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Protein

Ubiquinone biosynthesis monooxygenase COQ6, mitochondrial

Gene

Coq6

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

FAD-dependent monooxygenase required for the C5-ring hydroxylation during ubiquinone biosynthesis. Catalyzes the hydroxylation of 3-polyprenyl-4-hydroxybenzoic acid to 3-polyprenyl-4,5-dihydroxybenzoic acid. The electrons required for the hydroxylation reaction may be funneled indirectly from NADPH via a ferredoxin/ferredoxin reductase system to COQ6.UniRule annotation

Cofactori

FADUniRule annotation

Pathwayi: ubiquinone biosynthesis

This protein is involved in the pathway ubiquinone biosynthesis, which is part of Cofactor biosynthesis.UniRule annotation
View all proteins of this organism that are known to be involved in the pathway ubiquinone biosynthesis and in Cofactor biosynthesis.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Monooxygenase, Oxidoreductase

Keywords - Biological processi

Ubiquinone biosynthesis

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

UniPathwayiUPA00232.

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquinone biosynthesis monooxygenase COQ6, mitochondrialUniRule annotation (EC:1.14.13.-UniRule annotation)
Alternative name(s):
Coenzyme Q10 monooxygenase 6UniRule annotation
Gene namesi
Name:Coq6UniRule annotation
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 12

Organism-specific databases

MGIiMGI:1924408. Coq6.

Subcellular locationi

GO - Cellular componenti

  • cell projection Source: UniProtKB-SubCell
  • Golgi apparatus Source: UniProtKB-SubCell
  • mitochondrial inner membrane Source: UniProtKB-SubCell
  • mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Golgi apparatus, Membrane, Mitochondrion, Mitochondrion inner membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3535MitochondrionSequence analysisAdd
BLAST
Chaini36 – 476441Ubiquinone biosynthesis monooxygenase COQ6, mitochondrialPRO_0000207584Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei219 – 2191N6-succinyllysineCombined sources

Proteomic databases

EPDiQ8R1S0.
MaxQBiQ8R1S0.
PaxDbiQ8R1S0.
PRIDEiQ8R1S0.

PTM databases

iPTMnetiQ8R1S0.
PhosphoSiteiQ8R1S0.

Expressioni

Tissue specificityi

Expressed in the kidney, in podocytes.1 Publication

Developmental stagei

At 12.5 dpc, expressed in the metanephric mesenchyme. At 16.5 dpc, expressed in the condensing metanephric mesenchyme surrounding the ureter tips. At 18.5 dpc, expressed in whole kidney.1 Publication

Gene expression databases

BgeeiQ8R1S0.
CleanExiMM_COQ6.
ExpressionAtlasiQ8R1S0. baseline and differential.
GenevisibleiQ8R1S0. MM.

Interactioni

Subunit structurei

Component of a multi-subunit COQ enzyme complex, composed of at least COQ3, COQ4, COQ5, COQ6, COQ7 and COQ9. Interacts with ADCK4 and COQ7.UniRule annotation

Protein-protein interaction databases

IntActiQ8R1S0. 1 interaction.
MINTiMINT-4111022.
STRINGi10090.ENSMUSP00000021661.

Structurei

3D structure databases

ProteinModelPortaliQ8R1S0.
SMRiQ8R1S0. Positions 43-471.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the UbiH/COQ6 family.UniRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG3855. Eukaryota.
COG0654. LUCA.
GeneTreeiENSGT00390000015152.
HOGENOMiHOG000255772.
HOVERGENiHBG029533.
InParanoidiQ8R1S0.
KOiK06126.
OMAiDMRLGLC.
OrthoDBiEOG7H793X.
PhylomeDBiQ8R1S0.
TreeFamiTF105772.

Family and domain databases

Gene3Di3.50.50.60. 2 hits.
HAMAPiMF_03193. COQ6_monooxygenase.
InterProiIPR002938. FAD-bd.
IPR023753. FAD/NAD-binding_dom.
IPR018168. Ubi_Hdrlase_CS.
IPR010971. UbiH/COQ6.
IPR000689. UbQ_mOase_COQ6.
[Graphical view]
PfamiPF01494. FAD_binding_3. 2 hits.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 2 hits.
TIGRFAMsiTIGR01989. COQ6. 1 hit.
TIGR01988. Ubi-OHases. 1 hit.
PROSITEiPS01304. UBIH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8R1S0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAARIGSMAG LLCVRWWSSA QLAARGGPLV ASQRWAGSSA DTVYDVVVSG
60 70 80 90 100
GGLVGSAMAC ALGHDIHFHD KKILLLEAGP KKALEKLSET YSNRVSSISP
110 120 130 140 150
GSTTLLSSFG AWDHICNMRC KAFRRMQVWD SCSEALIMFD RDNLDDMGYI
160 170 180 190 200
VENDVIMYAL TKQLEAVADR VKVLYESKAV GYSWPGAFSM ADSSPWVHIT
210 220 230 240 250
LGDGSTLQTK LLIGADGHKS GVRQAAGIQN VSWKYDQSAV VATLHLSEAT
260 270 280 290 300
ENNVAWQRFL PSGPIALLPL SDTLSSLVWS TSHEHAAELV SMDEEEFVDA
310 320 330 340 350
INSAFWSDVH HTDFVDSASA MVRHAVALLK PTKVSARQLP PSIAKVDAKS
360 370 380 390 400
RALFPLGLGH AAEYVRPRVA LIGDAAHRIH PLAGQGVNMG FGDISSLVHH
410 420 430 440 450
LSTAAFNGKD LGSMSHLTGY ETDRQRHNTA LLAATDLLKR LYSTSATPLV
460 470
LLRTWGLQAT NAVSPLKEQI MAFASK
Length:476
Mass (Da):51,393
Last modified:September 5, 2012 - v3
Checksum:iB431032EFE97D9E5
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti33 – 331Q → R in AAH51055 (PubMed:15489334).Curated
Sequence conflicti441 – 4411L → I in BAC37039 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK077863 mRNA. Translation: BAC37039.1.
AK131889 mRNA. Translation: BAE20853.1.
AK167380 mRNA. Translation: BAE39473.1.
AC120402 Genomic DNA. No translation available.
CH466590 Genomic DNA. Translation: EDL02790.1.
BC024135 mRNA. Translation: AAH24135.1.
BC051055 mRNA. Translation: AAH51055.1.
BC132168 mRNA. Translation: AAI32169.1.
BC132170 mRNA. Translation: AAI32171.1.
CCDSiCCDS26044.1.
RefSeqiNP_766170.2. NM_172582.3.
XP_006515762.1. XM_006515699.2.
UniGeneiMm.280062.

Genome annotation databases

EnsembliENSMUST00000021661; ENSMUSP00000021661; ENSMUSG00000021235.
ENSMUST00000110276; ENSMUSP00000105905; ENSMUSG00000021235.
GeneIDi217707.
KEGGimmu:217707.
UCSCiuc007ofb.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK077863 mRNA. Translation: BAC37039.1.
AK131889 mRNA. Translation: BAE20853.1.
AK167380 mRNA. Translation: BAE39473.1.
AC120402 Genomic DNA. No translation available.
CH466590 Genomic DNA. Translation: EDL02790.1.
BC024135 mRNA. Translation: AAH24135.1.
BC051055 mRNA. Translation: AAH51055.1.
BC132168 mRNA. Translation: AAI32169.1.
BC132170 mRNA. Translation: AAI32171.1.
CCDSiCCDS26044.1.
RefSeqiNP_766170.2. NM_172582.3.
XP_006515762.1. XM_006515699.2.
UniGeneiMm.280062.

3D structure databases

ProteinModelPortaliQ8R1S0.
SMRiQ8R1S0. Positions 43-471.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ8R1S0. 1 interaction.
MINTiMINT-4111022.
STRINGi10090.ENSMUSP00000021661.

PTM databases

iPTMnetiQ8R1S0.
PhosphoSiteiQ8R1S0.

Proteomic databases

EPDiQ8R1S0.
MaxQBiQ8R1S0.
PaxDbiQ8R1S0.
PRIDEiQ8R1S0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000021661; ENSMUSP00000021661; ENSMUSG00000021235.
ENSMUST00000110276; ENSMUSP00000105905; ENSMUSG00000021235.
GeneIDi217707.
KEGGimmu:217707.
UCSCiuc007ofb.2. mouse.

Organism-specific databases

CTDi51004.
MGIiMGI:1924408. Coq6.

Phylogenomic databases

eggNOGiKOG3855. Eukaryota.
COG0654. LUCA.
GeneTreeiENSGT00390000015152.
HOGENOMiHOG000255772.
HOVERGENiHBG029533.
InParanoidiQ8R1S0.
KOiK06126.
OMAiDMRLGLC.
OrthoDBiEOG7H793X.
PhylomeDBiQ8R1S0.
TreeFamiTF105772.

Enzyme and pathway databases

UniPathwayiUPA00232.

Miscellaneous databases

NextBioi375980.
PROiQ8R1S0.
SOURCEiSearch...

Gene expression databases

BgeeiQ8R1S0.
CleanExiMM_COQ6.
ExpressionAtlasiQ8R1S0. baseline and differential.
GenevisibleiQ8R1S0. MM.

Family and domain databases

Gene3Di3.50.50.60. 2 hits.
HAMAPiMF_03193. COQ6_monooxygenase.
InterProiIPR002938. FAD-bd.
IPR023753. FAD/NAD-binding_dom.
IPR018168. Ubi_Hdrlase_CS.
IPR010971. UbiH/COQ6.
IPR000689. UbQ_mOase_COQ6.
[Graphical view]
PfamiPF01494. FAD_binding_3. 2 hits.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 2 hits.
TIGRFAMsiTIGR01989. COQ6. 1 hit.
TIGR01988. Ubi-OHases. 1 hit.
PROSITEiPS01304. UBIH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Forelimb, Placenta and Stomach.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Czech II and FVB/N.
    Tissue: Brain, Liver and Mammary tumor.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brown adipose tissue, Heart, Kidney and Liver.
  6. "COQ6 mutations in human patients produce nephrotic syndrome with sensorineural deafness."
    Heeringa S.F., Chernin G., Chaki M., Zhou W., Sloan A.J., Ji Z., Xie L.X., Salviati L., Hurd T.W., Vega-Warner V., Killen P.D., Raphael Y., Ashraf S., Ovunc B., Schoeb D.S., McLaughlin H.M., Airik R., Vlangos C.N.
    , Gbadegesin R., Hinkes B., Saisawat P., Trevisson E., Doimo M., Casarin A., Pertegato V., Giorgi G., Prokisch H., Rotig A., Nurnberg G., Becker C., Wang S., Ozaltin F., Topaloglu R., Bakkaloglu A., Bakkaloglu S.A., Muller D., Beissert A., Mir S., Berdeli A., Varpizen S., Zenker M., Matejas V., Santos-Ocana C., Navas P., Kusakabe T., Kispert A., Akman S., Soliman N.A., Krick S., Mundel P., Reiser J., Nurnberg P., Clarke C.F., Wiggins R.C., Faul C., Hildebrandt F.
    J. Clin. Invest. 121:2013-2024(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  7. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-219, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiCOQ6_MOUSE
AccessioniPrimary (citable) accession number: Q8R1S0
Secondary accession number(s): Q3TJM2, Q80V13, Q8BJY5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2002
Last sequence update: September 5, 2012
Last modified: May 11, 2016
This is version 114 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.