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Protein

Ubiquinone biosynthesis protein COQ9, mitochondrial

Gene

Coq9

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

Functioni

Lipid-binding protein involved in the biosynthesis of coenzyme Q, also named ubiquinone, an essential lipid-soluble electron transporter for aerobic cellular respiration (PubMed:25339443). Binds a phospholipid of at least 10 carbons in each acyl group. May be required to present its bound-lipid to COQ7 (By similarity).By similarity2 Publications

Pathwayi

GO - Molecular functioni

GO - Biological processi

  • mitochondrial electron transport, NADH to ubiquinone Source: MGI
  • ubiquinone biosynthetic process Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Ubiquinone biosynthesis

Keywords - Ligandi

Lipid-binding

Enzyme and pathway databases

UniPathwayiUPA00232.

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquinone biosynthesis protein COQ9, mitochondrial
Gene namesi
Name:Coq9
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:1915164. Coq9.

Subcellular locationi

GO - Cellular componenti

  • mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Disruption phenotypei

Encephalomyopathy due to a widespread coenzyme Q deficiency and accumulation of demethoxyubiquinone. Lethality between 3 and 6 months of age, due to neuronal death and demyelinization with severe vacuolization and astrogliosis in the brain.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4545MitochondrionSequence AnalysisAdd
BLAST
Chaini46 – 313268Ubiquinone biosynthesis protein COQ9, mitochondrialPRO_0000228638Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei81 – 811Phosphoserine1 Publication
Modified residuei170 – 1701N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ8K1Z0.
PaxDbiQ8K1Z0.
PRIDEiQ8K1Z0.

PTM databases

PhosphoSiteiQ8K1Z0.

Expressioni

Gene expression databases

BgeeiQ8K1Z0.
CleanExiMM_COQ9.
GenevestigatoriQ8K1Z0.

Interactioni

Subunit structurei

Homodimer. Interacts with COQ7.By similarity

Protein-protein interaction databases

IntActiQ8K1Z0. 1 interaction.
MINTiMINT-1851066.
STRINGi10090.ENSMUSP00000034234.

Structurei

3D structure databases

ProteinModelPortaliQ8K1Z0.
SMRiQ8K1Z0. Positions 88-306.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni236 – 2394Lipid bindingBy similarity

Domaini

Structurally similar to the bacterial FadR protein (fatty acid metabolism regulator protein).By similarity

Sequence similaritiesi

Belongs to the COQ9 family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG5590.
GeneTreeiENSGT00390000009328.
HOGENOMiHOG000231991.
HOVERGENiHBG079760.
InParanoidiQ8K1Z0.
KOiK18587.
OMAiIPYIEKW.
OrthoDBiEOG75B85W.
PhylomeDBiQ8K1Z0.
TreeFamiTF324653.

Family and domain databases

InterProiIPR013718. COQ9.
IPR012762. Ubiq_biosynth_COQ9.
[Graphical view]
PfamiPF08511. COQ9. 1 hit.
[Graphical view]
TIGRFAMsiTIGR02396. diverge_rpsU. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q8K1Z0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAATAAVSGV LGRLGWRLLQ LRCLPVARCR PALVPRAFHT AVGFRSSEEQ
60 70 80 90 100
KQQPPHSSSQ QHSETQGPEF SRPPPRYTDQ SGEEEEDYES EEQLQHRILT
110 120 130 140 150
AALEFVPAHG WTAEAIAEGA QSLGLSSAAA SMFGSDGSEL ILHFVTQCNA
160 170 180 190 200
RLNQVLEEEQ KLVQLGQAEK RKTDQFLRDA VETRLRMLIP YIEHWPRALS
210 220 230 240 250
ILLLPHNIPP SLNLLTSMVD DMWHYAGDQS TDFNWYTRRA VLAGIYNTTE
260 270 280 290 300
LVMMQDSSPD FEDTWRFLEN RINDAMNMGH TAKQVKSTGE ALVQGLMGAA
310
VTLKNLTGLN QRR
Length:313
Mass (Da):35,083
Last modified:October 1, 2002 - v1
Checksum:i9B8D8FED0724F138
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti208 – 2081I → N in BAB23347 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK004527 mRNA. Translation: BAB23347.1.
AK154343 mRNA. Translation: BAE32528.1.
AK158979 mRNA. Translation: BAE34754.1.
BC036386 mRNA. Translation: AAH36386.1.
CCDSiCCDS22550.1.
RefSeqiNP_080728.1. NM_026452.2.
UniGeneiMm.169234.

Genome annotation databases

EnsembliENSMUST00000034234; ENSMUSP00000034234; ENSMUSG00000031782.
GeneIDi67914.
KEGGimmu:67914.
UCSCiuc009mxd.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK004527 mRNA. Translation: BAB23347.1.
AK154343 mRNA. Translation: BAE32528.1.
AK158979 mRNA. Translation: BAE34754.1.
BC036386 mRNA. Translation: AAH36386.1.
CCDSiCCDS22550.1.
RefSeqiNP_080728.1. NM_026452.2.
UniGeneiMm.169234.

3D structure databases

ProteinModelPortaliQ8K1Z0.
SMRiQ8K1Z0. Positions 88-306.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ8K1Z0. 1 interaction.
MINTiMINT-1851066.
STRINGi10090.ENSMUSP00000034234.

PTM databases

PhosphoSiteiQ8K1Z0.

Proteomic databases

MaxQBiQ8K1Z0.
PaxDbiQ8K1Z0.
PRIDEiQ8K1Z0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000034234; ENSMUSP00000034234; ENSMUSG00000031782.
GeneIDi67914.
KEGGimmu:67914.
UCSCiuc009mxd.1. mouse.

Organism-specific databases

CTDi57017.
MGIiMGI:1915164. Coq9.

Phylogenomic databases

eggNOGiCOG5590.
GeneTreeiENSGT00390000009328.
HOGENOMiHOG000231991.
HOVERGENiHBG079760.
InParanoidiQ8K1Z0.
KOiK18587.
OMAiIPYIEKW.
OrthoDBiEOG75B85W.
PhylomeDBiQ8K1Z0.
TreeFamiTF324653.

Enzyme and pathway databases

UniPathwayiUPA00232.

Miscellaneous databases

NextBioi325934.
PROiQ8K1Z0.
SOURCEiSearch...

Gene expression databases

BgeeiQ8K1Z0.
CleanExiMM_COQ9.
GenevestigatoriQ8K1Z0.

Family and domain databases

InterProiIPR013718. COQ9.
IPR012762. Ubiq_biosynth_COQ9.
[Graphical view]
PfamiPF08511. COQ9. 1 hit.
[Graphical view]
TIGRFAMsiTIGR02396. diverge_rpsU. 1 hit.
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 and NOD.
    Tissue: Visual cortex.
  2. "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: C57BL/6J.
    Tissue: Mammary gland.
  3. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-81, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  4. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  5. Cited for: FUNCTION, PATHWAY, DISRUPTION PHENOTYPE.
  6. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
    Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
    Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-170, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  7. Cited for: FUNCTION, PATHWAY.

Entry informationi

Entry nameiCOQ9_MOUSE
AccessioniPrimary (citable) accession number: Q8K1Z0
Secondary accession number(s): Q9CT61
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 21, 2006
Last sequence update: October 1, 2002
Last modified: May 27, 2015
This is version 97 of the entry and version 1 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

External Data

Dasty 3

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 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.