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Protein

Cellular retinoic acid-binding protein 2

Gene

Crabp2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Transports retinoic acid to the nucleus. Regulates the access of retinoic acid to the nuclear retinoic acid receptors.1 Publication

GO - Molecular functioni

  1. cyclin binding Source: MGI
  2. retinal binding Source: UniProtKB-KW
  3. retinoic acid binding Source: MGI
  4. retinol binding Source: UniProtKB-KW
  5. transporter activity Source: InterPro

GO - Biological processi

  1. embryonic forelimb morphogenesis Source: MGI
  2. positive regulation of collateral sprouting Source: MGI
  3. retinoic acid metabolic process Source: MGI
Complete GO annotation...

Keywords - Biological processi

Transport

Keywords - Ligandi

Retinol-binding, Vitamin A

Enzyme and pathway databases

ReactomeiREACT_297274. Orphan transporters.
REACT_306383. Signaling by Retinoic Acid.

Names & Taxonomyi

Protein namesi
Recommended name:
Cellular retinoic acid-binding protein 2
Alternative name(s):
Cellular retinoic acid-binding protein II
Short name:
CRABP-II
Gene namesi
Name:Crabp2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:88491. Crabp2.

Subcellular locationi

Cytoplasm 1 Publication. Endoplasmic reticulum By similarity. Nucleus 1 Publication
Note: Upon ligand binding, a conformation change exposes a nuclear localization motif and the protein is transported into the nucleus.

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. endoplasmic reticulum Source: UniProtKB-SubCell
  3. extracellular vesicular exosome Source: MGI
  4. nucleoplasm Source: MGI
  5. nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 138138Cellular retinoic acid-binding protein 2PRO_0000067416Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki102 – 102Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity

Post-translational modificationi

Sumoylated in response to retinoic acid binding, sumoylation is critical for dissociation from ER and subsequent nuclear translocation.

Keywords - PTMi

Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQBiP22935.
PaxDbiP22935.
PRIDEiP22935.

PTM databases

PhosphoSiteiP22935.

Expressioni

Tissue specificityi

Embryo and skin of adult mouse.

Inductioni

By retinoic acid.

Gene expression databases

BgeeiP22935.
CleanExiMM_CRABP2.
GenevestigatoriP22935.

Interactioni

Subunit structurei

Interacts with importin alpha (By similarity). Interacts with RXR and RARA.By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000005019.

Structurei

3D structure databases

ProteinModelPortaliP22935.
SMRiP22935. Positions 2-138.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni133 – 1353Retinoic acid bindingBy similarity

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi21 – 3111Nuclear localization signalBy similarityAdd
BLAST

Domaini

Forms a beta-barrel structure that accommodates hydrophobic ligands in its interior.By similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG300013.
GeneTreeiENSGT00760000118898.
HOGENOMiHOG000004831.
HOVERGENiHBG005633.
InParanoidiP22935.
KOiK17289.
OMAiWEMKSSE.
OrthoDBiEOG7NW6BZ.
PhylomeDBiP22935.
TreeFamiTF316894.

Family and domain databases

Gene3Di2.40.128.20. 1 hit.
InterProiIPR012674. Calycin.
IPR011038. Calycin-like.
IPR000463. Fatty_acid-bd.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
[Graphical view]
PfamiPF00061. Lipocalin. 1 hit.
[Graphical view]
PRINTSiPR00178. FATTYACIDBP.
SUPFAMiSSF50814. SSF50814. 1 hit.
PROSITEiPS00214. FABP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P22935-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPNFSGNWKI IRSENFEEML KALGVNMMMR KIAVAAASKP AVEIKQENDT
60 70 80 90 100
FYIKTSTTVR TTEINFKIGE EFEEQTVDGR PCKSLVKWES GNKMVCEQRL
110 120 130
LKGEGPKTSW SRELTNDGEL ILTMTADDVV CTRVYVRE
Length:138
Mass (Da):15,746
Last modified:January 22, 2007 - v2
Checksum:i6040CE1A6CD6E39D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M35523 mRNA. Translation: AAA37454.1.
M87539, M87538 Genomic DNA. Translation: AAA37452.1.
BC018397 mRNA. Translation: AAH18397.1.
CCDSiCCDS17460.1.
PIRiA42495.
RefSeqiNP_031785.1. NM_007759.2.
UniGeneiMm.4757.

Genome annotation databases

EnsembliENSMUST00000005019; ENSMUSP00000005019; ENSMUSG00000004885.
GeneIDi12904.
KEGGimmu:12904.
UCSCiuc008ptk.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M35523 mRNA. Translation: AAA37454.1.
M87539, M87538 Genomic DNA. Translation: AAA37452.1.
BC018397 mRNA. Translation: AAH18397.1.
CCDSiCCDS17460.1.
PIRiA42495.
RefSeqiNP_031785.1. NM_007759.2.
UniGeneiMm.4757.

3D structure databases

ProteinModelPortaliP22935.
SMRiP22935. Positions 2-138.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000005019.

Chemistry

BindingDBiP22935.
ChEMBLiCHEMBL4172.

PTM databases

PhosphoSiteiP22935.

Proteomic databases

MaxQBiP22935.
PaxDbiP22935.
PRIDEiP22935.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000005019; ENSMUSP00000005019; ENSMUSG00000004885.
GeneIDi12904.
KEGGimmu:12904.
UCSCiuc008ptk.1. mouse.

Organism-specific databases

CTDi1382.
MGIiMGI:88491. Crabp2.

Phylogenomic databases

eggNOGiNOG300013.
GeneTreeiENSGT00760000118898.
HOGENOMiHOG000004831.
HOVERGENiHBG005633.
InParanoidiP22935.
KOiK17289.
OMAiWEMKSSE.
OrthoDBiEOG7NW6BZ.
PhylomeDBiP22935.
TreeFamiTF316894.

Enzyme and pathway databases

ReactomeiREACT_297274. Orphan transporters.
REACT_306383. Signaling by Retinoic Acid.

Miscellaneous databases

NextBioi282524.
PROiP22935.
SOURCEiSearch...

Gene expression databases

BgeeiP22935.
CleanExiMM_CRABP2.
GenevestigatoriP22935.

Family and domain databases

Gene3Di2.40.128.20. 1 hit.
InterProiIPR012674. Calycin.
IPR011038. Calycin-like.
IPR000463. Fatty_acid-bd.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
[Graphical view]
PfamiPF00061. Lipocalin. 1 hit.
[Graphical view]
PRINTSiPR00178. FATTYACIDBP.
SUPFAMiSSF50814. SSF50814. 1 hit.
PROSITEiPS00214. FABP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning of cDNA encoding a second cellular retinoic acid-binding protein."
    Giguere V., Lyn S., Yip P., Siu C.-H., Amin S.
    Proc. Natl. Acad. Sci. U.S.A. 87:6233-6237(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The murine gene for cellular retinoic acid-binding protein type II. Genomic organization, chromosomal localization, and post-transcriptional regulation by retinoic acid."
    Macgregor T.M., Copeland N.G., Jenkins N.A., Giguere V.
    J. Biol. Chem. 267:7777-7783(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Czech II.
    Tissue: Mammary gland.
  4. "Physical and functional interactions between cellular retinoic acid binding protein II and the retinoic acid-dependent nuclear complex."
    Delva L., Bastie J.-N., Rochette-Egly C., Kraiba R., Balitrand N., Despouy G., Chambon P., Chomienne C.
    Mol. Cell. Biol. 19:7158-7167(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiRABP2_MOUSE
AccessioniPrimary (citable) accession number: P22935
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 31, 1991
Last sequence update: January 22, 2007
Last modified: March 31, 2015
This is version 116 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.