Q2IBC5 · CAV2_RAT

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. 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.

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 Componentacrosomal membrane
Cellular Componentcaveola
Cellular Componentcaveolar macromolecular signaling complex
Cellular Componentcell surface
Cellular Componentcytoplasmic vesicle
Cellular Componentfocal adhesion
Cellular ComponentGolgi apparatus
Cellular ComponentGolgi membrane
Cellular Componentlipid droplet
Cellular Componentmembrane
Cellular Componentmembrane raft
Cellular Componentnuclear envelope
Cellular Componentnuclear inner membrane
Cellular Componentperinuclear region of cytoplasm
Cellular Componentplasma membrane
Cellular Componentplasma membrane raft
Cellular Componentprotein-containing complex
Cellular Componentsynapse
Molecular FunctionD1 dopamine receptor binding
Molecular Functionmitogen-activated protein kinase kinase kinase binding
Molecular Functionmolecular adaptor activity
Molecular Functionphosphoprotein binding
Molecular Functionprotein heterodimerization activity
Molecular Functionprotein homodimerization activity
Molecular Functionprotein kinase binding
Molecular Functionprotein-macromolecule adaptor activity
Molecular Functionscaffold protein binding
Molecular FunctionSNARE binding
Molecular Functionsyntaxin binding
Biological Processbasement membrane organization
Biological Processcaveola assembly
Biological Processcell differentiation
Biological Processcell population proliferation
Biological Processchemical synaptic transmission
Biological Processendoplasmic reticulum organization
Biological Processendothelial cell proliferation
Biological Processinsulin receptor signaling pathway
Biological Processmitochondrion organization
Biological Processnegative regulation of endothelial cell proliferation
Biological Processnegative regulation of skeletal muscle cell proliferation
Biological Processnegative regulation of transforming growth factor beta receptor signaling pathway
Biological Processpositive regulation by host of viral process
Biological Processpositive regulation of dopamine receptor signaling pathway
Biological Processpositive regulation of endothelial cell proliferation
Biological Processpositive regulation of MAPK cascade
Biological Processpositive regulation of peptidyl-tyrosine phosphorylation
Biological Processpositive regulation of protein localization to nucleus
Biological Processreceptor-mediated endocytosis of virus by host cell
Biological Processregulation of cytosolic calcium ion concentration
Biological Processregulation of mitotic nuclear division
Biological Processskeletal muscle cell proliferation
Biological Processskeletal muscle fiber development
Biological Processtransforming growth factor beta receptor signaling pathway
Biological Processvesicle docking
Biological Processvesicle fusion
Biological Processvesicle organization
Biological Processviral release from host cell

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Caveolin-2

Gene names

    • Name
      Cav2

Organism names

  • Taxonomic identifier
  • Strain
    • Sprague-Dawley
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus

Accessions

  • Primary accession
    Q2IBC5
  • Secondary accessions
    • Q6P6R8
    • Q8VIK7

Proteomes

Organism-specific databases

Subcellular Location

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, in response to insulin, is translocated to the nucleus in complex with MAPK1. Tyr-27-phosphorylated form is located both in the cytoplasm and plasma membrane. The CAV1-mediated Ser-23-phosphorylated form locates to the plasma membrane. The Ser-36-phosphorylated form resides in intracellular compartments (By similarity).

Features

Showing features for topological domain, intramembrane.

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

Keywords

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis19Abolishes phosphorylation, insulin-stimulated interaction with phosphorylated MAPK1, MAPK1 nuclear translocation and activation, reduction of insulin-induced DNA binding of STAT3 but no effect on 'S-727' phosphorylation of STAT3. Completely abolishes phosphorylation, decreases insulin-induced DNA binding and impairs nuclear location of STAT3, inhibits insulin-induced 'S-727' phosphorylation of STAT3, and eliminates binding to RASA1, SRC and NCK1; when associated with A-27.
Mutagenesis27Abolishes phosphorylation and insulin-induced nuclear location, but no effect on insulin-induced 'S-727' phosphorylation of STAT3 nor on MAPK1 phosphorylation. Completely abolishes insulin-induced phosphorylation, nuclear location, nuclear translocation of MAPK1 and STAT3 and 'S-727' phosphorylation of STAT3 and MAPK1 phosphorylation; when associated with A-19.

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00003851791-162Caveolin-2
Modified residue19Phosphotyrosine; by SRC
Modified residue20Phosphoserine
Modified residue23Phosphoserine
Modified residue27Phosphotyrosine; by SRC
Modified residue36Phosphoserine

Post-translational modification

Phosphorylated on serine and tyrosine residues. CAV1 promotes phosphorylation on Ser-23 which targets the complex to the plasma membrane, lipid rafts and caveolae. Phosphorylation on Ser-36 appears to modulate mitosis in endothelial cells (By similarity).
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

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

In the retina, mainly expressed in vessels, but also diffuse expression in the inner and outer plexiform layers and in the inner nuclear layer.

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

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)
    18,266
  • Last updated
    2009-09-22 v2
  • Checksum
    7F8423C6B42F2F55
MGLETEKADVQLFMADDAYSHHSVVDYTDPEKYVDSSQDRDPHQLNSHLKLGFEDLIAEPPTTHSFDKVWICSHALFEISKYVIYKFLTVFLAIPLAFIAGILFATLSCLHIWILMPFVKTCLMVLPSVQTIWKSVTDVVIGPLCTSVGRIFSSVSMQLSHD

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
A0A0A0MXU8A0A0A0MXU8_RATCav2162

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict28in Ref. 2; AAR16307
Sequence conflict29in Ref. 1; AAL33581
Sequence conflict124in Ref. 1; AAL33581
Sequence conflict162in Ref. 1; AAL33581

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF439780
EMBL· GenBank· DDBJ
AAL33581.1
EMBL· GenBank· DDBJ
mRNA
DP000027
EMBL· GenBank· DDBJ
AAR16307.1
EMBL· GenBank· DDBJ
Genomic DNA
BC062059
EMBL· GenBank· DDBJ
AAH62059.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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