COQ6_HUMAN
ID COQ6_HUMAN Reviewed; 468 AA.
AC Q9Y2Z9; B7Z3K8; Q53GG6; Q86U30; Q96CA1; Q96CK2;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2002, sequence version 2.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Ubiquinone biosynthesis monooxygenase COQ6, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03193};
DE EC=1.14.13.- {ECO:0000255|HAMAP-Rule:MF_03193};
DE AltName: Full=Coenzyme Q10 monooxygenase 6 {ECO:0000255|HAMAP-Rule:MF_03193};
DE Flags: Precursor;
GN Name=COQ6 {ECO:0000255|HAMAP-Rule:MF_03193}; ORFNames=CGI-10;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=10810093; DOI=10.1101/gr.10.5.703;
RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT "Identification of novel human genes evolutionarily conserved in
RT Caenorhabditis elegans by comparative proteomics.";
RL Genome Res. 10:703-713(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Subthalamic nucleus;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Fetal liver;
RA Li W.B., Gruber C., Jessee J., Polayes D.;
RT "Full-length cDNA libraries and normalization.";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT MET-406.
RC TISSUE=Heart;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT LYS-287.
RC TISSUE=Colon, and Lung;
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 [8]
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 [9]
RP INTERACTION WITH COQ8B AND COQ7.
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 [10]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=26260787; DOI=10.1074/jbc.m115.675744;
RA Ozeir M., Pelosi L., Ismail A., Mellot-Draznieks C., Fontecave M.,
RA Pierrel F.;
RT "Coq6 is responsible for the C4-deamination reaction in coenzyme Q
RT biosynthesis in Saccharomyces cerevisiae.";
RL J. Biol. Chem. 290:24140-24151(2015).
RN [11]
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 [12]
RP VARIANTS COQ10D6 ARG-255 AND ASP-353, TISSUE SPECIFICITY, AND ALTERNATIVE
RP SPLICING.
RX PubMed=21540551; DOI=10.1172/jci45693;
RA Heeringa S.F., Chernin G., Chaki M., Zhou W., Sloan A.J., Ji Z., Xie L.X.,
RA Salviati L., Hurd T.W., Vega-Warner V., Killen P.D., Raphael Y., Ashraf S.,
RA Ovunc B., Schoeb D.S., McLaughlin H.M., Airik R., Vlangos C.N.,
RA Gbadegesin R., Hinkes B., Saisawat P., Trevisson E., Doimo M., Casarin A.,
RA Pertegato V., Giorgi G., Prokisch H., Rotig A., Nurnberg G., Becker C.,
RA Wang S., Ozaltin F., Topaloglu R., Bakkaloglu A., Bakkaloglu S.A.,
RA Muller D., Beissert A., Mir S., Berdeli A., Varpizen S., Zenker M.,
RA Matejas V., Santos-Ocana C., Navas P., Kusakabe T., Kispert A., Akman S.,
RA Soliman N.A., Krick S., Mundel P., Reiser J., Nurnberg P., Clarke C.F.,
RA Wiggins R.C., Faul C., Hildebrandt F.;
RT "COQ6 mutations in human patients produce nephrotic syndrome with
RT sensorineural deafness.";
RL J. Clin. Invest. 121:2013-2024(2011).
RN [13]
RP VARIANT HIS-208, CHARACTERIZATION OF VARIANT HIS-208, AND INVOLVEMENT IN
RP SCHWANNOMATOSIS SUSCEPTIBILITY.
RX PubMed=24763291; DOI=10.1038/gim.2014.39;
RA Zhang K., Lin J.W., Wang J., Wu X., Gao H., Hsieh Y.C., Hwu P., Liu Y.R.,
RA Su L., Chiou H.Y., Wang D., Yuan Y.C., Whang-Peng J., Chiu W.T., Yen Y.;
RT "A germline missense mutation in COQ6 is associated with susceptibility to
RT familial schwannomatosis.";
RL Genet. Med. 16:787-792(2014).
RN [14]
RP VARIANT COQ10D6 LEU-261.
RX PubMed=28044327; DOI=10.1111/cge.12960;
RA Gigante M., Diella S., Santangelo L., Trevisson E., Acosta M.J.,
RA Amatruda M., Finzi G., Caridi G., Murer L., Accetturo M., Ranieri E.,
RA Ghiggeri G.M., Giordano M., Grandaliano G., Salviati L., Gesualdo L.;
RT "Further phenotypic heterogeneity of CoQ10 deficiency associated with
RT steroid resistant nephrotic syndrome and novel COQ2 and COQ6 variants.";
RL Clin. Genet. 92:224-226(2017).
CC -!- FUNCTION: FAD-dependent monooxygenase required for the C5-ring
CC hydroxylation during ubiquinone biosynthesis. Catalyzes the
CC hydroxylation of 3-hexaprenyl-4-hydroxybenzoic acid (HHB) to 3-
CC hexaprenyl-4,5-dihydroxybenzoic acid (DHHB). The electrons required for
CC the hydroxylation reaction may be funneled indirectly from NADPH via a
CC ferredoxin/ferredoxin reductase system to COQ6 (By similarity). Is able
CC to perform the deamination reaction at C4 of 3-hexaprenyl-4-amino-5-
CC hydroxybenzoic acid (HHAB) to produce DHHB when expressed in yeast
CC cells lacking COQ9, even if utilization of para-aminobenzoic acid
CC (pABA) involving C4-deamination seems not to occur in bacteria, plants
CC and mammals, where only C5 hydroxylation of HHB has been shown
CC (PubMed:26260787). {ECO:0000255|HAMAP-Rule:MF_03193,
CC ECO:0000269|PubMed:26260787}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-hydroxy-3-all-trans-hexaprenylbenzoate + 2 H(+) + O2 + 2
CC reduced [2Fe-2S]-[ferredoxin] = 3,4-dihydroxy-5-all-trans-
CC hexaprenylbenzoate + H2O + 2 oxidized [2Fe-2S]-[ferredoxin];
CC Xref=Rhea:RHEA:20361, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:58373,
CC ChEBI:CHEBI:84492; Evidence={ECO:0000255|HAMAP-Rule:MF_03193};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03193};
CC -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_03193}.
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 COQ7 (PubMed:24270420). {ECO:0000255|HAMAP-
CC Rule:MF_03193, ECO:0000269|PubMed:24270420}.
CC -!- INTERACTION:
CC Q9Y2Z9; Q9NZJ6: COQ3; NbExp=4; IntAct=EBI-718148, EBI-10897372;
CC Q9Y2Z9; Q9Y3A0: COQ4; NbExp=3; IntAct=EBI-718148, EBI-12284865;
CC Q9Y2Z9; Q5HYK3: COQ5; NbExp=9; IntAct=EBI-718148, EBI-12577722;
CC Q9Y2Z9; Q99807: COQ7; NbExp=3; IntAct=EBI-718148, EBI-11017131;
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_03193}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_03193}; Matrix side {ECO:0000255|HAMAP-Rule:MF_03193}. Golgi
CC apparatus {ECO:0000255|HAMAP-Rule:MF_03193}. Cell projection
CC {ECO:0000255|HAMAP-Rule:MF_03193}. Note=Localizes to cell processes and
CC Golgi apparatus in podocytes. {ECO:0000255|HAMAP-Rule:MF_03193}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=a;
CC IsoId=Q9Y2Z9-1; Sequence=Displayed;
CC Name=2; Synonyms=b;
CC IsoId=Q9Y2Z9-2; Sequence=VSP_044060, VSP_044062;
CC Name=3; Synonyms=c;
CC IsoId=Q9Y2Z9-3; Sequence=VSP_044061;
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:21540551}.
CC -!- DISEASE: Coenzyme Q10 deficiency, primary, 6 (COQ10D6) [MIM:614650]: An
CC autosomal recessive disorder characterized by onset in infancy of
CC severe progressive nephrotic syndrome resulting in end-stage renal
CC failure and sensorineural deafness. Renal biopsy usually shows focal
CC segmental glomerulosclerosis. {ECO:0000269|PubMed:21540551,
CC ECO:0000269|PubMed:28044327}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Note=Mutations in COQ6 may play a role in susceptibility to
CC Schwannomatosis, a cancer predisposition syndrome in which patients
CC develop multiple non-vestibular schwannomas, benign neoplasms that
CC arise from Schwann cells of the cranial, peripheral, and autonomic
CC nerves. {ECO:0000269|PubMed:24763291}.
CC -!- SIMILARITY: Belongs to the UbiH/COQ6 family. {ECO:0000255|HAMAP-
CC Rule:MF_03193}.
CC -!- CAUTION: Based on current literature, utilization of para-aminobenzoic
CC acid (pABA) involving C4-deamination is still unclear, and seems not to
CC occur in bacteria, plants and mammals where only C5 hydroxylation of
CC HHB has been shown, even if human COQ6 is able to support C4-
CC deamination in yeast cells lacking COQ9. {ECO:0000305|PubMed:26260787}.
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DR EMBL; AF132944; AAD27719.1; -; mRNA.
DR EMBL; AK296040; BAH12244.1; -; mRNA.
DR EMBL; BX248000; CAD62332.1; -; mRNA.
DR EMBL; AK222965; BAD96685.1; -; mRNA.
DR EMBL; AC005480; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471061; EAW81148.1; -; Genomic_DNA.
DR EMBL; BC014181; AAH14181.1; -; mRNA.
DR EMBL; BC014483; AAH14483.1; -; mRNA.
DR CCDS; CCDS9823.1; -. [Q9Y2Z9-1]
DR CCDS; CCDS9824.2; -. [Q9Y2Z9-3]
DR RefSeq; NP_872282.1; NM_182476.2. [Q9Y2Z9-1]
DR RefSeq; NP_872286.2; NM_182480.2. [Q9Y2Z9-3]
DR AlphaFoldDB; Q9Y2Z9; -.
DR SMR; Q9Y2Z9; -.
DR BioGRID; 119212; 70.
DR ComplexPortal; CPX-3642; CoQ biosynthetic complex.
DR IntAct; Q9Y2Z9; 63.
DR STRING; 9606.ENSP00000333946; -.
DR iPTMnet; Q9Y2Z9; -.
DR PhosphoSitePlus; Q9Y2Z9; -.
DR BioMuta; COQ6; -.
DR DMDM; 26006952; -.
DR EPD; Q9Y2Z9; -.
DR jPOST; Q9Y2Z9; -.
DR MassIVE; Q9Y2Z9; -.
DR MaxQB; Q9Y2Z9; -.
DR PaxDb; Q9Y2Z9; -.
DR PeptideAtlas; Q9Y2Z9; -.
DR PRIDE; Q9Y2Z9; -.
DR ProteomicsDB; 6528; -.
DR ProteomicsDB; 69762; -.
DR ProteomicsDB; 85949; -. [Q9Y2Z9-1]
DR Antibodypedia; 47346; 202 antibodies from 24 providers.
DR DNASU; 51004; -.
DR Ensembl; ENST00000334571.7; ENSP00000333946.2; ENSG00000119723.17. [Q9Y2Z9-1]
DR Ensembl; ENST00000394026.8; ENSP00000377594.4; ENSG00000119723.17. [Q9Y2Z9-3]
DR GeneID; 51004; -.
DR KEGG; hsa:51004; -.
DR MANE-Select; ENST00000334571.7; ENSP00000333946.2; NM_182476.3; NP_872282.1.
DR UCSC; uc001xph.4; human. [Q9Y2Z9-1]
DR CTD; 51004; -.
DR DisGeNET; 51004; -.
DR GeneCards; COQ6; -.
DR GeneReviews; COQ6; -.
DR HGNC; HGNC:20233; COQ6.
DR HPA; ENSG00000119723; Low tissue specificity.
DR MalaCards; COQ6; -.
DR MIM; 614647; gene.
DR MIM; 614650; phenotype.
DR neXtProt; NX_Q9Y2Z9; -.
DR OpenTargets; ENSG00000119723; -.
DR Orphanet; 280406; Familial steroid-resistant nephrotic syndrome with sensorineural deafness.
DR Orphanet; 93921; Schwannomatosis.
DR PharmGKB; PA134940980; -.
DR VEuPathDB; HostDB:ENSG00000119723; -.
DR eggNOG; KOG3855; Eukaryota.
DR GeneTree; ENSGT00390000015152; -.
DR InParanoid; Q9Y2Z9; -.
DR OMA; SDVACII; -.
DR OrthoDB; 655400at2759; -.
DR PhylomeDB; Q9Y2Z9; -.
DR TreeFam; TF105772; -.
DR BioCyc; MetaCyc:ENSG00000119723-MON; -.
DR PathwayCommons; Q9Y2Z9; -.
DR Reactome; R-HSA-2142789; Ubiquinol biosynthesis.
DR SignaLink; Q9Y2Z9; -.
DR UniPathway; UPA00232; -.
DR BioGRID-ORCS; 51004; 71 hits in 1090 CRISPR screens.
DR GenomeRNAi; 51004; -.
DR Pharos; Q9Y2Z9; Tbio.
DR PRO; PR:Q9Y2Z9; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q9Y2Z9; protein.
DR Bgee; ENSG00000119723; Expressed in right adrenal gland cortex and 131 other tissues.
DR ExpressionAtlas; Q9Y2Z9; baseline and differential.
DR Genevisible; Q9Y2Z9; HS.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-SubCell.
DR GO; GO:0031314; C:extrinsic component of mitochondrial inner membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:ComplexPortal.
DR GO; GO:0005739; C:mitochondrion; IDA:LIFEdb.
DR GO; GO:0110142; C:ubiquinone biosynthesis complex; IPI:ComplexPortal.
DR GO; GO:0008681; F:2-octaprenyl-6-methoxyphenol hydroxylase activity; IEA:InterPro.
DR GO; GO:0106364; F:4-hydroxy-3-all-trans-hexaprenylbenzoate oxygenase activity; IEA:RHEA.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
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:InterPro.
DR GO; GO:0006744; P:ubiquinone biosynthetic process; IBA:GO_Central.
DR Gene3D; 3.50.50.60; -; 2.
DR HAMAP; MF_03193; COQ6_monooxygenase; 1.
DR InterPro; IPR002938; FAD-bd.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR018168; Ubi_Hdrlase_CS.
DR InterPro; IPR010971; UbiH/COQ6.
DR InterPro; IPR000689; UbQ_mOase_COQ6.
DR Pfam; PF01494; FAD_binding_3; 2.
DR SUPFAM; SSF51905; SSF51905; 1.
DR TIGRFAMs; TIGR01989; COQ6; 1.
DR TIGRFAMs; TIGR01988; Ubi-OHases; 1.
DR PROSITE; PS01304; UBIH; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell projection; Deafness; Disease variant; FAD;
KW Flavoprotein; Golgi apparatus; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Monooxygenase; Oxidoreductase;
KW Primary mitochondrial disease; Reference proteome; Transit peptide;
KW Ubiquinone biosynthesis.
FT TRANSIT 1..28
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 29..468
FT /note="Ubiquinone biosynthesis monooxygenase COQ6,
FT mitochondrial"
FT /id="PRO_0000207583"
FT VAR_SEQ 2..119
FT /note="AARLVSRCGAVRAAPHSGPLVSWRRWSGASTDTVYDVVVSGGGLVGAAMACA
FT LGYDIHFHDKKILLLEAGPKKVLEKLSETYSNRVSSISPGSATLLSSFGAWDHICNMRY
FT RAFRRMQ -> IFTFMTRKSCCSKQVQRKYWRNCQKLTATGSAPFPLALQRFSV (in
FT isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_044060"
FT VAR_SEQ 2..54
FT /note="AARLVSRCGAVRAAPHSGPLVSWRRWSGASTDTVYDVVVSGGGLVGAAMACA
FT L -> RGQGPPLSSFGVWLASRAASDPSRPRRQ (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044061"
FT VAR_SEQ 460..461
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_044062"
FT VARIANT 208
FT /note="D -> H (probable disease-associated variant found in
FT patients with Schwannomatosis; loss of function;
FT dbSNP:rs606231262)"
FT /evidence="ECO:0000269|PubMed:24763291"
FT /id="VAR_075225"
FT VARIANT 255
FT /note="G -> R (in COQ10D6; dbSNP:rs1057519350)"
FT /evidence="ECO:0000269|PubMed:21540551"
FT /id="VAR_068216"
FT VARIANT 261
FT /note="P -> L (in COQ10D6; unknown pathological
FT significance; dbSNP:rs371260604)"
FT /evidence="ECO:0000269|PubMed:28044327"
FT /id="VAR_078122"
FT VARIANT 287
FT /note="E -> K (in dbSNP:rs17851169)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_068217"
FT VARIANT 300
FT /note="D -> Y (in dbSNP:rs1044640)"
FT /id="VAR_052691"
FT VARIANT 339
FT /note="D -> V (in dbSNP:rs2074930)"
FT /id="VAR_033813"
FT VARIANT 353
FT /note="A -> D (in COQ10D6; dbSNP:rs397514479)"
FT /evidence="ECO:0000269|PubMed:21540551"
FT /id="VAR_068218"
FT VARIANT 395
FT /note="T -> M (in dbSNP:rs34746680)"
FT /id="VAR_033814"
FT VARIANT 406
FT /note="V -> M (in dbSNP:rs8500)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_014953"
FT CONFLICT 22..30
FT /note="VSWRRWSGA -> AVLAQVVRR (in Ref. 1; AAD27719)"
FT /evidence="ECO:0000305"
FT CONFLICT 317
FT /note="A -> P (in Ref. 1; AAD27719)"
FT /evidence="ECO:0000305"
FT CONFLICT 336..337
FT /note="AR -> PW (in Ref. 1; AAD27719)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 468 AA; 50870 MW; 9613629BA501B60B CRC64;
MAARLVSRCG AVRAAPHSGP LVSWRRWSGA STDTVYDVVV SGGGLVGAAM ACALGYDIHF
HDKKILLLEA GPKKVLEKLS ETYSNRVSSI SPGSATLLSS FGAWDHICNM RYRAFRRMQV
WDACSEALIM FDKDNLDDMG YIVENDVIMH ALTKQLEAVS DRVTVLYRSK AIRYTWPCPF
PMADSSPWVH ITLGDGSTFQ TKLLIGADGH NSGVRQAVGI QNVSWNYDQS AVVATLHLSE
ATENNVAWQR FLPSGPIALL PLSDTLSSLV WSTSHEHAAE LVSMDEEKFV DAVNSAFWSD
ADHTDFIDTA GAMLQYAVSL LKPTKVSARQ LPPSVARVDA KSRVLFPLGL GHAAEYVRPR
VALIGDAAHR VHPLAGQGVN MGFGDISSLA HHLSTAAFNG KDLGSVSHLT GYETERQRHN
TALLAATDLL KRLYSTSASP LVLLRTWGLQ ATNAVSPLKE QIMAFASK
