COQ6_RAT
ID COQ6_RAT Reviewed; 476 AA.
AC Q68FU7;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 113.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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 [3]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
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).
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, ECO:0000269|PubMed:21540551}. Note=Localizes to cell
CC processes and Golgi apparatus in podocytes. {ECO:0000255|HAMAP-
CC Rule:MF_03193, ECO:0000269|PubMed:21540551}.
CC -!- TISSUE SPECIFICITY: In the kidney, expressed almost exclusively in
CC glomerular podocytes. In the inner ear, expressed in the spiral
CC ganglion, as well as in stria vascularis and spiral ligament cells.
CC {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; CH473982; EDL81500.1; -; Genomic_DNA.
DR EMBL; BC079342; AAH79342.1; -; mRNA.
DR RefSeq; NP_001011983.1; NM_001011983.1.
DR AlphaFoldDB; Q68FU7; -.
DR SMR; Q68FU7; -.
DR STRING; 10116.ENSRNOP00000014914; -.
DR PhosphoSitePlus; Q68FU7; -.
DR PaxDb; Q68FU7; -.
DR PRIDE; Q68FU7; -.
DR Ensembl; ENSRNOT00000014913; ENSRNOP00000014914; ENSRNOG00000011164.
DR GeneID; 299195; -.
DR KEGG; rno:299195; -.
DR UCSC; RGD:1311149; rat.
DR CTD; 51004; -.
DR RGD; 1311149; Coq6.
DR eggNOG; KOG3855; Eukaryota.
DR GeneTree; ENSGT00390000015152; -.
DR HOGENOM; CLU_009665_8_0_1; -.
DR InParanoid; Q68FU7; -.
DR OMA; SDVACII; -.
DR OrthoDB; 655400at2759; -.
DR PhylomeDB; Q68FU7; -.
DR TreeFam; TF105772; -.
DR UniPathway; UPA00232; -.
DR PRO; PR:Q68FU7; -.
DR Proteomes; UP000002494; Chromosome 6.
DR Proteomes; UP000234681; Chromosome 6.
DR Bgee; ENSRNOG00000011164; Expressed in heart and 20 other tissues.
DR Genevisible; Q68FU7; RN.
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:RGD.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0110142; C:ubiquinone biosynthesis complex; ISO:RGD.
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 2: Evidence at transcript 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..42
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03193"
FT CHAIN 43..476
FT /note="Ubiquinone biosynthesis monooxygenase COQ6,
FT mitochondrial"
FT /id="PRO_0000418621"
SQ SEQUENCE 476 AA; 51496 MW; CD4D2BC7D7C03880 CRC64;
MAARIGPMAG LLCVRWWSTA QLAARGGPLV ACRRWTSSST DSVYDVVVSG GGMVGSAMAC
ALGHDIHFHD KKILLLEAGP KKTLEKLSET YSNRVSSISL GSTTLLSSFG AWDHICNMRC
KAFRRMQVWD SCSEALIMFD KDNLDDMGYI VENDVIMHAI TKQLEAVADR VKVLYESKAV
GYAWPGPFSL ADSSPWVHIT LGDGSTLQTK LLIGADGHNS GVRQAAGIQN VGWNYDQSAV
VATLHLSEAT ENNVAWQRFL PSGPIALLPL SDTLSSLVWS TSHAHAAELV SMHEEEFVDA
INSAFWSDVH HTDFVDSASA MVHHAVALLK PTKVSARQLP PSVAKVDAKS RALFPLGLGH
AAEYVRPRVA LIGDAAHRVH PLAGQGVNMG FGDISSLIHY LSTAAFNGKD LGSMSHLTGY
ETDRQRHNTA LLAATDLLKR LYSTSTTPLV LLRTWGLQAT NAVSPLKEQI MAFASR
