##gff-version 3 Q9BX84 UniProtKB Chain 1 2022 . . . ID=PRO_0000215329;Note=Transient receptor potential cation channel subfamily M member 6 Q9BX84 UniProtKB Topological domain 1 741 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q9BX84 UniProtKB Transmembrane 742 762 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q9BX84 UniProtKB Topological domain 763 841 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q9BX84 UniProtKB Transmembrane 842 862 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q9BX84 UniProtKB Topological domain 863 905 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q9BX84 UniProtKB Transmembrane 906 926 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q9BX84 UniProtKB Topological domain 927 939 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q9BX84 UniProtKB Transmembrane 940 960 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q9BX84 UniProtKB Topological domain 961 972 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q9BX84 UniProtKB Transmembrane 973 993 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q9BX84 UniProtKB Topological domain 994 1012 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q9BX84 UniProtKB Intramembrane 1013 1033 . . . Note=Pore-forming;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q9BX84 UniProtKB Topological domain 1034 1047 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q9BX84 UniProtKB Transmembrane 1048 1068 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q9BX84 UniProtKB Topological domain 1069 2022 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q9BX84 UniProtKB Domain 1750 1980 . . . Note=Alpha-type protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00501 Q9BX84 UniProtKB Region 1479 1516 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9BX84 UniProtKB Region 1997 2022 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9BX84 UniProtKB Compositional bias 1491 1516 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9BX84 UniProtKB Compositional bias 2002 2022 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9BX84 UniProtKB Active site 1923 1923 . . . Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q9BX84 UniProtKB Binding site 1780 1780 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 Q9BX84 UniProtKB Binding site 1804 1804 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 Q9BX84 UniProtKB Binding site 1876 1876 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 Q9BX84 UniProtKB Binding site 1909 1909 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 Q9BX84 UniProtKB Binding site 1925 1925 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 Q9BX84 UniProtKB Binding site 1933 1933 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 Q9BX84 UniProtKB Binding site 1950 1956 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 Q9BX84 UniProtKB Binding site 1966 1966 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 Q9BX84 UniProtKB Binding site 1968 1968 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 Q9BX84 UniProtKB Binding site 1972 1972 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 Q9BX84 UniProtKB Modified residue 1851 1851 . . . Note=Phosphothreonine%3B by autocatalysis;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18258429;Dbxref=PMID:18258429 Q9BX84 UniProtKB Alternative sequence 1 11 . . . ID=VSP_012069;Note=In isoform TRPM6b. MKEQPVLERLQ->MIILSK;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:14976260;Dbxref=PMID:14976260 Q9BX84 UniProtKB Alternative sequence 1 11 . . . ID=VSP_012070;Note=In isoform TRPM6c. MKEQPVLERLQ->MTAPVT;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:14976260;Dbxref=PMID:14976260 Q9BX84 UniProtKB Alternative sequence 281 281 . . . ID=VSP_012071;Note=In isoform M6-kinase 3. R->P;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:14976260;Dbxref=PMID:14976260 Q9BX84 UniProtKB Alternative sequence 282 1734 . . . ID=VSP_012072;Note=In isoform M6-kinase 3. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:14976260;Dbxref=PMID:14976260 Q9BX84 UniProtKB Alternative sequence 500 1666 . . . ID=VSP_012073;Note=In isoform M6-kinase 2. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:14976260;Dbxref=PMID:14976260 Q9BX84 UniProtKB Alternative sequence 547 1595 . . . ID=VSP_012074;Note=In isoform M6-kinase 1. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:14976260;Dbxref=PMID:14976260 Q9BX84 UniProtKB Alternative sequence 1926 1943 . . . ID=VSP_012075;Note=In isoform TRPM6t. GVGENLTDPSVIKPEVKQ->ALWFWDSMLKARLGGWRM;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:14976260;Dbxref=PMID:14976260 Q9BX84 UniProtKB Alternative sequence 1944 2022 . . . ID=VSP_012076;Note=In isoform TRPM6t. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:14976260;Dbxref=PMID:14976260 Q9BX84 UniProtKB Natural variant 75 75 . . . ID=VAR_042387;Note=In a lung adenocarcinoma sample%3B somatic mutation. G->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17344846;Dbxref=dbSNP:rs1193127627,PMID:17344846 Q9BX84 UniProtKB Natural variant 141 141 . . . ID=VAR_019963;Note=In HOMG1%3B impairs heterodimer formation resulting in intracellular retention. S->L;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12032568,ECO:0000269|PubMed:14976260;Dbxref=dbSNP:rs121912625,PMID:12032568,PMID:14976260 Q9BX84 UniProtKB Natural variant 338 338 . . . ID=VAR_042388;Note=M->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17344846;Dbxref=dbSNP:rs56155062,PMID:17344846 Q9BX84 UniProtKB Natural variant 708 708 . . . ID=VAR_071480;Note=In HOMG1%3B loss of function%3B no effect on cell membrane localization. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23942199;Dbxref=PMID:23942199 Q9BX84 UniProtKB Natural variant 872 872 . . . ID=VAR_071481;Note=In HOMG1%3B loss of function%3B no effect on cell membrane localization. E->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23942199;Dbxref=PMID:23942199 Q9BX84 UniProtKB Natural variant 948 948 . . . ID=VAR_052380;Note=F->L;Dbxref=dbSNP:rs13290391 Q9BX84 UniProtKB Natural variant 1007 1007 . . . ID=VAR_042389;Note=In a lung large cell carcinoma sample%3B somatic mutation. W->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17344846;Dbxref=PMID:17344846 Q9BX84 UniProtKB Natural variant 1053 1053 . . . ID=VAR_071482;Note=In HOMG1%3B loss of function%3B no effect on cell membrane localization. Y->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23942199;Dbxref=PMID:23942199 Q9BX84 UniProtKB Natural variant 1071 1071 . . . ID=VAR_019964;Note=N->D;Dbxref=dbSNP:rs2274922 Q9BX84 UniProtKB Natural variant 1143 1143 . . . ID=VAR_071483;Note=In HOMG1%3B loss of function%3B no effect on cell membrane localization. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23942199;Dbxref=PMID:23942199 Q9BX84 UniProtKB Natural variant 1243 1243 . . . ID=VAR_042390;Note=H->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17344846;Dbxref=dbSNP:rs55694430,PMID:17344846 Q9BX84 UniProtKB Natural variant 1274 1274 . . . ID=VAR_042391;Note=Q->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17344846;Dbxref=dbSNP:rs34608911,PMID:17344846 Q9BX84 UniProtKB Natural variant 1393 1393 . . . ID=VAR_019965;Note=V->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17344846;Dbxref=dbSNP:rs3750425,PMID:17344846 Q9BX84 UniProtKB Natural variant 1584 1584 . . . ID=VAR_019966;Note=K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17344846;Dbxref=dbSNP:rs2274924,PMID:17344846 Q9BX84 UniProtKB Natural variant 1663 1663 . . . ID=VAR_042392;Note=No effect on function or cell membrane localization. Q->R;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17344846,ECO:0000269|PubMed:23942199;Dbxref=dbSNP:rs55679040,PMID:17344846,PMID:23942199 Q9BX84 UniProtKB Natural variant 1673 1673 . . . ID=VAR_042393;Note=L->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17344846;Dbxref=dbSNP:rs56254742,PMID:17344846 Q9BX84 UniProtKB Natural variant 1724 1724 . . . ID=VAR_042394;Note=T->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17344846;Dbxref=dbSNP:rs56290308,PMID:17344846 Q9BX84 UniProtKB Natural variant 1754 1754 . . . ID=VAR_071484;Note=In HOMG1%3B loss of function%3B no effect on cell membrane localization. S->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23942199;Dbxref=PMID:23942199 Q9BX84 UniProtKB Mutagenesis 1804 1804 . . . Note=Abolishes kinase activity but does not affect expression levels or binding to RACK1. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18258429;Dbxref=PMID:18258429 Q9BX84 UniProtKB Mutagenesis 1851 1851 . . . Note=Significantly decreases autophosphorylation. Does not alter binding to RACK1 but prevents inhibition by RACK1. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18258429;Dbxref=PMID:18258429 Q9BX84 UniProtKB Mutagenesis 1851 1851 . . . Note=Significantly decreases autophosphorylation. Does not alter binding to RACK1 or inhibition by RACK1. T->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18258429;Dbxref=PMID:18258429