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P22935

- RABP2_MOUSE

UniProt

P22935 - RABP2_MOUSE

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Protein

Cellular retinoic acid-binding protein 2

Gene
Crabp2
Organism
Mus musculus (Mouse)
Status
Reviewed - 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. retinal binding Source: UniProtKB-KW
  2. retinoic acid binding Source: MGI
  3. retinol binding Source: UniProtKB-KW
  4. transporter activity Source: InterPro

GO - Biological processi

  1. embryonic forelimb morphogenesis Source: MGI
  2. retinoic acid metabolic process Source: MGI
Complete GO annotation...

Keywords - Biological processi

Transport

Keywords - Ligandi

Retinol-binding, Vitamin A

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: Chromosome 3

Organism-specific databases

MGIiMGI:88491. Crabp2.

Subcellular locationi

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

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. endoplasmic reticulum Source: UniProtKB-SubCell
  3. nucleus Source: UniProtKB-SubCell
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.

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000005019.

Structurei

3D structure databases

ProteinModelPortaliP22935.
SMRiP22935. Positions 2-138.

Family & Domainsi

Region

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

Motif

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

Domaini

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG300013.
GeneTreeiENSGT00750000117272.
HOGENOMiHOG000004831.
HOVERGENiHBG005633.
InParanoidiP22935.
KOiK17289.
OMAiGELVLTM.
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

MPNFSGNWKI IRSENFEEML KALGVNMMMR KIAVAAASKP AVEIKQENDT    50
FYIKTSTTVR TTEINFKIGE EFEEQTVDGR PCKSLVKWES GNKMVCEQRL 100
LKGEGPKTSW SRELTNDGEL ILTMTADDVV CTRVYVRE 138
Length:138
Mass (Da):15,746
Last modified:January 23, 2007 - v2
Checksum:i6040CE1A6CD6E39D
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
M35523 mRNA. Translation: AAA37454.1 .
M87539 , M87538 Genomic DNA. Translation: AAA37452.1 .
BC018397 mRNA. Translation: AAH18397.1 .
CCDSi CCDS17460.1.
PIRi A42495.
RefSeqi NP_031785.1. NM_007759.2.
UniGenei Mm.4757.

3D structure databases

ProteinModelPortali P22935.
SMRi P22935. Positions 2-138.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10090.ENSMUSP00000005019.

Chemistry

BindingDBi P22935.
ChEMBLi CHEMBL4172.

PTM databases

PhosphoSitei P22935.

Proteomic databases

MaxQBi P22935.
PaxDbi P22935.
PRIDEi P22935.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000005019 ; ENSMUSP00000005019 ; ENSMUSG00000004885 .
GeneIDi 12904.
KEGGi mmu:12904.
UCSCi uc008ptk.1. mouse.

Organism-specific databases

CTDi 1382.
MGIi MGI:88491. Crabp2.

Phylogenomic databases

eggNOGi NOG300013.
GeneTreei ENSGT00750000117272.
HOGENOMi HOG000004831.
HOVERGENi HBG005633.
InParanoidi P22935.
KOi K17289.
OMAi GELVLTM.
OrthoDBi EOG7NW6BZ.
PhylomeDBi P22935.
TreeFami TF316894.

Miscellaneous databases

NextBioi 282524.
PROi P22935.
SOURCEi Search...

Gene expression databases

Bgeei P22935.
CleanExi MM_CRABP2.
Genevestigatori P22935.

Family and domain databases

Gene3Di 2.40.128.20. 1 hit.
InterProi IPR012674. Calycin.
IPR011038. Calycin-like.
IPR000463. Fatty_acid-bd.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
[Graphical view ]
Pfami PF00061. Lipocalin. 1 hit.
[Graphical view ]
PRINTSi PR00178. FATTYACIDBP.
SUPFAMi SSF50814. SSF50814. 1 hit.
PROSITEi PS00214. FABP. 1 hit.
[Graphical view ]
ProtoNeti Search...

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(1990) [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(1992) [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(2004) [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(1999) [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: August 1, 1991
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 109 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

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