ID   RABP1_TAKRU             Reviewed;         137 AA.
AC   O42386;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 101.
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;
OS   Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX   NCBI_TaxID=31033;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9608736; DOI=10.1023/a:1008864224100;
RA   Kleinjan D.A., Dekker S., Guy J.A., Grosveld F.G.;
RT   "Cloning and sequencing of the CRABP-I locus from chicken and pufferfish:
RT   analysis of the promoter regions in transgenic mice.";
RL   Transgenic Res. 7:85-94(1998).
CC   -!- FUNCTION: Cytosolic CRABPs may regulate the access of retinoic acid to
CC       the nuclear retinoic acid receptors.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
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; Y12240; CAA72929.1; -; Genomic_DNA.
DR   EMBL; Y12241; CAA72929.1; JOINED; Genomic_DNA.
DR   EMBL; Y12242; CAA72929.1; JOINED; Genomic_DNA.
DR   AlphaFoldDB; O42386; -.
DR   SMR; O42386; -.
DR   STRING; 31033.ENSTRUP00000040844; -.
DR   eggNOG; KOG4015; Eukaryota.
DR   InParanoid; O42386; -.
DR   Proteomes; UP000005226; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016918; F:retinal binding; IEA:UniProtKB-KW.
DR   GO; GO:0001972; F:retinoic acid binding; IEA:InterPro.
DR   GO; GO:0019841; F:retinol binding; IEA:UniProtKB-KW.
DR   GO; GO:0034653; P:retinoic acid catabolic process; IEA:InterPro.
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   3: Inferred from homology;
KW   Cytoplasm; Reference proteome; Retinol-binding; Transport; Vitamin A.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..137
FT                   /note="Cellular retinoic acid-binding protein 1"
FT                   /id="PRO_0000067410"
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"
SQ   SEQUENCE   137 AA;  15608 MW;  FFB67A3C809DD29F CRC64;
     MPNFAGTWKM KSSENFDELL KALGVNTMLR KVAVAAASNP HVEIRQDGEK FYIKTSTTVR
     TTEINFHIGE EFDEETVDGR KCKSLPTWES ENKIRCKQTL VEGDGPKTFW TRELNGDELT
     LVFGADDVVC TRIYVRE