##gff-version 3 P04274 UniProtKB Chain 1 418 . . . ID=PRO_0000069133;Note=Beta-2 adrenergic receptor P04274 UniProtKB Topological domain 1 34 . . . Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250 P04274 UniProtKB Transmembrane 35 58 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000250;evidence=ECO:0000250 P04274 UniProtKB Topological domain 59 71 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250 P04274 UniProtKB Transmembrane 72 95 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000250;evidence=ECO:0000250 P04274 UniProtKB Topological domain 96 106 . . . Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250 P04274 UniProtKB Transmembrane 107 129 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000250;evidence=ECO:0000250 P04274 UniProtKB Topological domain 130 150 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250 P04274 UniProtKB Transmembrane 151 174 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000250;evidence=ECO:0000250 P04274 UniProtKB Topological domain 175 196 . . . Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250 P04274 UniProtKB Transmembrane 197 220 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000250;evidence=ECO:0000250 P04274 UniProtKB Topological domain 221 274 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250 P04274 UniProtKB Transmembrane 275 298 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000250;evidence=ECO:0000250 P04274 UniProtKB Topological domain 299 305 . . . Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250 P04274 UniProtKB Transmembrane 306 329 . . . Note=Helical%3B Name%3D7;Ontology_term=ECO:0000250;evidence=ECO:0000250 P04274 UniProtKB Topological domain 330 418 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250 P04274 UniProtKB Region 394 418 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P04274 UniProtKB Motif 415 418 . . . Note=PDZ-binding P04274 UniProtKB Modified residue 141 141 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07550 P04274 UniProtKB Modified residue 261 261 . . . Note=Phosphoserine%3B by PKA;Ontology_term=ECO:0000255;evidence=ECO:0000255 P04274 UniProtKB Modified residue 262 262 . . . Note=Phosphoserine%3B by PKA;Ontology_term=ECO:0000255;evidence=ECO:0000255 P04274 UniProtKB Modified residue 345 345 . . . Note=Phosphoserine%3B by PKA;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07550 P04274 UniProtKB Modified residue 346 346 . . . Note=Phosphoserine%3B by PKA;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07550 P04274 UniProtKB Modified residue 355 355 . . . Note=Phosphoserine%3B by BARK;Ontology_term=ECO:0000305;evidence=ECO:0000305 P04274 UniProtKB Modified residue 356 356 . . . Note=Phosphoserine%3B by BARK;Ontology_term=ECO:0000305;evidence=ECO:0000305 P04274 UniProtKB Modified residue 387 387 . . . Note=4-hydroxyproline;Ontology_term=ECO:0000250;evidence=ECO:0000250 P04274 UniProtKB Modified residue 400 400 . . . Note=4-hydroxyproline;Ontology_term=ECO:0000250;evidence=ECO:0000250 P04274 UniProtKB Lipidation 265 265 . . . Note=S-palmitoyl cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07550 P04274 UniProtKB Lipidation 341 341 . . . Note=S-palmitoyl cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07550 P04274 UniProtKB Glycosylation 6 6 . . . Note=N-linked (GlcNAc...) asparagine P04274 UniProtKB Glycosylation 15 15 . . . Note=N-linked (GlcNAc...) asparagine P04274 UniProtKB Disulfide bond 106 191 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00521 P04274 UniProtKB Disulfide bond 184 190 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00521 P04274 UniProtKB Mutagenesis 79 79 . . . Note=Small decrease in agonist binding. No effect on antagonist binding. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2899076;Dbxref=PMID:2899076 P04274 UniProtKB Mutagenesis 113 113 . . . Note=Drastic decrease in agonist and antagonist binding. Stimulates adenylyl cyclase activity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2899076;Dbxref=PMID:2899076 P04274 UniProtKB Mutagenesis 204 204 . . . Note=Decrease in catechol agonist binding. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2547766;Dbxref=PMID:2547766 P04274 UniProtKB Mutagenesis 207 207 . . . Note=Decrease in catechol agonist binding. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2547766;Dbxref=PMID:2547766