##gff-version 3
Q9H1Y3	UniProtKB	Chain	1	402	.	.	.	ID=PRO_0000197813;Note=Opsin-3	
Q9H1Y3	UniProtKB	Topological domain	1	40	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9H1Y3	UniProtKB	Transmembrane	41	65	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9H1Y3	UniProtKB	Topological domain	66	77	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9H1Y3	UniProtKB	Transmembrane	78	102	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9H1Y3	UniProtKB	Topological domain	103	117	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9H1Y3	UniProtKB	Transmembrane	118	137	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9H1Y3	UniProtKB	Topological domain	138	153	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9H1Y3	UniProtKB	Transmembrane	154	177	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9H1Y3	UniProtKB	Topological domain	178	201	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9H1Y3	UniProtKB	Transmembrane	202	229	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9H1Y3	UniProtKB	Topological domain	230	255	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9H1Y3	UniProtKB	Transmembrane	256	279	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9H1Y3	UniProtKB	Topological domain	280	287	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9H1Y3	UniProtKB	Transmembrane	288	312	.	.	.	Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9H1Y3	UniProtKB	Topological domain	313	402	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9H1Y3	UniProtKB	Modified residue	299	299	.	.	.	Note=N6-(retinylidene)lysine	
Q9H1Y3	UniProtKB	Lipidation	325	325	.	.	.	Note=S-palmitoyl cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q9H1Y3	UniProtKB	Glycosylation	5	5	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9H1Y3	UniProtKB	Glycosylation	198	198	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9H1Y3	UniProtKB	Disulfide bond	114	188	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00521	
Q9H1Y3	UniProtKB	Alternative sequence	126	231	.	.	.	ID=VSP_010209;Note=In isoform 2. IVSIATLTVLAYERYIRVVHARVINFSWAWRAITYIWLYSLAWAGAPLLGWNRYILDVHGLGCTVDWKSKDANDSSFVLFLFLGCLVVPLGVIAHCYGHILYSIRM->WISQLQAATREARASMGPVQQGTICMQ;Ontology_term=ECO:0000305;evidence=ECO:0000305	
Q9H1Y3	UniProtKB	Natural variant	167	167	.	.	.	ID=VAR_050613;Note=A->V;Dbxref=dbSNP:rs12072790	
Q9H1Y3	UniProtKB	Natural variant	183	183	.	.	.	ID=VAR_050614;Note=V->I;Dbxref=dbSNP:rs2273712	
Q9H1Y3	UniProtKB	Mutagenesis	299	299	.	.	.	Note=Abolishes binding of 11-cis retinal and all-trans retinal. No effect on G-alpha (i) protein signaling. K->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:31097585;Dbxref=PMID:31097585	
Q9H1Y3	UniProtKB	Sequence conflict	390	396	.	.	.	Note=NGSKVDV->IGVQSLML;Ontology_term=ECO:0000305;evidence=ECO:0000305