##gff-version 3 Q7Z2W7 UniProtKB Chain 1 1104 . . . ID=PRO_0000215333;Note=Transient receptor potential cation channel subfamily M member 8 Q7Z2W7 UniProtKB Topological domain 1 691 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q7Z2W7 UniProtKB Transmembrane 692 712 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q7Z2W7 UniProtKB Topological domain 713 734 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q7Z2W7 UniProtKB Transmembrane 735 755 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q7Z2W7 UniProtKB Topological domain 756 759 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q7Z2W7 UniProtKB Transmembrane 760 780 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q7Z2W7 UniProtKB Topological domain 781 794 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q7Z2W7 UniProtKB Transmembrane 795 815 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q7Z2W7 UniProtKB Topological domain 816 829 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q7Z2W7 UniProtKB Transmembrane 830 850 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q7Z2W7 UniProtKB Topological domain 851 958 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q7Z2W7 UniProtKB Transmembrane 959 979 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q7Z2W7 UniProtKB Topological domain 980 1104 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q7Z2W7 UniProtKB Region 187 195 . . . Note=Epitope%3B activates specific cytotoxic T lymphocytes Q7Z2W7 UniProtKB Coiled coil 1071 1104 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 Q7Z2W7 UniProtKB Glycosylation 934 934 . . . Note=N-linked (GlcNAc...) (complex) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17065148;Dbxref=PMID:17065148 Q7Z2W7 UniProtKB Alternative sequence 1 188 . . . ID=VSP_053268;Note=In isoform 2. Missing;Ontology_term=ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:15489334,ECO:0000303|PubMed:22128173;Dbxref=PMID:15489334,PMID:22128173 Q7Z2W7 UniProtKB Alternative sequence 1 77 . . . ID=VSP_012330;Note=In isoform 3. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:22128173;Dbxref=PMID:22128173 Q7Z2W7 UniProtKB Alternative sequence 1 2 . . . ID=VSP_054505;Note=In isoform 4. MS->MQ;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:15489334;Dbxref=PMID:15489334 Q7Z2W7 UniProtKB Alternative sequence 3 314 . . . ID=VSP_054506;Note=In isoform 4. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:15489334;Dbxref=PMID:15489334 Q7Z2W7 UniProtKB Alternative sequence 234 242 . . . ID=VSP_012332;Note=In isoform 2 and isoform 3. GYFLAQYLM->VPVGQEEVC;Ontology_term=ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:15489334,ECO:0000303|PubMed:22128173;Dbxref=PMID:15489334,PMID:22128173 Q7Z2W7 UniProtKB Alternative sequence 243 1104 . . . ID=VSP_012333;Note=In isoform 2 and isoform 3. Missing;Ontology_term=ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:15489334,ECO:0000303|PubMed:22128173;Dbxref=PMID:15489334,PMID:22128173 Q7Z2W7 UniProtKB Alternative sequence 675 784 . . . ID=VSP_054507;Note=In isoform 4. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:15489334;Dbxref=PMID:15489334 Q7Z2W7 UniProtKB Natural variant 247 247 . . . ID=VAR_052383;Note=R->T;Dbxref=dbSNP:rs13004520 Q7Z2W7 UniProtKB Natural variant 251 251 . . . ID=VAR_052384;Note=Y->C;Dbxref=dbSNP:rs17868387 Q7Z2W7 UniProtKB Natural variant 419 419 . . . ID=VAR_059837;Note=S->N;Dbxref=dbSNP:rs7593557 Q7Z2W7 UniProtKB Natural variant 462 462 . . . ID=VAR_052385;Note=M->T;Dbxref=dbSNP:rs28902173 Q7Z2W7 UniProtKB Natural variant 732 732 . . . ID=VAR_052386;Note=T->I;Dbxref=dbSNP:rs17862932 Q7Z2W7 UniProtKB Natural variant 821 821 . . . ID=VAR_052387;Note=N->S;Dbxref=dbSNP:rs28902201 Q7Z2W7 UniProtKB Mutagenesis 821 821 . . . Note=No effect on glycosylation or ability to form functional channels. N->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17065148;Dbxref=PMID:17065148 Q7Z2W7 UniProtKB Mutagenesis 934 934 . . . Note=Abolishes glycosylation. N->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17065148;Dbxref=PMID:17065148 Q7Z2W7 UniProtKB Mutagenesis 946 946 . . . Note=No effect on glycosylation or channel activity. H->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17065148;Dbxref=PMID:17065148 Q7Z2W7 UniProtKB Mutagenesis 1089 1089 . . . Note=Abolishes multimerization and channel activity. Reduces cell surface expression. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17065148;Dbxref=PMID:17065148 Q7Z2W7 UniProtKB Sequence conflict 58 58 . . . Note=T->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q7Z2W7 UniProtKB Sequence conflict 693 693 . . . Note=W->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q7Z2W7 UniProtKB Sequence conflict 795 795 . . . Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305