COQ7_HUMAN
ID COQ7_HUMAN Reviewed; 217 AA.
AC Q99807; B2RDA9; Q9BTT7; Q9H0T5; Q9UEW5; Q9UNR5;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 3.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=5-demethoxyubiquinone hydroxylase, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03194};
DE Short=DMQ hydroxylase {ECO:0000255|HAMAP-Rule:MF_03194};
DE EC=1.14.99.60 {ECO:0000255|HAMAP-Rule:MF_03194};
DE AltName: Full=Timing protein clk-1 homolog {ECO:0000255|HAMAP-Rule:MF_03194};
DE AltName: Full=Ubiquinone biosynthesis monooxygenase COQ7 {ECO:0000255|HAMAP-Rule:MF_03194};
DE Flags: Precursor;
GN Name=COQ7 {ECO:0000255|HAMAP-Rule:MF_03194};
OS Homo sapiens (Human).
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 [MRNA] (ISOFORM 1), AND VARIANT MET-103.
RX PubMed=10373327; DOI=10.1006/geno.1999.5838;
RA Asaumi S., Kuroyanagi H., Seki N., Shirasawa T.;
RT "Orthologues of the Caenorhabditis elegans longevity gene clk-1 in mouse
RT and human.";
RL Genomics 58:293-301(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT MET-103.
RC TISSUE=Brain;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT MET-103.
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 39-217 (ISOFORMS 1/2), AND VARIANT MET-103.
RX PubMed=10501970; DOI=10.1007/s003359901147;
RA Vajo Z., King L.M., Jonassen T., Wilkin D.J., Ho N., Munnich A.,
RA Clarke C.F., Francomano C.A.;
RT "Conservation of the Caenorhabditis elegans timing gene clk-1 from yeast to
RT human: a gene required for ubiquinone biosynthesis with potential
RT implications for aging.";
RL Mamm. Genome 10:1000-1004(1999).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 85-130 (ISOFORMS 1/2), AND VARIANT MET-103.
RC TISSUE=Placenta;
RX PubMed=9020081; DOI=10.1126/science.275.5302.980;
RA Ewbank J.J., Barnes T.M., Lakowski B., Lussier M., Bussey H., Hekimi S.;
RT "Structural and functional conservation of the Caenorhabditis elegans
RT timing gene clk-1.";
RL Science 275:980-983(1997).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP INTERACTION WITH COQ8B AND COQ6.
RX PubMed=24270420; DOI=10.1172/jci69000;
RA Ashraf S., Gee H.Y., Woerner S., Xie L.X., Vega-Warner V., Lovric S.,
RA Fang H., Song X., Cattran D.C., Avila-Casado C., Paterson A.D.,
RA Nitschke P., Bole-Feysot C., Cochat P., Esteve-Rudd J., Haberberger B.,
RA Allen S.J., Zhou W., Airik R., Otto E.A., Barua M., Al-Hamed M.H.,
RA Kari J.A., Evans J., Bierzynska A., Saleem M.A., Bockenhauer D., Kleta R.,
RA El Desoky S., Hacihamdioglu D.O., Gok F., Washburn J., Wiggins R.C.,
RA Choi M., Lifton R.P., Levy S., Han Z., Salviati L., Prokisch H.,
RA Williams D.S., Pollak M., Clarke C.F., Pei Y., Antignac C., Hildebrandt F.;
RT "ADCK4 mutations promote steroid-resistant nephrotic syndrome through CoQ10
RT biosynthesis disruption.";
RL J. Clin. Invest. 123:5179-5189(2013).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [12]
RP INTERACTION WITH COQ9.
RX PubMed=25339443; DOI=10.1073/pnas.1413128111;
RA Lohman D.C., Forouhar F., Beebe E.T., Stefely M.S., Minogue C.E.,
RA Ulbrich A., Stefely J.A., Sukumar S., Luna-Sanchez M., Jochem A., Lew S.,
RA Seetharaman J., Xiao R., Wang H., Westphall M.S., Wrobel R.L.,
RA Everett J.K., Mitchell J.C., Lopez L.C., Coon J.J., Tong L.,
RA Pagliarini D.J.;
RT "Mitochondrial COQ9 is a lipid-binding protein that associates with COQ7 to
RT enable coenzyme Q biosynthesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:E4697-4705(2014).
RN [13]
RP INVOLVEMENT IN COQ10D8, AND VARIANT COQ10D8 GLU-141.
RX PubMed=26084283; DOI=10.1136/jmedgenet-2015-102986;
RA Freyer C., Stranneheim H., Naess K., Mourier A., Felser A., Maffezzini C.,
RA Lesko N., Bruhn H., Engvall M., Wibom R., Barbaro M., Hinze Y.,
RA Magnusson M., Andeer R., Zetterstroem R.H., von Doebeln U., Wredenberg A.,
RA Wedell A.;
RT "Rescue of primary ubiquinone deficiency due to a novel COQ7 defect using
RT 2,4-dihydroxybensoic acid.";
RL J. Med. Genet. 52:779-783(2015).
RN [14]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ARG-28.
RX PubMed=25961505; DOI=10.1038/ncb3170;
RA Monaghan R.M., Barnes R.G., Fisher K., Andreou T., Rooney N., Poulin G.B.,
RA Whitmarsh A.J.;
RT "A nuclear role for the respiratory enzyme CLK-1 in regulating
RT mitochondrial stress responses and longevity.";
RL Nat. Cell Biol. 17:782-792(2015).
RN [15]
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).
CC -!- FUNCTION: Catalyzes the hydroxylation of 2-polyprenyl-3-methyl-6-
CC methoxy-1,4-benzoquinol (DMQH2) during ubiquinone biosynthesis (By
CC similarity). Has also a structural role in the COQ enzyme complex,
CC stabilizing other COQ polypeptides (By similarity). Involved in
CC lifespan determination in a ubiquinone-independent manner (By
CC similarity). Plays a role in modulating mitochondrial stress responses,
CC acting in the nucleus, perhaps via regulating gene expression,
CC independent of its characterized mitochondrial function in ubiquinone
CC biosynthesis (PubMed:25961505). {ECO:0000255|HAMAP-Rule:MF_03194,
CC ECO:0000269|PubMed:25961505}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 6-methoxy-3-methyl-2-all-trans-polyprenyl-1,4-benzoquinol +
CC AH2 + O2 = A + a 3-demethylubiquinol + H2O; Xref=Rhea:RHEA:50908,
CC Rhea:RHEA-COMP:10859, Rhea:RHEA-COMP:10914, ChEBI:CHEBI:13193,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499,
CC ChEBI:CHEBI:84167, ChEBI:CHEBI:84422; EC=1.14.99.60;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03194};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03194};
CC Note=Binds 2 iron ions per subunit. {ECO:0000255|HAMAP-Rule:MF_03194};
CC -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_03194}.
CC -!- SUBUNIT: Component of a multi-subunit COQ enzyme complex, composed of
CC at least COQ3, COQ4, COQ5, COQ6, COQ7 and COQ9 (By similarity).
CC Interacts with COQ8B and COQ6 (PubMed:24270420). Interacts with COQ9
CC (PubMed:25339443). {ECO:0000255|HAMAP-Rule:MF_03194,
CC ECO:0000269|PubMed:24270420, ECO:0000269|PubMed:25339443}.
CC -!- INTERACTION:
CC Q99807; Q9NZJ6: COQ3; NbExp=5; IntAct=EBI-11017131, EBI-10897372;
CC Q99807; Q9Y3A0: COQ4; NbExp=5; IntAct=EBI-11017131, EBI-12284865;
CC Q99807; Q5HYK3: COQ5; NbExp=7; IntAct=EBI-11017131, EBI-12577722;
CC Q99807; Q9Y2Z9: COQ6; NbExp=3; IntAct=EBI-11017131, EBI-718148;
CC Q99807; O75208: COQ9; NbExp=8; IntAct=EBI-11017131, EBI-724524;
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_03194}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_03194}; Matrix side {ECO:0000255|HAMAP-Rule:MF_03194}.
CC Mitochondrion {ECO:0000269|PubMed:25961505}. Nucleus
CC {ECO:0000269|PubMed:25961505}. Chromosome
CC {ECO:0000269|PubMed:25961505}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q99807-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q99807-2; Sequence=VSP_039068;
CC -!- TISSUE SPECIFICITY: Expressed dominantly in heart and skeletal muscle.
CC -!- DISEASE: Coenzyme Q10 deficiency, primary, 8 (COQ10D8) [MIM:616733]: An
CC autosomal recessive disorder resulting from mitochondrial dysfunction
CC and characterized by decreased levels of coenzyme Q10. Patients
CC manifest neonatal lung hypoplasia, contractures, early infantile
CC hypertension and cardiac hypertrophy, secondary to prenatal kidney
CC dysplasia, with neonatal and infantile renal dysfunction. Clinical
CC features also include progressive peripheral neuropathy, muscular
CC hypotonia and atrophy, and mild psychomotor delay with hearing and
CC visual impairment. {ECO:0000269|PubMed:26084283}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the COQ7 family. {ECO:0000255|HAMAP-
CC Rule:MF_03194}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF098948; AAD43648.1; -; mRNA.
DR EMBL; AL136647; CAB66582.1; -; mRNA.
DR EMBL; AK024291; BAB14876.1; -; mRNA.
DR EMBL; AK315470; BAG37856.1; -; mRNA.
DR EMBL; AC099518; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471186; EAW50268.1; -; Genomic_DNA.
DR EMBL; BC003185; AAH03185.1; -; mRNA.
DR EMBL; AF032900; AAC69451.1; -; mRNA.
DR EMBL; U81276; AAC51120.1; -; mRNA.
DR CCDS; CCDS10574.1; -. [Q99807-1]
DR CCDS; CCDS53993.1; -. [Q99807-2]
DR RefSeq; NP_001177912.1; NM_001190983.1. [Q99807-2]
DR RefSeq; NP_057222.2; NM_016138.4. [Q99807-1]
DR AlphaFoldDB; Q99807; -.
DR SMR; Q99807; -.
DR BioGRID; 115523; 25.
DR ComplexPortal; CPX-3642; CoQ biosynthetic complex.
DR DIP; DIP-62092N; -.
DR IntAct; Q99807; 38.
DR STRING; 9606.ENSP00000322316; -.
DR ChEMBL; CHEMBL4630851; -.
DR iPTMnet; Q99807; -.
DR PhosphoSitePlus; Q99807; -.
DR BioMuta; COQ7; -.
DR DMDM; 311033465; -.
DR EPD; Q99807; -.
DR jPOST; Q99807; -.
DR MassIVE; Q99807; -.
DR MaxQB; Q99807; -.
DR PaxDb; Q99807; -.
DR PeptideAtlas; Q99807; -.
DR PRIDE; Q99807; -.
DR ProteomicsDB; 78485; -. [Q99807-1]
DR ProteomicsDB; 78486; -. [Q99807-2]
DR TopDownProteomics; Q99807-1; -. [Q99807-1]
DR TopDownProteomics; Q99807-2; -. [Q99807-2]
DR Antibodypedia; 42924; 191 antibodies from 25 providers.
DR DNASU; 10229; -.
DR Ensembl; ENST00000321998.10; ENSP00000322316.5; ENSG00000167186.11. [Q99807-1]
DR Ensembl; ENST00000544894.6; ENSP00000442923.2; ENSG00000167186.11. [Q99807-2]
DR Ensembl; ENST00000568985.5; ENSP00000456734.1; ENSG00000167186.11. [Q99807-1]
DR GeneID; 10229; -.
DR KEGG; hsa:10229; -.
DR MANE-Select; ENST00000321998.10; ENSP00000322316.5; NM_016138.5; NP_057222.2.
DR UCSC; uc002dfr.4; human. [Q99807-1]
DR CTD; 10229; -.
DR DisGeNET; 10229; -.
DR GeneCards; COQ7; -.
DR GeneReviews; COQ7; -.
DR HGNC; HGNC:2244; COQ7.
DR HPA; ENSG00000167186; Low tissue specificity.
DR MalaCards; COQ7; -.
DR MIM; 601683; gene.
DR MIM; 616733; phenotype.
DR neXtProt; NX_Q99807; -.
DR OpenTargets; ENSG00000167186; -.
DR PharmGKB; PA26761; -.
DR VEuPathDB; HostDB:ENSG00000167186; -.
DR eggNOG; KOG4061; Eukaryota.
DR GeneTree; ENSGT00390000014520; -.
DR HOGENOM; CLU_071892_2_0_1; -.
DR InParanoid; Q99807; -.
DR OMA; HYNDQVR; -.
DR OrthoDB; 1242061at2759; -.
DR PhylomeDB; Q99807; -.
DR TreeFam; TF314559; -.
DR BioCyc; MetaCyc:ENSG00000167186-MON; -.
DR BRENDA; 1.14.99.60; 2681.
DR PathwayCommons; Q99807; -.
DR Reactome; R-HSA-2142789; Ubiquinol biosynthesis.
DR SignaLink; Q99807; -.
DR UniPathway; UPA00232; -.
DR BioGRID-ORCS; 10229; 144 hits in 1081 CRISPR screens.
DR ChiTaRS; COQ7; human.
DR GeneWiki; COQ7; -.
DR GenomeRNAi; 10229; -.
DR Pharos; Q99807; Tbio.
DR PRO; PR:Q99807; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q99807; protein.
DR Bgee; ENSG00000167186; Expressed in hindlimb stylopod muscle and 153 other tissues.
DR ExpressionAtlas; Q99807; baseline and differential.
DR Genevisible; Q99807; HS.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0031314; C:extrinsic component of mitochondrial inner membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:ComplexPortal.
DR GO; GO:0005739; C:mitochondrion; IDA:WormBase.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0110142; C:ubiquinone biosynthesis complex; IPI:ComplexPortal.
DR GO; GO:0008682; F:3-demethoxyubiquinol 3-hydroxylase activity; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; IDA:WormBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016709; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen; IEA:UniProtKB-UniRule.
DR GO; GO:0008340; P:determination of adult lifespan; IBA:GO_Central.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:WormBase.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:WormBase.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR GO; GO:2000377; P:regulation of reactive oxygen species metabolic process; IMP:WormBase.
DR GO; GO:0006744; P:ubiquinone biosynthetic process; IBA:GO_Central.
DR CDD; cd01042; DMQH; 1.
DR HAMAP; MF_01658; COQ7; 1.
DR InterPro; IPR009078; Ferritin-like_SF.
DR InterPro; IPR011566; Ubq_synth_Coq7.
DR PANTHER; PTHR11237; PTHR11237; 1.
DR Pfam; PF03232; COQ7; 1.
DR SUPFAM; SSF47240; SSF47240; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chromosome; Disease variant; Iron; Membrane;
KW Metal-binding; Mitochondrion; Mitochondrion inner membrane; Monooxygenase;
KW Nucleus; Oxidoreductase; Primary mitochondrial disease; Reference proteome;
KW Repeat; Transit peptide; Ubiquinone biosynthesis.
FT TRANSIT 1..35
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03194"
FT CHAIN 36..217
FT /note="5-demethoxyubiquinone hydroxylase, mitochondrial"
FT /id="PRO_0000079251"
FT REPEAT 48..129
FT /note="1"
FT REPEAT 130..217
FT /note="2"
FT REGION 11..29
FT /note="Required for nuclear localization"
FT /evidence="ECO:0000269|PubMed:25961505"
FT REGION 48..217
FT /note="2 X approximate tandem repeats"
FT BINDING 60
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03194"
FT BINDING 90
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03194"
FT BINDING 90
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03194"
FT BINDING 93
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03194"
FT BINDING 142
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03194"
FT BINDING 178
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03194"
FT BINDING 178
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03194"
FT BINDING 181
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03194"
FT VAR_SEQ 1..38
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11230166"
FT /id="VSP_039068"
FT VARIANT 103
FT /note="T -> M (in dbSNP:rs11074359)"
FT /evidence="ECO:0000269|PubMed:10373327,
FT ECO:0000269|PubMed:10501970, ECO:0000269|PubMed:11230166,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:9020081"
FT /id="VAR_055148"
FT VARIANT 141
FT /note="V -> E (in COQ10D8; dbSNP:rs864321686)"
FT /evidence="ECO:0000269|PubMed:26084283"
FT /id="VAR_076370"
FT MUTAGEN 28
FT /note="R->A: Reduces nuclear localization. Increases level
FT of reactive oxygen species (ROS)."
FT /evidence="ECO:0000269|PubMed:25961505"
FT CONFLICT 45
FT /note="S -> N (in Ref. 7; AAC69451)"
FT /evidence="ECO:0000305"
FT CONFLICT 69
FT /note="G -> W (in Ref. 2; CAB66582)"
FT /evidence="ECO:0000305"
FT CONFLICT 72
FT /note="A -> R (in Ref. 7; AAC69451)"
FT /evidence="ECO:0000305"
FT CONFLICT 172
FT /note="K -> R (in Ref. 7; AAC69451)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 217 AA; 24277 MW; 37BEC3CEA621B77B CRC64;
MSCAGAAAAP RLWRLRPGAR RSLSAYGRRT SVRFRSSGMT LDNISRAAVD RIIRVDHAGE
YGANRIYAGQ MAVLGRTSVG PVIQKMWDQE KDHLKKFNEL MVTFRVRPTV LMPLWNVLGF
ALGAGTALLG KEGAMACTVA VEESIAHHYN NQIRTLMEED PEKYEELLQL IKKFRDEELE
HHDIGLDHDA ELAPAYAVLK SIIQAGCRVA IYLSERL
