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P22935

- RABP2_MOUSE

UniProt

P22935 - RABP2_MOUSE

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
  1. 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

    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 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. nucleus Source: UniProtKB-SubCell

    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.
    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

    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: October 1, 2014
    This is version 110 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