##gff-version 3 P15390 UniProtKB Chain 1 1840 . . . ID=PRO_0000048496;Note=Sodium channel protein type 4 subunit alpha P15390 UniProtKB Topological domain 1 131 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305 P15390 UniProtKB Transmembrane 132 150 . . . Note=Helical%3B Name%3DS1 of repeat I;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P35499 P15390 UniProtKB Topological domain 151 157 . . . Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305 P15390 UniProtKB Transmembrane 158 178 . . . Note=Helical%3B Name%3DS2 of repeat I;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P35499 P15390 UniProtKB Topological domain 179 192 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305 P15390 UniProtKB Transmembrane 193 210 . . . Note=Helical%3B Name%3DS3 of repeat I;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P35499 P15390 UniProtKB Topological domain 211 216 . . . Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305 P15390 UniProtKB Transmembrane 217 233 . . . Note=Helical%3B Name%3DS4 of repeat I;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P35499 P15390 UniProtKB Topological domain 234 252 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305 P15390 UniProtKB Transmembrane 253 272 . . . Note=Helical%3B Name%3DS5 of repeat I;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P35499 P15390 UniProtKB Topological domain 273 385 . . . Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305 P15390 UniProtKB Intramembrane 386 410 . . . Note=Pore-forming;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P35499 P15390 UniProtKB Topological domain 411 417 . . . Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305 P15390 UniProtKB Transmembrane 418 438 . . . Note=Helical%3B Name%3DS6 of repeat I;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P35499 P15390 UniProtKB Topological domain 439 572 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305 P15390 UniProtKB Transmembrane 573 591 . . . Note=Helical%3B Name%3DS1 of repeat II;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P35499 P15390 UniProtKB Topological domain 592 602 . . . Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305 P15390 UniProtKB Transmembrane 603 622 . . . Note=Helical%3B Name%3DS2 of repeat II;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P35499 P15390 UniProtKB Topological domain 623 636 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305 P15390 UniProtKB Transmembrane 637 656 . . . Note=Helical%3B Name%3DS3 of repeat II;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P35499 P15390 UniProtKB Topological domain 657 658 . . . Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305 P15390 UniProtKB Transmembrane 659 676 . . . Note=Helical%3B Name%3DS4 of repeat II;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P35499 P15390 UniProtKB Topological domain 677 692 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305 P15390 UniProtKB Transmembrane 693 711 . . . Note=Helical%3B Name%3DS5 of repeat II;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P35499 P15390 UniProtKB Topological domain 712 740 . . . Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305 P15390 UniProtKB Intramembrane 741 761 . . . Note=Pore-forming;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P35499 P15390 UniProtKB Topological domain 762 772 . . . Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305 P15390 UniProtKB Transmembrane 773 791 . . . Note=Helical%3B Name%3DS6 of repeat II;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P35499 P15390 UniProtKB Topological domain 792 1025 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305 P15390 UniProtKB Transmembrane 1026 1043 . . . Note=Helical%3B Name%3DS1 of repeat III;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P35499 P15390 UniProtKB Topological domain 1044 1056 . . . Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305 P15390 UniProtKB Transmembrane 1057 1075 . . . Note=Helical%3B Name%3DS2 of repeat III;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P35499 P15390 UniProtKB Topological domain 1076 1089 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305 P15390 UniProtKB Transmembrane 1090 1108 . . . Note=Helical%3B Name%3DS3 of repeat III;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P35499 P15390 UniProtKB Topological domain 1109 1116 . . . Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305 P15390 UniProtKB Transmembrane 1117 1135 . . . Note=Helical%3B Name%3DS4 of repeat III;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P35499 P15390 UniProtKB Topological domain 1136 1152 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305 P15390 UniProtKB Transmembrane 1153 1172 . . . Note=Helical%3B Name%3DS5 of repeat III;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P35499 P15390 UniProtKB Topological domain 1173 1223 . . . Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305 P15390 UniProtKB Intramembrane 1224 1245 . . . Note=Pore-forming;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P35499 P15390 UniProtKB Topological domain 1246 1262 . . . Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305 P15390 UniProtKB Transmembrane 1263 1284 . . . Note=Helical%3B Name%3DS6 of repeat III;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P35499 P15390 UniProtKB Topological domain 1285 1347 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305 P15390 UniProtKB Transmembrane 1348 1365 . . . Note=Helical%3B Name%3DS1 of repeat IV;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P35499 P15390 UniProtKB Topological domain 1366 1376 . . . Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305 P15390 UniProtKB Transmembrane 1377 1395 . . . Note=Helical%3B Name%3DS2 of repeat IV;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P35499 P15390 UniProtKB Topological domain 1396 1407 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305 P15390 UniProtKB Transmembrane 1408 1425 . . . Note=Helical%3B Name%3DS3 of repeat IV;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P35499 P15390 UniProtKB Topological domain 1426 1438 . . . Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305 P15390 UniProtKB Transmembrane 1439 1455 . . . Note=Helical%3B Name%3DS4 of repeat IV;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P35499 P15390 UniProtKB Topological domain 1456 1474 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305 P15390 UniProtKB Transmembrane 1475 1492 . . . Note=Helical%3B Name%3DS5 of repeat IV;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P35499 P15390 UniProtKB Topological domain 1493 1514 . . . Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305 P15390 UniProtKB Intramembrane 1515 1537 . . . Note=Pore-forming;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P35499 P15390 UniProtKB Topological domain 1538 1567 . . . Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305 P15390 UniProtKB Transmembrane 1568 1590 . . . Note=Helical%3B Name%3DS6 of repeat IV;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P35499 P15390 UniProtKB Topological domain 1591 1840 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305 P15390 UniProtKB Repeat 113 448 . . . Note=I;Ontology_term=ECO:0000305;evidence=ECO:0000305 P15390 UniProtKB Repeat 554 826 . . . Note=II;Ontology_term=ECO:0000305;evidence=ECO:0000305 P15390 UniProtKB Repeat 1006 1319 . . . Note=III;Ontology_term=ECO:0000305;evidence=ECO:0000305 P15390 UniProtKB Repeat 1328 1626 . . . Note=IV;Ontology_term=ECO:0000305;evidence=ECO:0000305 P15390 UniProtKB Domain 1720 1749 . . . Note=IQ;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00116 P15390 UniProtKB Region 36 63 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P15390 UniProtKB Region 481 522 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P15390 UniProtKB Region 854 884 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P15390 UniProtKB Region 925 983 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P15390 UniProtKB Region 1303 1305 . . . Note=Important for rapid channel inactivation;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28012039;Dbxref=PMID:28012039 P15390 UniProtKB Region 1775 1840 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P15390 UniProtKB Compositional bias 36 59 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P15390 UniProtKB Compositional bias 481 499 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P15390 UniProtKB Compositional bias 864 884 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P15390 UniProtKB Compositional bias 968 983 . . . Note=Acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P15390 UniProtKB Compositional bias 1775 1796 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P15390 UniProtKB Compositional bias 1811 1827 . . . Note=Pro residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P15390 UniProtKB Site 401 401 . . . Note=Important for inhibition by tetrodotoxin;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16303569;Dbxref=PMID:16303569 P15390 UniProtKB Modified residue 56 56 . . . Note=Phosphoserine%3B by PKA;Ontology_term=ECO:0000255;evidence=ECO:0000255 P15390 UniProtKB Modified residue 251 251 . . . Note=Phosphoserine%3B by PKA;Ontology_term=ECO:0000255;evidence=ECO:0000255 P15390 UniProtKB Modified residue 487 487 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:22673903;Dbxref=PMID:22673903 P15390 UniProtKB Modified residue 1321 1321 . . . Note=Phosphoserine%3B by PKA;Ontology_term=ECO:0000255;evidence=ECO:0000255 P15390 UniProtKB Modified residue 1321 1321 . . . Note=Phosphoserine%3B by PKC;Ontology_term=ECO:0000250;evidence=ECO:0000250 P15390 UniProtKB Glycosylation 288 288 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 P15390 UniProtKB Glycosylation 291 291 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 P15390 UniProtKB Glycosylation 297 297 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 P15390 UniProtKB Glycosylation 303 303 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 P15390 UniProtKB Glycosylation 309 309 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 P15390 UniProtKB Glycosylation 315 315 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 P15390 UniProtKB Glycosylation 327 327 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 P15390 UniProtKB Glycosylation 356 356 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 P15390 UniProtKB Glycosylation 1198 1198 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 P15390 UniProtKB Disulfide bond 280 354 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P35499 P15390 UniProtKB Disulfide bond 363 369 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P35499 P15390 UniProtKB Disulfide bond 723 723 . . . Note=Interchain%3B with SCN2B or SCN4B;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04775 P15390 UniProtKB Disulfide bond 723 723 . . . Note=Interchain%3B with the conotoxin GVIIJ (when the channel is not linked to SCN2B or SCN4B%3B the bond to SCN2B or SCN4B protects the channel from the inhibition by toxin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04775 P15390 UniProtKB Disulfide bond 725 731 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P35499 P15390 UniProtKB Disulfide bond 763 772 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P35499 P15390 UniProtKB Disulfide bond 1546 1561 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P35499 P15390 UniProtKB Natural variant 120 120 . . . Note=In strain: COP%3B prostatic cancer cell lines. V->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9613589;Dbxref=PMID:9613589 P15390 UniProtKB Natural variant 916 916 . . . Note=In strain: COP%3B prostatic cancer cell lines. Q->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9613589;Dbxref=PMID:9613589 P15390 UniProtKB Natural variant 1202 1202 . . . Note=In strain: COP%3B prostatic cancer cell lines. S->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9613589;Dbxref=PMID:9613589 P15390 UniProtKB Natural variant 1257 1257 . . . Note=In strain: COP%3B prostatic cancer cell lines. H->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9613589;Dbxref=PMID:9613589 P15390 UniProtKB Natural variant 1755 1755 . . . Note=In strain: COP%3B prostatic cancer cell lines. D->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9613589;Dbxref=PMID:9613589 P15390 UniProtKB Natural variant 1803 1803 . . . Note=In strain: COP%3B prostatic cancer cell lines. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9613589;Dbxref=PMID:9613589 P15390 UniProtKB Mutagenesis 401 401 . . . Note=Strongly reduced sensitivity to tetrodotoxin. Y->C%2CN;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16303569;Dbxref=PMID:16303569 P15390 UniProtKB Mutagenesis 1240 1241 . . . Note=Strongly reduced sensitivity to saxitoxin. MD->TI;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23077250;Dbxref=PMID:23077250 P15390 UniProtKB Mutagenesis 1303 1305 . . . Note=Loss of rapid channel inactivation. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28012039;Dbxref=PMID:28012039 P15390 UniProtKB Mutagenesis 1379 1379 . . . Note=Become sensitive to the spider beta/delta-theraphotoxin-Pre1a%2C which inhibits inactivation of the channel. Y->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28428547;Dbxref=PMID:28428547 P15390 UniProtKB Mutagenesis 1380 1380 . . . Note=No change in sensitivity to the spider beta/delta-theraphotoxin-Pre1a. N->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28428547;Dbxref=PMID:28428547 P15390 UniProtKB Helix 1569 1594 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5JR0 P15390 UniProtKB Helix 1722 1732 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6MUE