COQ9_MOUSE
ID COQ9_MOUSE Reviewed; 313 AA.
AC Q8K1Z0; Q9CT61;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Ubiquinone biosynthesis protein COQ9, mitochondrial;
DE Flags: Precursor;
GN Name=Coq9;
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, and NOD; TISSUE=Visual cortex;
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 MRNA].
RC STRAIN=C57BL/6J; TISSUE=Mammary gland;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-81, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17208939; DOI=10.1074/mcp.m600218-mcp200;
RA Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.;
RT "Mitochondrial phosphoproteome revealed by an improved IMAC method and
RT MS/MS/MS.";
RL Mol. Cell. Proteomics 6:669-676(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-81, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=18614015; DOI=10.1016/j.cell.2008.06.016;
RA Pagliarini D.J., Calvo S.E., Chang B., Sheth S.A., Vafai S.B., Ong S.E.,
RA Walford G.A., Sugiana C., Boneh A., Chen W.K., Hill D.E., Vidal M.,
RA Evans J.G., Thorburn D.R., Carr S.A., Mootha V.K.;
RT "A mitochondrial protein compendium elucidates complex I disease biology.";
RL Cell 134:112-123(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-81, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
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 [7]
RP FUNCTION, PATHWAY, AND DISRUPTION PHENOTYPE.
RX PubMed=23255162; DOI=10.1093/hmg/dds530;
RA Garcia-Corzo L., Luna-Sanchez M., Doerrier C., Garcia J.A., Guaras A.,
RA Acin-Perez R., Bullejos-Peregrin J., Lopez A., Escames G., Enriquez J.A.,
RA Acuna-Castroviejo D., Lopez L.C.;
RT "Dysfunctional Coq9 protein causes predominant encephalomyopathy associated
RT with CoQ deficiency.";
RL Hum. Mol. Genet. 22:1233-1248(2013).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-170, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
RN [9]
RP FUNCTION, AND PATHWAY.
RX PubMed=25339443; DOI=10.1073/pnas.1413128111;
RA Lohman D.C., Forouhar F., Beebe E.T., Stefely M.S., Minogue C.E.,
RA Ulbrich A., Stefely J.A., Sukumar S., Luna-Sanchez M., Jochem A., Lew S.,
RA Seetharaman J., Xiao R., Wang H., Westphall M.S., Wrobel R.L.,
RA Everett J.K., Mitchell J.C., Lopez L.C., Coon J.J., Tong L.,
RA Pagliarini D.J.;
RT "Mitochondrial COQ9 is a lipid-binding protein that associates with COQ7 to
RT enable coenzyme Q biosynthesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:E4697-4705(2014).
CC -!- FUNCTION: Lipid-binding protein involved in the biosynthesis of
CC coenzyme Q, also named ubiquinone, an essential lipid-soluble electron
CC transporter for aerobic cellular respiration (PubMed:25339443). Binds a
CC phospholipid of at least 10 carbons in each acyl group. May be required
CC to present its bound-lipid to COQ7 (By similarity).
CC {ECO:0000250|UniProtKB:O75208, ECO:0000269|PubMed:23255162,
CC ECO:0000269|PubMed:25339443}.
CC -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis.
CC {ECO:0000269|PubMed:23255162, ECO:0000269|PubMed:25339443}.
CC -!- SUBUNIT: Homodimer. Interacts with COQ7.
CC {ECO:0000250|UniProtKB:O75208}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:18614015}.
CC -!- DOMAIN: Structurally similar to the bacterial FadR protein (fatty acid
CC metabolism regulator protein). {ECO:0000250|UniProtKB:O75208}.
CC -!- DISRUPTION PHENOTYPE: Encephalomyopathy due to a widespread coenzyme Q
CC deficiency and accumulation of demethoxyubiquinone. Lethality between 3
CC and 6 months of age, due to neuronal death and demyelinization with
CC severe vacuolization and astrogliosis in the brain.
CC {ECO:0000269|PubMed:23255162}.
CC -!- SIMILARITY: Belongs to the COQ9 family. {ECO:0000305}.
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DR EMBL; AK004527; BAB23347.1; -; mRNA.
DR EMBL; AK154343; BAE32528.1; -; mRNA.
DR EMBL; AK158979; BAE34754.1; -; mRNA.
DR EMBL; BC036386; AAH36386.1; -; mRNA.
DR CCDS; CCDS22550.1; -.
DR RefSeq; NP_080728.1; NM_026452.2.
DR AlphaFoldDB; Q8K1Z0; -.
DR SMR; Q8K1Z0; -.
DR BioGRID; 212531; 28.
DR ComplexPortal; CPX-3662; CoQ biosynthetic complex.
DR STRING; 10090.ENSMUSP00000034234; -.
DR iPTMnet; Q8K1Z0; -.
DR PhosphoSitePlus; Q8K1Z0; -.
DR EPD; Q8K1Z0; -.
DR jPOST; Q8K1Z0; -.
DR MaxQB; Q8K1Z0; -.
DR PaxDb; Q8K1Z0; -.
DR PeptideAtlas; Q8K1Z0; -.
DR PRIDE; Q8K1Z0; -.
DR ProteomicsDB; 285251; -.
DR Antibodypedia; 44070; 122 antibodies from 24 providers.
DR DNASU; 67914; -.
DR Ensembl; ENSMUST00000034234; ENSMUSP00000034234; ENSMUSG00000031782.
DR GeneID; 67914; -.
DR KEGG; mmu:67914; -.
DR UCSC; uc009mxd.1; mouse.
DR CTD; 57017; -.
DR MGI; MGI:1915164; Coq9.
DR VEuPathDB; HostDB:ENSMUSG00000031782; -.
DR eggNOG; KOG2969; Eukaryota.
DR GeneTree; ENSGT00390000009328; -.
DR HOGENOM; CLU_057411_0_2_1; -.
DR InParanoid; Q8K1Z0; -.
DR OMA; WFLAGDK; -.
DR OrthoDB; 1304924at2759; -.
DR PhylomeDB; Q8K1Z0; -.
DR TreeFam; TF324653; -.
DR UniPathway; UPA00232; -.
DR BioGRID-ORCS; 67914; 4 hits in 75 CRISPR screens.
DR ChiTaRS; Coq9; mouse.
DR PRO; PR:Q8K1Z0; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q8K1Z0; protein.
DR Bgee; ENSMUSG00000031782; Expressed in myocardium of ventricle and 259 other tissues.
DR ExpressionAtlas; Q8K1Z0; baseline and differential.
DR Genevisible; Q8K1Z0; MM.
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:0008289; F:lipid binding; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; IMP:MGI.
DR GO; GO:0006744; P:ubiquinone biosynthetic process; IMP:UniProtKB.
DR InterPro; IPR013718; COQ9.
DR InterPro; IPR012762; Ubiq_biosynth_COQ9.
DR PANTHER; PTHR21427; PTHR21427; 1.
DR Pfam; PF08511; COQ9; 1.
DR TIGRFAMs; TIGR02396; diverge_rpsU; 1.
PE 1: Evidence at protein level;
KW Acetylation; Lipid-binding; Mitochondrion; Phosphoprotein;
KW Reference proteome; Transit peptide; Ubiquinone biosynthesis.
FT TRANSIT 1..45
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 46..313
FT /note="Ubiquinone biosynthesis protein COQ9, mitochondrial"
FT /id="PRO_0000228638"
FT REGION 44..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..68
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 236..239
FT /ligand="1,2-diacylglycero-3-phosphoethanolamine"
FT /ligand_id="ChEBI:CHEBI:57613"
FT /evidence="ECO:0000250|UniProtKB:O75208"
FT MOD_RES 81
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17208939,
FT ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:21183079"
FT MOD_RES 170
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT CONFLICT 208
FT /note="I -> N (in Ref. 1; BAB23347)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 313 AA; 35083 MW; 9B8D8FED0724F138 CRC64;
MAATAAVSGV LGRLGWRLLQ LRCLPVARCR PALVPRAFHT AVGFRSSEEQ KQQPPHSSSQ
QHSETQGPEF SRPPPRYTDQ SGEEEEDYES EEQLQHRILT AALEFVPAHG WTAEAIAEGA
QSLGLSSAAA SMFGSDGSEL ILHFVTQCNA RLNQVLEEEQ KLVQLGQAEK RKTDQFLRDA
VETRLRMLIP YIEHWPRALS ILLLPHNIPP SLNLLTSMVD DMWHYAGDQS TDFNWYTRRA
VLAGIYNTTE LVMMQDSSPD FEDTWRFLEN RINDAMNMGH TAKQVKSTGE ALVQGLMGAA
VTLKNLTGLN QRR
