##gff-version 3
P35368	UniProtKB	Chain	1	520	.	.	.	ID=PRO_0000069069;Note=Alpha-1B adrenergic receptor	
P35368	UniProtKB	Topological domain	1	45	.	.	.	Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P35368	UniProtKB	Transmembrane	46	70	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P35368	UniProtKB	Topological domain	71	83	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P35368	UniProtKB	Transmembrane	84	105	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P35368	UniProtKB	Topological domain	106	115	.	.	.	Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P35368	UniProtKB	Transmembrane	116	141	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P35368	UniProtKB	Topological domain	142	161	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P35368	UniProtKB	Transmembrane	162	184	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P35368	UniProtKB	Topological domain	185	201	.	.	.	Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P35368	UniProtKB	Transmembrane	202	224	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P35368	UniProtKB	Topological domain	225	295	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P35368	UniProtKB	Transmembrane	296	319	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P35368	UniProtKB	Topological domain	320	326	.	.	.	Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P35368	UniProtKB	Transmembrane	327	351	.	.	.	Note=Helical%3B Name%3D7;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P35368	UniProtKB	Topological domain	352	520	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P35368	UniProtKB	Region	394	432	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P35368	UniProtKB	Region	479	520	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P35368	UniProtKB	Motif	368	380	.	.	.	Note=Nuclear localization signal	
P35368	UniProtKB	Compositional bias	407	425	.	.	.	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P35368	UniProtKB	Modified residue	264	264	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P97717	
P35368	UniProtKB	Lipidation	365	365	.	.	.	Note=S-palmitoyl cysteine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P35368	UniProtKB	Glycosylation	10	10	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P35368	UniProtKB	Glycosylation	24	24	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P35368	UniProtKB	Glycosylation	29	29	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P35368	UniProtKB	Glycosylation	34	34	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P35368	UniProtKB	Disulfide bond	118	195	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00521	
P35368	UniProtKB	Natural variant	51	51	.	.	.	ID=VAR_019510;Note=V->G;Dbxref=dbSNP:rs8192448	
P35368	UniProtKB	Mutagenesis	368	380	.	.	.	Note=Abolishes targeting to the nuclear membrane of cardiac myocytes. RGRGRRRRRRRRR->AGAGAAAAAAAAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22120526;Dbxref=PMID:22120526	
P35368	UniProtKB	Sequence conflict	371	371	.	.	.	Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P35368	UniProtKB	Sequence conflict	498	501	.	.	.	Note=AAAD->PRH;Ontology_term=ECO:0000305;evidence=ECO:0000305