##gff-version 3 Q92911 UniProtKB Chain 1 643 . . . ID=PRO_0000105383;Note=Sodium/iodide cotransporter Q92911 UniProtKB Topological domain 1 16 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q92911 UniProtKB Transmembrane 17 37 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q92911 UniProtKB Topological domain 38 53 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q92911 UniProtKB Transmembrane 54 74 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q92911 UniProtKB Topological domain 75 88 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q92911 UniProtKB Transmembrane 89 109 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q92911 UniProtKB Topological domain 110 136 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q92911 UniProtKB Transmembrane 137 157 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q92911 UniProtKB Topological domain 158 163 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q92911 UniProtKB Transmembrane 164 184 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q92911 UniProtKB Topological domain 185 186 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q92911 UniProtKB Transmembrane 187 207 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q92911 UniProtKB Topological domain 208 241 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q92911 UniProtKB Transmembrane 242 262 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q92911 UniProtKB Topological domain 263 286 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q92911 UniProtKB Transmembrane 287 307 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q92911 UniProtKB Topological domain 308 326 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q92911 UniProtKB Transmembrane 327 347 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q92911 UniProtKB Topological domain 348 391 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q92911 UniProtKB Transmembrane 392 412 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q92911 UniProtKB Topological domain 413 416 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q92911 UniProtKB Transmembrane 417 437 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q92911 UniProtKB Topological domain 438 444 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q92911 UniProtKB Transmembrane 445 465 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q92911 UniProtKB Topological domain 466 525 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q92911 UniProtKB Transmembrane 526 546 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q92911 UniProtKB Topological domain 547 643 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q92911 UniProtKB Region 623 643 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q92911 UniProtKB Site 242 242 . . . Note=Required for homodimerization;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:31310151;Dbxref=PMID:31310151 Q92911 UniProtKB Site 243 243 . . . Note=Required for homodimerization;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:31310151;Dbxref=PMID:31310151 Q92911 UniProtKB Site 471 471 . . . Note=Required for homodimerization;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:31310151;Dbxref=PMID:31310151 Q92911 UniProtKB Modified residue 556 556 . . . Note=Phosphoserine%3B by PKA;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q92911 UniProtKB Glycosylation 489 489 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q92911 UniProtKB Glycosylation 502 502 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q92911 UniProtKB Natural variant 93 93 . . . ID=VAR_010263;Note=In TDH1. G->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9745458;Dbxref=dbSNP:rs121909178,PMID:9745458 Q92911 UniProtKB Natural variant 102 102 . . . ID=VAR_010264;Note=A->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9329364;Dbxref=PMID:9329364 Q92911 UniProtKB Natural variant 267 267 . . . ID=VAR_010265;Note=In TDH1. Q->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9486973;Dbxref=dbSNP:rs121909176,PMID:9486973 Q92911 UniProtKB Natural variant 298 298 . . . ID=VAR_052490;Note=C->G;Dbxref=dbSNP:rs8108188 Q92911 UniProtKB Natural variant 354 354 . . . ID=VAR_010266;Note=In TDH1. T->P;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:9171822,ECO:0000269|PubMed:9745458;Dbxref=dbSNP:rs121909174,PMID:9171822,PMID:9745458 Q92911 UniProtKB Natural variant 395 395 . . . ID=VAR_010267;Note=In TDH1. G->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10487695;Dbxref=dbSNP:rs121909180,PMID:10487695 Q92911 UniProtKB Natural variant 536 536 . . . ID=VAR_010268;Note=Requires 2 nucleotide substitutions. T->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9329364;Dbxref=PMID:9329364 Q92911 UniProtKB Natural variant 543 543 . . . ID=VAR_010269;Note=In TDH1. G->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9745458;Dbxref=dbSNP:rs121909179,PMID:9745458 Q92911 UniProtKB Natural variant 556 556 . . . ID=VAR_010270;Note=Requires 2 nucleotide substitutions. S->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9329364;Dbxref=PMID:9329364 Q92911 UniProtKB Mutagenesis 226 226 . . . Note=Significant loss of iodide transport activity but no effect on its localization to the cell membrane. H->A%2CD%2CE%2CK;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18708479;Dbxref=PMID:18708479 Q92911 UniProtKB Mutagenesis 237 237 . . . Note=Loss of localization to the cell membrane%2C significant loss of iodide transport activity but no effect on homodimerization. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:31310151;Dbxref=PMID:31310151 Q92911 UniProtKB Mutagenesis 242 242 . . . Note=Loss of localization to the cell membrane%2C significant loss of iodide transport activity but no effect on homodimerization. Reduced homodimerization%3B when associated with A-471. Loss of iodide transport activity%3B when associated with F-535. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:31310151;Dbxref=PMID:31310151 Q92911 UniProtKB Mutagenesis 243 243 . . . Note=Loss of localization to the cell membrane%2C significant loss of iodide transport activity but no effect on homodimerization. Reduced homodimerization%3B when associated with A-471. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:31310151;Dbxref=PMID:31310151 Q92911 UniProtKB Mutagenesis 471 471 . . . Note=No effect on localization to the cell membrane%2C iodide transport activity and homodimerization. Significant loss of homodimerization%3B when associated with A-242 or A243. Q->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:31310151;Dbxref=PMID:31310151 Q92911 UniProtKB Mutagenesis 525 525 . . . Note=Loss of localization to the cell membrane%2C significant loss of iodide transport activity but no effect on homodimerization. Loss of iodide transport activity%3B when associated with A-242. A->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:31310151;Dbxref=PMID:31310151