##gff-version 3
P30558	UniProtKB	Signal peptide	1	21	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
P30558	UniProtKB	Propeptide	22	41	.	.	.	ID=PRO_0000012742;Note=Removed for receptor activation;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P30558	UniProtKB	Chain	42	430	.	.	.	ID=PRO_0000012743;Note=Proteinase-activated receptor 1	
P30558	UniProtKB	Topological domain	42	107	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P30558	UniProtKB	Transmembrane	108	133	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P30558	UniProtKB	Topological domain	134	142	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P30558	UniProtKB	Transmembrane	143	162	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P30558	UniProtKB	Topological domain	163	181	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P30558	UniProtKB	Transmembrane	182	203	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P30558	UniProtKB	Topological domain	204	223	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P30558	UniProtKB	Transmembrane	224	244	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P30558	UniProtKB	Topological domain	245	273	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P30558	UniProtKB	Transmembrane	274	293	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P30558	UniProtKB	Topological domain	294	316	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P30558	UniProtKB	Transmembrane	317	339	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P30558	UniProtKB	Topological domain	340	354	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P30558	UniProtKB	Transmembrane	355	379	.	.	.	Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P30558	UniProtKB	Topological domain	380	430	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P30558	UniProtKB	Site	41	42	.	.	.	Note=Cleavage%3B by thrombin and CTSG;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P25116	
P30558	UniProtKB	Modified residue	423	423	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P25116	
P30558	UniProtKB	Glycosylation	67	67	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19349973;Dbxref=PMID:19349973	
P30558	UniProtKB	Glycosylation	80	80	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P30558	UniProtKB	Glycosylation	255	255	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P30558	UniProtKB	Disulfide bond	180	259	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00521	
P30558	UniProtKB	Sequence conflict	162	162	.	.	.	Note=F->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P30558	UniProtKB	Sequence conflict	189	189	.	.	.	Note=G->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P30558	UniProtKB	Sequence conflict	223	223	.	.	.	Note=R->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P30558	UniProtKB	Sequence conflict	262	262	.	.	.	Note=V->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P30558	UniProtKB	Sequence conflict	365	365	.	.	.	Note=S->T;Ontology_term=ECO:0000305;evidence=ECO:0000305