##gff-version 3
P15384	UniProtKB	Chain	1	525	.	.	.	ID=PRO_0000053979;Note=Potassium voltage-gated channel subfamily A member 3	
P15384	UniProtKB	Topological domain	1	184	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P15384	UniProtKB	Transmembrane	185	203	.	.	.	Note=Helical%3B Name%3DSegment S1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P15384	UniProtKB	Topological domain	204	244	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P15384	UniProtKB	Transmembrane	245	266	.	.	.	Note=Helical%3B Name%3DSegment S2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P15384	UniProtKB	Topological domain	267	277	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P15384	UniProtKB	Transmembrane	278	298	.	.	.	Note=Helical%3B Name%3DSegment S3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P15384	UniProtKB	Topological domain	299	312	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P15384	UniProtKB	Transmembrane	313	331	.	.	.	Note=Helical%3B Voltage-sensor%3B Name%3DSegment S4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P15384	UniProtKB	Topological domain	332	347	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P15384	UniProtKB	Transmembrane	348	367	.	.	.	Note=Helical%3B Name%3DSegment S5;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P15384	UniProtKB	Topological domain	368	408	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P15384	UniProtKB	Transmembrane	409	431	.	.	.	Note=Helical%3B Name%3DSegment S6;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P15384	UniProtKB	Topological domain	432	525	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P15384	UniProtKB	Region	1	23	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P15384	UniProtKB	Motif	394	399	.	.	.	Note=Selectivity filter;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P15384	UniProtKB	Motif	523	525	.	.	.	Note=PDZ-binding	
P15384	UniProtKB	Site	228	228	.	.	.	Note=Not glycosylated;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22613618;Dbxref=PMID:22613618	
P15384	UniProtKB	Modified residue	470	470	.	.	.	Note=Phosphoserine%3B by PKA;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P15384	UniProtKB	Lipidation	267	267	.	.	.	Note=S-palmitoyl cysteine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P15384	UniProtKB	Glycosylation	229	229	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22613618;Dbxref=PMID:22613618	
P15384	UniProtKB	Sequence conflict	106	106	.	.	.	Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P15384	UniProtKB	Sequence conflict	181	181	.	.	.	Note=G->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P15384	UniProtKB	Sequence conflict	430	430	.	.	.	Note=V->L;Ontology_term=ECO:0000305;evidence=ECO:0000305