COQ3_MOUSE
ID COQ3_MOUSE Reviewed; 370 AA.
AC Q8BMS4; Q3TCX5; Q6P918; Q8BM28;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Ubiquinone biosynthesis O-methyltransferase, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03190};
DE AltName: Full=3-demethylubiquinol 3-O-methyltransferase {ECO:0000255|HAMAP-Rule:MF_03190};
DE EC=2.1.1.64 {ECO:0000255|HAMAP-Rule:MF_03190};
DE AltName: Full=Polyprenyldihydroxybenzoate methyltransferase {ECO:0000255|HAMAP-Rule:MF_03190};
DE EC=2.1.1.114 {ECO:0000255|HAMAP-Rule:MF_03190};
DE Flags: Precursor;
GN Name=Coq3 {ECO:0000255|HAMAP-Rule:MF_03190};
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=Skin, and Urinary bladder;
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 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Pancreas, Spleen,
RC 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 [4]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-144; LYS-150 AND LYS-197, AND
RP IDENTIFICATION BY MASS 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).
CC -!- FUNCTION: O-methyltransferase that catalyzes the 2 O-methylation steps
CC in the ubiquinone biosynthetic pathway. {ECO:0000255|HAMAP-
CC Rule:MF_03190}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3,4-dihydroxy-5-all-trans-polyprenylbenzoate + S-adenosyl-L-
CC methionine = 3-methoxy,4-hydroxy-5-all-trans-polyprenylbenzoate +
CC H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:44452, Rhea:RHEA-
CC COMP:10930, Rhea:RHEA-COMP:10931, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:64694,
CC ChEBI:CHEBI:84443; EC=2.1.1.114; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_03190};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 3-demethylubiquinol + S-adenosyl-L-methionine = a ubiquinol
CC + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:44380, Rhea:RHEA-
CC COMP:9566, Rhea:RHEA-COMP:10914, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17976, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:84422; EC=2.1.1.64; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_03190};
CC -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_03190}.
CC -!- SUBUNIT: Component of a multi-subunit COQ enzyme complex, composed of
CC at least COQ3, COQ4, COQ5, COQ6, COQ7 and COQ9. {ECO:0000255|HAMAP-
CC Rule:MF_03190}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_03190}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_03190}; Matrix side {ECO:0000255|HAMAP-Rule:MF_03190}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. UbiG/COQ3 family. {ECO:0000255|HAMAP-Rule:MF_03190}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC29030.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK028680; BAC26063.1; -; mRNA.
DR EMBL; AK035318; BAC29030.1; ALT_INIT; mRNA.
DR EMBL; AK170488; BAE41830.1; -; mRNA.
DR EMBL; BC060960; AAH60960.1; -; mRNA.
DR CCDS; CCDS18003.1; -.
DR RefSeq; NP_766275.1; NM_172687.1.
DR RefSeq; XP_006537871.1; XM_006537808.2.
DR AlphaFoldDB; Q8BMS4; -.
DR SMR; Q8BMS4; -.
DR BioGRID; 230924; 5.
DR ComplexPortal; CPX-3662; CoQ biosynthetic complex.
DR IntAct; Q8BMS4; 1.
DR MINT; Q8BMS4; -.
DR STRING; 10090.ENSMUSP00000029909; -.
DR iPTMnet; Q8BMS4; -.
DR PhosphoSitePlus; Q8BMS4; -.
DR SwissPalm; Q8BMS4; -.
DR EPD; Q8BMS4; -.
DR jPOST; Q8BMS4; -.
DR MaxQB; Q8BMS4; -.
DR PaxDb; Q8BMS4; -.
DR PeptideAtlas; Q8BMS4; -.
DR PRIDE; Q8BMS4; -.
DR ProteomicsDB; 283353; -.
DR Antibodypedia; 31993; 173 antibodies from 22 providers.
DR DNASU; 230027; -.
DR Ensembl; ENSMUST00000029909; ENSMUSP00000029909; ENSMUSG00000028247.
DR GeneID; 230027; -.
DR KEGG; mmu:230027; -.
DR UCSC; uc008sdj.1; mouse.
DR CTD; 51805; -.
DR MGI; MGI:101813; Coq3.
DR VEuPathDB; HostDB:ENSMUSG00000028247; -.
DR eggNOG; KOG1270; Eukaryota.
DR GeneTree; ENSGT00390000007284; -.
DR HOGENOM; CLU_042432_0_1_1; -.
DR InParanoid; Q8BMS4; -.
DR OMA; RGTHDWE; -.
DR OrthoDB; 1542938at2759; -.
DR PhylomeDB; Q8BMS4; -.
DR TreeFam; TF314553; -.
DR Reactome; R-MMU-2142789; Ubiquinol biosynthesis.
DR UniPathway; UPA00232; -.
DR BioGRID-ORCS; 230027; 14 hits in 74 CRISPR screens.
DR ChiTaRS; Coq3; mouse.
DR PRO; PR:Q8BMS4; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q8BMS4; protein.
DR Bgee; ENSMUSG00000028247; Expressed in soleus muscle and 245 other tissues.
DR Genevisible; Q8BMS4; MM.
DR GO; GO:0031314; C:extrinsic component of mitochondrial inner membrane; IEA:UniProtKB-UniRule.
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:0008425; F:2-polyprenyl-6-methoxy-1,4-benzoquinone methyltransferase activity; IEA:InterPro.
DR GO; GO:0008689; F:3-demethylubiquinone-9 3-O-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0004395; F:hexaprenyldihydroxybenzoate methyltransferase activity; ISO:MGI.
DR GO; GO:0008168; F:methyltransferase activity; IBA:GO_Central.
DR GO; GO:0008171; F:O-methyltransferase activity; ISO:MGI.
DR GO; GO:0006071; P:glycerol metabolic process; ISO:MGI.
DR GO; GO:0032259; P:methylation; ISO:MGI.
DR GO; GO:0010795; P:regulation of ubiquinone biosynthetic process; ISO:MGI.
DR GO; GO:0006744; P:ubiquinone biosynthetic process; ISO:MGI.
DR Gene3D; 3.40.50.150; -; 1.
DR HAMAP; MF_00472; UbiG; 1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR010233; UbiG_MeTrfase.
DR SUPFAM; SSF53335; SSF53335; 1.
DR TIGRFAMs; TIGR01983; UbiG; 1.
PE 1: Evidence at protein level;
KW Acetylation; Membrane; Methyltransferase; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; S-adenosyl-L-methionine;
KW Transferase; Transit peptide; Ubiquinone biosynthesis.
FT TRANSIT 1..86
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03190"
FT CHAIN 87..370
FT /note="Ubiquinone biosynthesis O-methyltransferase,
FT mitochondrial"
FT /id="PRO_0000035927"
FT REGION 336..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 352..370
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 125
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03190"
FT BINDING 155
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03190"
FT BINDING 176
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03190"
FT BINDING 223
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03190"
FT MOD_RES 144
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 150
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 197
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT CONFLICT 298
FT /note="N -> Y (in Ref. 2; AAH60960)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 370 AA; 40957 MW; 5023BC29E2DB3E45 CRC64;
MWRGGRLGSR GVRLLETLGF GCPSAVAQPP RLTSRSAYSG TQLTRNLQIK PWELGEHGTM
CFRSYRMALS CLSRVKTYRT PWKRLYSTSQ TTVDSREVKN FQALAHTWWD EYGKFAPLHS
MNDLRVPFIR DNLLKTSASH HPGKPLSGMK ILDVGCGGGL LTEPLGRLGA SVVGIDPVAE
NIKIAQHHKS FDPVLDKRIQ YKVCSLEEAV DESAECFDAV VASEVVEHVS HLEMFIQCCY
QVLKPGGSLF ITTVNKTQLS YALGIVFAEQ IAGIVPKGTH TWEKFVSPEK LESILEPNGL
SVETVAGLVY NPFSGYWHWS ENTSLNYAAH AVRSRAQEHQ EPAESALKGE TGALHANTSG
SPSVREEQRT
