##gff-version 3 Q63881 UniProtKB Chain 1 630 . . . ID=PRO_0000054067;Note=Potassium voltage-gated channel subfamily D member 2 Q63881 UniProtKB Topological domain 1 182 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 Q63881 UniProtKB Transmembrane 183 204 . . . Note=Helical%3B Name%3DSegment S1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 Q63881 UniProtKB Topological domain 205 228 . . . Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 Q63881 UniProtKB Transmembrane 229 250 . . . Note=Helical%3B Name%3DSegment S2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 Q63881 UniProtKB Topological domain 251 261 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 Q63881 UniProtKB Transmembrane 262 279 . . . Note=Helical%3B Name%3DSegment S3;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 Q63881 UniProtKB Topological domain 280 286 . . . Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 Q63881 UniProtKB Transmembrane 287 306 . . . Note=Helical%3B Voltage-sensor%3B Name%3DSegment S4;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 Q63881 UniProtKB Topological domain 307 321 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 Q63881 UniProtKB Transmembrane 322 343 . . . Note=Helical%3B Name%3DSegment S5;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 Q63881 UniProtKB Topological domain 344 357 . . . Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 Q63881 UniProtKB Intramembrane 358 369 . . . Note=Helical%3B Name%3DPore helix;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 Q63881 UniProtKB Intramembrane 370 377 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 Q63881 UniProtKB Topological domain 378 384 . . . Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 Q63881 UniProtKB Transmembrane 385 413 . . . Note=Helical%3B Name%3DSegment S6;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 Q63881 UniProtKB Topological domain 414 630 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 Q63881 UniProtKB Region 2 20 . . . Note=Interaction with KCNIP1%2C KCNIP2%2C and other family members;Ontology_term=ECO:0000305,ECO:0000305;evidence=ECO:0000305|PubMed:14980206,ECO:0000305|PubMed:14980207;Dbxref=PMID:14980206,PMID:14980207 Q63881 UniProtKB Region 71 90 . . . Note=Interaction with KCNIP1;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:14980207;Dbxref=PMID:14980207 Q63881 UniProtKB Region 308 321 . . . Note=S4-S5 linker;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 Q63881 UniProtKB Region 474 630 . . . Note=Important for normal channel activation and inactivation%2C for interaction with KCNIP2%2C and probably other family members as well;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16820361;Dbxref=PMID:16820361 Q63881 UniProtKB Region 474 489 . . . Note=Required for dendritic targeting;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12592409;Dbxref=PMID:12592409 Q63881 UniProtKB Region 600 623 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q63881 UniProtKB Motif 370 375 . . . Note=Selectivity filter;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 Q63881 UniProtKB Motif 627 630 . . . Note=PDZ-binding;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11923279,ECO:0000269|PubMed:14559911;Dbxref=PMID:11923279,PMID:14559911 Q63881 UniProtKB Binding site 105 105 . . . Ontology_term=ECO:0007744;evidence=ECO:0007744|PDB:1NN7 Q63881 UniProtKB Binding site 132 132 . . . Ontology_term=ECO:0007744;evidence=ECO:0007744|PDB:1NN7 Q63881 UniProtKB Binding site 133 133 . . . Ontology_term=ECO:0007744;evidence=ECO:0007744|PDB:1NN7 Q63881 UniProtKB Modified residue 38 38 . . . Note=Phosphothreonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10681507;Dbxref=PMID:10681507 Q63881 UniProtKB Modified residue 438 438 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24404150;Dbxref=PMID:24404150 Q63881 UniProtKB Modified residue 548 548 . . . Note=Phosphoserine;Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:19441798,ECO:0007744|PubMed:22673903;Dbxref=PMID:19441798,PMID:22673903 Q63881 UniProtKB Modified residue 552 552 . . . Note=Phosphoserine;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:10681507,ECO:0000269|PubMed:12451113,ECO:0000269|PubMed:12829703,ECO:0000269|PubMed:18650329,ECO:0000269|PubMed:19441798,ECO:0007744|PubMed:22673903;Dbxref=PMID:10681507,PMID:12451113,PMID:12829703,PMID:18650329,PMID:19441798,PMID:22673903 Q63881 UniProtKB Modified residue 572 572 . . . Note=Phosphoserine;Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:19441798,ECO:0007744|PubMed:22673903;Dbxref=PMID:19441798,PMID:22673903 Q63881 UniProtKB Modified residue 575 575 . . . Note=Phosphoserine;Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:19441798,ECO:0007744|PubMed:22673903;Dbxref=PMID:19441798,PMID:22673903 Q63881 UniProtKB Modified residue 602 602 . . . Note=Phosphothreonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11080179;Dbxref=PMID:11080179 Q63881 UniProtKB Modified residue 607 607 . . . Note=Phosphothreonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11080179;Dbxref=PMID:11080179 Q63881 UniProtKB Modified residue 616 616 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11080179;Dbxref=PMID:11080179 Q63881 UniProtKB Mutagenesis 7 11 . . . Note=Greatly reduces interaction with KCNIP1. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14980207;Dbxref=PMID:14980207 Q63881 UniProtKB Mutagenesis 8 8 . . . Note=Abolishes interaction with KCNP1%3B when associated with A-11. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14980206;Dbxref=PMID:14980206 Q63881 UniProtKB Mutagenesis 11 11 . . . Note=Abolishes interaction with KCNP1%3B when associated with A-8. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14980206;Dbxref=PMID:14980206 Q63881 UniProtKB Mutagenesis 66 66 . . . Note=Abolishes expression. L->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12835418;Dbxref=PMID:12835418 Q63881 UniProtKB Mutagenesis 71 71 . . . Note=Abolishes interaction with KCNIP1. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14980207;Dbxref=PMID:14980207 Q63881 UniProtKB Mutagenesis 73 73 . . . Note=Abolishes interaction with KCNIP1. D->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14980207;Dbxref=PMID:14980207 Q63881 UniProtKB Mutagenesis 74 74 . . . Note=Abolishes interaction with KCNIP1. F->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14980207;Dbxref=PMID:14980207 Q63881 UniProtKB Mutagenesis 79 79 . . . Note=Abolishes interaction with KCNIP1. E->L%2CR;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14980207;Dbxref=PMID:14980207 Q63881 UniProtKB Mutagenesis 93 93 . . . Note=Greatly reduces expression and changes multimerization. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12835418;Dbxref=PMID:12835418 Q63881 UniProtKB Mutagenesis 105 105 . . . Note=Abolishes tetramerization and assembly of a functional channel. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12754210;Dbxref=PMID:12754210 Q63881 UniProtKB Mutagenesis 111 111 . . . Note=Abolishes tetramerization and assembly of a functional channel%3B when associated with A-105%3B A-132 and A-133. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12754210;Dbxref=PMID:12754210 Q63881 UniProtKB Mutagenesis 132 132 . . . Note=Abolishes tetramerization and assembly of a functional channel%3B when associated with A-105%3B A-111 and A-133. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12754210;Dbxref=PMID:12754210 Q63881 UniProtKB Mutagenesis 133 133 . . . Note=Abolishes tetramerization and assembly of a functional channel%3B when associated with A-105%3B A-111 and A-132. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12754210;Dbxref=PMID:12754210 Q63881 UniProtKB Mutagenesis 481 482 . . . Note=Loss of dendritic targeted expression. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12592409;Dbxref=PMID:12592409 Q63881 UniProtKB Mutagenesis 552 552 . . . Note=Abolishes PKA-mediated modulation of cell surface expression and channel activity. S->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12451113,ECO:0000269|PubMed:18650329;Dbxref=PMID:12451113,PMID:18650329 Q63881 UniProtKB Mutagenesis 627 630 . . . Note=Abolishes interaction with DLG4. Missing;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11923279,ECO:0000269|PubMed:14559911;Dbxref=PMID:11923279,PMID:14559911 Q63881 UniProtKB Helix 1 6 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1S6C Q63881 UniProtKB Helix 9 17 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1S6C Q63881 UniProtKB Beta strand 43 47 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1NN7 Q63881 UniProtKB Beta strand 50 54 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1NN7 Q63881 UniProtKB Helix 56 60 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1NN7 Q63881 UniProtKB Beta strand 64 66 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1NN7 Q63881 UniProtKB Helix 70 75 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1NN7 Q63881 UniProtKB Helix 78 80 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1NN7 Q63881 UniProtKB Beta strand 81 85 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1NN7 Q63881 UniProtKB Turn 89 91 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1NN7 Q63881 UniProtKB Helix 92 101 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1NN7 Q63881 UniProtKB Helix 112 122 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1NN7 Q63881 UniProtKB Helix 131 145 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1NN7