ID   RABP1_PELSI             Reviewed;         137 AA.
AC   Q5R2J5;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 72.
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   Pelodiscus sinensis (Chinese softshell turtle) (Trionyx sinensis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Testudinata; Testudines; Cryptodira; Trionychia;
OC   Trionychidae; Pelodiscus.
OX   NCBI_TaxID=13735;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=15642085; DOI=10.1111/j.1525-142x.2005.05002.x;
RA   Kuraku S., Usuda R., Kuratani S.;
RT   "Comprehensive survey of carapacial ridge-specific genes in turtle implies
RT   co-option of some regulatory genes in carapace evolution.";
RL   Evol. Dev. 7:3-17(2005).
CC   -!- FUNCTION: Cytosolic CRABPs may regulate the access of retinoic acid to
CC       the nuclear retinoic acid receptors. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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; AB124564; BAD74114.1; -; mRNA.
DR   RefSeq; NP_001273817.1; NM_001286888.1.
DR   AlphaFoldDB; Q5R2J5; -.
DR   SMR; Q5R2J5; -.
DR   STRING; 13735.ENSPSIP00000011738; -.
DR   GeneID; 102454528; -.
DR   KEGG; pss:102454528; -.
DR   CTD; 1381; -.
DR   eggNOG; KOG4015; Eukaryota.
DR   OrthoDB; 1443155at2759; -.
DR   Proteomes; UP000007267; Unassembled WGS sequence.
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   2: Evidence at transcript level;
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_0000067412"
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;  15690 MW;  B5033377D0C56D6B CRC64;
     MPNFAGTWKM KSSENFDELL RALGVNAMLR KVAVAAASKP HVEIRQDGDQ FYIKTSTTVR
     TTEINFQVGE SFQEETVDGR KCRSLATWEN ENKIYCKQTL IEGEGPKTYW TRELVNDELI
     LTFGADDVVC TRIYVRE