##gff-version 3 Q14003 UniProtKB Chain 1 757 . . . ID=PRO_0000054055;Note=Potassium voltage-gated channel subfamily C member 3 Q14003 UniProtKB Topological domain 1 290 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q14003 UniProtKB Transmembrane 291 309 . . . Note=Helical%3B Name%3DSegment S1;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q14003 UniProtKB Transmembrane 351 370 . . . Note=Helical%3B Name%3DSegment S2;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q14003 UniProtKB Topological domain 371 379 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q14003 UniProtKB Transmembrane 380 398 . . . Note=Helical%3B Name%3DSegment S3;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q14003 UniProtKB Transmembrane 412 434 . . . Note=Helical%3B Voltage-sensor%3B Name%3DSegment S4;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q14003 UniProtKB Topological domain 435 447 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q14003 UniProtKB Transmembrane 448 469 . . . Note=Helical%3B Name%3DSegment S5;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q14003 UniProtKB Transmembrane 518 539 . . . Note=Helical%3B Name%3DSegment S6;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q14003 UniProtKB Topological domain 540 757 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q14003 UniProtKB Region 1 87 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q14003 UniProtKB Region 1 78 . . . Note=Important for normal N-type inactivation;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26997484;Dbxref=PMID:26997484 Q14003 UniProtKB Region 210 232 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q14003 UniProtKB Region 556 613 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q14003 UniProtKB Region 682 746 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q14003 UniProtKB Motif 503 508 . . . Note=Selectivity filter;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q14003 UniProtKB Compositional bias 1 16 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q14003 UniProtKB Compositional bias 20 63 . . . Note=Pro residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q14003 UniProtKB Compositional bias 565 604 . . . Note=Pro residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q14003 UniProtKB Modified residue 625 625 . . . Note=Omega-N-methylarginine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q63959 Q14003 UniProtKB Modified residue 686 686 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q63959 Q14003 UniProtKB Modified residue 691 691 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q63959 Q14003 UniProtKB Glycosylation 320 320 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q14003 UniProtKB Glycosylation 336 336 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q14003 UniProtKB Glycosylation 483 483 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q14003 UniProtKB Natural variant 41 41 . . . ID=VAR_074192;Note=Q->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25756792;Dbxref=dbSNP:rs185017345,PMID:25756792 Q14003 UniProtKB Natural variant 63 63 . . . ID=VAR_074193;Note=D->G;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10712820,ECO:0000269|PubMed:25756792;Dbxref=dbSNP:rs375912738,PMID:10712820,PMID:25756792 Q14003 UniProtKB Natural variant 129 129 . . . ID=VAR_074194;Note=In SCA13%3B uncertain significance%3B changes channel activity%3B shifts the voltage dependence of activation. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25756792;Dbxref=PMID:25756792 Q14003 UniProtKB Natural variant 263 263 . . . ID=VAR_074195;Note=Changes channel activity%3B activates more quickly and deactivates more slowly. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21479265;Dbxref=PMID:21479265 Q14003 UniProtKB Natural variant 366 366 . . . ID=VAR_074196;Note=In SCA13%3B uncertain significance%3B dominant negative that decreases channel activity%3B decreases protein abundance%3B decreases protein stability%3B decreases localization to the plasma membrane%3B no effect on tetramerization. R->H;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:19953606,ECO:0000269|PubMed:23734863;Dbxref=dbSNP:rs769502387,PMID:19953606,PMID:23734863 Q14003 UniProtKB Natural variant 420 420 . . . ID=VAR_029530;Note=In SCA13%3B dominant negative that induces loss of channel activity%3B decreases protein abundance%3B decreases protein stability%3B decreases localization to the plasma membrane and alters the localization of the wild-type protein%3B impairs N-glycosylation%3B no effect on tetramerization. R->H;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16501573,ECO:0000269|PubMed:19953606,ECO:0000269|PubMed:22289912,ECO:0000269|PubMed:23734863,ECO:0000269|PubMed:25152487,ECO:0000269|PubMed:25756792;Dbxref=dbSNP:rs104894699,PMID:16501573,PMID:19953606,PMID:22289912,PMID:23734863,PMID:25152487,PMID:25756792 Q14003 UniProtKB Natural variant 423 423 . . . ID=VAR_074197;Note=In SCA13%3B dominant negative that reduces channel activity%3B alters gating%3B decreases protein abundance%3B decreases localization to the plasma membrane%3B no effect on tetramerization. R->H;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:19953606,ECO:0000269|PubMed:21479265,ECO:0000269|PubMed:22289912,ECO:0000269|PubMed:23734863,ECO:0000269|PubMed:25756792;Dbxref=dbSNP:rs797044872,PMID:19953606,PMID:21479265,PMID:22289912,PMID:23734863,PMID:25756792 Q14003 UniProtKB Natural variant 448 448 . . . ID=VAR_029531;Note=In SCA13%3B alters gating%3B slows channel closing%3B decreases protein abundance%3B no effect on localization to the plasma membrane%3B no effect on N-glycosylation%3B no effect on tetramerization. F->L;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16501573,ECO:0000269|PubMed:22289912,ECO:0000269|PubMed:23734863,ECO:0000269|PubMed:25152487;Dbxref=dbSNP:rs104894700,PMID:16501573,PMID:22289912,PMID:23734863,PMID:25152487 Q14003 UniProtKB Natural variant 477 477 . . . ID=VAR_074198;Note=In SCA13%3B uncertain significance%3B no effect on channel activity. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25756792;Dbxref=dbSNP:rs148033381,PMID:25756792 Q14003 UniProtKB Natural variant 535 535 . . . ID=VAR_074199;Note=In SCA13%3B changes channel activity%3B shifts the voltage dependence of activation. V->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25756792;Dbxref=PMID:25756792 Q14003 UniProtKB Natural variant 591 591 . . . ID=VAR_074200;Note=In SCA13%3B uncertain significance%3B reduces channel activity%3B shifts the voltage dependence of activation. S->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25756792;Dbxref=dbSNP:rs549394447,PMID:25756792 Q14003 UniProtKB Natural variant 643 643 . . . ID=VAR_074201;Note=In SCA13%3B uncertain significance%3B no effect on channel activity. G->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25756792;Dbxref=dbSNP:rs778523009,PMID:25756792 Q14003 UniProtKB Natural variant 645 645 . . . ID=VAR_074202;Note=In SCA13%3B uncertain significance%3B no effect on channel activity. P->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25756792;Dbxref=dbSNP:rs1460306526,PMID:25756792 Q14003 UniProtKB Natural variant 746 746 . . . ID=VAR_074203;Note=In SCA13%3B uncertain significance%3B no effect on channel activity. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25756792;Dbxref=dbSNP:rs958323371,PMID:25756792 Q14003 UniProtKB Mutagenesis 1 78 . . . Note=Loss of N-type inactivation. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26997484;Dbxref=PMID:26997484 Q14003 UniProtKB Mutagenesis 366 366 . . . Note=Decreases protein abundance. R->K%2CA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23734863;Dbxref=PMID:23734863 Q14003 UniProtKB Mutagenesis 420 420 . . . Note=Decreases protein abundance. R->K%2CA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23734863;Dbxref=PMID:23734863 Q14003 UniProtKB Mutagenesis 423 423 . . . Note=Decreases protein abundance. R->K%2CA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23734863;Dbxref=PMID:23734863 Q14003 UniProtKB Mutagenesis 592 592 . . . Note=Loss of interaction with ACTR3. No effect on voltage-dependent channel opening or current amplitude%2C but decreased rate of inactivation during prolonged depolarization. G->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26997484;Dbxref=PMID:26997484