##gff-version 3 P08482 UniProtKB Chain 1 460 . . . ID=PRO_0000069019;Note=Muscarinic acetylcholine receptor M1 P08482 UniProtKB Topological domain 1 22 . . . Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11229 P08482 UniProtKB Transmembrane 23 48 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11229 P08482 UniProtKB Topological domain 49 62 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11229 P08482 UniProtKB Transmembrane 63 84 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11229 P08482 UniProtKB Topological domain 85 95 . . . Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11229 P08482 UniProtKB Transmembrane 96 121 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11229 P08482 UniProtKB Topological domain 122 142 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11229 P08482 UniProtKB Transmembrane 143 164 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11229 P08482 UniProtKB Topological domain 165 185 . . . Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11229 P08482 UniProtKB Transmembrane 186 209 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11229 P08482 UniProtKB Topological domain 210 366 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11229 P08482 UniProtKB Transmembrane 367 390 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11229 P08482 UniProtKB Topological domain 391 397 . . . Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11229 P08482 UniProtKB Transmembrane 398 420 . . . Note=Helical%3B Name%3D7;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11229 P08482 UniProtKB Topological domain 421 460 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11229 P08482 UniProtKB Region 225 257 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P08482 UniProtKB Region 274 297 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P08482 UniProtKB Region 310 351 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P08482 UniProtKB Compositional bias 231 248 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P08482 UniProtKB Modified residue 230 230 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P12657 P08482 UniProtKB Modified residue 254 254 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:22673903;Dbxref=PMID:22673903 P08482 UniProtKB Modified residue 428 428 . . . Note=Phosphothreonine;Ontology_term=ECO:0000255;evidence=ECO:0000255 P08482 UniProtKB Modified residue 451 451 . . . Note=Phosphoserine;Ontology_term=ECO:0000255;evidence=ECO:0000255 P08482 UniProtKB Modified residue 455 455 . . . Note=Phosphothreonine;Ontology_term=ECO:0000255;evidence=ECO:0000255 P08482 UniProtKB Modified residue 457 457 . . . Note=Phosphoserine;Ontology_term=ECO:0000255;evidence=ECO:0000255 P08482 UniProtKB Glycosylation 2 2 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498 P08482 UniProtKB Glycosylation 12 12 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498 P08482 UniProtKB Disulfide bond 98 178 . . . Ontology_term=ECO:0000305;evidence=ECO:0000305