##gff-version 3
P25122	UniProtKB	Chain	1	585	.	.	.	ID=PRO_0000054053;Note=Potassium voltage-gated channel subfamily C member 1	
P25122	UniProtKB	Topological domain	1	190	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P25122	UniProtKB	Transmembrane	191	209	.	.	.	Note=Helical%3B Name%3DSegment S1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P25122	UniProtKB	Transmembrane	248	267	.	.	.	Note=Helical%3B Name%3DSegment S2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P25122	UniProtKB	Topological domain	268	276	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P25122	UniProtKB	Transmembrane	277	295	.	.	.	Note=Helical%3B Name%3DSegment S3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P25122	UniProtKB	Transmembrane	309	331	.	.	.	Note=Helical%3B Voltage-sensor%3B Name%3DSegment S4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P25122	UniProtKB	Topological domain	332	344	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P25122	UniProtKB	Transmembrane	345	366	.	.	.	Note=Helical%3B Name%3DSegment S5;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P25122	UniProtKB	Transmembrane	415	436	.	.	.	Note=Helical%3B Name%3DSegment S6;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P25122	UniProtKB	Topological domain	437	585	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P25122	UniProtKB	Region	121	147	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P25122	UniProtKB	Motif	400	405	.	.	.	Note=Selectivity filter;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P25122	UniProtKB	Modified residue	44	44	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:22673903;Dbxref=PMID:22673903	
P25122	UniProtKB	Modified residue	130	130	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:22673903;Dbxref=PMID:22673903	
P25122	UniProtKB	Modified residue	142	142	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:22673903;Dbxref=PMID:22673903	
P25122	UniProtKB	Modified residue	158	158	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:22673903;Dbxref=PMID:22673903	
P25122	UniProtKB	Modified residue	160	160	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:22673903;Dbxref=PMID:22673903	
P25122	UniProtKB	Modified residue	474	474	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P15388	
P25122	UniProtKB	Modified residue	483	483	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P15388	
P25122	UniProtKB	Glycosylation	220	220	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255,ECO:0000269|PubMed:24161696;Dbxref=PMID:24161696	
P25122	UniProtKB	Glycosylation	229	229	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255,ECO:0000269|PubMed:24161696;Dbxref=PMID:24161696	
P25122	UniProtKB	Alternative sequence	502	511	.	.	.	ID=VSP_001016;Note=In isoform 2. DSKLNGEVAK->GRKPLRGMSI;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P25122	UniProtKB	Alternative sequence	512	585	.	.	.	ID=VSP_001017;Note=In isoform 2. Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P25122	UniProtKB	Mutagenesis	220	220	.	.	.	Note=Reduces extent of N-glycosylation. Abolishes N-glycosylation%3B when associated with Q-229. N->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24161696;Dbxref=PMID:24161696	
P25122	UniProtKB	Mutagenesis	229	229	.	.	.	Note=Reduces extent of N-glycosylation. Abolishes N-glycosylation%3B when associated with Q-220. N->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24161696;Dbxref=PMID:24161696