##gff-version 3 Q01337 UniProtKB Chain 1 458 . . . ID=PRO_0000069106;Note=Alpha-2C adrenergic receptor Q01337 UniProtKB Topological domain 1 51 . . . Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q01337 UniProtKB Transmembrane 52 76 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q01337 UniProtKB Topological domain 77 88 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q01337 UniProtKB Transmembrane 89 114 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q01337 UniProtKB Topological domain 115 124 . . . Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q01337 UniProtKB Transmembrane 125 147 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q01337 UniProtKB Topological domain 148 168 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q01337 UniProtKB Transmembrane 169 191 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q01337 UniProtKB Topological domain 192 207 . . . Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q01337 UniProtKB Transmembrane 208 231 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q01337 UniProtKB Topological domain 232 379 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q01337 UniProtKB Transmembrane 380 403 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q01337 UniProtKB Topological domain 404 416 . . . Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q01337 UniProtKB Transmembrane 417 437 . . . Note=Helical%3B Name%3D7;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q01337 UniProtKB Topological domain 438 458 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q01337 UniProtKB Region 245 343 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q01337 UniProtKB Compositional bias 277 292 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q01337 UniProtKB Site 131 131 . . . Note=Implicated in ligand binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q01337 UniProtKB Site 214 214 . . . Note=Implicated in catechol agonist binding and receptor activation;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q01337 UniProtKB Site 218 218 . . . Note=Implicated in catechol agonist binding and receptor activation;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q01337 UniProtKB Glycosylation 19 19 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q01337 UniProtKB Glycosylation 33 33 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q01337 UniProtKB Disulfide bond 124 202 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00521 Q01337 UniProtKB Sequence conflict 196 196 . . . Note=G->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q01337 UniProtKB Sequence conflict 296 296 . . . Note=G->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q01337 UniProtKB Sequence conflict 298 298 . . . Note=L->V;Ontology_term=ECO:0000305;evidence=ECO:0000305