Cav1
entrez
12389
canonical
uniprot
P49817
canonical
ensembl
ENSMUSG00000007655
resolver
ensp
ENSMUSP00000007799
resolver
ensp
ENSMUSP00000111113
resolver
ensp
ENSMUSP00000111114
resolver
ensp
ENSMUSP00000111116
resolver
ensp
ENSMUSP00000289549
resolver
ensp
ENSMUSP00000289550
resolver
ensp
ENSMUSP00000289551
resolver
genesymbol
Cav1
resolver
genesymbol_syn
Cav
resolver
uniprot
Q8C1X7
resolver
uniprot
Q8CBP4
resolver
uniprot
Q9QYH3
resolver
uniprot
Q9QYH4
resolver
uniprot_entry
CAV1_MOUSE
resolver
uniprot_sec
Q8C1X7
resolver
uniprot_sec
Q8CBP4
resolver
uniprot_sec
Q9QYH3
resolver
uniprot_sec
Q9QYH4
resolver
amino_acid_sequence
MSGGKYVDSEGHLYTVPIREQGNIYKPNNKAMADEVTEKQVYDAHTKEIDLVNRDPKHLNDDVVKIDFEDVIAEPEGTHSFDGIWKASFTTFTVTKYWFYRLLSTIFGIPMALIWGIYFAILSFLHIWAVVPCIKSFLIEIQCISRVYSIYVHTFCDPLFEAIGKIFSNIRISTQKEI
uniprot
proteins
function
FUNCTION: May act as a scaffolding protein within caveolar membranes (By similarity). 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 (PubMed:19546242). 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 (PubMed:10816572). 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) (PubMed:34799735). {ECO:0000250|UniProtKB:Q03135, ECO:0000269|PubMed:10816572, ECO:0000269|PubMed:19546242, ECO:0000269|PubMed:34799735}.
uniprot
proteins
mass_dalton
20539
uniprot
proteins
post_translational_modification
PTM: The N-terminus of both isoforms are blocked.; PTM: Phosphorylated at Tyr-14 by ABL1 in response to oxidative stress. {ECO:0000269|PubMed:12036959, ECO:0000269|PubMed:12531427}.; PTM: 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. {ECO:0000250|UniProtKB:Q03135}.
uniprot
proteins
protein_family
Caveolin family
uniprot
proteins
pubmed
10631317
uniprot
proteins
pubmed
10816572
uniprot
proteins
pubmed
12036959
uniprot
proteins
pubmed
12531427
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15592455
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
16877379
uniprot
proteins
pubmed
19131326
uniprot
proteins
pubmed
19546242
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
21610094
uniprot
proteins
pubmed
23806337
uniprot
proteins
pubmed
30188967
uniprot
proteins
pubmed
34799735
uniprot
proteins
pubmed
7608210
uniprot
proteins
pubmed
7926819
uniprot
proteins
sequence_length
178
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cell membrane {ECO:0000250|UniProtKB:Q03135}; Peripheral membrane protein {ECO:0000250}. Membrane, caveola {ECO:0000269|PubMed:19546242, ECO:0000269|PubMed:21610094}; Peripheral membrane protein {ECO:0000269|PubMed:21610094}. Membrane raft {ECO:0000250|UniProtKB:Q03135}. Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:P33724}. Cytoplasm {ECO:0000250|UniProtKB:Q03135}. Note=Colocalized with DPP4 in membrane rafts. Potential hairpin-like structure in the membrane. Membrane protein of caveolae (By similarity). In the presence of DSG2 localizes to the cytoplasm away from cell borders (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q03135}.
uniprot
proteins