##gff-version 3
Q01338	UniProtKB	Chain	1	465	.	.	.	ID=PRO_0000069081;Note=Alpha-2A adrenergic receptor	
Q01338	UniProtKB	Topological domain	1	48	.	.	.	Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q01338	UniProtKB	Transmembrane	49	74	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q01338	UniProtKB	Topological domain	75	85	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q01338	UniProtKB	Transmembrane	86	111	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q01338	UniProtKB	Topological domain	112	121	.	.	.	Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q01338	UniProtKB	Transmembrane	122	144	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q01338	UniProtKB	Topological domain	145	164	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q01338	UniProtKB	Transmembrane	165	188	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q01338	UniProtKB	Topological domain	189	207	.	.	.	Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q01338	UniProtKB	Transmembrane	208	232	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q01338	UniProtKB	Topological domain	233	389	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q01338	UniProtKB	Transmembrane	390	414	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q01338	UniProtKB	Topological domain	415	424	.	.	.	Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q01338	UniProtKB	Transmembrane	425	445	.	.	.	Note=Helical%3B Name%3D7;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q01338	UniProtKB	Topological domain	446	465	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q01338	UniProtKB	Region	242	378	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q01338	UniProtKB	Compositional bias	303	334	.	.	.	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q01338	UniProtKB	Site	128	128	.	.	.	Note=Implicated in ligand binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q01338	UniProtKB	Site	215	215	.	.	.	Note=Implicated in catechol agonist binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q01338	UniProtKB	Site	219	219	.	.	.	Note=Implicated in catechol agonist binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q01338	UniProtKB	Modified residue	346	346	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P22909	
Q01338	UniProtKB	Modified residue	368	368	.	.	.	Note=Omega-N-methylarginine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:24129315;Dbxref=PMID:24129315	
Q01338	UniProtKB	Lipidation	457	457	.	.	.	Note=S-palmitoyl cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q01338	UniProtKB	Glycosylation	25	25	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q01338	UniProtKB	Glycosylation	29	29	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q01338	UniProtKB	Disulfide bond	121	203	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00521