##gff-version 3 P59158 UniProtKB Chain 1 1002 . . . ID=PRO_0000178027;Note=Solute carrier family 12 member 3 P59158 UniProtKB Topological domain 1 135 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P55017 P59158 UniProtKB Transmembrane 136 164 . . . Note=Discontinuously helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P55017 P59158 UniProtKB Topological domain 165 165 . . . Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P55017 P59158 UniProtKB Transmembrane 166 191 . . . Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P55017 P59158 UniProtKB Topological domain 192 210 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P55017 P59158 UniProtKB Transmembrane 211 247 . . . Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P55017 P59158 UniProtKB Topological domain 248 255 . . . Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P55017 P59158 UniProtKB Transmembrane 256 275 . . . Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P55017 P59158 UniProtKB Topological domain 276 276 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P55017 P59158 UniProtKB Transmembrane 277 303 . . . Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P55017 P59158 UniProtKB Topological domain 304 337 . . . Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P55017 P59158 UniProtKB Transmembrane 338 358 . . . Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P55017 P59158 UniProtKB Topological domain 359 364 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P55017 P59158 UniProtKB Transmembrane 365 394 . . . Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P55017 P59158 UniProtKB Topological domain 395 451 . . . Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P55017 P59158 UniProtKB Transmembrane 452 483 . . . Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P55017 P59158 UniProtKB Topological domain 484 503 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P55017 P59158 UniProtKB Transmembrane 504 521 . . . Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P55017 P59158 UniProtKB Topological domain 522 523 . . . Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P55017 P59158 UniProtKB Transmembrane 524 552 . . . Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P55017 P59158 UniProtKB Topological domain 553 563 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P55017 P59158 UniProtKB Transmembrane 564 582 . . . Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P55017 P59158 UniProtKB Topological domain 583 583 . . . Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P55017 P59158 UniProtKB Transmembrane 584 604 . . . Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P55017 P59158 UniProtKB Topological domain 605 1002 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P55017 P59158 UniProtKB Binding site 146 146 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P55017 P59158 UniProtKB Binding site 149 149 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P55017 P59158 UniProtKB Binding site 351 351 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P55017 P59158 UniProtKB Binding site 352 352 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P55017 P59158 UniProtKB Binding site 353 353 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P55017 P59158 UniProtKB Binding site 462 462 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P55017 P59158 UniProtKB Binding site 465 465 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P55017 P59158 UniProtKB Binding site 466 466 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P55017 P59158 UniProtKB Binding site 538 538 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P55017 P59158 UniProtKB Binding site 646 646 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P55017 P59158 UniProtKB Binding site 653 653 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P55017 P59158 UniProtKB Binding site 675 675 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P55017 P59158 UniProtKB Binding site 739 739 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P55017 P59158 UniProtKB Binding site 778 778 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P55017 P59158 UniProtKB Binding site 779 779 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P55017 P59158 UniProtKB Modified residue 41 41 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079 P59158 UniProtKB Modified residue 44 44 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P55017 P59158 UniProtKB Modified residue 47 47 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079 P59158 UniProtKB Modified residue 48 48 . . . Note=Phosphothreonine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079 P59158 UniProtKB Modified residue 53 53 . . . Note=Phosphothreonine;Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:16263722,ECO:0007744|PubMed:21183079;Dbxref=PMID:16263722,PMID:21183079 P59158 UniProtKB Modified residue 58 58 . . . Note=Phosphothreonine;Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:16263722,ECO:0007744|PubMed:21183079;Dbxref=PMID:16263722,PMID:21183079 P59158 UniProtKB Modified residue 71 71 . . . Note=Phosphoserine;Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:16263722,ECO:0007744|PubMed:21183079;Dbxref=PMID:16263722,PMID:21183079 P59158 UniProtKB Modified residue 89 89 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P55017 P59158 UniProtKB Modified residue 122 122 . . . Note=Phosphothreonine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079 P59158 UniProtKB Modified residue 124 124 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079 P59158 UniProtKB Glycosylation 404 404 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 P59158 UniProtKB Glycosylation 424 424 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 P59158 UniProtKB Disulfide bond 414 419 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P55017 P59158 UniProtKB Disulfide bond 428 434 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P55017 P59158 UniProtKB Mutagenesis 53 53 . . . Note=Reduced phosphorylation by OXSR1/OSR1 and STK39/SPAK%3B when associated with A-58 and A-71. Substantial reduction in MAPK1/3 (ERK1/2) phosphorylation in response to IL18%2C with or without IL12. T->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16263722,ECO:0000269|PubMed:26099046;Dbxref=PMID:16263722,PMID:26099046 P59158 UniProtKB Mutagenesis 58 58 . . . Note=Reduced phosphorylation by OXSR1/OSR1 and STK39/SPAK%3B when associated with A-53 and A-71. No effect on MAPK1/3 (ERK1/2) phosphorylation in response to IL18%2C with or without IL12. Substantial reduction in MAPK1/3 (ERK1/2) phosphorylation in response to IL18%2C with or without IL12%3B when associated with A-53 and A-71. T->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16263722,ECO:0000269|PubMed:26099046;Dbxref=PMID:16263722,PMID:26099046 P59158 UniProtKB Mutagenesis 71 71 . . . Note=Reduced phosphorylation by OXSR1/OSR1 and STK39/SPAK%3B when associated with A-53 and A-58. No effect on MAPK1/3 (ERK1/2) phosphorylation in response to IL18%2C with or without IL12. Substantial reduction in MAPK1/3 (ERK1/2) phosphorylation in response to IL18%2C with or without IL12%3B when associated with A-53 and A-58. S->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16263722,ECO:0000269|PubMed:26099046;Dbxref=PMID:16263722,PMID:26099046 P59158 UniProtKB Mutagenesis 156 156 . . . Note=Knockin mice display typical Gitelman syndrome features%2C characterized by hypokalemia%2C hypomagnesemia and increased fractional excretion of K(+) and Mg(2+) with a normal blood pressure level%3B when associated with S-210. R->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:36370249;Dbxref=PMID:36370249 P59158 UniProtKB Mutagenesis 210 210 . . . Note=Knockin mice display typical Gitelman syndrome features%2C characterized by hypokalemia%2C hypomagnesemia and increased fractional excretion of K(+) and Mg(2+) with a normal blood pressure level%3B when associated with Q-156. G->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:36370249;Dbxref=PMID:36370249 P59158 UniProtKB Mutagenesis 224 224 . . . Note=Does not affect protein processing and glycosylation. A->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15068971;Dbxref=PMID:15068971 P59158 UniProtKB Mutagenesis 347 347 . . . Note=Impairs protein processing and glycosylation. P->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15068971;Dbxref=PMID:15068971 P59158 UniProtKB Mutagenesis 586 586 . . . Note=Does not affect protein processing and glycosylation. Decreases localization at the plasma membrane. A->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15068971;Dbxref=PMID:15068971 P59158 UniProtKB Mutagenesis 611 611 . . . Note=Does not affect protein processing and glycosylation. Decreases localization at the plasma membrane and affinity for sodium and chloride ions. G->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15068971;Dbxref=PMID:15068971 P59158 UniProtKB Mutagenesis 628 628 . . . Note=Does not affect protein processing and glycosylation. Decreases localization at the plasma membrane. G->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15068971;Dbxref=PMID:15068971 P59158 UniProtKB Mutagenesis 831 831 . . . Note=Impairs protein processing and glycosylation. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15068971;Dbxref=PMID:15068971 P59158 UniProtKB Mutagenesis 833 833 . . . Note=Does not affect protein processing and glycosylation. R->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15068971;Dbxref=PMID:15068971 P59158 UniProtKB Mutagenesis 900 900 . . . Note=Does not affect protein processing and glycosylation. R->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15068971;Dbxref=PMID:15068971 P59158 UniProtKB Mutagenesis 936 936 . . . Note=Does not affect protein processing and glycosylation. Decreases localization at the plasma membrane. R->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15068971;Dbxref=PMID:15068971 P59158 UniProtKB Mutagenesis 949 1002 . . . Note=Impairs protein processing and glycosylation. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15068971;Dbxref=PMID:15068971 P59158 UniProtKB Mutagenesis 990 1002 . . . Note=Impairs protein processing and glycosylation. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15068971;Dbxref=PMID:15068971 P59158 UniProtKB Mutagenesis 996 996 . . . Note=Does not affect protein processing and glycosylation. Decreases localization at the plasma membrane. V->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15068971;Dbxref=PMID:15068971 P59158 UniProtKB Mutagenesis 998 998 . . . Note=Impairs protein processing and glycosylation. T->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15068971;Dbxref=PMID:15068971