##gff-version 3
P15409	UniProtKB	Chain	1	348	.	.	.	ID=PRO_0000197687;Note=Rhodopsin	
P15409	UniProtKB	Topological domain	1	36	.	.	.	Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P15409	UniProtKB	Transmembrane	37	61	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P02699	
P15409	UniProtKB	Topological domain	62	73	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P15409	UniProtKB	Transmembrane	74	96	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P02699	
P15409	UniProtKB	Topological domain	97	110	.	.	.	Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P15409	UniProtKB	Transmembrane	111	133	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P02699	
P15409	UniProtKB	Topological domain	134	152	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P15409	UniProtKB	Transmembrane	153	173	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P02699	
P15409	UniProtKB	Topological domain	174	202	.	.	.	Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P15409	UniProtKB	Transmembrane	203	224	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P02699	
P15409	UniProtKB	Topological domain	225	252	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P15409	UniProtKB	Transmembrane	253	274	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P02699	
P15409	UniProtKB	Topological domain	275	286	.	.	.	Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P15409	UniProtKB	Transmembrane	287	308	.	.	.	Note=Helical%3B Name%3D7;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P02699	
P15409	UniProtKB	Topological domain	309	348	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P15409	UniProtKB	Region	330	348	.	.	.	Note=Interaction with SAG;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P02699	
P15409	UniProtKB	Motif	134	136	.	.	.	Note='Ionic lock' involved in activated form stabilization;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P02699	
P15409	UniProtKB	Binding site	201	201	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P02699	
P15409	UniProtKB	Binding site	279	279	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P02699	
P15409	UniProtKB	Site	113	113	.	.	.	Note=Plays an important role in the conformation switch to the active conformation;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P02699	
P15409	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P02699	
P15409	UniProtKB	Modified residue	296	296	.	.	.	Note=N6-(retinylidene)lysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P02699	
P15409	UniProtKB	Modified residue	334	334	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11910029;Dbxref=PMID:11910029	
P15409	UniProtKB	Modified residue	336	336	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P02700	
P15409	UniProtKB	Modified residue	338	338	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11910029;Dbxref=PMID:11910029	
P15409	UniProtKB	Modified residue	340	340	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P02699	
P15409	UniProtKB	Modified residue	342	342	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P02699	
P15409	UniProtKB	Modified residue	343	343	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11910029;Dbxref=PMID:11910029	
P15409	UniProtKB	Lipidation	322	322	.	.	.	Note=S-palmitoyl cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P02699	
P15409	UniProtKB	Lipidation	323	323	.	.	.	Note=S-palmitoyl cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P02699	
P15409	UniProtKB	Glycosylation	2	2	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P15409	UniProtKB	Glycosylation	15	15	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P15409	UniProtKB	Disulfide bond	110	187	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00521	
P15409	UniProtKB	Sequence conflict	20	20	.	.	.	Note=V->G;Ontology_term=ECO:0000305;evidence=ECO:0000305