##gff-version 3 P0DMA5 UniProtKB Chain 1 1959 . . . ID=PRO_0000424959;Note=Sodium channel protein type 10 subunit alpha P0DMA5 UniProtKB Topological domain 1 125 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305 P0DMA5 UniProtKB Transmembrane 126 149 . . . Note=Helical%3B Name%3DS1 of repeat I;Ontology_term=ECO:0000255;evidence=ECO:0000255 P0DMA5 UniProtKB Topological domain 150 154 . . . Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305 P0DMA5 UniProtKB Transmembrane 155 174 . . . Note=Helical%3B Name%3DS2 of repeat I;Ontology_term=ECO:0000255;evidence=ECO:0000255 P0DMA5 UniProtKB Topological domain 175 187 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305 P0DMA5 UniProtKB Transmembrane 188 206 . . . Note=Helical%3B Name%3DS3 of repeat I;Ontology_term=ECO:0000255;evidence=ECO:0000255 P0DMA5 UniProtKB Topological domain 207 212 . . . Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305 P0DMA5 UniProtKB Transmembrane 213 232 . . . Note=Helical%3B Voltage-sensor%3B Name%3DS4 of repeat I;Ontology_term=ECO:0000255;evidence=ECO:0000255 P0DMA5 UniProtKB Topological domain 233 248 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305 P0DMA5 UniProtKB Transmembrane 249 272 . . . Note=Helical%3B Name%3DS5 of repeat I;Ontology_term=ECO:0000255;evidence=ECO:0000255 P0DMA5 UniProtKB Topological domain 273 340 . . . Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305 P0DMA5 UniProtKB Intramembrane 341 365 . . . Note=Pore-forming;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:D0E0C2 P0DMA5 UniProtKB Topological domain 366 372 . . . Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305 P0DMA5 UniProtKB Transmembrane 373 398 . . . Note=Helical%3B Name%3DS6 of repeat I;Ontology_term=ECO:0000255;evidence=ECO:0000255 P0DMA5 UniProtKB Topological domain 399 659 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305 P0DMA5 UniProtKB Transmembrane 660 684 . . . Note=Helical%3B Name%3DS1 of repeat II;Ontology_term=ECO:0000255;evidence=ECO:0000255 P0DMA5 UniProtKB Topological domain 685 695 . . . Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305 P0DMA5 UniProtKB Transmembrane 696 719 . . . Note=Helical%3B Name%3DS2 of repeat II;Ontology_term=ECO:0000255;evidence=ECO:0000255 P0DMA5 UniProtKB Topological domain 720 727 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305 P0DMA5 UniProtKB Transmembrane 728 747 . . . Note=Helical%3B Name%3DS3 of repeat II;Ontology_term=ECO:0000255;evidence=ECO:0000255 P0DMA5 UniProtKB Topological domain 748 753 . . . Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305 P0DMA5 UniProtKB Transmembrane 754 773 . . . Note=Helical%3B Voltage-sensor%3B Name%3DS4 of repeat II;Ontology_term=ECO:0000255;evidence=ECO:0000255 P0DMA5 UniProtKB Topological domain 774 789 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305 P0DMA5 UniProtKB Transmembrane 790 810 . . . Note=Helical%3B Name%3DS5 of repeat II;Ontology_term=ECO:0000255;evidence=ECO:0000255 P0DMA5 UniProtKB Topological domain 811 834 . . . Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305 P0DMA5 UniProtKB Intramembrane 835 855 . . . Note=Pore-forming;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:D0E0C2 P0DMA5 UniProtKB Topological domain 856 864 . . . Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305 P0DMA5 UniProtKB Transmembrane 865 890 . . . Note=Helical%3B Name%3DS6 of repeat II;Ontology_term=ECO:0000255;evidence=ECO:0000255 P0DMA5 UniProtKB Topological domain 891 1149 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305 P0DMA5 UniProtKB Transmembrane 1150 1173 . . . Note=Helical%3B Name%3DS1 of repeat III;Ontology_term=ECO:0000255;evidence=ECO:0000255 P0DMA5 UniProtKB Topological domain 1174 1186 . . . Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305 P0DMA5 UniProtKB Transmembrane 1187 1212 . . . Note=Helical%3B Name%3DS2 of repeat III;Ontology_term=ECO:0000255;evidence=ECO:0000255 P0DMA5 UniProtKB Topological domain 1213 1218 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305 P0DMA5 UniProtKB Transmembrane 1219 1240 . . . Note=Helical%3B Name%3DS3 of repeat III;Ontology_term=ECO:0000255;evidence=ECO:0000255 P0DMA5 UniProtKB Topological domain 1241 1244 . . . Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305 P0DMA5 UniProtKB Transmembrane 1245 1266 . . . Note=Helical%3B Voltage-sensor%3B Name%3DS4 of repeat III;Ontology_term=ECO:0000255;evidence=ECO:0000255 P0DMA5 UniProtKB Topological domain 1267 1285 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305 P0DMA5 UniProtKB Transmembrane 1286 1313 . . . Note=Helical%3B Name%3DS5 of repeat III;Ontology_term=ECO:0000255;evidence=ECO:0000255 P0DMA5 UniProtKB Topological domain 1314 1355 . . . Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305 P0DMA5 UniProtKB Intramembrane 1356 1377 . . . Note=Pore-forming;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:D0E0C2 P0DMA5 UniProtKB Topological domain 1378 1393 . . . Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305 P0DMA5 UniProtKB Transmembrane 1394 1420 . . . Note=Helical%3B Name%3DS6 of repeat III;Ontology_term=ECO:0000255;evidence=ECO:0000255 P0DMA5 UniProtKB Topological domain 1421 1473 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305 P0DMA5 UniProtKB Transmembrane 1474 1497 . . . Note=Helical%3B Name%3DS1 of repeat IV;Ontology_term=ECO:0000255;evidence=ECO:0000255 P0DMA5 UniProtKB Topological domain 1498 1508 . . . Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305 P0DMA5 UniProtKB Transmembrane 1509 1532 . . . Note=Helical%3B Name%3DS2 of repeat IV;Ontology_term=ECO:0000255;evidence=ECO:0000255 P0DMA5 UniProtKB Topological domain 1533 1538 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305 P0DMA5 UniProtKB Transmembrane 1539 1562 . . . Note=Helical%3B Name%3DS3 of repeat IV;Ontology_term=ECO:0000255;evidence=ECO:0000255 P0DMA5 UniProtKB Topological domain 1563 1574 . . . Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305 P0DMA5 UniProtKB Transmembrane 1575 1596 . . . Note=Helical%3B Voltage-sensor%3B Name%3DS4 of repeat IV;Ontology_term=ECO:0000255;evidence=ECO:0000255 P0DMA5 UniProtKB Topological domain 1597 1611 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305 P0DMA5 UniProtKB Transmembrane 1612 1634 . . . Note=Helical%3B Name%3DS5 of repeat IV;Ontology_term=ECO:0000255;evidence=ECO:0000255 P0DMA5 UniProtKB Topological domain 1635 1648 . . . Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305 P0DMA5 UniProtKB Intramembrane 1649 1671 . . . Note=Pore-forming;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:D0E0C2 P0DMA5 UniProtKB Topological domain 1672 1699 . . . Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305 P0DMA5 UniProtKB Transmembrane 1700 1724 . . . Note=Helical%3B Name%3DS6 of repeat IV;Ontology_term=ECO:0000255;evidence=ECO:0000255 P0DMA5 UniProtKB Topological domain 1725 1959 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305 P0DMA5 UniProtKB Repeat 116 404 . . . Note=I;Ontology_term=ECO:0000305;evidence=ECO:0000305 P0DMA5 UniProtKB Repeat 647 911 . . . Note=II;Ontology_term=ECO:0000305;evidence=ECO:0000305 P0DMA5 UniProtKB Repeat 1142 1451 . . . Note=III;Ontology_term=ECO:0000305;evidence=ECO:0000305 P0DMA5 UniProtKB Repeat 1460 1759 . . . Note=IV;Ontology_term=ECO:0000305;evidence=ECO:0000305 P0DMA5 UniProtKB Domain 1853 1882 . . . Note=IQ P0DMA5 UniProtKB Region 30 53 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P0DMA5 UniProtKB Region 442 484 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P0DMA5 UniProtKB Region 510 578 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P0DMA5 UniProtKB Region 1004 1034 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P0DMA5 UniProtKB Region 1071 1097 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P0DMA5 UniProtKB Region 1901 1959 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P0DMA5 UniProtKB Compositional bias 453 469 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P0DMA5 UniProtKB Compositional bias 470 484 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P0DMA5 UniProtKB Compositional bias 1907 1944 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P0DMA5 UniProtKB Modified residue 440 440 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q14524 P0DMA5 UniProtKB Modified residue 443 443 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q14524 P0DMA5 UniProtKB Modified residue 466 466 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q14524 P0DMA5 UniProtKB Modified residue 478 478 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q14524 P0DMA5 UniProtKB Modified residue 612 612 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q14524 P0DMA5 UniProtKB Modified residue 615 615 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q14524 P0DMA5 UniProtKB Modified residue 1453 1453 . . . Note=Phosphoserine%3B by PKC;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q14524 P0DMA5 UniProtKB Glycosylation 288 288 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 P0DMA5 UniProtKB Glycosylation 311 311 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 P0DMA5 UniProtKB Glycosylation 334 334 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 P0DMA5 UniProtKB Disulfide bond 276 318 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:D0E0C2 P0DMA5 UniProtKB Disulfide bond 857 866 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:D0E0C2 P0DMA5 UniProtKB Mutagenesis 215 215 . . . Note=Complete loss of inhibition by the venom of Centruroides sculpturatus. Decrease in inhibition by the venom of Centruroides sculpturatus%3B when associated with G-218. R->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:35662692;Dbxref=PMID:35662692 P0DMA5 UniProtKB Mutagenesis 218 218 . . . Note=Decrease in inhibition by the venom of Centruroides sculpturatus%3B when associated with G-215. R->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:35662692;Dbxref=PMID:35662692 P0DMA5 UniProtKB Mutagenesis 746 747 . . . Note=No effect on inhibition by the venom of Centruroides sculpturatus. IA->TS;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24159039;Dbxref=PMID:24159039 P0DMA5 UniProtKB Mutagenesis 756 759 . . . Note=No change in inhibition by the venom of Centruroides sculpturatus. RTFR->GTFG;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:35662692;Dbxref=PMID:35662692 P0DMA5 UniProtKB Mutagenesis 859 862 . . . Note=Complete loss of inhibition by the venom of Centruroides sculpturatus. QVSE->EVSQ;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:24159039,ECO:0000269|PubMed:35662692;Dbxref=PMID:24159039,PMID:35662692