##gff-version 3
P22462	UniProtKB	Chain	1	638	.	.	.	ID=PRO_0000054054;Note=Potassium voltage-gated channel subfamily C member 2	
P22462	UniProtKB	Topological domain	1	229	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P22462	UniProtKB	Transmembrane	230	248	.	.	.	Note=Helical%3B Name%3DSegment S1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P22462	UniProtKB	Transmembrane	284	303	.	.	.	Note=Helical%3B Name%3DSegment S2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P22462	UniProtKB	Topological domain	304	314	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P22462	UniProtKB	Transmembrane	315	337	.	.	.	Note=Helical%3B Name%3DSegment S3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P22462	UniProtKB	Transmembrane	346	368	.	.	.	Note=Helical%3B Voltage-sensor%3B Name%3DSegment S4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P22462	UniProtKB	Topological domain	369	381	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P22462	UniProtKB	Transmembrane	382	401	.	.	.	Note=Helical%3B Name%3DSegment S5;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P22462	UniProtKB	Transmembrane	451	473	.	.	.	Note=Helical%3B Name%3DSegment S6;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P22462	UniProtKB	Topological domain	474	638	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P22462	UniProtKB	Region	47	75	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P22462	UniProtKB	Region	538	572	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P22462	UniProtKB	Motif	437	442	.	.	.	Note=Selectivity filter;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P22462	UniProtKB	Compositional bias	56	74	.	.	.	Note=Pro residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P22462	UniProtKB	Modified residue	564	564	.	.	.	Note=Phosphoserine%3B by PKA;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P22462	UniProtKB	Modified residue	600	600	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q14B80	
P22462	UniProtKB	Glycosylation	259	259	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P22462	UniProtKB	Glycosylation	266	266	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P22462	UniProtKB	Alternative sequence	594	638	.	.	.	ID=VSP_001018;Note=In isoform 2. GYEKSRSLNNIAGLAGNALRLSPVTSPYNSPCPLRRSRSPIPSIL->ASTLEPMESTSQTKGDTRPEAHWNCAHLLNFGCPTGSSFPTL;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:1879548;Dbxref=PMID:1879548	
P22462	UniProtKB	Alternative sequence	594	638	.	.	.	ID=VSP_001019;Note=In isoform 3. GYEKSRSLNNIAGLAGNALRLSPVTSPYNSPCPLRRSRSPIPSIL->DNCKDVVITGYTQAEARSLT;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:2367536;Dbxref=PMID:2367536	
P22462	UniProtKB	Alternative sequence	594	638	.	.	.	ID=VSP_001020;Note=In isoform 4. GYEKSRSLNNIAGLAGNALRLSPVTSPYNSPCPLRRSRSPIPSIL->VLYRIYHGFLPAENGTLRFSHSKDCTGNFCY;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:1378392;Dbxref=PMID:1378392	
P22462	UniProtKB	Mutagenesis	563	563	.	.	.	Note=Does not abolish channel activity inhibition in presence of nitric oxide (NO)%3B when associated with A-564. Absence of channel activity inhibition in presence of cAMP%3B when associated with A-564. S->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11281123,ECO:0000269|PubMed:7643197;Dbxref=PMID:11281123,PMID:7643197	
P22462	UniProtKB	Mutagenesis	564	564	.	.	.	Note=Does not abolish channel activity inhibition in presence of nitric oxide (NO)%3B when associated with A-564. Absence of channel activity inhibition in presence of cAMP%3B when associated with A-563. S->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11281123,ECO:0000269|PubMed:7643197;Dbxref=PMID:11281123,PMID:7643197	
P22462	UniProtKB	Sequence conflict	2	2	.	.	.	Note=G->S;Ontology_term=ECO:0000305;evidence=ECO:0000305