Q2IBF0 · CAV1_GORGO
- ProteinCaveolin-1
- GeneCAV1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids178 (go to sequence)
- Protein existenceInferred from homology
- Annotation score5/5
Function
function
May act as a scaffolding protein within caveolar membranes. Forms a stable heterooligomeric complex with CAV2 that targets to lipid rafts and drives caveolae formation. Mediates the recruitment of CAVIN proteins (CAVIN1/2/3/4) to the caveolae (By similarity).
Interacts directly with G-protein alpha subunits and can functionally regulate their activity (By similarity).
Involved in the costimulatory signal essential for T-cell receptor (TCR)-mediated T-cell activation. Its binding to DPP4 induces T-cell proliferation and NF-kappa-B activation in a T-cell receptor/CD3-dependent manner (By similarity).
Recruits CTNNB1 to caveolar membranes and may regulate CTNNB1-mediated signaling through the Wnt pathway (By similarity).
Negatively regulates TGFB1-mediated activation of SMAD2/3 by mediating the internalization of TGFBR1 from membrane rafts leading to its subsequent degradation (By similarity).
Binds 20(S)-hydroxycholesterol (20(S)-OHC) (By similarity).
Interacts directly with G-protein alpha subunits and can functionally regulate their activity (By similarity).
Involved in the costimulatory signal essential for T-cell receptor (TCR)-mediated T-cell activation. Its binding to DPP4 induces T-cell proliferation and NF-kappa-B activation in a T-cell receptor/CD3-dependent manner (By similarity).
Recruits CTNNB1 to caveolar membranes and may regulate CTNNB1-mediated signaling through the Wnt pathway (By similarity).
Negatively regulates TGFB1-mediated activation of SMAD2/3 by mediating the internalization of TGFBR1 from membrane rafts leading to its subsequent degradation (By similarity).
Binds 20(S)-hydroxycholesterol (20(S)-OHC) (By similarity).
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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Aspect | Term | |
---|---|---|
Cellular Component | caveola | |
Cellular Component | cytoplasmic vesicle | |
Cellular Component | endosome | |
Cellular Component | Golgi apparatus | |
Cellular Component | Golgi membrane | |
Cellular Component | membrane raft | |
Cellular Component | perinuclear region of cytoplasm | |
Molecular Function | molecular adaptor activity | |
Molecular Function | oxysterol binding | |
Molecular Function | protein kinase binding | |
Molecular Function | transmembrane transporter binding | |
Biological Process | caveola assembly | |
Biological Process | cell differentiation | |
Biological Process | negative regulation of canonical Wnt signaling pathway | |
Biological Process | negative regulation of endothelial cell proliferation | |
Biological Process | negative regulation of transcription by RNA polymerase II | |
Biological Process | receptor internalization | |
Biological Process | regulation of cytosolic calcium ion concentration | |
Biological Process | T cell costimulation |
Names & Taxonomy
Protein names
- Recommended nameCaveolin-1
Gene names
Organism names
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Gorilla
Accessions
- Primary accessionQ2IBF0
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Golgi apparatus membrane ; Peripheral membrane protein
Cell membrane ; Peripheral membrane protein
Membrane, caveola ; Peripheral membrane protein
Note: Colocalized with DPP4 in membrane rafts. Potential hairpin-like structure in the membrane. Membrane protein of caveolae (By similarity).
Features
Showing features for topological domain, intramembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 2-104 | Cytoplasmic | ||||
Sequence: SGGKYVDSEGHLYTVPIREQGNIYKPNNKAMADELSEKQVYDAHTKEIDLVNRDPKHLNDDVVKIDFEDVIAEPEGTHSFDGIWKASFTTFTVTKYWFYRLLS | ||||||
Intramembrane | 105-125 | Helical | ||||
Sequence: ALFGIPMALIWGIYFAILSFL | ||||||
Topological domain | 126-178 | Cytoplasmic | ||||
Sequence: HIWAVVPCIKSFLIEIQCISRVYSIYVHTVCDPLFEAVGKIFSNVRINLQKEI |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain, cross-link, lipidation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Modified residue | 2 | N-acetylserine | ||||
Sequence: S | ||||||
Modified residue | 2 | Phosphoserine | ||||
Sequence: S | ||||||
Chain | PRO_0000235204 | 2-178 | Caveolin-1 | |||
Sequence: SGGKYVDSEGHLYTVPIREQGNIYKPNNKAMADELSEKQVYDAHTKEIDLVNRDPKHLNDDVVKIDFEDVIAEPEGTHSFDGIWKASFTTFTVTKYWFYRLLSALFGIPMALIWGIYFAILSFLHIWAVVPCIKSFLIEIQCISRVYSIYVHTVCDPLFEAVGKIFSNVRINLQKEI | ||||||
Modified residue | 5 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Cross-link | 5 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate | ||||
Sequence: K | ||||||
Modified residue | 6 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 9 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 14 | Phosphotyrosine; by ABL1 | ||||
Sequence: Y | ||||||
Modified residue | 25 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Cross-link | 26 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | ||||||
Cross-link | 30 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | ||||||
Modified residue | 37 | Phosphoserine | ||||
Sequence: S | ||||||
Cross-link | 39 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | ||||||
Cross-link | 47 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | ||||||
Cross-link | 57 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | ||||||
Lipidation | 133 | S-palmitoyl cysteine | ||||
Sequence: C | ||||||
Lipidation | 143 | S-palmitoyl cysteine | ||||
Sequence: C | ||||||
Lipidation | 156 | S-palmitoyl cysteine | ||||
Sequence: C |
Post-translational modification
Phosphorylated at Tyr-14 by ABL1 in response to oxidative stress.
Ubiquitinated. Undergo monoubiquitination and multi- and/or polyubiquitination. Monoubiquitination of N-terminal lysines promotes integration in a ternary complex with UBXN6 and VCP which promotes oligomeric CAV1 targeting to lysosomes for degradation. Ubiquitinated by ZNRF1; leading to degradation and modulation of the TLR4-mediated immune response.
Keywords
- PTM
Interaction
Subunit
Homooligomer. Interacts with GLIPR2. Interacts with NOSTRIN (By similarity).
Interacts with SNAP25 and STX1A (By similarity).
Interacts (via the N-terminus) with DPP4; the interaction is direct (By similarity).
Interacts with CTNNB1, CDH1 and JUP. Interacts with PACSIN2; this interaction induces membrane tubulation (By similarity).
Interacts with SLC7A9 (By similarity).
Interacts with BMX and BTK. Interacts with TGFBR1. Interacts with CAVIN3 (via leucine-zipper domain) in a cholesterol-sensitive manner. Interacts with CAVIN1. Interacts with EHD2 in a cholesterol-dependent manner. Forms a ternary complex with UBXN6 and VCP; mediates CAV1 targeting to lysosomes for degradation. Interacts with ABCG1; this interaction regulates ABCG1-mediated cholesterol efflux (By similarity).
Interacts with NEU3; this interaction enhances NEU3 sialidase activity within caveola. Interacts (via C-terminus) with SPRY1, SPRY2 (via C-terminus), SPRY3, and SPRY4 (By similarity).
Interacts with IGFBP5; this interaction allows trafficking of IGFBP5 from the plasma membrane to the nucleus (By similarity).
Interacts with SNAP25 and STX1A (By similarity).
Interacts (via the N-terminus) with DPP4; the interaction is direct (By similarity).
Interacts with CTNNB1, CDH1 and JUP. Interacts with PACSIN2; this interaction induces membrane tubulation (By similarity).
Interacts with SLC7A9 (By similarity).
Interacts with BMX and BTK. Interacts with TGFBR1. Interacts with CAVIN3 (via leucine-zipper domain) in a cholesterol-sensitive manner. Interacts with CAVIN1. Interacts with EHD2 in a cholesterol-dependent manner. Forms a ternary complex with UBXN6 and VCP; mediates CAV1 targeting to lysosomes for degradation. Interacts with ABCG1; this interaction regulates ABCG1-mediated cholesterol efflux (By similarity).
Interacts with NEU3; this interaction enhances NEU3 sialidase activity within caveola. Interacts (via C-terminus) with SPRY1, SPRY2 (via C-terminus), SPRY3, and SPRY4 (By similarity).
Interacts with IGFBP5; this interaction allows trafficking of IGFBP5 from the plasma membrane to the nucleus (By similarity).
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 2-94 | Required for homooligomerization | ||||
Sequence: SGGKYVDSEGHLYTVPIREQGNIYKPNNKAMADELSEKQVYDAHTKEIDLVNRDPKHLNDDVVKIDFEDVIAEPEGTHSFDGIWKASFTTFTV | ||||||
Region | 82-94 | Interaction with CAVIN3 | ||||
Sequence: DGIWKASFTTFTV | ||||||
Region | 131-142 | Interacts with SPRY1, SPRY2, SPRY3 and SPRY4 | ||||
Sequence: VPCIKSFLIEIQ | ||||||
Region | 149-160 | Interacts with SPRY1, SPRY2, and SPRY4 | ||||
Sequence: SIYVHTVCDPLF | ||||||
Region | 167-178 | Interacts with SPRY1, SPRY2, SPRY3 and SPRY4 | ||||
Sequence: FSNVRINLQKEI |
Sequence similarities
Belongs to the caveolin family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length178
- Mass (Da)20,472
- Last updated2006-03-07 v1
- Checksum2424DE9B5E6521D5
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
DP000025 EMBL· GenBank· DDBJ | ABC87448.1 EMBL· GenBank· DDBJ | Genomic DNA |