##gff-version 3
P29974	UniProtKB	Chain	1	684	.	.	.	ID=PRO_0000219309;Note=CGMP-gated cation channel alpha-1	
P29974	UniProtKB	Topological domain	1	156	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q00194	
P29974	UniProtKB	Transmembrane	157	177	.	.	.	Note=Helical%3B Name%3DS1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q00194	
P29974	UniProtKB	Topological domain	178	190	.	.	.	Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q00194	
P29974	UniProtKB	Transmembrane	191	209	.	.	.	Note=Helical%3B Name%3DS2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q00194	
P29974	UniProtKB	Topological domain	210	231	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q00194	
P29974	UniProtKB	Transmembrane	232	251	.	.	.	Note=Helical%3B Name%3DS3;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q00194	
P29974	UniProtKB	Topological domain	252	258	.	.	.	Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q00194	
P29974	UniProtKB	Transmembrane	259	280	.	.	.	Note=Helical%3B Name%3DS4;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q00194	
P29974	UniProtKB	Topological domain	281	291	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q00194	
P29974	UniProtKB	Transmembrane	292	318	.	.	.	Note=Helical%3B Name%3DS5;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q00194	
P29974	UniProtKB	Topological domain	319	361	.	.	.	Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q00194	
P29974	UniProtKB	Transmembrane	362	393	.	.	.	Note=Helical%3B Name%3DS6;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q00194	
P29974	UniProtKB	Topological domain	394	684	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q00194	
P29974	UniProtKB	Region	34	145	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P29974	UniProtKB	Region	342	352	.	.	.	Note=P-helix;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q00194	
P29974	UniProtKB	Region	353	361	.	.	.	Note=Selectivity filter;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q00194	
P29974	UniProtKB	Region	394	476	.	.	.	Note=C-linker;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q00194	
P29974	UniProtKB	Region	477	604	.	.	.	Note=Cyclic nucleotide-binding domain (CNBD);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q00194	
P29974	UniProtKB	Coiled coil	615	658	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q00194	
P29974	UniProtKB	Compositional bias	51	70	.	.	.	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P29974	UniProtKB	Compositional bias	105	145	.	.	.	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P29974	UniProtKB	Binding site	479	601	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
P29974	UniProtKB	Binding site	538	538	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
P29974	UniProtKB	Binding site	553	553	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
P29974	UniProtKB	Glycosylation	321	321	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q00194	
P29974	UniProtKB	Sequence conflict	113	114	.	.	.	Note=NK->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P29974	UniProtKB	Sequence conflict	200	200	.	.	.	Note=D->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P29974	UniProtKB	Sequence conflict	576	576	.	.	.	Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P29974	UniProtKB	Sequence conflict	635	635	.	.	.	Note=R->C;Ontology_term=ECO:0000305;evidence=ECO:0000305