Q2IBF0 · CAV1_GORGO

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).

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 Componentendosome
Cellular ComponentGolgi apparatus
Cellular ComponentGolgi membrane
Cellular Componentmembrane raft
Cellular Componentperinuclear region of cytoplasm
Molecular Functionmolecular adaptor activity
Molecular Functionoxysterol binding
Molecular Functionprotein kinase binding
Molecular Functiontransmembrane transporter binding
Biological Processcaveola assembly
Biological Processcell differentiation
Biological Processnegative regulation of canonical Wnt signaling pathway
Biological Processnegative regulation of endothelial cell proliferation
Biological Processnegative regulation of transcription by RNA polymerase II
Biological Processreceptor internalization
Biological Processregulation of cytosolic calcium ion concentration
Biological ProcessT cell costimulation

Names & Taxonomy

Protein names

  • Recommended name
    Caveolin-1

Gene names

    • Name
      CAV1

Organism names

Accessions

  • Primary accession
    Q2IBF0

Proteomes

Subcellular Location

Golgi apparatus membrane
; Peripheral membrane protein
Cell membrane
; Peripheral membrane protein
Membrane, caveola
; Peripheral membrane protein
Membrane raft
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.

TypeIDPosition(s)Description
Topological domain2-104Cytoplasmic
Intramembrane105-125Helical
Topological domain126-178Cytoplasmic

Keywords

PTM/Processing

Features

Showing features for initiator methionine, modified residue, chain, cross-link, lipidation.

TypeIDPosition(s)Description
Initiator methionine1Removed
Modified residue2N-acetylserine
Modified residue2Phosphoserine
ChainPRO_00002352042-178Caveolin-1
Modified residue5N6-acetyllysine; alternate
Cross-link5Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate
Modified residue6Phosphotyrosine
Modified residue9Phosphoserine
Modified residue14Phosphotyrosine; by ABL1
Modified residue25Phosphotyrosine
Cross-link26Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Cross-link30Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Modified residue37Phosphoserine
Cross-link39Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Cross-link47Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Cross-link57Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Lipidation133S-palmitoyl cysteine
Lipidation143S-palmitoyl cysteine
Lipidation156S-palmitoyl cysteine

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

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).

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region2-94Required for homooligomerization
Region82-94Interaction with CAVIN3
Region131-142Interacts with SPRY1, SPRY2, SPRY3 and SPRY4
Region149-160Interacts with SPRY1, SPRY2, and SPRY4
Region167-178Interacts with SPRY1, SPRY2, SPRY3 and SPRY4

Sequence similarities

Belongs to the caveolin family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    178
  • Mass (Da)
    20,472
  • Last updated
    2006-03-07 v1
  • Checksum
    2424DE9B5E6521D5
MSGGKYVDSEGHLYTVPIREQGNIYKPNNKAMADELSEKQVYDAHTKEIDLVNRDPKHLNDDVVKIDFEDVIAEPEGTHSFDGIWKASFTTFTVTKYWFYRLLSALFGIPMALIWGIYFAILSFLHIWAVVPCIKSFLIEIQCISRVYSIYVHTVCDPLFEAVGKIFSNVRINLQKEI

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
DP000025
EMBL· GenBank· DDBJ
ABC87448.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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