##gff-version 3 P51793 UniProtKB Chain 1 760 . . . ID=PRO_0000094443;Note=H(+)/Cl(-) exchange transporter 4 P51793 UniProtKB Topological domain 1 67 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P35523 P51793 UniProtKB Transmembrane 68 105 . . . Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P35523 P51793 UniProtKB Transmembrane 151 174 . . . Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P35523 P51793 UniProtKB Intramembrane 183 190 . . . Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P35523 P51793 UniProtKB Transmembrane 200 218 . . . Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P35523 P51793 UniProtKB Transmembrane 224 243 . . . Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P35523 P51793 UniProtKB Intramembrane 255 267 . . . Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P35523 P51793 UniProtKB Intramembrane 271 279 . . . Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P35523 P51793 UniProtKB Transmembrane 291 309 . . . Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P35523 P51793 UniProtKB Transmembrane 333 358 . . . Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P35523 P51793 UniProtKB Transmembrane 365 385 . . . Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P35523 P51793 UniProtKB Transmembrane 442 462 . . . Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P35523 P51793 UniProtKB Transmembrane 467 486 . . . Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P35523 P51793 UniProtKB Intramembrane 514 528 . . . Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P35523 P51793 UniProtKB Intramembrane 532 543 . . . Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P35523 P51793 UniProtKB Intramembrane 544 547 . . . Note=Note%3DLoop between two helices;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P35523 P51793 UniProtKB Transmembrane 548 566 . . . Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P35523 P51793 UniProtKB Topological domain 567 760 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P35523 P51793 UniProtKB Domain 600 666 . . . Note=CBS 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00703 P51793 UniProtKB Domain 697 755 . . . Note=CBS 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00703 P51793 UniProtKB Region 14 63 . . . Note=Required for localization in the endoplasmic reticulum;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17023393;Dbxref=PMID:17023393 P51793 UniProtKB Region 667 696 . . . Note=Required for localization in the endoplasmic reticulum;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28972156;Dbxref=PMID:28972156 P51793 UniProtKB Motif 180 184 . . . Note=Selectivity filter part_1;Ontology_term=ECO:0000250;evidence=ECO:0000250 P51793 UniProtKB Motif 222 226 . . . Note=Selectivity filter part_2;Ontology_term=ECO:0000250;evidence=ECO:0000250 P51793 UniProtKB Motif 467 471 . . . Note=Selectivity filter part_3;Ontology_term=ECO:0000250;evidence=ECO:0000250 P51793 UniProtKB Binding site 181 181 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 P51793 UniProtKB Binding site 469 469 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 P51793 UniProtKB Binding site 572 572 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 P51793 UniProtKB Binding site 610 610 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 P51793 UniProtKB Binding site 631 633 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P51795 P51793 UniProtKB Binding site 738 741 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P51795 P51793 UniProtKB Site 224 224 . . . Note=Mediates proton transfer from the outer aqueous phase to the interior of the protein%3B involved in linking H(+) and Cl(-) transport P51793 UniProtKB Site 281 281 . . . Note=Mediates proton transfer from the protein to the inner aqueous phase P51793 UniProtKB Alternative sequence 1 94 . . . ID=VSP_054658;Note=In isoform 2. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:14702039;Dbxref=PMID:14702039 P51793 UniProtKB Natural variant 15 15 . . . ID=VAR_083577;Note=In MRXSRC%3B uncertain significance%3B no reduction in outwardly-rectifying currents%3B does not affect its localization in endoplasmic reticulum membrane. D->N;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:26034137,ECO:0000269|PubMed:27550844;Dbxref=dbSNP:rs879255591,PMID:26034137,PMID:27550844 P51793 UniProtKB Natural variant 78 78 . . . ID=VAR_077819;Note=In MRXSRC%3B marked reduction in outwardly-rectifying currents. G->S;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:25644381,ECO:0000269|PubMed:27550844;Dbxref=dbSNP:rs1569226551,PMID:25644381,PMID:27550844 P51793 UniProtKB Natural variant 212 212 . . . ID=VAR_083578;Note=In MRXSRC%3B marked reduction in outwardly-rectifying currents%3B does not affect its localization in endoplasmic reticulum membrane. V->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27550844;Dbxref=dbSNP:rs879255580,PMID:27550844 P51793 UniProtKB Natural variant 221 221 . . . ID=VAR_083579;Note=In MRXSRC%3B marked reduction in outwardly-rectifying currents%3B does not affect its localization in endoplasmic reticulum membrane. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27550844;Dbxref=dbSNP:rs879255581,PMID:27550844 P51793 UniProtKB Natural variant 221 221 . . . ID=VAR_077820;Note=In MRXSRC%3B marked reduction in outwardly-rectifying currents. L->V;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:25644381,ECO:0000269|PubMed:27550844;Dbxref=dbSNP:rs1569230006,PMID:25644381,PMID:27550844 P51793 UniProtKB Natural variant 275 275 . . . ID=VAR_083580;Note=In MRXSRC%3B marked reduction in outwardly-rectifying currents%3B does not affect its localization in endoplasmic reticulum. V->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27550844;Dbxref=dbSNP:rs879255585,PMID:27550844 P51793 UniProtKB Natural variant 534 534 . . . ID=VAR_083581;Note=In MRXSRC%3B marked reduction in outwardly-rectifying currents%3B does not affect its localization in endoplasmic reticulum membrane. S->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27550844;Dbxref=dbSNP:rs879255582,PMID:27550844 P51793 UniProtKB Natural variant 536 536 . . . ID=VAR_077821;Note=In MRXSRC%3B marked reduction in outwardly-rectifying currents. V->M;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:25644381,ECO:0000269|PubMed:27550844;Dbxref=dbSNP:rs1569231897,PMID:25644381,PMID:27550844 P51793 UniProtKB Natural variant 544 544 . . . ID=VAR_077822;Note=In MRXSRC%3B has normal localization to structures resembling endoplasmic reticulum membranes%3B almost abolishes the outwardly-rectifying currents. G->R;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:23647072,ECO:0000269|PubMed:27550844;Dbxref=dbSNP:rs587777161,PMID:23647072,PMID:27550844 P51793 UniProtKB Natural variant 555 555 . . . ID=VAR_083582;Note=In MRXSRC%3B marked reduction in outwardly-rectifying currents%3B does not affect its localization in endoplasmic reticulum membrane. A->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27550844;Dbxref=dbSNP:rs879255583,PMID:27550844 P51793 UniProtKB Natural variant 718 718 . . . ID=VAR_083583;Note=In MRXSRC%3B marked reduction in outwardly-rectifying currents%3B does not affect its localization in endoplasmic reticulum membrane. R->W;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27550844;Dbxref=dbSNP:rs879255584,PMID:27550844 P51793 UniProtKB Natural variant 731 731 . . . ID=VAR_077823;Note=In MRXSRC%3B marked reduction in outwardly-rectifying currents. G->R;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:25644381,ECO:0000269|PubMed:27550844;Dbxref=dbSNP:rs1569233549,PMID:25644381,PMID:27550844 P51793 UniProtKB Mutagenesis 224 224 . . . Note=Restores chloride translocation%2C but not proton transport%3B when associated with A-281. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18063579;Dbxref=PMID:18063579 P51793 UniProtKB Mutagenesis 281 281 . . . Note=Abolishes translocation of protons and chloride ions. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18063579;Dbxref=PMID:18063579 P51793 UniProtKB Sequence conflict 178 178 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 P51793 UniProtKB Sequence conflict 498 499 . . . Note=II->YY;Ontology_term=ECO:0000305;evidence=ECO:0000305 P51793 UniProtKB Sequence conflict 659 659 . . . Note=K->N;Ontology_term=ECO:0000305;evidence=ECO:0000305