##gff-version 3
P28334	UniProtKB	Chain	1	386	.	.	.	ID=PRO_0000068917;Note=5-hydroxytryptamine receptor 1B	
P28334	UniProtKB	Topological domain	1	45	.	.	.	Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P28334	UniProtKB	Transmembrane	46	71	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P28334	UniProtKB	Topological domain	72	80	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P28334	UniProtKB	Transmembrane	81	106	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P28334	UniProtKB	Topological domain	107	119	.	.	.	Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P28334	UniProtKB	Transmembrane	120	141	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P28334	UniProtKB	Topological domain	142	161	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P28334	UniProtKB	Transmembrane	162	183	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P28334	UniProtKB	Topological domain	184	201	.	.	.	Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P28334	UniProtKB	Transmembrane	202	224	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P28334	UniProtKB	Topological domain	225	311	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P28334	UniProtKB	Transmembrane	312	332	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P28334	UniProtKB	Topological domain	333	345	.	.	.	Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P28334	UniProtKB	Transmembrane	346	367	.	.	.	Note=Helical%3B Name%3D7;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P28334	UniProtKB	Topological domain	368	386	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P28334	UniProtKB	Region	255	278	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P28334	UniProtKB	Motif	142	144	.	.	.	Note=DRY motif%3B important for ligand-induced conformation changes and signaling;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P28334	UniProtKB	Motif	361	365	.	.	.	Note=NPxxY motif%3B important for ligand-induced conformation changes and signaling;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P28334	UniProtKB	Binding site	125	125	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P28222	
P28334	UniProtKB	Binding site	130	130	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P28222	
P28334	UniProtKB	Binding site	197	197	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P28222	
P28334	UniProtKB	Site	351	351	.	.	.	Note=Important for species-specific agonist sensitivity;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P28334	UniProtKB	Lipidation	384	384	.	.	.	Note=S-palmitoyl cysteine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P28334	UniProtKB	Glycosylation	24	24	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P28334	UniProtKB	Glycosylation	28	28	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P28334	UniProtKB	Disulfide bond	118	195	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00521