COX3_HUMAN
ID COX3_HUMAN Reviewed; 261 AA.
AC P00414; Q14Y83;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 201.
DE RecName: Full=Cytochrome c oxidase subunit 3;
DE EC=7.1.1.9;
DE AltName: Full=Cytochrome c oxidase polypeptide III;
GN Name=MT-CO3; Synonyms=COIII, COXIII, MTCO3;
OS Homo sapiens (Human).
OG Mitochondrion.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=7219534; DOI=10.1038/290457a0;
RA Anderson S., Bankier A.T., Barrell B.G., de Bruijn M.H.L., Coulson A.R.,
RA Drouin J., Eperon I.C., Nierlich D.P., Roe B.A., Sanger F., Schreier P.H.,
RA Smith A.J.H., Staden R., Young I.G.;
RT "Sequence and organization of the human mitochondrial genome.";
RL Nature 290:457-465(1981).
RN [2]
RP SEQUENCE REVISION TO 118.
RA Kogelnik A., Brown M.;
RL Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-31.
RX PubMed=16776823; DOI=10.1186/1471-2164-7-151;
RA Thangaraj K., Chaubey G., Singh V.K., Vanniarajan A., Thanseem I.,
RA Reddy A.G., Singh L.;
RT "In situ origin of deep rooting lineages of mitochondrial Macrohaplogroup
RT 'M' in India.";
RL BMC Genomics 7:151-151(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 167-261.
RC TISSUE=Endometrial adenocarcinoma;
RA Swanson K.V., Griffiss J.;
RL Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [6]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.90 ANGSTROMS), AND SUBUNIT.
RX PubMed=28844695; DOI=10.1016/j.cell.2017.07.050;
RA Guo R., Zong S., Wu M., Gu J., Yang M.;
RT "Architecture of human mitochondrial respiratory megacomplex I2III2IV2.";
RL Cell 170:1247-1257(2017).
RN [7]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.60 ANGSTROMS) OF 2-261.
RX PubMed=30030519; DOI=10.1038/s41422-018-0071-1;
RA Zong S., Wu M., Gu J., Liu T., Guo R., Yang M.;
RT "Structure of the intact 14-subunit human cytochrome c oxidase.";
RL Cell Res. 28:1026-1034(2018).
RN [8]
RP VARIANT LEU-251.
RX PubMed=18587274; DOI=10.3858/emm.2008.40.3.354;
RA Choi B.O., Hwang J.H., Kim J., Cho E.M., Cho S.Y., Hwang S.J., Lee H.W.,
RA Kim S.J., Chung K.W.;
RT "A MELAS syndrome family harboring two mutations in mitochondrial genome.";
RL Exp. Mol. Med. 40:354-360(2008).
RN [9]
RP VARIANTS ILE-91; ARG-177 AND ILE-254.
RX PubMed=1757091; DOI=10.1007/bf00206061;
RA Marzuki S., Noer A.S., Lertrit P., Thyagarajan D., Kapsa R.,
RA Utthanaphol P., Byrne E.;
RT "Normal variants of human mitochondrial DNA and translation products: the
RT building of a reference data base.";
RL Hum. Genet. 88:139-145(1991).
RN [10]
RP VARIANTS LHON SER-78 AND THR-200.
RX PubMed=8240356; DOI=10.1006/bbrc.1993.2321;
RA Johns D.R., Neufeld M.J.;
RT "Cytochrome c oxidase mutations in Leber hereditary optic neuropathy.";
RL Biochem. Biophys. Res. Commun. 196:810-815(1993).
RN [11]
RP VARIANT LEU-251.
RX PubMed=7496173; DOI=10.1016/0960-8966(94)00079-o;
RA Manfredi G., Schon E.A., Moraes C.T., Bonilla E., Berry G.T., Sladky J.T.,
RA Dimauro S.;
RT "A new mutation associated with MELAS is located in a mitochondrial DNA
RT polypeptide-coding gene.";
RL Neuromuscul. Disord. 5:391-398(1995).
RN [12]
RP VARIANT MT-C4D 94-PHE--PHE-98 DEL, AND INVOLVEMENT IN RM-MT.
RX PubMed=8630495; DOI=10.1038/ng0496-410;
RA Keightley J.A., Hoffbuhr K.C., Burton M.D., Salas V.M., Johnston W.S.W.,
RA Penn A.M.W., Buist N.R.M., Kennaway N.G.;
RT "A microdeletion in cytochrome c oxidase (COX) subunit III associated with
RT COX deficiency and recurrent myoglobinuria.";
RL Nat. Genet. 12:410-416(1996).
RN [13]
RP VARIANTS ARG-3 AND SER-35.
RX PubMed=9461455; DOI=10.1093/nar/26.4.967;
RA Rieder M.J., Taylor S.L., Tobe V.O., Nickerson D.A.;
RT "Automating the identification of DNA variations using quality-based
RT fluorescence re-sequencing: analysis of the human mitochondrial genome.";
RL Nucleic Acids Res. 26:967-973(1998).
CC -!- FUNCTION: Component of the cytochrome c oxidase, the last enzyme in the
CC mitochondrial electron transport chain which drives oxidative
CC phosphorylation. The respiratory chain contains 3 multisubunit
CC complexes succinate dehydrogenase (complex II, CII), ubiquinol-
CC cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III,
CC CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to
CC transfer electrons derived from NADH and succinate to molecular oxygen,
CC creating an electrochemical gradient over the inner membrane that
CC drives transmembrane transport and the ATP synthase. Cytochrome c
CC oxidase is the component of the respiratory chain that catalyzes the
CC reduction of oxygen to water. Electrons originating from reduced
CC cytochrome c in the intermembrane space (IMS) are transferred via the
CC dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1
CC to the active site in subunit 1, a binuclear center (BNC) formed by
CC heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2
CC water molecules using 4 electrons from cytochrome c in the IMS and 4
CC protons from the mitochondrial matrix. {ECO:0000250|UniProtKB:P00420}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-
CC [cytochrome c] + 4 H(+)(out) + 2 H2O; Xref=Rhea:RHEA:11436,
CC Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033,
CC ChEBI:CHEBI:29034; EC=7.1.1.9;
CC Evidence={ECO:0000250|UniProtKB:P00420};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11437;
CC Evidence={ECO:0000250|UniProtKB:P00420};
CC -!- SUBUNIT: Component of the cytochrome c oxidase (complex IV, CIV), a
CC multisubunit enzyme composed of 14 subunits. The complex is composed of
CC a catalytic core of 3 subunits MT-CO1, MT-CO2 and MT-CO3, encoded in
CC the mitochondrial DNA, and 11 supernumerary subunits COX4I1 (or
CC COX4I2), COX5A, COX5B, COX6A1 (or COX6A2), COX6B1 (or COX6B2), COX6C,
CC COX7A2 (or COX7A1), COX7B, COX7C, COX8A and NDUFA4, which are encoded
CC in the nuclear genome (PubMed:30030519). The complex exists as a
CC monomer or a dimer and forms supercomplexes (SCs) in the inner
CC mitochondrial membrane with NADH-ubiquinone oxidoreductase (complex I,
CC CI) and ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex,
CC complex III, CIII), resulting in different assemblies (supercomplex
CC SCI(1)III(2)IV(1) and megacomplex MCI(2)III(2)IV(2)) (PubMed:28844695).
CC {ECO:0000269|PubMed:28844695, ECO:0000269|PubMed:30030519}.
CC -!- INTERACTION:
CC P00414; P37840: SNCA; NbExp=3; IntAct=EBI-3932264, EBI-985879;
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:30030519}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:30030519}.
CC -!- DISEASE: Leber hereditary optic neuropathy (LHON) [MIM:535000]: A
CC maternally inherited form of Leber hereditary optic neuropathy, a
CC mitochondrial disease resulting in bilateral painless loss of central
CC vision due to selective degeneration of the retinal ganglion cells and
CC their axons. The disorder shows incomplete penetrance and male
CC predominance. Cardiac conduction defects and neurological defects have
CC also been described in some LHON patients. LHON results from primary
CC mitochondrial DNA mutations affecting the respiratory chain complexes.
CC {ECO:0000269|PubMed:8240356}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Mitochondrial complex IV deficiency (MT-C4D) [MIM:220110]: A
CC disorder of the mitochondrial respiratory chain with heterogeneous
CC clinical manifestations, ranging from isolated myopathy to severe
CC multisystem disease affecting several tissues and organs. Features
CC include hypertrophic cardiomyopathy, hepatomegaly and liver
CC dysfunction, hypotonia, muscle weakness, exercise intolerance,
CC developmental delay, delayed motor development and intellectual
CC disability. Some affected individuals manifest a fatal hypertrophic
CC cardiomyopathy resulting in neonatal death. A subset of patients
CC manifest Leigh syndrome. {ECO:0000269|PubMed:8630495}. Note=The disease
CC is caused by variants affecting the gene represented in this entry.
CC -!- DISEASE: Recurrent myoglobinuria mitochondrial (RM-MT) [MIM:550500]:
CC Recurrent myoglobinuria is characterized by recurrent attacks of
CC rhabdomyolysis (necrosis or disintegration of skeletal muscle)
CC associated with muscle pain and weakness, and followed by excretion of
CC myoglobin in the urine. {ECO:0000269|PubMed:8630495}. Note=The gene
CC represented in this entry may be involved in disease pathogenesis.
CC -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 3 family.
CC {ECO:0000305}.
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DR EMBL; J01415; AAB58949.2; -; Genomic_DNA.
DR EMBL; V00662; CAA24032.1; -; Genomic_DNA.
DR EMBL; DQ654394; ABG27956.1; -; Genomic_DNA.
DR EMBL; DQ654395; ABG27958.1; -; Genomic_DNA.
DR EMBL; DQ654396; ABG27960.1; -; Genomic_DNA.
DR EMBL; DQ654397; ABG27962.1; -; Genomic_DNA.
DR EMBL; DQ654398; ABG27964.1; -; Genomic_DNA.
DR EMBL; DQ654399; ABG27966.1; -; Genomic_DNA.
DR EMBL; DQ654400; ABG27968.1; -; Genomic_DNA.
DR EMBL; DQ654401; ABG27970.1; -; Genomic_DNA.
DR EMBL; DQ654402; ABG27972.1; -; Genomic_DNA.
DR EMBL; DQ654403; ABG27974.1; -; Genomic_DNA.
DR EMBL; DQ654404; ABG27976.1; -; Genomic_DNA.
DR EMBL; DQ654405; ABG27978.1; -; Genomic_DNA.
DR EMBL; DQ654406; ABG27980.1; -; Genomic_DNA.
DR EMBL; DQ654407; ABG27982.1; -; Genomic_DNA.
DR EMBL; DQ654408; ABG27984.1; -; Genomic_DNA.
DR EMBL; DQ654409; ABG27986.1; -; Genomic_DNA.
DR EMBL; DQ654410; ABG27988.1; -; Genomic_DNA.
DR EMBL; DQ654411; ABG27990.1; -; Genomic_DNA.
DR EMBL; DQ654412; ABG27992.1; -; Genomic_DNA.
DR EMBL; DQ654413; ABG27994.1; -; Genomic_DNA.
DR EMBL; DQ654414; ABG27996.1; -; Genomic_DNA.
DR EMBL; DQ654415; ABG27998.1; -; Genomic_DNA.
DR EMBL; DQ654416; ABG28000.1; -; Genomic_DNA.
DR EMBL; DQ654417; ABG28002.1; -; Genomic_DNA.
DR EMBL; DQ654418; ABG28004.1; -; Genomic_DNA.
DR EMBL; DQ654419; ABG28006.1; -; Genomic_DNA.
DR EMBL; DQ654420; ABG28008.1; -; Genomic_DNA.
DR EMBL; DQ654421; ABG28010.1; -; Genomic_DNA.
DR EMBL; DQ654422; ABG28012.1; -; Genomic_DNA.
DR EMBL; DQ654423; ABG28014.1; -; Genomic_DNA.
DR EMBL; DQ654424; ABG28016.1; -; Genomic_DNA.
DR EMBL; DQ654425; ABG28018.1; -; Genomic_DNA.
DR EMBL; DQ654426; ABG28020.1; -; Genomic_DNA.
DR EMBL; DQ654427; ABG28022.1; -; Genomic_DNA.
DR EMBL; DQ654428; ABG28024.1; -; Genomic_DNA.
DR EMBL; DQ654429; ABG28026.1; -; Genomic_DNA.
DR EMBL; DQ654430; ABG28028.1; -; Genomic_DNA.
DR EMBL; DQ654431; ABG28030.1; -; Genomic_DNA.
DR EMBL; DQ654432; ABG28032.1; -; Genomic_DNA.
DR EMBL; DQ654433; ABG28034.1; -; Genomic_DNA.
DR EMBL; DQ654434; ABG28036.1; -; Genomic_DNA.
DR EMBL; DQ654435; ABG28038.1; -; Genomic_DNA.
DR EMBL; DQ654436; ABG28040.1; -; Genomic_DNA.
DR EMBL; DQ654437; ABG28042.1; -; Genomic_DNA.
DR EMBL; DQ654438; ABG28044.1; -; Genomic_DNA.
DR EMBL; DQ654439; ABG28046.1; -; Genomic_DNA.
DR EMBL; DQ654440; ABG28048.1; -; Genomic_DNA.
DR EMBL; DQ654441; ABG28050.1; -; Genomic_DNA.
DR EMBL; DQ654442; ABG28052.1; -; Genomic_DNA.
DR EMBL; DQ654443; ABG28054.1; -; Genomic_DNA.
DR EMBL; AF004341; AAB63452.1; -; Genomic_DNA.
DR PIR; A00482; OTHU3.
DR RefSeq; YP_003024032.1; NC_012920.1.
DR PDB; 5Z62; EM; 3.60 A; C=2-261.
DR PDBsum; 5Z62; -.
DR AlphaFoldDB; P00414; -.
DR SMR; P00414; -.
DR BioGRID; 110617; 15.
DR ComplexPortal; CPX-6123; Mitochondrial respiratory chain complex IV.
DR CORUM; P00414; -.
DR IntAct; P00414; 12.
DR MINT; P00414; -.
DR STRING; 9606.ENSP00000354982; -.
DR DrugBank; DB02659; Cholic Acid.
DR DrugBank; DB04464; N-Formylmethionine.
DR TCDB; 3.D.4.11.1; the proton-translocating cytochrome oxidase (cox) superfamily.
DR iPTMnet; P00414; -.
DR PhosphoSitePlus; P00414; -.
DR BioMuta; MT-CO3; -.
DR DMDM; 6648058; -.
DR EPD; P00414; -.
DR jPOST; P00414; -.
DR MassIVE; P00414; -.
DR PaxDb; P00414; -.
DR PeptideAtlas; P00414; -.
DR PRIDE; P00414; -.
DR ProteomicsDB; 51248; -.
DR TopDownProteomics; P00414; -.
DR Antibodypedia; 35359; 143 antibodies from 24 providers.
DR DNASU; 4514; -.
DR Ensembl; ENST00000362079.2; ENSP00000354982.2; ENSG00000198938.2.
DR GeneID; 4514; -.
DR KEGG; hsa:4514; -.
DR CTD; 4514; -.
DR DisGeNET; 4514; -.
DR GeneCards; MT-CO3; -.
DR GeneReviews; MT-CO3; -.
DR HGNC; HGNC:7422; MT-CO3.
DR HPA; ENSG00000198938; Tissue enhanced (brain, heart muscle).
DR MalaCards; MT-CO3; -.
DR MIM; 220110; phenotype.
DR MIM; 516050; gene.
DR MIM; 535000; phenotype.
DR MIM; 550500; phenotype.
DR neXtProt; NX_P00414; -.
DR OpenTargets; ENSG00000198938; -.
DR Orphanet; 99845; Genetic recurrent myoglobinuria.
DR Orphanet; 254905; Isolated cytochrome C oxidase deficiency.
DR Orphanet; 104; Leber hereditary optic neuropathy.
DR Orphanet; 550; MELAS.
DR VEuPathDB; HostDB:ENSG00000198938; -.
DR eggNOG; KOG4664; Eukaryota.
DR GeneTree; ENSGT00390000013064; -.
DR HOGENOM; CLU_044071_0_0_1; -.
DR InParanoid; P00414; -.
DR OMA; SIYWWGS; -.
DR OrthoDB; 1304563at2759; -.
DR PhylomeDB; P00414; -.
DR TreeFam; TF343435; -.
DR BioCyc; MetaCyc:HS00028-MON; -.
DR PathwayCommons; P00414; -.
DR Reactome; R-HSA-5628897; TP53 Regulates Metabolic Genes.
DR Reactome; R-HSA-611105; Respiratory electron transport.
DR Reactome; R-HSA-9707564; Cytoprotection by HMOX1.
DR SignaLink; P00414; -.
DR SIGNOR; P00414; -.
DR BioGRID-ORCS; 4514; 0 hits in 1 CRISPR screen.
DR ChiTaRS; COX3; human.
DR GeneWiki; MT-CO3; -.
DR GenomeRNAi; 4514; -.
DR Pharos; P00414; Tbio.
DR PRO; PR:P00414; -.
DR Proteomes; UP000005640; Mitochondrion.
DR RNAct; P00414; protein.
DR Bgee; ENSG00000198938; Expressed in mucosa of stomach and 94 other tissues.
DR ExpressionAtlas; P00414; baseline and differential.
DR Genevisible; P00414; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome.
DR GO; GO:0031966; C:mitochondrial membrane; IDA:ComplexPortal.
DR GO; GO:0005751; C:mitochondrial respiratory chain complex IV; IPI:ComplexPortal.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0045277; C:respiratory chain complex IV; IDA:UniProtKB.
DR GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0009055; F:electron transfer activity; IBA:GO_Central.
DR GO; GO:0015453; F:oxidoreduction-driven active transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0009060; P:aerobic respiration; IBA:GO_Central.
DR GO; GO:0045333; P:cellular respiration; IC:ComplexPortal.
DR GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IBA:GO_Central.
DR GO; GO:0008535; P:respiratory chain complex IV assembly; IMP:UniProtKB.
DR CDD; cd01665; Cyt_c_Oxidase_III; 1.
DR Gene3D; 1.20.120.80; -; 1.
DR InterPro; IPR024791; Cyt_c/ubiquinol_Oxase_su3.
DR InterPro; IPR033945; Cyt_c_oxase_su3_dom.
DR InterPro; IPR000298; Cyt_c_oxidase-like_su3.
DR InterPro; IPR035973; Cyt_c_oxidase_su3-like_sf.
DR InterPro; IPR013833; Cyt_c_oxidase_su3_a-hlx.
DR PANTHER; PTHR11403; PTHR11403; 1.
DR Pfam; PF00510; COX3; 1.
DR SUPFAM; SSF81452; SSF81452; 1.
DR PROSITE; PS50253; COX3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disease variant; Leber hereditary optic neuropathy; Membrane;
KW Mitochondrion; Mitochondrion inner membrane; Primary mitochondrial disease;
KW Reference proteome; Translocase; Transmembrane; Transmembrane helix.
FT CHAIN 1..261
FT /note="Cytochrome c oxidase subunit 3"
FT /id="PRO_0000183793"
FT TOPO_DOM 1..15
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000269|PubMed:30030519"
FT TRANSMEM 16..34
FT /note="Helical; Name=I"
FT /evidence="ECO:0000250|UniProtKB:P00415"
FT TOPO_DOM 35..40
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000269|PubMed:30030519"
FT TRANSMEM 41..66
FT /note="Helical; Name=II"
FT /evidence="ECO:0000250|UniProtKB:P00415"
FT TOPO_DOM 67..72
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000269|PubMed:30030519"
FT TRANSMEM 73..105
FT /note="Helical; Name=III"
FT /evidence="ECO:0000250|UniProtKB:P00415"
FT TOPO_DOM 106..128
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000269|PubMed:30030519"
FT TRANSMEM 129..152
FT /note="Helical; Name=IV"
FT /evidence="ECO:0000250|UniProtKB:P00415"
FT TOPO_DOM 153..155
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000269|PubMed:30030519"
FT TRANSMEM 156..183
FT /note="Helical; Name=V"
FT /evidence="ECO:0000250|UniProtKB:P00415"
FT TOPO_DOM 184..190
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000269|PubMed:30030519"
FT TRANSMEM 191..223
FT /note="Helical; Name=VI"
FT /evidence="ECO:0000250|UniProtKB:P00415"
FT TOPO_DOM 224..232
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000269|PubMed:30030519"
FT TRANSMEM 233..256
FT /note="Helical; Name=VII"
FT /evidence="ECO:0000250|UniProtKB:P00415"
FT TOPO_DOM 257..261
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000269|PubMed:30030519"
FT VARIANT 3
FT /note="H -> R (in dbSNP:rs1556423637)"
FT /evidence="ECO:0000269|PubMed:9461455"
FT /id="VAR_008573"
FT VARIANT 35
FT /note="F -> S"
FT /evidence="ECO:0000269|PubMed:9461455"
FT /id="VAR_008574"
FT VARIANT 78
FT /note="G -> S (in LHON; secondary mutation; does not seem
FT to directly cause the disease; dbSNP:rs267606611)"
FT /evidence="ECO:0000269|PubMed:8240356"
FT /id="VAR_002167"
FT VARIANT 91
FT /note="V -> I (in dbSNP:rs2853825)"
FT /evidence="ECO:0000269|PubMed:1757091"
FT /id="VAR_008575"
FT VARIANT 94..98
FT /note="Missing (in MT-C4D; with RM-MT)"
FT /evidence="ECO:0000269|PubMed:8630495"
FT /id="VAR_033057"
FT VARIANT 177
FT /note="Q -> R"
FT /evidence="ECO:0000269|PubMed:1757091"
FT /id="VAR_008576"
FT VARIANT 200
FT /note="A -> T (in LHON; possible rare primary mutation;
FT dbSNP:rs200613617)"
FT /evidence="ECO:0000269|PubMed:8240356"
FT /id="VAR_002168"
FT VARIANT 251
FT /note="F -> L (found in two patients with a diagnosis of
FT mitochondrial encephalomyopathy with lactic acidosis and
FT stroke-like episodes syndrome; unknown pathological
FT significance; dbSNP:rs1556423753)"
FT /evidence="ECO:0000269|PubMed:18587274,
FT ECO:0000269|PubMed:7496173"
FT /id="VAR_002169"
FT VARIANT 254
FT /note="V -> I (in dbSNP:rs200809063)"
FT /evidence="ECO:0000269|PubMed:1757091"
FT /id="VAR_008577"
FT CONFLICT 118
FT /note="P -> R (in Ref. 1; CAA24032)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 261 AA; 29951 MW; A04385EF748B7C14 CRC64;
MTHQSHAYHM VKPSPWPLTG ALSALLMTSG LAMWFHFHSM TLLMLGLLTN TLTMYQWWRD
VTRESTYQGH HTPPVQKGLR YGMILFITSE VFFFAGFFWA FYHSSLAPTP QLGGHWPPTG
ITPLNPLEVP LLNTSVLLAS GVSITWAHHS LMENNRNQMI QALLITILLG LYFTLLQASE
YFESPFTISD GIYGSTFFVA TGFHGLHVII GSTFLTICFI RQLMFHFTSK HHFGFEAAAW
YWHFVDVVWL FLYVSIYWWG S
