##gff-version 3
P10499	UniProtKB	Chain	1	495	.	.	.	ID=PRO_0000053970;Note=Potassium voltage-gated channel subfamily A member 1	
P10499	UniProtKB	Topological domain	1	164	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142	
P10499	UniProtKB	Transmembrane	165	186	.	.	.	Note=Helical%3B Name%3DSegment S1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142	
P10499	UniProtKB	Topological domain	187	220	.	.	.	Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142	
P10499	UniProtKB	Transmembrane	221	242	.	.	.	Note=Helical%3B Name%3DSegment S2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142	
P10499	UniProtKB	Topological domain	243	253	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142	
P10499	UniProtKB	Transmembrane	254	274	.	.	.	Note=Helical%3B Name%3DSegment S3;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142	
P10499	UniProtKB	Topological domain	275	287	.	.	.	Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142	
P10499	UniProtKB	Transmembrane	288	308	.	.	.	Note=Helical%3B Voltage-sensor%3B Name%3DSegment S4;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142	
P10499	UniProtKB	Topological domain	309	323	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142	
P10499	UniProtKB	Transmembrane	324	345	.	.	.	Note=Helical%3B Name%3DSegment S5;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142	
P10499	UniProtKB	Topological domain	346	359	.	.	.	Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142	
P10499	UniProtKB	Intramembrane	360	371	.	.	.	Note=Helical%3B Name%3DPore helix;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142	
P10499	UniProtKB	Intramembrane	372	379	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142	
P10499	UniProtKB	Topological domain	380	386	.	.	.	Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142	
P10499	UniProtKB	Transmembrane	387	415	.	.	.	Note=Helical%3B Name%3DSegment S6;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142	
P10499	UniProtKB	Topological domain	416	495	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142	
P10499	UniProtKB	Region	1	128	.	.	.	Note=Tetramerization domain;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P10499	UniProtKB	Region	1	30	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P10499	UniProtKB	Region	310	323	.	.	.	Note=S4-S5 linker;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142	
P10499	UniProtKB	Motif	372	377	.	.	.	Note=Selectivity filter;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142	
P10499	UniProtKB	Motif	493	495	.	.	.	Note=PDZ-binding;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P10499	UniProtKB	Modified residue	23	23	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:22673903;Dbxref=PMID:22673903	
P10499	UniProtKB	Modified residue	322	322	.	.	.	Note=Phosphoserine%3B by PKA;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P10499	UniProtKB	Modified residue	437	437	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:22673903;Dbxref=PMID:22673903	
P10499	UniProtKB	Modified residue	439	439	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:22673903;Dbxref=PMID:22673903	
P10499	UniProtKB	Modified residue	446	446	.	.	.	Note=Phosphoserine%3B by PKA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8038169;Dbxref=PMID:8038169	
P10499	UniProtKB	Lipidation	243	243	.	.	.	Note=S-palmitoyl cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q09470	
P10499	UniProtKB	Glycosylation	207	207	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P10499	UniProtKB	Natural variant	400	400	.	.	.	Note=In RNA edited version. I->V	
P10499	UniProtKB	Mutagenesis	309	309	.	.	.	Note=In ADMS: Dominant negative mutation that abolishes channel activity%3B leads to myokymia%2C neuromyotonia%2C spontaneous epileptic seizures and premature death. S->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22206926;Dbxref=PMID:22206926	
P10499	UniProtKB	Mutagenesis	352	352	.	.	.	Note=Is not blocked by the scorpion mesomartoxin. A->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25514171;Dbxref=PMID:25514171	
P10499	UniProtKB	Mutagenesis	355	355	.	.	.	Note=Is not blocked by the scorpion mesomartoxin. H->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25514171;Dbxref=PMID:25514171	
P10499	UniProtKB	Mutagenesis	357	357	.	.	.	Note=Is not blocked by the scorpion mesomartoxin. S->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25514171;Dbxref=PMID:25514171	
P10499	UniProtKB	Mutagenesis	379	379	.	.	.	Note=Is blocked by the scorpion mesomartoxin%2C with an IC(50)%3D16.60 nM. Y->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25514171;Dbxref=PMID:25514171	
P10499	UniProtKB	Mutagenesis	381	381	.	.	.	Note=Is not blocked by the scorpion mesomartoxin. V->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25514171;Dbxref=PMID:25514171	
P10499	UniProtKB	Mutagenesis	443	443	.	.	.	Note=Abolishes phosphorylation by PKA%3B when associated with A-446. R->C	
P10499	UniProtKB	Mutagenesis	446	446	.	.	.	Note=Abolishes phosphorylation by PKA%3B when associated with C-443. S->A	
P10499	UniProtKB	Beta strand	38	43	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1EXB	
P10499	UniProtKB	Beta strand	46	51	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1EXB	
P10499	UniProtKB	Helix	52	56	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1EXB	
P10499	UniProtKB	Turn	62	64	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1EXB	
P10499	UniProtKB	Helix	66	69	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1EXB	
P10499	UniProtKB	Helix	70	72	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1EXB	
P10499	UniProtKB	Turn	75	78	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1EXB	
P10499	UniProtKB	Beta strand	79	82	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1EXB	
P10499	UniProtKB	Helix	86	97	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1EXB	
P10499	UniProtKB	Helix	110	119	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1EXB