##gff-version 3
P33724	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q03135	
P33724	UniProtKB	Chain	2	178	.	.	.	ID=PRO_0000004762;Note=Caveolin-1	
P33724	UniProtKB	Topological domain	2	104	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P33724	UniProtKB	Intramembrane	105	125	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P33724	UniProtKB	Topological domain	126	178	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P33724	UniProtKB	Region	2	94	.	.	.	Note=Required for homooligomerization;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q03135	
P33724	UniProtKB	Region	82	94	.	.	.	Note=Interaction with CAVIN3;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q03135	
P33724	UniProtKB	Region	131	142	.	.	.	Note=Interacts with SPRY1%2C SPRY2%2C SPRY3 and SPRY4;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P49817	
P33724	UniProtKB	Region	149	160	.	.	.	Note=Interacts with SPRY1%2C SPRY2%2C and SPRY4;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P49817	
P33724	UniProtKB	Region	167	178	.	.	.	Note=Interacts with SPRY1%2C SPRY2%2C SPRY3 and SPRY4;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P49817	
P33724	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q03135	
P33724	UniProtKB	Modified residue	2	2	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P41350	
P33724	UniProtKB	Modified residue	5	5	.	.	.	Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q03135	
P33724	UniProtKB	Modified residue	6	6	.	.	.	Note=Phosphotyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q03135	
P33724	UniProtKB	Modified residue	9	9	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P49817	
P33724	UniProtKB	Modified residue	14	14	.	.	.	Note=Phosphotyrosine%3B by ABL1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P49817	
P33724	UniProtKB	Modified residue	25	25	.	.	.	Note=Phosphotyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q03135	
P33724	UniProtKB	Modified residue	37	37	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q03135	
P33724	UniProtKB	Lipidation	133	133	.	.	.	Note=S-palmitoyl cysteine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7896831;Dbxref=PMID:7896831	
P33724	UniProtKB	Lipidation	143	143	.	.	.	Note=S-palmitoyl cysteine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7896831;Dbxref=PMID:7896831	
P33724	UniProtKB	Lipidation	156	156	.	.	.	Note=S-palmitoyl cysteine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7896831;Dbxref=PMID:7896831	
P33724	UniProtKB	Cross-link	5	5	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q03135	
P33724	UniProtKB	Cross-link	26	26	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q03135	
P33724	UniProtKB	Cross-link	30	30	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q03135	
P33724	UniProtKB	Cross-link	39	39	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q03135	
P33724	UniProtKB	Cross-link	47	47	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q03135	
P33724	UniProtKB	Cross-link	57	57	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q03135	
P33724	UniProtKB	Alternative sequence	1	31	.	.	.	ID=VSP_018691;Note=In isoform Beta. Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305