Q2IBC5 · CAV2_RAT
- ProteinCaveolin-2
- GeneCav2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids162 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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 annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCaveolin-2
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus
Accessions
- Primary accessionQ2IBC5
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-86 | Cytoplasmic | ||||
Sequence: MGLETEKADVQLFMADDAYSHHSVVDYTDPEKYVDSSQDRDPHQLNSHLKLGFEDLIAEPPTTHSFDKVWICSHALFEISKYVIYK | ||||||
Intramembrane | 87-107 | Helical | ||||
Sequence: FLTVFLAIPLAFIAGILFATL | ||||||
Topological domain | 108-162 | Cytoplasmic | ||||
Sequence: SCLHIWILMPFVKTCLMVLPSVQTIWKSVTDVVIGPLCTSVGRIFSSVSMQLSHD |
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 19 | Abolishes 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. | ||||
Sequence: Y → A | ||||||
Mutagenesis | 27 | Abolishes 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. | ||||
Sequence: Y → A |
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000385179 | 1-162 | Caveolin-2 | |||
Sequence: MGLETEKADVQLFMADDAYSHHSVVDYTDPEKYVDSSQDRDPHQLNSHLKLGFEDLIAEPPTTHSFDKVWICSHALFEISKYVIYKFLTVFLAIPLAFIAGILFATLSCLHIWILMPFVKTCLMVLPSVQTIWKSVTDVVIGPLCTSVGRIFSSVSMQLSHD | ||||||
Modified residue | 19 | Phosphotyrosine; by SRC | ||||
Sequence: Y | ||||||
Modified residue | 20 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 23 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 27 | Phosphotyrosine; by SRC | ||||
Sequence: Y | ||||||
Modified residue | 36 | Phosphoserine | ||||
Sequence: S |
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
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
- PTM
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
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
Sequence
- Sequence statusComplete
- Length162
- Mass (Da)18,266
- Last updated2009-09-22 v2
- Checksum7F8423C6B42F2F55
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A0A0MXU8 | A0A0A0MXU8_RAT | Cav2 | 162 |
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 28 | in Ref. 2; AAR16307 | ||||
Sequence: T → A | ||||||
Sequence conflict | 29 | in Ref. 1; AAL33581 | ||||
Sequence: D → G | ||||||
Sequence conflict | 124 | in Ref. 1; AAL33581 | ||||
Sequence: M → V | ||||||
Sequence conflict | 162 | in Ref. 1; AAL33581 | ||||
Sequence: D → N |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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 |