COQ2_RAT
ID COQ2_RAT Reviewed; 374 AA.
AC Q499N4;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 95.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
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 [2]
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).
RN [3]
RP FUNCTION.
RX PubMed=22387164; DOI=10.1016/j.yjmcc.2012.02.005;
RA Gharib A., De Paulis D., Li B., Augeul L., Couture-Lepetit E., Gomez L.,
RA Angoulvant D., Ovize M.;
RT "Opposite and tissue-specific effects of coenzyme Q2 on mPTP opening and
RT ROS production between heart and liver mitochondria: role of complex I.";
RL J. Mol. Cell. Cardiol. 52:1091-1095(2012).
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 group (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 (By
CC similarity). CoQ9 is a vital molecule that transports electrons from
CC mitochondrial respiratory chain complexes (By similarity). CoQs also
CC function as cofactors for uncoupling protein and plays a role as
CC regulator 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 (PubMed:22387164).
CC {ECO:0000250|UniProtKB:Q66JT7, ECO:0000250|UniProtKB:Q96H96,
CC ECO:0000269|PubMed:20526342, ECO:0000269|PubMed:22387164}.
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:0000250|UniProtKB:Q96H96};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44565;
CC Evidence={ECO:0000250|UniProtKB:Q96H96};
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}.
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DR EMBL; BC099827; AAH99827.1; -; mRNA.
DR RefSeq; NP_001037720.1; NM_001044255.1.
DR AlphaFoldDB; Q499N4; -.
DR SMR; Q499N4; -.
DR STRING; 10116.ENSRNOP00000002987; -.
DR PhosphoSitePlus; Q499N4; -.
DR PaxDb; Q499N4; -.
DR PRIDE; Q499N4; -.
DR GeneID; 498332; -.
DR KEGG; rno:498332; -.
DR CTD; 27235; -.
DR RGD; 1306722; Coq2.
DR eggNOG; KOG1381; Eukaryota.
DR InParanoid; Q499N4; -.
DR OrthoDB; 1343847at2759; -.
DR PhylomeDB; Q499N4; -.
DR BRENDA; 2.5.1.39; 5301.
DR Reactome; R-RNO-1268020; Mitochondrial protein import.
DR Reactome; R-RNO-2142789; Ubiquinol biosynthesis.
DR UniPathway; UPA00232; -.
DR PRO; PR:Q499N4; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0031305; C:integral component of mitochondrial inner membrane; ISS:UniProtKB.
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:RGD.
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:RGD.
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..63
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03189"
FT CHAIN 64..374
FT /note="4-hydroxybenzoate polyprenyltransferase,
FT mitochondrial"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03189"
FT /id="PRO_0000228625"
FT TOPO_DOM 64..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..153
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:Q96H96"
FT TRANSMEM 154..174
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03189"
FT TOPO_DOM 175..176
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:Q96H96"
FT TRANSMEM 177..197
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03189"
FT TOPO_DOM 198..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..300
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:Q96H96"
FT TRANSMEM 301..321
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03189"
FT TOPO_DOM 322..332
FT /note="Mitochondrial matrix"
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 intermembrane"
FT /evidence="ECO:0000250|UniProtKB:Q96H96"
SQ SEQUENCE 374 AA; 40406 MW; E464573BC4989C14 CRC64;
MLRLGGAGLV RGLRVVSPAW LRGPGGLPLA LARTTGTSGA RDRRAPASGT QRGRALSLSA
AAVVNSAPRP LQPYLRLMRL DKPIGTWLLY LPCTWSIGLA ADPGCFPDWY MLSLFGTGAI
LMRGAGCTIN DMWDRDFDKK VERTANRPIA AGDISAFQSF VFLGAQLTLA LGVLLHLNYY
SIAMGAASLL LVVTYPLMKR VTFWPQLALG LTFNWGALLG WSAVKGSCDP AVCLPLYFSG
VMWTLIYDTI YAHQDKKDDA LIGLKSTALL FRENTKQWLS GFGVAMVGAL SLVGASSGQT
LPYYAAVAAV GAHLAHQIYT VDIHRAEDCW EKFTSNRTVG LLLFLGIVLG NLYKDKPDET
KGVDAVGEES ERTS
