##gff-version 3 P00395 UniProtKB Chain 1 513 . . . ID=PRO_0000183345;Note=Cytochrome c oxidase subunit 1 P00395 UniProtKB Topological domain 1 11 . . . Note=Mitochondrial matrix;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30030519;Dbxref=PMID:30030519 P00395 UniProtKB Transmembrane 12 40 . . . Note=Helical%3B Name%3DI;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00396 P00395 UniProtKB Topological domain 41 50 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30030519;Dbxref=PMID:30030519 P00395 UniProtKB Transmembrane 51 86 . . . Note=Helical%3B Name%3DII;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00396 P00395 UniProtKB Topological domain 87 94 . . . Note=Mitochondrial matrix;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30030519;Dbxref=PMID:30030519 P00395 UniProtKB Transmembrane 95 117 . . . Note=Helical%3B Name%3DIII;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00396 P00395 UniProtKB Topological domain 118 140 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30030519;Dbxref=PMID:30030519 P00395 UniProtKB Transmembrane 141 170 . . . Note=Helical%3B Name%3DIV;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00396 P00395 UniProtKB Topological domain 171 182 . . . Note=Mitochondrial matrix;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30030519;Dbxref=PMID:30030519 P00395 UniProtKB Transmembrane 183 212 . . . Note=Helical%3B Name%3DV;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00396 P00395 UniProtKB Topological domain 213 227 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30030519;Dbxref=PMID:30030519 P00395 UniProtKB Transmembrane 228 261 . . . Note=Helical%3B Name%3DVI;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00396 P00395 UniProtKB Topological domain 262 269 . . . Note=Mitochondrial matrix;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30030519;Dbxref=PMID:30030519 P00395 UniProtKB Transmembrane 270 286 . . . Note=Helical%3B Name%3DVII;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00396 P00395 UniProtKB Topological domain 287 298 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30030519;Dbxref=PMID:30030519 P00395 UniProtKB Transmembrane 299 327 . . . Note=Helical%3B Name%3DVIII;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00396 P00395 UniProtKB Topological domain 328 335 . . . Note=Mitochondrial matrix;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30030519;Dbxref=PMID:30030519 P00395 UniProtKB Transmembrane 336 357 . . . Note=Helical%3B Name%3DIX;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00396 P00395 UniProtKB Topological domain 358 370 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30030519;Dbxref=PMID:30030519 P00395 UniProtKB Transmembrane 371 400 . . . Note=Helical%3B Name%3DX;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00396 P00395 UniProtKB Topological domain 401 406 . . . Note=Mitochondrial matrix;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30030519;Dbxref=PMID:30030519 P00395 UniProtKB Transmembrane 407 433 . . . Note=Helical%3B Name%3DXI;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00396 P00395 UniProtKB Topological domain 434 446 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30030519;Dbxref=PMID:30030519 P00395 UniProtKB Transmembrane 447 478 . . . Note=Helical%3B Name%3DXII;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00396 P00395 UniProtKB Topological domain 479 513 . . . Note=Mitochondrial matrix;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30030519;Dbxref=PMID:30030519 P00395 UniProtKB Binding site 40 40 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00401 P00395 UniProtKB Binding site 45 45 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00401 P00395 UniProtKB Binding site 61 61 . . . Note=Axial binding residue;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30030519;Dbxref=PMID:30030519 P00395 UniProtKB Binding site 240 240 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30030519;Dbxref=PMID:30030519 P00395 UniProtKB Binding site 244 244 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00396 P00395 UniProtKB Binding site 290 290 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30030519;Dbxref=PMID:30030519 P00395 UniProtKB Binding site 291 291 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30030519;Dbxref=PMID:30030519 P00395 UniProtKB Binding site 368 368 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30030519;Dbxref=PMID:30030519 P00395 UniProtKB Binding site 369 369 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30030519;Dbxref=PMID:30030519 P00395 UniProtKB Binding site 376 376 . . . Note=Axial binding residue;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30030519;Dbxref=PMID:30030519 P00395 UniProtKB Binding site 378 378 . . . Note=Axial binding residue;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30030519;Dbxref=PMID:30030519 P00395 UniProtKB Cross-link 240 244 . . . Note=1'-histidyl-3'-tyrosine (His-Tyr);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00396 P00395 UniProtKB Natural variant 10 10 . . . ID=VAR_008566;Note=T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1757091;Dbxref=PMID:1757091 P00395 UniProtKB Natural variant 94 94 . . . ID=VAR_008567;Note=F->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1757091;Dbxref=PMID:1757091 P00395 UniProtKB Natural variant 125 125 . . . ID=VAR_064154;Note=In CRC%3B displays steady-state catalytic activity linked to proton pumping that is approximately 34%25 of wild-type%3B an intrinsic proton leak is find in the enzyme%2C which will lead to decreased overall energy-conversion efficiency of the respiratory chain%2C perturbing transport processes such as protein%2C ion and metabolite trafficking. G->D;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16407113,ECO:0000269|PubMed:19218458;Dbxref=dbSNP:rs281865417,PMID:16407113,PMID:19218458 P00395 UniProtKB Natural variant 142 142 . . . ID=VAR_033055;Note=In MT-C4D%3B significant decrease in enzyme activity. S->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16284789;Dbxref=dbSNP:rs267606883,PMID:16284789 P00395 UniProtKB Natural variant 155 155 . . . ID=VAR_008568;Note=V->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1757091;Dbxref=dbSNP:rs370673798,PMID:1757091 P00395 UniProtKB Natural variant 196 196 . . . ID=VAR_033056;Note=In MT-C4D. L->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12140182;Dbxref=dbSNP:rs28461189,PMID:12140182 P00395 UniProtKB Natural variant 224 224 . . . ID=VAR_008569;Note=G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1757091;Dbxref=PMID:1757091 P00395 UniProtKB Natural variant 235 235 . . . ID=VAR_011342;Note=F->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7530363;Dbxref=dbSNP:rs2853818,PMID:7530363 P00395 UniProtKB Natural variant 273 273 . . . ID=VAR_008385;Note=Found in two patients with acquired idiopathic sideroblastic anemia. M->T;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:9389715,ECO:0000269|PubMed:9851701;Dbxref=dbSNP:rs199476127,PMID:9389715,PMID:9851701 P00395 UniProtKB Natural variant 280 280 . . . ID=VAR_008386;Note=Found in two patients with acquired idiopathic sideroblastic anemia. I->T;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:9389715,ECO:0000269|PubMed:9851701;Dbxref=dbSNP:rs199476126,PMID:9389715,PMID:9851701 P00395 UniProtKB Natural variant 305 305 . . . ID=VAR_008570;Note=F->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1757091;Dbxref=dbSNP:rs368552121,PMID:1757091 P00395 UniProtKB Natural variant 415 415 . . . ID=VAR_011343;Note=T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7530363;Dbxref=dbSNP:rs372136420,PMID:7530363 P00395 UniProtKB Natural variant 458 458 . . . ID=VAR_064155;Note=In CRC%3B the mutant is probably not expressed%2C indicating that the amino acid substitution results in a severely altered overall structure of the enzyme. S->P;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16407113,ECO:0000269|PubMed:19218458;Dbxref=dbSNP:rs267606884,PMID:16407113,PMID:19218458 P00395 UniProtKB Natural variant 513 513 . . . ID=VAR_008387;Note=In LHON%3B secondary mutation%3B does not seem to directly cause the disease. S->SKQK;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1322638;Dbxref=PMID:1322638