##gff-version 3
P48303	UniProtKB	Chain	1	383	.	.	.	ID=PRO_0000069414;Note=Sphingosine 1-phosphate receptor 1	
P48303	UniProtKB	Topological domain	1	47	.	.	.	Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P48303	UniProtKB	Transmembrane	48	69	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P48303	UniProtKB	Topological domain	70	83	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P48303	UniProtKB	Transmembrane	84	105	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P48303	UniProtKB	Topological domain	106	117	.	.	.	Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P48303	UniProtKB	Transmembrane	118	139	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P48303	UniProtKB	Topological domain	140	161	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P48303	UniProtKB	Transmembrane	162	183	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P48303	UniProtKB	Topological domain	184	197	.	.	.	Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P48303	UniProtKB	Transmembrane	198	225	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P48303	UniProtKB	Topological domain	226	258	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P48303	UniProtKB	Transmembrane	259	279	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P48303	UniProtKB	Topological domain	280	290	.	.	.	Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P48303	UniProtKB	Transmembrane	291	311	.	.	.	Note=Helical%3B Name%3D7;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P48303	UniProtKB	Topological domain	312	383	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P48303	UniProtKB	Region	349	383	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P48303	UniProtKB	Compositional bias	369	383	.	.	.	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P48303	UniProtKB	Binding site	121	122	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
P48303	UniProtKB	Binding site	266	270	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
P48303	UniProtKB	Modified residue	11	11	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O08530	
P48303	UniProtKB	Modified residue	237	237	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P21453	
P48303	UniProtKB	Modified residue	352	352	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:22673903;Dbxref=PMID:22673903	
P48303	UniProtKB	Modified residue	354	354	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P48303	UniProtKB	Lipidation	329	329	.	.	.	Note=S-palmitoyl cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P48303	UniProtKB	Glycosylation	31	31	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P48303	UniProtKB	Disulfide bond	185	192	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00521	
P48303	UniProtKB	Disulfide bond	283	288	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00521