDB; 54609; -.
DR   Pumba; P29762; -.
DR   Antibodypedia; 1541; 279 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   AGR; HGNC:2338; -.
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; THWTREL; -.
DR   OrthoDB; 46617at2759; -.
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 1143 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 142 other cell types or tissues.
DR   ExpressionAtlas; P29762; baseline and differential.
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:0007165; P:signal transduction; TAS:ProtInc.
DR   CDD; cd19460; CRABP1; 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:SF62; CELLULAR RETINOIC ACID-BINDING PROTEIN 1; 1.
DR   PANTHER; PTHR11955; FATTY ACID BINDING PROTEIN; 1.
DR   Pfam; PF00061; Lipocalin; 1.
DR   PRINTS; PR00178; FATTYACIDBP.
DR   SUPFAM; SSF50814; Lipocalins; 1.
DR   PROSITE; PS00214; FABP; 1.
DR   Genevisible; P29762; HS.
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
//