COQ5_MOUSE
ID COQ5_MOUSE Reviewed; 327 AA.
AC Q9CXI0; Q9D6Y6; Q9D900;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=2-methoxy-6-polyprenyl-1,4-benzoquinol methylase, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03191};
DE EC=2.1.1.201 {ECO:0000255|HAMAP-Rule:MF_03191};
DE AltName: Full=Ubiquinone biosynthesis methyltransferase COQ5 {ECO:0000255|HAMAP-Rule:MF_03191};
DE Flags: Precursor;
GN Name=Coq5 {ECO:0000255|HAMAP-Rule:MF_03191}; Synonyms=D5Ertd33e;
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; TISSUE=Corpora quadrigemina, Head, Liver, and Pancreas;
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].
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, and Pancreas;
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).
CC -!- FUNCTION: Methyltransferase required for the conversion of 2-
CC polyprenyl-6-methoxy-1,4-benzoquinol (DDMQH2) to 2-polyprenyl-3-methyl-
CC 6-methoxy-1,4-benzoquinol (DMQH2). {ECO:0000255|HAMAP-Rule:MF_03191}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2-methoxy-6-all-trans-polyprenyl-1,4-benzoquinol + S-
CC adenosyl-L-methionine = a 6-methoxy-3-methyl-2-all-trans-polyprenyl-
CC 1,4-benzoquinol + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:28286, Rhea:RHEA-COMP:10858, Rhea:RHEA-COMP:10859,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:84166, ChEBI:CHEBI:84167; EC=2.1.1.201;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03191};
CC -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_03191}.
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_03191}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_03191}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_03191}; Matrix side {ECO:0000255|HAMAP-Rule:MF_03191}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. MenG/UbiE family. {ECO:0000255|HAMAP-Rule:MF_03191}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB26525.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK007496; BAB25069.1; -; mRNA.
DR EMBL; AK009825; BAB26525.1; ALT_FRAME; mRNA.
DR EMBL; AK014348; BAB29289.1; -; mRNA.
DR EMBL; AK045993; BAC32564.1; -; mRNA.
DR EMBL; AK050334; BAC34194.1; -; mRNA.
DR EMBL; BC052345; AAH52345.1; -; mRNA.
DR CCDS; CCDS19585.1; -.
DR RefSeq; NP_080780.1; NM_026504.2.
DR AlphaFoldDB; Q9CXI0; -.
DR SMR; Q9CXI0; -.
DR ComplexPortal; CPX-3662; CoQ biosynthetic complex.
DR STRING; 10090.ENSMUSP00000048001; -.
DR iPTMnet; Q9CXI0; -.
DR PhosphoSitePlus; Q9CXI0; -.
DR EPD; Q9CXI0; -.
DR jPOST; Q9CXI0; -.
DR MaxQB; Q9CXI0; -.
DR PaxDb; Q9CXI0; -.
DR PeptideAtlas; Q9CXI0; -.
DR PRIDE; Q9CXI0; -.
DR ProteomicsDB; 285250; -.
DR Antibodypedia; 45543; 110 antibodies from 21 providers.
DR DNASU; 52064; -.
DR Ensembl; ENSMUST00000040421; ENSMUSP00000048001; ENSMUSG00000041733.
DR GeneID; 52064; -.
DR KEGG; mmu:52064; -.
DR UCSC; uc008zdo.1; mouse.
DR CTD; 84274; -.
DR MGI; MGI:1098643; Coq5.
DR VEuPathDB; HostDB:ENSMUSG00000041733; -.
DR eggNOG; KOG1540; Eukaryota.
DR GeneTree; ENSGT00390000001654; -.
DR HOGENOM; CLU_037990_0_1_1; -.
DR InParanoid; Q9CXI0; -.
DR OMA; VRNFENL; -.
DR OrthoDB; 1125002at2759; -.
DR PhylomeDB; Q9CXI0; -.
DR TreeFam; TF106217; -.
DR BRENDA; 2.1.1.201; 3474.
DR UniPathway; UPA00232; -.
DR BioGRID-ORCS; 52064; 12 hits in 72 CRISPR screens.
DR ChiTaRS; Coq5; mouse.
DR PRO; PR:Q9CXI0; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9CXI0; protein.
DR Bgee; ENSMUSG00000041733; Expressed in hindlimb stylopod muscle and 266 other tissues.
DR ExpressionAtlas; Q9CXI0; baseline and differential.
DR Genevisible; Q9CXI0; 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:0005759; C:mitochondrial matrix; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0110142; C:ubiquinone biosynthesis complex; ISO:MGI.
DR GO; GO:0043333; F:2-octaprenyl-6-methoxy-1,4-benzoquinone methylase activity; ISO:MGI.
DR GO; GO:0008168; F:methyltransferase activity; IBA:GO_Central.
DR GO; GO:0032259; P:methylation; ISO:MGI.
DR GO; GO:0006744; P:ubiquinone biosynthetic process; ISO:MGI.
DR Gene3D; 3.40.50.150; -; 1.
DR HAMAP; MF_01813; MenG_UbiE_methyltr; 1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR004033; UbiE/COQ5_MeTrFase.
DR InterPro; IPR023576; UbiE/COQ5_MeTrFase_CS.
DR Pfam; PF01209; Ubie_methyltran; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR TIGRFAMs; TIGR01934; MenG_MenH_UbiE; 1.
DR PROSITE; PS51608; SAM_MT_UBIE; 1.
DR PROSITE; PS01183; UBIE_1; 1.
DR PROSITE; PS01184; UBIE_2; 1.
PE 1: Evidence at protein level;
KW Membrane; Methyltransferase; Mitochondrion; Mitochondrion inner membrane;
KW Reference proteome; S-adenosyl-L-methionine; Transferase; Transit peptide;
KW Ubiquinone biosynthesis.
FT TRANSIT 1..49
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03191"
FT CHAIN 50..327
FT /note="2-methoxy-6-polyprenyl-1,4-benzoquinol methylase,
FT mitochondrial"
FT /id="PRO_0000228629"
FT BINDING 117
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03191"
FT BINDING 171
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03191"
FT BINDING 199..200
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03191"
FT CONFLICT 12
FT /note="V -> F (in Ref. 1; BAB29289)"
FT /evidence="ECO:0000305"
FT CONFLICT 210
FT /note="F -> L (in Ref. 1; BAB26525)"
FT /evidence="ECO:0000305"
FT CONFLICT 238
FT /note="P -> Q (in Ref. 1; BAB26525)"
FT /evidence="ECO:0000305"
FT CONFLICT 267
FT /note="I -> T (in Ref. 1; BAB26525)"
FT /evidence="ECO:0000305"
FT CONFLICT 272
FT /note="E -> G (in Ref. 1; BAB26525)"
FT /evidence="ECO:0000305"
FT CONFLICT 290
FT /note="K -> E (in Ref. 1; BAB26525)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 327 AA; 37336 MW; BFFD932B22F1A7CB CRC64;
MAAPRCCVLW RVCGRGWWRA TGHCRLPGCH RSWPWATLGT RSLSQEKRAA ETHFGFETVS
EGEKGSKVYQ VFENVAKKYD LMNDMMSLGI HRAWKDLLIR KMHPLPGTQL LDMAGGTGDI
AFRFLSYVQA QHQRRQRRQL RTQQNLSWEE IAKKYQNEED SLGGSLATVC DINREMLKVG
KQKALDQGHT AGLAWVLGDA EELPFDDDSF DVYTIAFGIR NVTHIDQALQ EAHRVLKPGG
RFLCLEFGQV NDPLISRLYD LYSFQVIPVI GEVIAGDWKS YQYLVESIRK FPNQEDFKDM
IEDAGFQRVT YENLTTGIVA IHSGFKL
