##gff-version 3
P35363	UniProtKB	Chain	1	471	.	.	.	ID=PRO_0000068948;Note=5-hydroxytryptamine receptor 2A	
P35363	UniProtKB	Topological domain	1	75	.	.	.	Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P35363	UniProtKB	Transmembrane	76	99	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P35363	UniProtKB	Topological domain	100	110	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P35363	UniProtKB	Transmembrane	111	132	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P35363	UniProtKB	Topological domain	133	148	.	.	.	Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P35363	UniProtKB	Transmembrane	149	171	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P35363	UniProtKB	Topological domain	172	191	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P35363	UniProtKB	Transmembrane	192	215	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P35363	UniProtKB	Topological domain	216	233	.	.	.	Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P35363	UniProtKB	Transmembrane	234	254	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P35363	UniProtKB	Topological domain	255	324	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P35363	UniProtKB	Transmembrane	325	346	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P35363	UniProtKB	Topological domain	347	362	.	.	.	Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P35363	UniProtKB	Transmembrane	363	384	.	.	.	Note=Helical%3B Name%3D7;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P35363	UniProtKB	Topological domain	385	471	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P35363	UniProtKB	Motif	172	174	.	.	.	Note=DRY motif%3B important for ligand-induced conformation changes;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P41595	
P35363	UniProtKB	Motif	376	380	.	.	.	Note=NPxxY motif%3B important for ligand-induced conformation changes and signaling;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P41595	
P35363	UniProtKB	Motif	469	471	.	.	.	Note=PDZ-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P28223	
P35363	UniProtKB	Binding site	155	155	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P41595	
P35363	UniProtKB	Binding site	160	160	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P41595	
P35363	UniProtKB	Binding site	229	229	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P41595	
P35363	UniProtKB	Site	229	229	.	.	.	Note=Hydrophobic barrier that decreases the speed of ligand binding and dissociation;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P28223	
P35363	UniProtKB	Modified residue	280	280	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P28223	
P35363	UniProtKB	Glycosylation	8	8	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P35363	UniProtKB	Glycosylation	38	38	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P35363	UniProtKB	Glycosylation	44	44	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P35363	UniProtKB	Glycosylation	51	51	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P35363	UniProtKB	Glycosylation	54	54	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P35363	UniProtKB	Disulfide bond	148	227	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00521	
P35363	UniProtKB	Disulfide bond	349	353	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00521