##gff-version 3
P61794	UniProtKB	Chain	1	364	.	.	.	ID=PRO_0000069419;Note=Lysophosphatidic acid receptor 1	
P61794	UniProtKB	Topological domain	1	50	.	.	.	Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92633	
P61794	UniProtKB	Transmembrane	51	75	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92633	
P61794	UniProtKB	Topological domain	76	83	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92633	
P61794	UniProtKB	Transmembrane	84	107	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92633	
P61794	UniProtKB	Topological domain	108	121	.	.	.	Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92633	
P61794	UniProtKB	Transmembrane	122	144	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92633	
P61794	UniProtKB	Topological domain	145	163	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92633	
P61794	UniProtKB	Transmembrane	164	184	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92633	
P61794	UniProtKB	Topological domain	185	204	.	.	.	Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92633	
P61794	UniProtKB	Transmembrane	205	225	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92633	
P61794	UniProtKB	Topological domain	226	255	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92633	
P61794	UniProtKB	Transmembrane	256	280	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92633	
P61794	UniProtKB	Topological domain	281	294	.	.	.	Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92633	
P61794	UniProtKB	Transmembrane	295	315	.	.	.	Note=Helical%3B Name%3D7;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92633	
P61794	UniProtKB	Topological domain	316	364	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92633	
P61794	UniProtKB	Binding site	39	39	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92633	
P61794	UniProtKB	Binding site	124	129	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92633	
P61794	UniProtKB	Binding site	210	210	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92633	
P61794	UniProtKB	Modified residue	341	341	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92633	
P61794	UniProtKB	Modified residue	351	351	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P61793	
P61794	UniProtKB	Glycosylation	27	27	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P61794	UniProtKB	Glycosylation	35	35	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P61794	UniProtKB	Disulfide bond	24	190	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92633	
P61794	UniProtKB	Disulfide bond	188	195	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92633	
P61794	UniProtKB	Disulfide bond	284	287	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92633