COQ6_MOUSE
ID COQ6_MOUSE Reviewed; 476 AA.
AC Q8R1S0; Q3TJM2; Q80V13; Q8BJY5;
DT 28-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2012, sequence version 3.
DT 03-AUG-2022, entry version 151.
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};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Forelimb, Placenta, and Stomach;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II, and FVB/N; TISSUE=Brain, Liver, and Mammary tumor;
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, and Liver;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
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 [7]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-219, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: FAD-dependent monooxygenase required for the C5-ring
CC hydroxylation during ubiquinone biosynthesis. Catalyzes the
CC hydroxylation of 3-polyprenyl-4-hydroxybenzoic acid to 3-polyprenyl-
CC 4,5-dihydroxybenzoic acid. The electrons required for the hydroxylation
CC reaction may be funneled indirectly from NADPH via a
CC ferredoxin/ferredoxin reductase system to COQ6. {ECO:0000255|HAMAP-
CC Rule:MF_03193}.
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. Interacts with COQ8B
CC and COQ7. {ECO:0000255|HAMAP-Rule:MF_03193}.
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,
CC ECO:0000269|PubMed:21540551}. Cell projection {ECO:0000255|HAMAP-
CC Rule:MF_03193}. Note=Localizes to cell processes and Golgi apparatus in
CC podocytes. {ECO:0000255|HAMAP-Rule:MF_03193}.
CC -!- TISSUE SPECIFICITY: Expressed in the kidney, in podocytes.
CC {ECO:0000269|PubMed:21540551}.
CC -!- DEVELOPMENTAL STAGE: At 12.5 dpc, expressed in the metanephric
CC mesenchyme. At 16.5 dpc, expressed in the condensing metanephric
CC mesenchyme surrounding the ureter tips. At 18.5 dpc, expressed in whole
CC kidney. {ECO:0000269|PubMed:21540551}.
CC -!- SIMILARITY: Belongs to the UbiH/COQ6 family. {ECO:0000255|HAMAP-
CC Rule:MF_03193}.
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DR EMBL; AK077863; BAC37039.1; -; mRNA.
DR EMBL; AK131889; BAE20853.1; -; mRNA.
DR EMBL; AK167380; BAE39473.1; -; mRNA.
DR EMBL; AC120402; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466590; EDL02790.1; -; Genomic_DNA.
DR EMBL; BC024135; AAH24135.1; -; mRNA.
DR EMBL; BC051055; AAH51055.1; -; mRNA.
DR EMBL; BC132168; AAI32169.1; -; mRNA.
DR EMBL; BC132170; AAI32171.1; -; mRNA.
DR CCDS; CCDS26044.1; -.
DR RefSeq; NP_766170.2; NM_172582.3.
DR RefSeq; XP_006515762.1; XM_006515699.2.
DR AlphaFoldDB; Q8R1S0; -.
DR SMR; Q8R1S0; -.
DR BioGRID; 229950; 1.
DR ComplexPortal; CPX-3662; CoQ biosynthetic complex.
DR STRING; 10090.ENSMUSP00000105905; -.
DR iPTMnet; Q8R1S0; -.
DR PhosphoSitePlus; Q8R1S0; -.
DR EPD; Q8R1S0; -.
DR MaxQB; Q8R1S0; -.
DR PaxDb; Q8R1S0; -.
DR PeptideAtlas; Q8R1S0; -.
DR PRIDE; Q8R1S0; -.
DR ProteomicsDB; 284090; -.
DR Antibodypedia; 47346; 202 antibodies from 24 providers.
DR DNASU; 217707; -.
DR Ensembl; ENSMUST00000021661; ENSMUSP00000021661; ENSMUSG00000021235.
DR Ensembl; ENSMUST00000110276; ENSMUSP00000105905; ENSMUSG00000021235.
DR GeneID; 217707; -.
DR KEGG; mmu:217707; -.
DR UCSC; uc007ofb.2; mouse.
DR CTD; 51004; -.
DR MGI; MGI:1924408; Coq6.
DR VEuPathDB; HostDB:ENSMUSG00000021235; -.
DR eggNOG; KOG3855; Eukaryota.
DR GeneTree; ENSGT00390000015152; -.
DR HOGENOM; CLU_009665_8_0_1; -.
DR InParanoid; Q8R1S0; -.
DR OMA; SDVACII; -.
DR OrthoDB; 655400at2759; -.
DR PhylomeDB; Q8R1S0; -.
DR TreeFam; TF105772; -.
DR UniPathway; UPA00232; -.
DR BioGRID-ORCS; 217707; 17 hits in 72 CRISPR screens.
DR ChiTaRS; Coq6; mouse.
DR PRO; PR:Q8R1S0; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q8R1S0; protein.
DR Bgee; ENSMUSG00000021235; Expressed in interventricular septum and 253 other tissues.
DR ExpressionAtlas; Q8R1S0; baseline and differential.
DR Genevisible; Q8R1S0; MM.
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; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0110142; C:ubiquinone biosynthesis complex; ISO:MGI.
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 Cell projection; FAD; Flavoprotein; Golgi apparatus; Membrane;
KW Mitochondrion; Mitochondrion inner membrane; Monooxygenase; Oxidoreductase;
KW Reference proteome; Transit peptide; Ubiquinone biosynthesis.
FT TRANSIT 1..35
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03193"
FT CHAIN 36..476
FT /note="Ubiquinone biosynthesis monooxygenase COQ6,
FT mitochondrial"
FT /id="PRO_0000207584"
FT MOD_RES 219
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT CONFLICT 33
FT /note="Q -> R (in Ref. 4; AAH51055)"
FT /evidence="ECO:0000305"
FT CONFLICT 441
FT /note="L -> I (in Ref. 1; BAC37039)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 476 AA; 51393 MW; B431032EFE97D9E5 CRC64;
MAARIGSMAG LLCVRWWSSA QLAARGGPLV ASQRWAGSSA DTVYDVVVSG GGLVGSAMAC
ALGHDIHFHD KKILLLEAGP KKALEKLSET YSNRVSSISP GSTTLLSSFG AWDHICNMRC
KAFRRMQVWD SCSEALIMFD RDNLDDMGYI VENDVIMYAL TKQLEAVADR VKVLYESKAV
GYSWPGAFSM ADSSPWVHIT LGDGSTLQTK LLIGADGHKS GVRQAAGIQN VSWKYDQSAV
VATLHLSEAT ENNVAWQRFL PSGPIALLPL SDTLSSLVWS TSHEHAAELV SMDEEEFVDA
INSAFWSDVH HTDFVDSASA MVRHAVALLK PTKVSARQLP PSIAKVDAKS RALFPLGLGH
AAEYVRPRVA LIGDAAHRIH PLAGQGVNMG FGDISSLVHH LSTAAFNGKD LGSMSHLTGY
ETDRQRHNTA LLAATDLLKR LYSTSATPLV LLRTWGLQAT NAVSPLKEQI MAFASK
