##gff-version 3 Q96PR1 UniProtKB Chain 1 638 . . . ID=PRO_0000310416;Note=Potassium voltage-gated channel subfamily C member 2 Q96PR1 UniProtKB Topological domain 1 229 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q96PR1 UniProtKB Transmembrane 230 250 . . . Note=Helical%3B Name%3DSegment S1;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q96PR1 UniProtKB Transmembrane 284 303 . . . Note=Helical%3B Name%3DSegment S2;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q96PR1 UniProtKB Topological domain 304 313 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q96PR1 UniProtKB Transmembrane 314 334 . . . Note=Helical%3B Name%3DSegment S3;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q96PR1 UniProtKB Transmembrane 346 368 . . . Note=Helical%3B Voltage-sensor%3B Name%3DSegment S4;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q96PR1 UniProtKB Topological domain 369 381 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q96PR1 UniProtKB Transmembrane 382 402 . . . Note=Helical%3B Name%3DSegment S5;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q96PR1 UniProtKB Transmembrane 453 473 . . . Note=Helical%3B Name%3DSegment S6;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q96PR1 UniProtKB Topological domain 474 638 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q96PR1 UniProtKB Region 38 93 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q96PR1 UniProtKB Region 437 442 . . . Note=Selectivity filter;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q96PR1 UniProtKB Region 538 572 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q96PR1 UniProtKB Compositional bias 56 72 . . . Note=Pro residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q96PR1 UniProtKB Modified residue 600 600 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q14B80 Q96PR1 UniProtKB Glycosylation 259 259 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q96PR1 UniProtKB Glycosylation 266 266 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q96PR1 UniProtKB Alternative sequence 539 593 . . . ID=VSP_044742;Note=In isoform 5. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:14702039;Dbxref=PMID:14702039 Q96PR1 UniProtKB Alternative sequence 539 558 . . . ID=VSP_029269;Note=In isoform 4. VLSGDDSTGSEPPLSPPERL->DNCKEVVITGYTQAEARSLT;Ontology_term=ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:14702039,ECO:0000303|PubMed:15489334;Dbxref=PMID:14702039,PMID:15489334 Q96PR1 UniProtKB Alternative sequence 559 638 . . . ID=VSP_029270;Note=In isoform 4. Missing;Ontology_term=ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:14702039,ECO:0000303|PubMed:15489334;Dbxref=PMID:14702039,PMID:15489334 Q96PR1 UniProtKB Alternative sequence 594 638 . . . ID=VSP_029271;Note=In isoform 2. GYEKSRSLNNIAGLAGNALRLSPVTSPYNSPCPLRRSRSPIPSIL->VLYRIYHGLLTAEKGTVEFSHTKDYTGNRLLLLNVP;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:8111118;Dbxref=PMID:8111118 Q96PR1 UniProtKB Alternative sequence 594 638 . . . ID=VSP_029272;Note=In isoform 3. GYEKSRSLNNIAGLAGNALRLSPVTSPYNSPCPLRRSRSPIPSIL->DNCKEVVITGYTQAEARSLT;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:8111118;Dbxref=PMID:8111118 Q96PR1 UniProtKB Alternative sequence 595 638 . . . ID=VSP_046002;Note=In isoform 6. YEKSRSLNNIAGLAGNALRLSPVTSPYNSPCPLRRSRSPIPSIL->IRNGHSILHHLDNGTKCHYLRIIF;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:14702039;Dbxref=PMID:14702039 Q96PR1 UniProtKB Natural variant 125 125 . . . ID=VAR_087366;Note=In DEE103%3B affects voltage-gated potassium channel activity%3B when expressed in Xenopus laevis oocytes%2C it results in a shift in voltage dependence of activation to more hyperpolarized potentials and a slower deactivation time. C->W;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:35314505;Dbxref=PMID:35314505 Q96PR1 UniProtKB Natural variant 135 135 . . . ID=VAR_087367;Note=In DEE103%3B affects voltage-gated potassium channel activity%3B when expressed in Xenopus laevis oocytes%2C it results in a shift in voltage dependence of activation to more hyperpolarized potentials and a slower deactivation time. E->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:35314505;Dbxref=PMID:35314505 Q96PR1 UniProtKB Natural variant 167 167 . . . ID=VAR_087368;Note=In DEE103%3B affects voltage-gated potassium channel activity%3B when expressed in Xenopus laevis oocytes%2C it causes a shift in voltage dependence of steady-state activation to more hyperpolarized potentials and results in a significant reduction of potassium currents. D->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:32392612;Dbxref=PMID:32392612 Q96PR1 UniProtKB Natural variant 219 219 . . . ID=VAR_087369;Note=Found in a patient with generalized epilepsy%3B likely pathogenic%3B loss of voltage-gated potassium channel activity%3B no current is detected when mutant channels are expressed in Xenopus laevis oocytes. F->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:35314505;Dbxref=PMID:35314505 Q96PR1 UniProtKB Natural variant 351 351 . . . ID=VAR_087370;Note=In DEE103. R->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:35314505;Dbxref=PMID:35314505 Q96PR1 UniProtKB Natural variant 382 382 . . . ID=VAR_087371;Note=Found in a patient with myoclonic-atonic epilepsy%3B uncertain significance. F->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:35314505;Dbxref=PMID:35314505 Q96PR1 UniProtKB Natural variant 405 405 . . . ID=VAR_087372;Note=In DEE103%3B affects voltage-gated potassium channel activity%3B results in a shift in voltage dependence of activation to more hyperpolarized potentials. R->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:36090251;Dbxref=PMID:36090251 Q96PR1 UniProtKB Natural variant 437 437 . . . ID=VAR_087373;Note=In DEE103%3B affects voltage-gated potassium channel activity%3B when expressed in Xenopus laevis oocytes%2C it results in a shift in voltage dependence of activation to more hyperpolarized potentials and a slower deactivation time. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:35314505;Dbxref=PMID:35314505 Q96PR1 UniProtKB Natural variant 471 471 . . . ID=VAR_087374;Note=In DEE103. V->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:31972370;Dbxref=PMID:31972370 Q96PR1 UniProtKB Sequence conflict 31 31 . . . Note=G->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q96PR1 UniProtKB Sequence conflict 305 305 . . . Note=P->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q96PR1 UniProtKB Sequence conflict 476 476 . . . Note=F->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q96PR1 UniProtKB Sequence conflict 487 487 . . . Note=Q->H;Ontology_term=ECO:0000305;evidence=ECO:0000305