ID   RABP2_RAT               Reviewed;         139 AA.
AC   P51673;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 141.
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   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Sprague-Dawley; TISSUE=Corpus luteum;
RX   PubMed=7750498; DOI=10.1210/endo.136.6.7750498;
RA   Bucco R.A., Melner M.H., Gordon D.S., Leers-Sucheta S., Ong D.E.;
RT   "Inducible expression of cellular retinoic acid-binding protein II in rat
RT   ovary: gonadotropin regulation during luteal development.";
RL   Endocrinology 136:2730-2740(1995).
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. Endoplasmic reticulum {ECO:0000250}.
CC       Nucleus {ECO:0000250}. Note=Upon ligand binding, a conformation change
CC       exposes a nuclear localization motif and the protein is transported
CC       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; U23407; AAA80225.1; -; mRNA.
DR   PIR; I53298; I53298.
DR   RefSeq; NP_058940.1; NM_017244.1.
DR   AlphaFoldDB; P51673; -.
DR   SMR; P51673; -.
DR   STRING; 10116.ENSRNOP00000015134; -.
DR   ChEMBL; CHEMBL4345; -.
DR   PhosphoSitePlus; P51673; -.
DR   PaxDb; P51673; -.
DR   GeneID; 29563; -.
DR   KEGG; rno:29563; -.
DR   UCSC; RGD:62070; rat.
DR   CTD; 1382; -.
DR   RGD; 62070; Crabp2.
DR   VEuPathDB; HostDB:ENSRNOG00000022101; -.
DR   eggNOG; KOG4015; Eukaryota.
DR   HOGENOM; CLU_113772_0_2_1; -.
DR   InParanoid; P51673; -.
DR   OMA; ISTWEGD; -.
DR   OrthoDB; 1443155at2759; -.
DR   PhylomeDB; P51673; -.
DR   TreeFam; TF316894; -.
DR   Reactome; R-RNO-5362517; Signaling by Retinoic Acid.
DR   PRO; PR:P51673; -.
DR   Proteomes; UP000002494; Chromosome 2.
DR   Bgee; ENSRNOG00000022101; Expressed in ovary and 18 other tissues.
DR   Genevisible; P51673; RN.
DR   GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR   GO; GO:0005829; C:cytosol; IDA:RGD.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; ISO:RGD.
DR   GO; GO:0030332; F:cyclin binding; ISO:RGD.
DR   GO; GO:0005504; F:fatty acid binding; IBA:GO_Central.
DR   GO; GO:0008289; F:lipid binding; TAS:RGD.
DR   GO; GO:0016918; F:retinal binding; IEA:UniProtKB-KW.
DR   GO; GO:0001972; F:retinoic acid binding; IDA:RGD.
DR   GO; GO:0019841; F:retinol binding; IEA:UniProtKB-KW.
DR   GO; GO:0035115; P:embryonic forelimb morphogenesis; ISO:RGD.
DR   GO; GO:0015908; P:fatty acid transport; IBA:GO_Central.
DR   GO; GO:0006869; P:lipid transport; NAS:RGD.
DR   GO; GO:0048672; P:positive regulation of collateral sprouting; ISO:RGD.
DR   GO; GO:0002138; P:retinoic acid biosynthetic process; IEP:RGD.
DR   GO; GO:0042573; P:retinoic acid metabolic process; ISO:RGD.
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..139
FT                   /note="Cellular retinoic acid-binding protein 2"
FT                   /id="PRO_0000067417"
FT   MOTIF           21..31
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000250"
FT   BINDING         134..136
FT                   /ligand="all-trans-retinoate"
FT                   /ligand_id="ChEBI:CHEBI:35291"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        103
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   139 AA;  15933 MW;  C32B812D6DC57841 CRC64;
     MPNFSGNWKI IRSENFEEML KALGVNMMMR KIAVAAASKP AVEIKQENDD TFYIKTSTTV
     RTTEINFKIG EEFEEQTVDG RPCKSLVKWE SENKMVCEQR LLKGEGPKTS WSRELTNDGE
     LILTMTADDV VCTRVYVRE