##gff-version 3 Q13698 UniProtKB Chain 1 1873 . . . ID=PRO_0000053943;Note=Voltage-dependent L-type calcium channel subunit alpha-1S Q13698 UniProtKB Topological domain 1 51 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q13698 UniProtKB Transmembrane 52 70 . . . Note=Helical%3B Name%3DS1 of repeat I;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07293 Q13698 UniProtKB Topological domain 71 85 . . . Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q13698 UniProtKB Transmembrane 86 106 . . . Note=Helical%3B Name%3DS2 of repeat I;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07293 Q13698 UniProtKB Topological domain 107 115 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q13698 UniProtKB Transmembrane 116 136 . . . Note=Helical%3B Name%3DS3 of repeat I;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07293 Q13698 UniProtKB Topological domain 137 160 . . . Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q13698 UniProtKB Transmembrane 161 179 . . . Note=Helical%3B Name%3DS4 of repeat I;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07293 Q13698 UniProtKB Topological domain 180 196 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q13698 UniProtKB Transmembrane 197 218 . . . Note=Helical%3B Name%3DS5 of repeat I;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07293 Q13698 UniProtKB Topological domain 219 279 . . . Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q13698 UniProtKB Intramembrane 280 301 . . . Note=Pore-forming;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07293 Q13698 UniProtKB Topological domain 302 309 . . . Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q13698 UniProtKB Transmembrane 310 330 . . . Note=Helical%3B Name%3DS6 of repeat I;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07293 Q13698 UniProtKB Topological domain 331 432 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q13698 UniProtKB Transmembrane 433 451 . . . Note=Helical%3B Name%3DS1 of repeat II;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07293 Q13698 UniProtKB Topological domain 452 462 . . . Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q13698 UniProtKB Transmembrane 463 483 . . . Note=Helical%3B Name%3DS2 of repeat II;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07293 Q13698 UniProtKB Topological domain 484 494 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q13698 UniProtKB Transmembrane 495 514 . . . Note=Helical%3B Name%3DS3 of repeat II;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07293 Q13698 UniProtKB Topological domain 515 523 . . . Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q13698 UniProtKB Transmembrane 524 542 . . . Note=Helical%3B Name%3DS4 of repeat II;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07293 Q13698 UniProtKB Topological domain 543 561 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q13698 UniProtKB Transmembrane 562 581 . . . Note=Helical%3B Name%3DS5 of repeat II;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07293 Q13698 UniProtKB Topological domain 582 601 . . . Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q13698 UniProtKB Intramembrane 602 623 . . . Note=Pore-forming;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07293 Q13698 UniProtKB Topological domain 624 633 . . . Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q13698 UniProtKB Transmembrane 634 653 . . . Note=Helical%3B Name%3DS6 of repeat II;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07293 Q13698 UniProtKB Topological domain 654 799 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q13698 UniProtKB Transmembrane 800 818 . . . Note=Helical%3B Name%3DS1 of repeat III;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07293 Q13698 UniProtKB Topological domain 819 830 . . . Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q13698 UniProtKB Transmembrane 831 850 . . . Note=Helical%3B Name%3DS2 of repeat III;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07293 Q13698 UniProtKB Topological domain 851 866 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q13698 UniProtKB Transmembrane 867 885 . . . Note=Helical%3B Name%3DS3 of repeat III;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07293 Q13698 UniProtKB Topological domain 886 892 . . . Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q13698 UniProtKB Transmembrane 893 911 . . . Note=Helical%3B Name%3DS4 of repeat III;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07293 Q13698 UniProtKB Topological domain 912 930 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q13698 UniProtKB Transmembrane 931 950 . . . Note=Helical%3B Name%3DS5 of repeat III;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07293 Q13698 UniProtKB Topological domain 951 1000 . . . Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q13698 UniProtKB Intramembrane 1001 1021 . . . Note=Pore-forming;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07293 Q13698 UniProtKB Topological domain 1022 1038 . . . Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q13698 UniProtKB Transmembrane 1039 1060 . . . Note=Helical%3B Name%3DS6 of repeat III;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07293 Q13698 UniProtKB Topological domain 1061 1118 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q13698 UniProtKB Transmembrane 1119 1140 . . . Note=Helical%3B Name%3DS1 of repeat IV;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07293 Q13698 UniProtKB Topological domain 1141 1148 . . . Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q13698 UniProtKB Transmembrane 1149 1170 . . . Note=Helical%3B Name%3DS2 of repeat IV;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07293 Q13698 UniProtKB Topological domain 1171 1180 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q13698 UniProtKB Transmembrane 1181 1200 . . . Note=Helical%3B Name%3DS3 of repeat IV;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07293 Q13698 UniProtKB Topological domain 1201 1231 . . . Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q13698 UniProtKB Transmembrane 1232 1250 . . . Note=Helical%3B Name%3DS4 of repeat IV;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07293 Q13698 UniProtKB Topological domain 1251 1268 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q13698 UniProtKB Transmembrane 1269 1289 . . . Note=Helical%3B Name%3DS5 of repeat IV;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07293 Q13698 UniProtKB Topological domain 1290 1311 . . . Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q13698 UniProtKB Intramembrane 1312 1330 . . . Note=Pore-forming;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07293 Q13698 UniProtKB Topological domain 1331 1356 . . . Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q13698 UniProtKB Transmembrane 1357 1381 . . . Note=Helical%3B Name%3DS6 of repeat IV;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07293 Q13698 UniProtKB Topological domain 1382 1873 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q13698 UniProtKB Repeat 38 337 . . . Note=I;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q13698 UniProtKB Repeat 418 664 . . . Note=II;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q13698 UniProtKB Repeat 786 1068 . . . Note=III;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q13698 UniProtKB Repeat 1105 1384 . . . Note=IV;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q13698 UniProtKB Region 1 23 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q13698 UniProtKB Region 357 374 . . . Note=Binding to the beta subunit;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q02789 Q13698 UniProtKB Region 675 717 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q13698 UniProtKB Region 731 757 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q13698 UniProtKB Region 747 760 . . . Note=Interaction with STAC%2C STAC2 and STAC3 (via SH3 domains);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29078335;Dbxref=PMID:29078335 Q13698 UniProtKB Region 988 1077 . . . Note=Dihydropyridine binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07293 Q13698 UniProtKB Region 1337 1403 . . . Note=Dihydropyridine binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07293 Q13698 UniProtKB Region 1349 1391 . . . Note=Phenylalkylamine binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07293 Q13698 UniProtKB Region 1522 1542 . . . Note=Interaction with calmodulin;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19473981;Dbxref=PMID:19473981 Q13698 UniProtKB Region 1731 1780 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q13698 UniProtKB Motif 290 293 . . . Note=Selectivity filter of repeat I;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07293 Q13698 UniProtKB Motif 612 615 . . . Note=Selectivity filter of repeat II;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07293 Q13698 UniProtKB Motif 1012 1015 . . . Note=Selectivity filter of repeat III;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07293 Q13698 UniProtKB Motif 1321 1324 . . . Note=Selectivity filter of repeat IV;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07293 Q13698 UniProtKB Compositional bias 1 20 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q13698 UniProtKB Compositional bias 675 710 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q13698 UniProtKB Compositional bias 1748 1772 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q13698 UniProtKB Binding site 292 292 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07293 Q13698 UniProtKB Binding site 614 614 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07293 Q13698 UniProtKB Binding site 1014 1014 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07293 Q13698 UniProtKB Modified residue 393 393 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q02789 Q13698 UniProtKB Modified residue 397 397 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q02789 Q13698 UniProtKB Modified residue 687 687 . . . Note=Phosphoserine%3B by PKA;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07293 Q13698 UniProtKB Modified residue 1575 1575 . . . Note=Phosphoserine%3B by PKA and CAMK2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07293 Q13698 UniProtKB Modified residue 1617 1617 . . . Note=Phosphoserine%3B by PKA;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07293 Q13698 UniProtKB Glycosylation 79 79 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q13698 UniProtKB Glycosylation 257 257 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q13698 UniProtKB Glycosylation 1141 1141 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q13698 UniProtKB Disulfide bond 226 254 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07293 Q13698 UniProtKB Disulfide bond 245 261 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07293 Q13698 UniProtKB Disulfide bond 957 968 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07293 Q13698 UniProtKB Disulfide bond 1338 1352 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07293 Q13698 UniProtKB Natural variant 69 69 . . . ID=VAR_046970;Note=A->G;Dbxref=dbSNP:rs12406479 Q13698 UniProtKB Natural variant 100 100 . . . ID=VAR_088226;Note=In CMYP18%3B uncertain significance. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28012042;Dbxref=PMID:28012042 Q13698 UniProtKB Natural variant 222 222 . . . ID=VAR_088227;Note=In CMYP18%3B uncertain significance. M->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:33060286;Dbxref=PMID:33060286 Q13698 UniProtKB Natural variant 275 275 . . . ID=VAR_088228;Note=In CMYP18. F->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28012042;Dbxref=PMID:28012042 Q13698 UniProtKB Natural variant 458 458 . . . ID=VAR_001498;Note=L->H;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:7713519,ECO:0000269|PubMed:9199552;Dbxref=dbSNP:rs12742169,PMID:7713519,PMID:9199552 Q13698 UniProtKB Natural variant 528 528 . . . ID=VAR_054953;Note=In HOKPP1. R->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19118277;Dbxref=dbSNP:rs80338778,PMID:19118277 Q13698 UniProtKB Natural variant 528 528 . . . ID=VAR_001499;Note=In HOKPP1. R->H;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18162704,ECO:0000269|PubMed:19118277,ECO:0000269|PubMed:7987325;Dbxref=dbSNP:rs80338777,PMID:18162704,PMID:19118277,PMID:7987325 Q13698 UniProtKB Natural variant 742 742 . . . ID=VAR_088229;Note=In CMYP18%3B decreased protein abundance. P->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28012042;Dbxref=PMID:28012042 Q13698 UniProtKB Natural variant 742 742 . . . ID=VAR_088230;Note=In CMYP18%3B decreased protein abundance. P->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28012042;Dbxref=PMID:28012042 Q13698 UniProtKB Natural variant 789 789 . . . ID=VAR_088231;Note=In CMYP18%3B uncertain significance. R->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:33060286;Dbxref=PMID:33060286 Q13698 UniProtKB Natural variant 789 789 . . . ID=VAR_088232;Note=In CMYP18%3B uncertain significance. R->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:31227654;Dbxref=dbSNP:rs1157720606,PMID:31227654 Q13698 UniProtKB Natural variant 900 900 . . . ID=VAR_054954;Note=In HOKPP1. R->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19118277;Dbxref=PMID:19118277 Q13698 UniProtKB Natural variant 1086 1086 . . . ID=VAR_001500;Note=In MHS5. R->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9199552;Dbxref=dbSNP:rs1800559,PMID:9199552 Q13698 UniProtKB Natural variant 1239 1239 . . . ID=VAR_001501;Note=In HOKPP1. R->G;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18162704,ECO:0000269|PubMed:19118277,ECO:0000269|PubMed:8004673;Dbxref=dbSNP:rs28930069,PMID:18162704,PMID:19118277,PMID:8004673 Q13698 UniProtKB Natural variant 1239 1239 . . . ID=VAR_001502;Note=In HOKPP1. R->H;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17418573,ECO:0000269|PubMed:18162704,ECO:0000269|PubMed:19118277,ECO:0000269|PubMed:8004673;Dbxref=dbSNP:rs28930068,PMID:17418573,PMID:18162704,PMID:19118277,PMID:8004673 Q13698 UniProtKB Natural variant 1367 1367 . . . ID=VAR_088233;Note=In CMYP18%3B uncertain significance%3B patient myotubes show decreased depolarization-induced release of sequestered calcium ion into cytosol compared to control. L->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28012042;Dbxref=PMID:28012042 Q13698 UniProtKB Natural variant 1485 1873 . . . ID=VAR_088234;Note=In CMYP18. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28012042;Dbxref=PMID:28012042 Q13698 UniProtKB Natural variant 1539 1539 . . . ID=VAR_001503;Note=R->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9199552;Dbxref=dbSNP:rs3850625,PMID:9199552 Q13698 UniProtKB Natural variant 1658 1658 . . . ID=VAR_046971;Note=R->H;Dbxref=dbSNP:rs13374149 Q13698 UniProtKB Natural variant 1800 1800 . . . ID=VAR_046972;Note=L->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15489334;Dbxref=dbSNP:rs12139527,PMID:15489334 Q13698 UniProtKB Natural variant 1840 1840 . . . ID=VAR_046973;Note=E->D;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:7713519,ECO:0000269|PubMed:8838325;Dbxref=dbSNP:rs1042379,PMID:7713519,PMID:8838325 Q13698 UniProtKB Sequence conflict 26 26 . . . Note=R->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q13698 UniProtKB Sequence conflict 265 265 . . . Note=W->C;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q13698 UniProtKB Sequence conflict 574 574 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q13698 UniProtKB Sequence conflict 627 628 . . . Note=YG->SS;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q13698 UniProtKB Sequence conflict 628 628 . . . Note=G->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q13698 UniProtKB Sequence conflict 916 919 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q13698 UniProtKB Sequence conflict 918 919 . . . Note=VQ->AR;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q13698 UniProtKB Sequence conflict 1180 1180 . . . Note=D->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q13698 UniProtKB Sequence conflict 1294 1295 . . . Note=LV->FE;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q13698 UniProtKB Sequence conflict 1318 1318 . . . Note=R->RHA;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q13698 UniProtKB Sequence conflict 1472 1472 . . . Note=R->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q13698 UniProtKB Sequence conflict 1510 1510 . . . Note=I->M;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q13698 UniProtKB Sequence conflict 1532 1532 . . . Note=H->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q13698 UniProtKB Sequence conflict 1671 1671 . . . Note=G->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q13698 UniProtKB Sequence conflict 1710 1710 . . . Note=V->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q13698 UniProtKB Sequence conflict 1815 1815 . . . Note=A->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q13698 UniProtKB Helix 1523 1536 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2VAY Q13698 UniProtKB Helix 1538 1541 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2VAY