##gff-version 3 O08530 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23806337;Dbxref=PMID:23806337 O08530 UniProtKB Chain 2 382 . . . ID=PRO_0000069413;Note=Sphingosine 1-phosphate receptor 1 O08530 UniProtKB Topological domain 2 46 . . . Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250 O08530 UniProtKB Transmembrane 47 68 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000250;evidence=ECO:0000250 O08530 UniProtKB Topological domain 69 82 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250 O08530 UniProtKB Transmembrane 83 104 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000250;evidence=ECO:0000250 O08530 UniProtKB Topological domain 105 116 . . . Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250 O08530 UniProtKB Transmembrane 117 138 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000250;evidence=ECO:0000250 O08530 UniProtKB Topological domain 139 160 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250 O08530 UniProtKB Transmembrane 161 182 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000250;evidence=ECO:0000250 O08530 UniProtKB Topological domain 183 196 . . . Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250 O08530 UniProtKB Transmembrane 197 224 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000250;evidence=ECO:0000250 O08530 UniProtKB Topological domain 225 257 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250 O08530 UniProtKB Transmembrane 258 278 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000250;evidence=ECO:0000250 O08530 UniProtKB Topological domain 279 289 . . . Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250 O08530 UniProtKB Transmembrane 290 310 . . . Note=Helical%3B Name%3D7;Ontology_term=ECO:0000250;evidence=ECO:0000250 O08530 UniProtKB Topological domain 311 382 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250 O08530 UniProtKB Region 348 382 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite O08530 UniProtKB Compositional bias 368 382 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite O08530 UniProtKB Binding site 120 121 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 O08530 UniProtKB Binding site 265 269 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 O08530 UniProtKB Modified residue 2 2 . . . Note=N-acetylvaline;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23806337;Dbxref=PMID:23806337 O08530 UniProtKB Modified residue 10 10 . . . Note=N6-acetyllysine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23806337;Dbxref=PMID:23806337 O08530 UniProtKB Modified residue 236 236 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P21453 O08530 UniProtKB Modified residue 351 351 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079 O08530 UniProtKB Modified residue 353 353 . . . Note=Phosphoserine;Ontology_term=ECO:0000255;evidence=ECO:0000255 O08530 UniProtKB Lipidation 328 328 . . . Note=S-palmitoyl cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250 O08530 UniProtKB Glycosylation 30 30 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 O08530 UniProtKB Disulfide bond 184 191 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00521 O08530 UniProtKB Disulfide bond 282 287 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00521 O08530 UniProtKB Sequence conflict 179 179 . . . Note=I->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 O08530 UniProtKB Sequence conflict 218 218 . . . Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 O08530 UniProtKB Sequence conflict 244 244 . . . Note=A->G;Ontology_term=ECO:0000305;evidence=ECO:0000305