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Q9WVC3

- CAV2_MOUSE

UniProt

Q9WVC3 - CAV2_MOUSE

Protein

Caveolin-2

Gene

Cav2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. Functioni

    May act as a scaffolding protein within caveolar membranes. Interacts directly with G-protein alpha subunits and can functionally regulate their activity. Acts as an accessory protein in conjunction with CAV1 in targeting to lipid rafts and driving caveolae formation. The Ser-36 phosphorylated form has a role in modulating mitosis in endothelial cells. Positive regulator of cellular mitogenesis of the MAPK signaling pathway. Required for the insulin-stimulated nuclear translocation and activation of MAPK1 and STAT3, and the subsequent regulation of cell cycle progression By similarity.By similarity

    GO - Molecular functioni

    1. D1 dopamine receptor binding Source: UniProtKB

    GO - Biological processi

    1. caveola assembly Source: UniProtKB
    2. endocytosis Source: MGI
    3. endoplasmic reticulum organization Source: MGI
    4. mitochondrion organization Source: MGI
    5. negative regulation of cell proliferation Source: MGI
    6. negative regulation of endothelial cell proliferation Source: MGI
    7. negative regulation of transforming growth factor beta receptor signaling pathway Source: MGI
    8. positive regulation of dopamine receptor signaling pathway Source: UniProtKB
    9. positive regulation of endothelial cell proliferation Source: MGI
    10. protein oligomerization Source: MGI
    11. regulation of mitosis Source: Ensembl
    12. skeletal muscle fiber development Source: MGI
    13. synaptic transmission Source: Ensembl
    14. vesicle docking Source: UniProtKB
    15. vesicle fusion Source: UniProtKB

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Caveolin-2
    Gene namesi
    Name:Cav2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 6

    Organism-specific databases

    MGIiMGI:107571. Cav2.

    Subcellular locationi

    Nucleus. Cytoplasm. Golgi apparatus membrane; Peripheral membrane protein. Cell membrane; Peripheral membrane protein. Membranecaveola; Peripheral membrane protein
    Note: Potential hairpin-like structure in the membrane. Membrane protein of caveolae. Tyr-19-phosphorylated form is enriched at sites of cell-cell contact and is translocated to the nucleus in complex with MAPK1 in response to insulin. Tyr-27-phosphorylated form is located both in the cytoplasm and plasma membrane. CAV1-mediated Ser-23-phosphorylated form locates to the plasma membrane. Ser-36-phosphorylated form resides in intracellular compartments By similarity.By similarity

    GO - Cellular componenti

    1. acrosomal membrane Source: MGI
    2. caveola Source: UniProtKB
    3. cell surface Source: Ensembl
    4. cytoplasmic vesicle Source: MGI
    5. cytosol Source: Ensembl
    6. extrinsic component of cytoplasmic side of plasma membrane Source: UniProtKB
    7. Golgi membrane Source: UniProtKB-SubCell
    8. integral component of plasma membrane Source: Ensembl
    9. lipid particle Source: Ensembl
    10. membrane Source: MGI
    11. membrane raft Source: HGNC
    12. nucleus Source: UniProtKB-SubCell
    13. perinuclear region of cytoplasm Source: UniProtKB
    14. plasma membrane Source: MGI
    15. protein complex Source: MGI
    16. transport vesicle Source: Ensembl

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Golgi apparatus, Membrane, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 162162Caveolin-2PRO_0000144138Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei19 – 191Phosphotyrosine; by SRC1 Publication
    Modified residuei23 – 231PhosphoserineBy similarity
    Modified residuei27 – 271Phosphotyrosine; by SRCBy similarity
    Modified residuei36 – 361PhosphoserineBy similarity

    Post-translational modificationi

    Phosphorylated on serine and tyrosine residues. CAV1 promotes phosphorylation on Ser-23 which then targets the complex to the plasma membrane, lipid rafts and caveolae. Phosphorylation on Ser-36 appears to modulate mitosis in endothelial cells. Phosphorylation on both Tyr-19 and Tyr-27 is required for insulin-induced 'Ser-727' phosphorylation of STAT3 and its activation. Phosphorylation on Tyr-19 is required for insulin-induced phosphorylation of MAPK1 and DNA binding of STAT3. Tyrosine phosphorylation is induced by both EGF and insulin By similarity.By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9WVC3.
    PaxDbiQ9WVC3.
    PRIDEiQ9WVC3.

    PTM databases

    PhosphoSiteiQ9WVC3.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9WVC3.
    BgeeiQ9WVC3.
    CleanExiMM_CAV2.
    GenevestigatoriQ9WVC3.

    Interactioni

    Subunit structurei

    Monomer or homodimer. Interacts with CAV1; the interaction forms a stable heterooligomeric complex that is required for targeting to lipid rafts and for caveolae formation. Tyrosine phosphorylated forms do not form heterooligomers with the Tyr-19-phosphorylated form existing as a monomer or dimer, and the Tyr-27-form as a monomer only. Interacts (tyrosine phosphorylated form) with the SH2 domain-containing proteins, RASA1, NCK1 and SRC. Interacts (tyrosine phosphorylated form) with INSR, the interaction (Tyr-27-phosphorylated form) is increased on insulin stimulation. Interacts (Tyr-19 phosphorylated form) with MAPK1 (phosphorylated form); the interaction, promoted by insulin, leads to nuclear location and MAPK1 activation. Interacts with STAT3; the interaction is increased on insulin-induced tyrosine phosphorylation leading to STAT activation By similarity.By similarity

    Protein-protein interaction databases

    IntActiQ9WVC3. 1 interaction.
    MINTiMINT-4089976.
    STRINGi10090.ENSMUSP00000000058.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9WVC3.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 8686CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini108 – 16255CytoplasmicSequence AnalysisAdd
    BLAST

    Intramembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Intramembranei87 – 10721HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the caveolin family.Curated

    Phylogenomic databases

    eggNOGiNOG74268.
    GeneTreeiENSGT00390000014924.
    HOGENOMiHOG000036550.
    HOVERGENiHBG003422.
    InParanoidiQ9WVC3.
    KOiK12958.
    OMAiSTHSFDK.
    OrthoDBiEOG7V1FSD.
    PhylomeDBiQ9WVC3.
    TreeFamiTF315736.

    Family and domain databases

    InterProiIPR001612. Caveolin.
    IPR018361. Caveolin_CS.
    [Graphical view]
    PANTHERiPTHR10844. PTHR10844. 1 hit.
    PfamiPF01146. Caveolin. 1 hit.
    [Graphical view]
    PROSITEiPS01210. CAVEOLIN. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9WVC3-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGLETEKADV QLFMADDAYS HHSGVDYADP EKYVDSSHDR DPHQLNSHLK    50
    LGFEDLIAEP ETTHSFDKVW ICSHALFEIS KYVMYKFLTV FLAIPLAFIA 100
    GILFATLSCL HIWILMPFVK TCLMVLPSVQ TIWKSVTDVV IGPLCTSVGR 150
    SFSSVSMQLS HD 162
    Length:162
    Mass (Da):18,227
    Last modified:November 1, 1999 - v1
    Checksum:i9E2E272FEC169458
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF141322 mRNA. Translation: AAD42349.1.
    AB049604 mRNA. Translation: BAB61728.1.
    AK004663 mRNA. Translation: BAB23453.1.
    AK009913 mRNA. Translation: BAB26582.1.
    AK151397 mRNA. Translation: BAE30365.1.
    AK158419 mRNA. Translation: BAE34498.1.
    BC023095 mRNA. Translation: AAH23095.1.
    CCDSiCCDS19923.1.
    RefSeqiNP_058596.1. NM_016900.4.
    UniGeneiMm.396075.

    Genome annotation databases

    EnsembliENSMUST00000000058; ENSMUSP00000000058; ENSMUSG00000000058.
    GeneIDi12390.
    KEGGimmu:12390.
    UCSCiuc009azm.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF141322 mRNA. Translation: AAD42349.1 .
    AB049604 mRNA. Translation: BAB61728.1 .
    AK004663 mRNA. Translation: BAB23453.1 .
    AK009913 mRNA. Translation: BAB26582.1 .
    AK151397 mRNA. Translation: BAE30365.1 .
    AK158419 mRNA. Translation: BAE34498.1 .
    BC023095 mRNA. Translation: AAH23095.1 .
    CCDSi CCDS19923.1.
    RefSeqi NP_058596.1. NM_016900.4.
    UniGenei Mm.396075.

    3D structure databases

    ProteinModelPortali Q9WVC3.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q9WVC3. 1 interaction.
    MINTi MINT-4089976.
    STRINGi 10090.ENSMUSP00000000058.

    PTM databases

    PhosphoSitei Q9WVC3.

    Proteomic databases

    MaxQBi Q9WVC3.
    PaxDbi Q9WVC3.
    PRIDEi Q9WVC3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000000058 ; ENSMUSP00000000058 ; ENSMUSG00000000058 .
    GeneIDi 12390.
    KEGGi mmu:12390.
    UCSCi uc009azm.1. mouse.

    Organism-specific databases

    CTDi 858.
    MGIi MGI:107571. Cav2.

    Phylogenomic databases

    eggNOGi NOG74268.
    GeneTreei ENSGT00390000014924.
    HOGENOMi HOG000036550.
    HOVERGENi HBG003422.
    InParanoidi Q9WVC3.
    KOi K12958.
    OMAi STHSFDK.
    OrthoDBi EOG7V1FSD.
    PhylomeDBi Q9WVC3.
    TreeFami TF315736.

    Miscellaneous databases

    NextBioi 281126.
    PROi Q9WVC3.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9WVC3.
    Bgeei Q9WVC3.
    CleanExi MM_CAV2.
    Genevestigatori Q9WVC3.

    Family and domain databases

    InterProi IPR001612. Caveolin.
    IPR018361. Caveolin_CS.
    [Graphical view ]
    PANTHERi PTHR10844. PTHR10844. 1 hit.
    Pfami PF01146. Caveolin. 1 hit.
    [Graphical view ]
    PROSITEi PS01210. CAVEOLIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The membrane-spanning domains of caveolins-1 and -2 mediate the formation of caveolin hetero-oligomers. Implications for the assembly of caveolae membranes in vivo."
      Das K., Lewis R.Y., Scherer P.E., Lisanti M.P.
      J. Biol. Chem. 274:18721-18728(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: 3T3-L1.
    2. "Identification of mouse caveolin-2 mRNA variant."
      Kogo H., Ishiguro K., Kuwaki S., Fujimoto T.
      Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Bone marrow, Inner ear, Lung and Tongue.
    4. "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: FVB/N.
      Tissue: Mammary gland.
    5. "Src-induced phosphorylation of caveolin-2 on tyrosine 19. Phospho-caveolin-2 (Tyr(P)19) is localized near focal adhesions, remains associated with lipid rafts/caveolae, but no longer forms a high molecular mass hetero-oligomer with caveolin-1."
      Lee H., Park D.S., Wang X.B., Scherer P.E., Schwartz P.E., Lisanti M.P.
      J. Biol. Chem. 277:34556-34567(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-19.
    6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.

    Entry informationi

    Entry nameiCAV2_MOUSE
    AccessioniPrimary (citable) accession number: Q9WVC3
    Secondary accession number(s): Q3TYR4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: November 1, 1999
    Last modified: October 1, 2014
    This is version 105 of the entry and version 1 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