COQ2_MOUSE
ID COQ2_MOUSE Reviewed; 374 AA.
AC Q66JT7; E9QPH1; Q9D7M9;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=4-hydroxybenzoate polyprenyltransferase, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03189};
DE Short=4-HB polyprenyltransferase {ECO:0000255|HAMAP-Rule:MF_03189};
DE EC=2.5.1.39 {ECO:0000305|PubMed:20526342};
DE AltName: Full=Para-hydroxybenzoate--polyprenyltransferase {ECO:0000255|HAMAP-Rule:MF_03189};
DE Short=PHB:PPT {ECO:0000255|HAMAP-Rule:MF_03189};
DE Short=PHB:polyprenyltransferase {ECO:0000255|HAMAP-Rule:MF_03189};
DE Flags: Precursor;
GN Name=Coq2 {ECO:0000255|HAMAP-Rule:MF_03189};
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=Tongue;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Jaw, and Limb;
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 [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=20526342; DOI=10.1038/nchembio.372;
RA Forsman U., Sjoeberg M., Turunen M., Sindelar P.J.;
RT "4-Nitrobenzoate inhibits coenzyme Q biosynthesis in mammalian cell
RT cultures.";
RL Nat. Chem. Biol. 6:515-517(2010).
CC -!- FUNCTION: Mediates the second step in the final reaction sequence of
CC coenzyme Q (CoQ) biosynthesis (PubMed:20526342). Catalyzes the
CC prenylation of para-hydroxybenzoate (PHB) with an all-trans polyprenyl
CC donor (such as all-trans-nonaprenyl diphosphate) (PubMed:20526342). The
CC length of the polyprenyl side chain varies depending on the species, in
CC humans, the side chain is comprised of 10 isoprenyls producing CoQ10
CC (also known as ubiquinone), whereas rodents predominantly generate CoQ9
CC (PubMed:20526342). However, this specificity is not complete, human
CC tissues have low amounts of CoQ9 and rodent organs contain some CoQ10
CC (By similarity). Plays a central role in the biosynthesis of CoQ9
CC (PubMed:20526342). CoQ9 is a vital molecule that transports electrons
CC from mitochondrial respiratory chain complexes (PubMed:20526342). CoQs
CC also function as cofactors for uncoupling protein and play a role as
CC regulators of the extracellularly-induced ceramide-dependent apoptotic
CC pathway (By similarity). Regulates mitochondrial permeability
CC transition pore (mPTP) opening and ROS production (pivotal events in
CC cell death) in a tissue specific manner (By similarity).
CC {ECO:0000250|UniProtKB:Q499N4, ECO:0000250|UniProtKB:Q96H96,
CC ECO:0000269|PubMed:20526342}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-hydroxybenzoate + an all-trans-polyprenyl diphosphate = a 4-
CC hydroxy-3-all-trans-polyprenylbenzoate + diphosphate;
CC Xref=Rhea:RHEA:44504, Rhea:RHEA-COMP:9514, Rhea:RHEA-COMP:9564,
CC ChEBI:CHEBI:17879, ChEBI:CHEBI:33019, ChEBI:CHEBI:58914,
CC ChEBI:CHEBI:78396; EC=2.5.1.39;
CC Evidence={ECO:0000305|PubMed:20526342};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44505;
CC Evidence={ECO:0000305|PubMed:20526342};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-hydroxybenzoate + all-trans-decaprenyl diphosphate = 4-
CC hydroxy-3-all-trans-decaprenylbenzoate + diphosphate;
CC Xref=Rhea:RHEA:44564, ChEBI:CHEBI:17879, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:60721, ChEBI:CHEBI:84503; EC=2.5.1.39;
CC Evidence={ECO:0000305|PubMed:20526342};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44565;
CC Evidence={ECO:0000305|PubMed:20526342};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-hydroxybenzoate + all-trans-nonaprenyl diphosphate = 4-
CC hydroxy-3-all-trans-nonaprenylbenzoate + diphosphate;
CC Xref=Rhea:RHEA:17709, ChEBI:CHEBI:17879, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58391, ChEBI:CHEBI:84502; EC=2.5.1.39;
CC Evidence={ECO:0000305|PubMed:20526342};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17710;
CC Evidence={ECO:0000305|PubMed:20526342};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03189};
CC -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis.
CC {ECO:0000305|PubMed:20526342}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_03189}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_03189}; Matrix side {ECO:0000255|HAMAP-Rule:MF_03189}.
CC -!- SIMILARITY: Belongs to the UbiA prenyltransferase family.
CC {ECO:0000255|HAMAP-Rule:MF_03189}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB26064.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK009092; BAB26064.1; ALT_SEQ; mRNA.
DR EMBL; AC109196; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC161510; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC080773; AAH80773.1; -; mRNA.
DR CCDS; CCDS19465.1; -.
DR RefSeq; NP_082254.2; NM_027978.2.
DR AlphaFoldDB; Q66JT7; -.
DR SMR; Q66JT7; -.
DR IntAct; Q66JT7; 12.
DR STRING; 10090.ENSMUSP00000031262; -.
DR PhosphoSitePlus; Q66JT7; -.
DR EPD; Q66JT7; -.
DR PaxDb; Q66JT7; -.
DR PRIDE; Q66JT7; -.
DR ProteomicsDB; 285249; -.
DR Antibodypedia; 25200; 60 antibodies from 18 providers.
DR DNASU; 71883; -.
DR Ensembl; ENSMUST00000031262; ENSMUSP00000031262; ENSMUSG00000029319.
DR GeneID; 71883; -.
DR KEGG; mmu:71883; -.
DR UCSC; uc008yhu.2; mouse.
DR CTD; 27235; -.
DR MGI; MGI:1919133; Coq2.
DR VEuPathDB; HostDB:ENSMUSG00000029319; -.
DR eggNOG; KOG1381; Eukaryota.
DR GeneTree; ENSGT00940000153771; -.
DR HOGENOM; CLU_034879_3_3_1; -.
DR InParanoid; Q66JT7; -.
DR OMA; MVVYPYG; -.
DR OrthoDB; 1343847at2759; -.
DR PhylomeDB; Q66JT7; -.
DR TreeFam; TF105873; -.
DR Reactome; R-MMU-1268020; Mitochondrial protein import.
DR Reactome; R-MMU-2142789; Ubiquinol biosynthesis.
DR UniPathway; UPA00232; -.
DR BioGRID-ORCS; 71883; 21 hits in 73 CRISPR screens.
DR ChiTaRS; Coq2; mouse.
DR PRO; PR:Q66JT7; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q66JT7; protein.
DR Bgee; ENSMUSG00000029319; Expressed in heart left ventricle and 70 other tissues.
DR ExpressionAtlas; Q66JT7; baseline and differential.
DR Genevisible; Q66JT7; MM.
DR GO; GO:0031305; C:integral component of mitochondrial inner membrane; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0002083; F:4-hydroxybenzoate decaprenyltransferase activity; ISS:UniProtKB.
DR GO; GO:0047293; F:4-hydroxybenzoate nonaprenyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008412; F:4-hydroxybenzoate octaprenyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0004659; F:prenyltransferase activity; ISO:MGI.
DR GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; IBA:GO_Central.
DR GO; GO:0006071; P:glycerol metabolic process; ISO:MGI.
DR GO; GO:0008299; P:isoprenoid biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006744; P:ubiquinone biosynthetic process; ISS:UniProtKB.
DR CDD; cd13959; PT_UbiA_COQ2; 1.
DR Gene3D; 1.10.357.140; -; 1.
DR HAMAP; MF_01635; UbiA; 1.
DR InterPro; IPR006370; HB_polyprenyltransferase-like.
DR InterPro; IPR039653; Prenyltransferase.
DR InterPro; IPR000537; UbiA_prenyltransferase.
DR InterPro; IPR030470; UbiA_prenylTrfase_CS.
DR InterPro; IPR044878; UbiA_sf.
DR PANTHER; PTHR11048; PTHR11048; 1.
DR Pfam; PF01040; UbiA; 1.
DR TIGRFAMs; TIGR01474; ubiA_proteo; 1.
DR PROSITE; PS00943; UBIA; 1.
PE 1: Evidence at protein level;
KW Isoprene biosynthesis; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Transferase;
KW Transit peptide; Transmembrane; Transmembrane helix;
KW Ubiquinone biosynthesis.
FT TRANSIT 1..34
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03189"
FT CHAIN 35..374
FT /note="4-hydroxybenzoate polyprenyltransferase,
FT mitochondrial"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03189"
FT /id="PRO_0000228624"
FT TOPO_DOM 35..83
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:Q96H96"
FT TRANSMEM 84..104
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03189"
FT TOPO_DOM 105..108
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:Q96H96"
FT TRANSMEM 109..129
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03189"
FT TOPO_DOM 130..148
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:Q96H96"
FT TRANSMEM 149..169
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03189"
FT TOPO_DOM 170..172
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:Q96H96"
FT TRANSMEM 173..193
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03189"
FT TOPO_DOM 194..200
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:Q96H96"
FT TRANSMEM 201..221
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03189"
FT TOPO_DOM 222..230
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:Q96H96"
FT TRANSMEM 231..251
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03189"
FT TOPO_DOM 252..277
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:Q96H96"
FT TRANSMEM 278..298
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03189"
FT TOPO_DOM 299..332
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:Q96H96"
FT TRANSMEM 333..353
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03189"
FT TOPO_DOM 354..374
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:Q96H96"
FT CONFLICT 198
FT /note="V -> M (in Ref. 3; AAH80773)"
FT /evidence="ECO:0000305"
FT CONFLICT 297
FT /note="N -> S (in Ref. 3; AAH80773)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 374 AA; 40504 MW; AD9E9B2644B5501B CRC64;
MLRWGGAGLA RGLRAVRSAW LRGPRGLPLA LVRSAGVPGA RDRRAPAPGT QRGRALSLSA
AAVVNSAPRP LQPYLRLMRL DKPIGTWLLY LPCTWSIGLA ADPGCFPDWY MLSLFGTGAI
LMRGAGCTIN DMWDRDFDKK VTRTANRPIA AGDISTFQSF VFLGGQLTLA LGVLLCLNYY
SIAMGAASLL LVVTYPLVKR ITFWPQLALG LTFNWGALLG WSAVKGSCDP AVCLPLYFSG
VMWTLIYDTI YAHQDKKDDA LIGLKSTALL FQENTRQWLS GFGVAMVAAL SLAGANNGQT
VPYYAAVAAV GAHLAHQIYT VDIHRAEDCW DKFTSNRTVG MLLFLGIVLG NLCKEKTEEA
KDAEAVRVGS EQTS
