##gff-version 3
Q64264	UniProtKB	Chain	1	421	.	.	.	ID=PRO_0000068904;Note=5-hydroxytryptamine receptor 1A	
Q64264	UniProtKB	Topological domain	1	36	.	.	.	Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q64264	UniProtKB	Transmembrane	37	62	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q64264	UniProtKB	Topological domain	63	73	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q64264	UniProtKB	Transmembrane	74	98	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q64264	UniProtKB	Topological domain	99	110	.	.	.	Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q64264	UniProtKB	Transmembrane	111	132	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q64264	UniProtKB	Topological domain	133	152	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q64264	UniProtKB	Transmembrane	153	178	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q64264	UniProtKB	Topological domain	179	191	.	.	.	Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q64264	UniProtKB	Transmembrane	192	217	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q64264	UniProtKB	Topological domain	218	345	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q64264	UniProtKB	Transmembrane	346	367	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q64264	UniProtKB	Topological domain	368	378	.	.	.	Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q64264	UniProtKB	Transmembrane	379	403	.	.	.	Note=Helical%3B Name%3D7;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q64264	UniProtKB	Topological domain	404	421	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q64264	UniProtKB	Region	237	268	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q64264	UniProtKB	Motif	133	135	.	.	.	Note=DRY motif%3B important for ligand-induced conformation changes;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q64264	UniProtKB	Motif	396	400	.	.	.	Note=NPxxY motif%3B important for ligand-induced conformation changes and signaling;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q64264	UniProtKB	Compositional bias	239	253	.	.	.	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q64264	UniProtKB	Binding site	116	116	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P28222	
Q64264	UniProtKB	Binding site	121	121	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P28222	
Q64264	UniProtKB	Binding site	189	189	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P28222	
Q64264	UniProtKB	Glycosylation	10	10	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q64264	UniProtKB	Glycosylation	11	11	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q64264	UniProtKB	Glycosylation	24	24	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q64264	UniProtKB	Glycosylation	30	30	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q64264	UniProtKB	Disulfide bond	109	187	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00521	
Q64264	UniProtKB	Natural variant	17	19	.	.	.	Note=In strain: C3H/An. EPF->DHL	
Q64264	UniProtKB	Sequence conflict	177	177	.	.	.	Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
Q64264	UniProtKB	Sequence conflict	242	242	.	.	.	Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
Q64264	UniProtKB	Sequence conflict	247	247	.	.	.	Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
Q64264	UniProtKB	Sequence conflict	263	263	.	.	.	Note=C->W;Ontology_term=ECO:0000305;evidence=ECO:0000305	
Q64264	UniProtKB	Sequence conflict	304	304	.	.	.	Note=H->D;Ontology_term=ECO:0000305;evidence=ECO:0000305