##gff-version 3 P63141 UniProtKB Chain 1 499 . . . ID=PRO_0000053973;Note=Potassium voltage-gated channel subfamily A member 2 P63141 UniProtKB Topological domain 1 160 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 P63141 UniProtKB Transmembrane 161 182 . . . Note=Helical%3B Name%3DSegment S1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 P63141 UniProtKB Topological domain 183 221 . . . Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 P63141 UniProtKB Transmembrane 222 243 . . . Note=Helical%3B Name%3DSegment S2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 P63141 UniProtKB Topological domain 244 254 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 P63141 UniProtKB Transmembrane 255 275 . . . Note=Helical%3B Name%3DSegment S3;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 P63141 UniProtKB Topological domain 276 289 . . . Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 P63141 UniProtKB Transmembrane 290 310 . . . Note=Helical%3B Voltage-sensor%3B Name%3DSegment S4;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 P63141 UniProtKB Topological domain 311 325 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 P63141 UniProtKB Transmembrane 326 347 . . . Note=Helical%3B Name%3DSegment S5;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 P63141 UniProtKB Topological domain 348 361 . . . Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 P63141 UniProtKB Intramembrane 362 373 . . . Note=Helical%3B Name%3DPore helix;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 P63141 UniProtKB Intramembrane 374 381 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 P63141 UniProtKB Topological domain 382 388 . . . Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 P63141 UniProtKB Transmembrane 389 417 . . . Note=Helical%3B Name%3DSegment S6;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 P63141 UniProtKB Topological domain 418 499 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 P63141 UniProtKB Region 1 125 . . . Note=Tetramerization domain;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 P63141 UniProtKB Region 1 26 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P63141 UniProtKB Region 312 325 . . . Note=S4-S5 linker;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 P63141 UniProtKB Motif 374 379 . . . Note=Selectivity filter;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 P63141 UniProtKB Motif 497 499 . . . Note=PDZ-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 P63141 UniProtKB Site 252 252 . . . Note=Important for normal%2C slow channel gating;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 P63141 UniProtKB Site 381 381 . . . Note=Important for binding with the scorpion mesomartoxin%3B when the scorpion mesomartoxin-rKv1.2/KCNA2 interaction is modeled%2C this residue is close to the 'Y-57' residue of the toxin;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 P63141 UniProtKB Modified residue 429 429 . . . Note=Phosphotyrosine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:18034455;Dbxref=PMID:18034455 P63141 UniProtKB Modified residue 434 434 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079 P63141 UniProtKB Modified residue 440 440 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079 P63141 UniProtKB Modified residue 441 441 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q09081 P63141 UniProtKB Modified residue 449 449 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q09081 P63141 UniProtKB Modified residue 458 458 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 P63141 UniProtKB Modified residue 468 468 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079 P63141 UniProtKB Lipidation 244 244 . . . Note=S-palmitoyl cysteine;Ontology_term=ECO:0000255;evidence=ECO:0000255 P63141 UniProtKB Glycosylation 207 207 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 P63141 UniProtKB Mutagenesis 402 402 . . . Note=In Pgu%3B chronic motor incoordination%3B decreases the number of functional channels at the cell surface. I->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20696761;Dbxref=PMID:20696761 P63141 UniProtKB Sequence conflict 33 33 . . . Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 P63141 UniProtKB Beta strand 34 39 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5WIE P63141 UniProtKB Beta strand 42 47 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5WIE P63141 UniProtKB Helix 48 51 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5WIE P63141 UniProtKB Turn 58 60 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5WIE P63141 UniProtKB Helix 62 65 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5WIE P63141 UniProtKB Helix 66 68 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5WIE P63141 UniProtKB Turn 71 74 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5WIE P63141 UniProtKB Beta strand 75 78 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5WIE P63141 UniProtKB Helix 85 94 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5WIE P63141 UniProtKB Helix 106 115 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5WIE P63141 UniProtKB Helix 120 129 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5WIE P63141 UniProtKB Helix 144 154 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5WIE P63141 UniProtKB Turn 156 158 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5WIE P63141 UniProtKB Helix 160 182 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5WIE P63141 UniProtKB Helix 186 189 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5WIE P63141 UniProtKB Turn 193 196 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5WIE P63141 UniProtKB Helix 202 206 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5WIE P63141 UniProtKB Helix 208 210 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5WIE P63141 UniProtKB Helix 221 243 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5WIE P63141 UniProtKB Beta strand 247 249 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5WIE P63141 UniProtKB Turn 250 252 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5WIE P63141 UniProtKB Helix 254 261 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5WIE P63141 UniProtKB Helix 283 287 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5WIE P63141 UniProtKB Helix 290 299 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5WIE P63141 UniProtKB Helix 300 309 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5WIE P63141 UniProtKB Helix 312 351 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5WIE P63141 UniProtKB Turn 361 364 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5WIE P63141 UniProtKB Helix 365 372 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5WIE P63141 UniProtKB Beta strand 378 380 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5WIE P63141 UniProtKB Helix 385 403 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5WIE P63141 UniProtKB Helix 405 418 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5WIE