ID   RABP2_XENLA             Reviewed;         138 AA.
AC   P50568; Q3KQ44;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Cellular retinoic acid-binding protein 2;
DE   AltName: Full=Cellular retinoic acid-binding protein;
DE            Short=CRABP;
DE            Short=xCRABP;
DE            Short=xCRABP-b;
GN   Name=crabp2; Synonyms=crabp;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC   TISSUE=Neurula;
RX   PubMed=7947321; DOI=10.1016/0925-4773(94)90095-7;
RA   Ho L., Mercola M., Gudas L.J.;
RT   "Xenopus laevis cellular retinoic acid-binding protein: temporal and
RT   spatial expression pattern during early embryogenesis.";
RL   Mech. Dev. 47:53-64(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Neurula;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Cytosolic CRABPs may regulate the access of retinoic acid to
CC       the nuclear retinoic acid receptors.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- TISSUE SPECIFICITY: During early embryogenesis, expression is generally
CC       restricted to tissues which are sensitive to retinoic acid (RA). During
CC       gastrulation, expressed in an anterior domain in the neuroectoderm in a
CC       region that will generate head structures, and in a posterior domain
CC       that contributes to tail formation. During neurula stages, expressed in
CC       both the presumptive telencephalon and rhombencephalon, and faintly
CC       around the developing cement gland. Also expressed in branchial neural
CC       crest cells. During tail bud stages, non-uniformly expressed in the
CC       telencephalon, mesencephalon and rhombencephalon.
CC       {ECO:0000269|PubMed:7947321}.
CC   -!- DEVELOPMENTAL STAGE: Expressed zygotically from the early gastrula
CC       stage. Expression increases throughout gastrulation and remains high
CC       during the early neurula and tail bud stages.
CC       {ECO:0000269|PubMed:7947321}.
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; S74933; AAB32580.1; -; mRNA.
DR   EMBL; BC106392; AAI06393.1; -; mRNA.
DR   PIR; I51265; I51265.
DR   RefSeq; NP_001079249.1; NM_001085780.1.
DR   AlphaFoldDB; P50568; -.
DR   SMR; P50568; -.
DR   DNASU; 378522; -.
DR   GeneID; 378522; -.
DR   CTD; 378522; -.
DR   Xenbase; XB-GENE-6252659; crabp2.L.
DR   OMA; QKRGPPI; -.
DR   OrthoDB; 1443155at2759; -.
DR   Proteomes; UP000186698; Genome assembly.
DR   Bgee; 378522; Expressed in zone of skin and 14 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:InterPro.
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:0048385; P:regulation of retinoic acid receptor signaling pathway; IEA:InterPro.
DR   Gene3D; 2.40.128.20; -; 1.
DR   InterPro; IPR012674; Calycin.
DR   InterPro; IPR031281; CRABP2.
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:SF60; PTHR11955:SF60; 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..138
FT                   /note="Cellular retinoic acid-binding protein 2"
FT                   /id="PRO_0000067413"
FT   MOTIF           21..31
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000250"
FT   BINDING         133..135
FT                   /ligand="all-trans-retinoate"
FT                   /ligand_id="ChEBI:CHEBI:35291"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   138 AA;  15655 MW;  008255888995EC15 CRC64;
     MPNFSGHWKM KQSENFEEML KALGVNLMLR KIAVAAASKP AVEIKQEGET FYIKTSTTVR
     TTEINFKIGE EFDEQTVDGR PCKSLAKWVS ENKMACEQKL LKGDGPKTAW TREMTNDGEL
     ILTMTADDVV CTRIYIRD