ID   RABP1_HIPCM             Reviewed;         137 AA.
AC   Q6T499;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 80.
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   Hippocampus comes (Tiger tail seahorse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Syngnathiaria; Syngnathiformes; Syngnathoidei; Syngnathidae; Hippocampus.
OX   NCBI_TaxID=109280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=15720396; DOI=10.1111/j.1742-4658.2005.04556.x;
RA   Melamed P., Xue Y., Poon J.F., Wu Q., Xie H., Yeo J., Foo T.W., Chua H.K.;
RT   "The male seahorse synthesizes and secretes a novel C-type lectin into the
RT   brood pouch during early pregnancy.";
RL   FEBS J. 272:1221-1235(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; AY437393; AAR11382.1; -; mRNA.
DR   RefSeq; XP_019742309.1; XM_019886750.1.
DR   AlphaFoldDB; Q6T499; -.
DR   SMR; Q6T499; -.
DR   STRING; 109280.ENSHCOP00000027026; -.
DR   PRIDE; Q6T499; -.
DR   Ensembl; ENSHCOT00000022765; ENSHCOP00000027026; ENSHCOG00000018495.
DR   GeneID; 109525887; -.
DR   KEGG; hcq:109525887; -.
DR   GeneTree; ENSGT00940000159422; -.
DR   OMA; NGDHFYI; -.
DR   OrthoDB; 1417203at2759; -.
DR   Proteomes; UP000264820; 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   2: Evidence at transcript level;
KW   Cytoplasm; 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_0000067411"
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;  15738 MW;  B0343E3092998FB2 CRC64;
     MPNFAGTWKM KSSENFDELL KALGVNAMLR KLAVTAASKP HVEIQQNGEQ FYIRTYTTIR
     TTEINFHIGE EFNEETVDGR KCKSLATWET ENKMYCKQTL LSGNGPKTFW TRELRGDELI
     LTFGADDVVC TRIYMRA