RABP2_MOUSE
ID RABP2_MOUSE Reviewed; 138 AA.
AC P22935;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 159.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2166951; DOI=10.1073/pnas.87.16.6233;
RA Giguere V., Lyn S., Yip P., Siu C.-H., Amin S.;
RT "Molecular cloning of cDNA encoding a second cellular retinoic acid-binding
RT protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:6233-6237(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1313808; DOI=10.1016/s0021-9258(18)42582-3;
RA Macgregor T.M., Copeland N.G., Jenkins N.A., Giguere V.;
RT "The murine gene for cellular retinoic acid-binding protein type II.
RT Genomic organization, chromosomal localization, and post-transcriptional
RT regulation by retinoic acid.";
RL J. Biol. Chem. 267:7777-7783(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10490651; DOI=10.1128/mcb.19.10.7158;
RA Delva L., Bastie J.-N., Rochette-Egly C., Kraiba R., Balitrand N.,
RA Despouy G., Chambon P., Chomienne C.;
RT "Physical and functional interactions between cellular retinoic acid
RT binding protein II and the retinoic acid-dependent nuclear complex.";
RL Mol. Cell. Biol. 19:7158-7167(1999).
CC -!- FUNCTION: Transports retinoic acid to the nucleus. Regulates the access
CC of retinoic acid to the nuclear retinoic acid receptors.
CC {ECO:0000269|PubMed:10490651}.
CC -!- SUBUNIT: Interacts with importin alpha (By similarity). Interacts with
CC RXR and RARA. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10490651}.
CC Endoplasmic reticulum {ECO:0000250}. Nucleus
CC {ECO:0000269|PubMed:10490651}. Note=Upon ligand binding, a conformation
CC change exposes a nuclear localization motif and the protein is
CC transported into the nucleus.
CC -!- TISSUE SPECIFICITY: Embryo and skin of adult mouse.
CC -!- INDUCTION: By retinoic acid.
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; M35523; AAA37454.1; -; mRNA.
DR EMBL; M87539; AAA37452.1; -; Genomic_DNA.
DR EMBL; M87538; AAA37452.1; JOINED; Genomic_DNA.
DR EMBL; BC018397; AAH18397.1; -; mRNA.
DR CCDS; CCDS17460.1; -.
DR PIR; A42495; A42495.
DR RefSeq; NP_031785.1; NM_007759.2.
DR AlphaFoldDB; P22935; -.
DR SMR; P22935; -.
DR STRING; 10090.ENSMUSP00000005019; -.
DR BindingDB; P22935; -.
DR ChEMBL; CHEMBL4172; -.
DR DrugCentral; P22935; -.
DR iPTMnet; P22935; -.
DR PhosphoSitePlus; P22935; -.
DR EPD; P22935; -.
DR MaxQB; P22935; -.
DR PaxDb; P22935; -.
DR PeptideAtlas; P22935; -.
DR PRIDE; P22935; -.
DR ProteomicsDB; 300387; -.
DR Antibodypedia; 20440; 716 antibodies from 39 providers.
DR DNASU; 12904; -.
DR Ensembl; ENSMUST00000005019; ENSMUSP00000005019; ENSMUSG00000004885.
DR GeneID; 12904; -.
DR KEGG; mmu:12904; -.
DR UCSC; uc008ptk.1; mouse.
DR CTD; 1382; -.
DR MGI; MGI:88491; Crabp2.
DR VEuPathDB; HostDB:ENSMUSG00000004885; -.
DR eggNOG; KOG4015; Eukaryota.
DR GeneTree; ENSGT00940000157619; -.
DR HOGENOM; CLU_113772_0_2_1; -.
DR InParanoid; P22935; -.
DR OMA; ISTWEGD; -.
DR OrthoDB; 1443155at2759; -.
DR PhylomeDB; P22935; -.
DR TreeFam; TF316894; -.
DR Reactome; R-MMU-5362517; Signaling by Retinoic Acid.
DR BioGRID-ORCS; 12904; 3 hits in 77 CRISPR screens.
DR PRO; PR:P22935; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; P22935; protein.
DR Bgee; ENSMUSG00000004885; Expressed in somite and 254 other tissues.
DR Genevisible; P22935; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:CACAO.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:CACAO.
DR GO; GO:0030332; F:cyclin binding; ISO:MGI.
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; IDA:MGI.
DR GO; GO:0019841; F:retinol binding; IEA:UniProtKB-KW.
DR GO; GO:0035115; P:embryonic forelimb morphogenesis; IMP:MGI.
DR GO; GO:0015908; P:fatty acid transport; IBA:GO_Central.
DR GO; GO:0048672; P:positive regulation of collateral sprouting; IDA:MGI.
DR GO; GO:0002138; P:retinoic acid biosynthetic process; IEA:Ensembl.
DR GO; GO:0042573; P:retinoic acid metabolic process; IDA:MGI.
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_0000067416"
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; 15746 MW; 6040CE1A6CD6E39D CRC64;
MPNFSGNWKI IRSENFEEML KALGVNMMMR KIAVAAASKP AVEIKQENDT FYIKTSTTVR
TTEINFKIGE EFEEQTVDGR PCKSLVKWES GNKMVCEQRL LKGEGPKTSW SRELTNDGEL
ILTMTADDVV CTRVYVRE
