##gff-version 3
Q29627	UniProtKB	Signal peptide	1	37	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q29627	UniProtKB	Chain	38	513	.	.	.	ID=PRO_0000012840;Note=Pituitary adenylate cyclase-activating polypeptide type I receptor	
Q29627	UniProtKB	Topological domain	38	172	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q29627	UniProtKB	Transmembrane	173	195	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q29627	UniProtKB	Topological domain	196	203	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q29627	UniProtKB	Transmembrane	204	222	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q29627	UniProtKB	Topological domain	223	244	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q29627	UniProtKB	Transmembrane	245	270	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q29627	UniProtKB	Topological domain	271	285	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q29627	UniProtKB	Transmembrane	286	308	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q29627	UniProtKB	Topological domain	309	326	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q29627	UniProtKB	Transmembrane	327	349	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q29627	UniProtKB	Topological domain	350	395	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q29627	UniProtKB	Transmembrane	396	416	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q29627	UniProtKB	Topological domain	417	430	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q29627	UniProtKB	Transmembrane	431	450	.	.	.	Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q29627	UniProtKB	Topological domain	451	513	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q29627	UniProtKB	Region	142	156	.	.	.	Note=Important for ligand binding and specificity;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q29627	UniProtKB	Modified residue	479	479	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P70205	
Q29627	UniProtKB	Modified residue	492	492	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P70205	
Q29627	UniProtKB	Glycosylation	65	65	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q29627	UniProtKB	Glycosylation	77	77	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q29627	UniProtKB	Glycosylation	134	134	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q29627	UniProtKB	Disulfide bond	51	80	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q29627	UniProtKB	Disulfide bond	71	135	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q29627	UniProtKB	Disulfide bond	94	151	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q29627	UniProtKB	Alternative sequence	366	393	.	.	.	ID=VSP_002004;Note=In isoform Short. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:8049255;Dbxref=PMID:8049255