Q2QLB1 · CAV2_HORSE

Function

function

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. 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).

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcaveola
Cellular Componentcytoplasmic vesicle
Cellular ComponentGolgi apparatus
Cellular ComponentGolgi membrane
Cellular Componentnucleus
Cellular Componentperinuclear region of cytoplasm
Cellular Componentplasma membrane raft
Molecular FunctionD1 dopamine receptor binding
Molecular Functionmolecular adaptor activity
Molecular Functionprotein kinase binding
Biological Processcaveola assembly
Biological Processcell differentiation
Biological Processendoplasmic reticulum organization
Biological Processinsulin receptor signaling pathway
Biological Processmitochondrion organization
Biological Processnegative regulation of endothelial cell proliferation
Biological Processpositive regulation of dopamine receptor signaling pathway
Biological Processregulation of cytosolic calcium ion concentration
Biological Processskeletal muscle fiber development
Biological Processvesicle docking
Biological Processvesicle fusion

Names & Taxonomy

Protein names

  • Recommended name
    Caveolin-2

Gene names

    • Name
      CAV2

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Perissodactyla > Equidae > Equus

Accessions

  • Primary accession
    Q2QLB1

Proteomes

Subcellular Location

Nucleus
Cytoplasm
Golgi apparatus membrane ; Peripheral membrane protein
Cell membrane ; Peripheral membrane protein
Membrane, caveola ; 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 (By similarity).

Features

Showing features for topological domain, intramembrane.

TypeIDPosition(s)Description
Topological domain1-86Cytoplasmic
Intramembrane87-107Helical
Topological domain108-162Cytoplasmic

Keywords

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00002263401-162Caveolin-2
Modified residue19Phosphotyrosine; by SRC
Modified residue20Phosphoserine
Modified residue23Phosphoserine
Modified residue27Phosphotyrosine; by SRC

Post-translational modification

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 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).

Keywords

Proteomic databases

Interaction

Subunit

Monomer or homodimer (By similarity).
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).

Protein-protein interaction databases

Structure

Family & Domains

Sequence similarities

Belongs to the caveolin family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    162
  • Mass (Da)
    18,094
  • Last updated
    2006-01-24 v1
  • Checksum
    1388FC382E933391
MGLETEKADVQLFLDDESYSRHSGVDYADPEKFADAGLDRDPHRLNSHLKVGFEDVIAEPVSTHSFDKVWICSHALFEISKYVIYKFLTVFLAIPLAFVAGILFATLSCLHIWIIMPFVKTCLMLLPSVQTIWKSVTDVVIAPLCTSAGRSFSSVSLQLSHD

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
DP000020
EMBL· GenBank· DDBJ
ABB89798.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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