ID   RABP2_BOVIN             Reviewed;         138 AA.
AC   Q5PXY7;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Cellular retinoic acid-binding protein 2;
DE   AltName: Full=Cellular retinoic acid-binding protein II;
DE            Short=CRABP-II;
GN   Name=CRABP2;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Jeong Y.-H., Lee S.-M., Park H.-Y., Kim H.-M., Yoon D.-H., Chung E.-R.,
RA   Kang M.-J.;
RT   "Bovine cellular retinoic acid binding protein 2.";
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Transports retinoic acid to the nucleus. Regulates the access
CC       of retinoic acid to the nuclear retinoic acid receptors (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with importin alpha, RXR and RARA. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Endoplasmic reticulum
CC       {ECO:0000250}. Nucleus {ECO:0000250}. Note=Upon ligand binding, a
CC       conformation change exposes a nuclear localization motif and the
CC       protein is transported into the nucleus. {ECO:0000250}.
CC   -!- DOMAIN: Forms a beta-barrel structure that accommodates hydrophobic
CC       ligands in its interior. {ECO:0000250}.
CC   -!- PTM: Sumoylated in response to retinoic acid binding, sumoylation is
CC       critical for dissociation from ER and subsequent nuclear translocation.
CC   -!- SIMILARITY: Belongs to the calycin superfamily. Fatty-acid binding
CC       protein (FABP) family. {ECO:0000305}.
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DR   EMBL; AY821680; AAV84002.1; -; mRNA.
DR   RefSeq; NP_001008670.1; NM_001008670.1.
DR   AlphaFoldDB; Q5PXY7; -.
DR   BMRB; Q5PXY7; -.
DR   SMR; Q5PXY7; -.
DR   STRING; 9913.ENSBTAP00000007515; -.
DR   PaxDb; Q5PXY7; -.
DR   PRIDE; Q5PXY7; -.
DR   GeneID; 493998; -.
DR   KEGG; bta:493998; -.
DR   CTD; 1382; -.
DR   eggNOG; KOG4015; Eukaryota.
DR   InParanoid; Q5PXY7; -.
DR   OrthoDB; 1443155at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; ISS:AgBase.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
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:0019841; F:retinol binding; IEA:UniProtKB-KW.
DR   GO; GO:0015908; P:fatty acid transport; IBA:GO_Central.
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; PTHR11955; 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; Endoplasmic reticulum; Isopeptide bond; Nucleus;
KW   Reference proteome; Retinol-binding; Transport; Ubl conjugation; Vitamin A.
FT   CHAIN           1..138
FT                   /note="Cellular retinoic acid-binding protein 2"
FT                   /id="PRO_0000067414"
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"
FT   CROSSLNK        102
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   138 AA;  15735 MW;  34A4C7D30775A0E3 CRC64;
     MPNFSGNWKI IRSENFEDLL KVLGVNVMLR KIAVAAASKP AVEIKQEGDT FYIKTSTTVR
     TTEINFKIGE EFEEQTVDGR PCKSLVKWES ENKMVCEQRL LKGEGPKTSW TRELTNDGEL
     ILTMTADDIV CTRVYVRE