Cavin1
entrez
19285
canonical
uniprot
O54724
canonical
ensembl
ENSMUSG00000004044
resolver
ensp
ENSMUSP00000058321
resolver
enst
ENSMUST00000060792
resolver
genesymbol
Cavin1
resolver
genesymbol_syn
Ptrf
resolver
uniprot
Q2TAW6
resolver
uniprot_entry
CAVN1_MOUSE
resolver
uniprot_sec
Q2TAW6
resolver
amino_acid_sequence
MEDVTLHIVERPYSGFPDASSEGPEPTQGEARATEEPSGTGSDELIKSDQVNGVLVLSLLDKIIGAVDQIQLTQAQLEERQAEMEGAVQSIQGELSKLGKAHATTSNTVSKLLEKVRKVSVNVKTVRGSLERQAGQIKKLEVNEAELLRRRNFKVMIYQDEVKLPAKLSVSKSLKESEALPEKEGDELGEGERPEDDTAAIELSSDEAVEVEEVIEESRAERIKRSGLRRVDDFKKAFSKEKMEKTKVRTRENLEKTRLKTKENLEKTRHTLEKRMNKLGTRLVPVERREKLKTSRDKLRKSFTPDHVVYARSKTAVYKVPPFTFHVKKIREGEVEVLKATEMVEVGPEDDEVGAERGEATDLLRGSSPDVHTLLEITEESDAVLVDKSDSD
uniprot
proteins
function
FUNCTION: Plays an important role in caveolae formation and organization. Essential for the formation of caveolae in all tissues (PubMed:18056712, PubMed:18191225, PubMed:18840361, PubMed:30188967). Core component of the CAVIN complex which is essential for recruitment of the complex to the caveolae in presence of calveolin-1 (CAV1) (PubMed:19546242). Essential for normal oligomerization of CAV1 (PubMed:23652019). Promotes ribosomal transcriptional activity in response to metabolic challenges in the adipocytes and plays an important role in the formation of the ribosomal transcriptional loop (PubMed:27528195). Dissociates transcription complexes paused by DNA-bound TTF1, thereby releasing both RNA polymerase I and pre-RNA from the template (PubMed:10589839, PubMed:11139612, PubMed:9582279). The caveolae biogenesis pathway is required for the secretion of proteins such as GASK1A (PubMed:30188967). {ECO:0000269|PubMed:10589839, ECO:0000269|PubMed:11139612, ECO:0000269|PubMed:18056712, ECO:0000269|PubMed:18191225, ECO:0000269|PubMed:18840361, ECO:0000269|PubMed:19546242, ECO:0000269|PubMed:23652019, ECO:0000269|PubMed:27528195, ECO:0000269|PubMed:30188967, ECO:0000269|PubMed:9582279}.
uniprot
proteins
mass_dalton
43954
uniprot
proteins
mutagenesis
MUTAGEN 158; /note="Y->F: Significant loss of phosphorylation and loss of regulation of ribosomal transcriptional activity."; /evidence="ECO:0000269|PubMed:27528195"; MUTAGEN 389; /note="S->A: Loss of phosphorylation."; /evidence="ECO:0000269|PubMed:25514038"; MUTAGEN 391; /note="S->A: Loss of phosphorylation."; /evidence="ECO:0000269|PubMed:25514038
uniprot
proteins
post_translational_modification
PTM: Phosphorylated. Present in active and inactive forms. Changes in phosphorylation pattern may alter activity. Phosphorylation at Tyr-158 is essential for its function in the regulation of the ribosomal transcriptional activity. {ECO:0000269|PubMed:11139612, ECO:0000269|PubMed:27528195}.; PTM: Monoubiquitinated. {ECO:0000269|PubMed:27528195}.
uniprot
proteins
protein_family
CAVIN family
uniprot
proteins
pubmed
10589839
uniprot
proteins
pubmed
10727401
uniprot
proteins
pubmed
11139612
uniprot
proteins
pubmed
11161808
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15592455
uniprot
proteins
pubmed
17242355
uniprot
proteins
pubmed
18056712
uniprot
proteins
pubmed
18191225
uniprot
proteins
pubmed
18840361
uniprot
proteins
pubmed
19131326
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
19546242
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
23652019
uniprot
proteins
pubmed
25514038
uniprot
proteins
pubmed
25588833
uniprot
proteins
pubmed
27528195
uniprot
proteins
pubmed
30188967
uniprot
proteins
pubmed
9582279
uniprot
proteins
sequence_length
392
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Membrane, caveola {ECO:0000269|PubMed:18056712, ECO:0000269|PubMed:18191225, ECO:0000269|PubMed:19546242, ECO:0000269|PubMed:25514038}. Cell membrane {ECO:0000269|PubMed:18056712, ECO:0000269|PubMed:18191225}. Microsome {ECO:0000250|UniProtKB:Q6NZI2}. Endoplasmic reticulum {ECO:0000269|PubMed:30188967}. Cytoplasm, cytosol {ECO:0000269|PubMed:18191225, ECO:0000269|PubMed:19546242}. Mitochondrion {ECO:0000250|UniProtKB:Q6NZI2}. Nucleus {ECO:0000269|PubMed:25514038, ECO:0000269|PubMed:27528195}. Note=Translocates to the cytoplasm from caveolae upon insulin stimulation (By similarity). Colocalizes with CAV1 in lipid rafts in adipocytes (PubMed:18056712). Localizes in the caveolae in a caveolin-dependent manner (PubMed:19546242). {ECO:0000250|UniProtKB:Q6NZI2, ECO:0000269|PubMed:18056712, ECO:0000269|PubMed:19546242}.
uniprot
proteins