COQ7_RAT
ID COQ7_RAT Reviewed; 179 AA.
AC Q63619; O08887;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 3.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=5-demethoxyubiquinone hydroxylase, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03194};
DE Short=DMQ hydroxylase {ECO:0000255|HAMAP-Rule:MF_03194};
DE EC=1.14.99.60 {ECO:0000255|HAMAP-Rule:MF_03194};
DE AltName: Full=Timing protein clk-1 homolog {ECO:0000255|HAMAP-Rule:MF_03194};
DE AltName: Full=Ubiquinone biosynthesis monooxygenase COQ7 {ECO:0000255|HAMAP-Rule:MF_03194};
DE Flags: Fragment;
GN Name=Coq7 {ECO:0000255|HAMAP-Rule:MF_03194};
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 [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Testis;
RX PubMed=8660658; DOI=10.1006/abbi.1996.0255;
RA Jonassen T., Marbois B.N., Kim L., Chin A., Xia Y.-R., Lusis A.J.,
RA Clarke C.F.;
RT "Isolation and sequencing of the rat Coq7 gene and the mapping of mouse
RT Coq7 to chromosome 7.";
RL Arch. Biochem. Biophys. 330:285-289(1996).
RN [2]
RP SEQUENCE REVISION TO 156.
RA Clarke C.F.;
RL Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the hydroxylation of 2-polyprenyl-3-methyl-6-
CC methoxy-1,4-benzoquinol (DMQH2) during ubiquinone biosynthesis. Has
CC also a structural role in the COQ enzyme complex, stabilizing other COQ
CC polypeptides. Involved in lifespan determination in a ubiquinone-
CC independent manner (By similarity). Plays a role in modulating
CC mitochondrial stress responses, acting in the nucleus, perhaps via
CC regulating gene expression, independent of its characterized
CC mitochondrial function in ubiquinone biosynthesis (By similarity).
CC {ECO:0000250|UniProtKB:Q99807, ECO:0000255|HAMAP-Rule:MF_03194}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 6-methoxy-3-methyl-2-all-trans-polyprenyl-1,4-benzoquinol +
CC AH2 + O2 = A + a 3-demethylubiquinol + H2O; Xref=Rhea:RHEA:50908,
CC Rhea:RHEA-COMP:10859, Rhea:RHEA-COMP:10914, ChEBI:CHEBI:13193,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499,
CC ChEBI:CHEBI:84167, ChEBI:CHEBI:84422; EC=1.14.99.60;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03194};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03194};
CC Note=Binds 2 iron ions per subunit. {ECO:0000255|HAMAP-Rule:MF_03194};
CC -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_03194}.
CC -!- SUBUNIT: Component of a multi-subunit COQ enzyme complex, composed of
CC at least COQ3, COQ4, COQ5, COQ6, COQ7 and COQ9. Interacts with COQ8B
CC and COQ6. Interacts with COQ9. {ECO:0000255|HAMAP-Rule:MF_03194}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_03194}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_03194}; Matrix side {ECO:0000255|HAMAP-Rule:MF_03194}.
CC -!- SIMILARITY: Belongs to the COQ7 family. {ECO:0000255|HAMAP-
CC Rule:MF_03194}.
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DR EMBL; CH473956; EDM17705.1; -; Genomic_DNA.
DR EMBL; U46149; AAB51656.1; -; mRNA.
DR PIR; T10806; T10806.
DR AlphaFoldDB; Q63619; -.
DR STRING; 10116.ENSRNOP00000022988; -.
DR iPTMnet; Q63619; -.
DR PhosphoSitePlus; Q63619; -.
DR PaxDb; Q63619; -.
DR PeptideAtlas; Q63619; -.
DR PRIDE; Q63619; -.
DR RGD; 2381; Coq7.
DR eggNOG; KOG4061; Eukaryota.
DR InParanoid; Q63619; -.
DR PhylomeDB; Q63619; -.
DR BRENDA; 1.14.99.60; 5301.
DR UniPathway; UPA00232; -.
DR Proteomes; UP000002494; Unplaced.
DR Proteomes; UP000234681; Chromosome 1.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISO:RGD.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0110142; C:ubiquinone biosynthesis complex; ISO:RGD.
DR GO; GO:0008682; F:3-demethoxyubiquinol 3-hydroxylase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0001306; P:age-dependent response to oxidative stress; ISO:RGD.
DR GO; GO:0034599; P:cellular response to oxidative stress; ISO:RGD.
DR GO; GO:0008340; P:determination of adult lifespan; ISO:RGD.
DR GO; GO:0001701; P:in utero embryonic development; ISO:RGD.
DR GO; GO:0042775; P:mitochondrial ATP synthesis coupled electron transport; ISO:RGD.
DR GO; GO:0070584; P:mitochondrion morphogenesis; ISO:RGD.
DR GO; GO:0001841; P:neural tube formation; ISO:RGD.
DR GO; GO:0022008; P:neurogenesis; ISO:RGD.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR GO; GO:2000377; P:regulation of reactive oxygen species metabolic process; IBA:GO_Central.
DR GO; GO:0022904; P:respiratory electron transport chain; ISO:RGD.
DR GO; GO:0006979; P:response to oxidative stress; ISO:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0006744; P:ubiquinone biosynthetic process; IGI:RGD.
DR CDD; cd01042; DMQH; 1.
DR HAMAP; MF_01658; COQ7; 1.
DR InterPro; IPR009078; Ferritin-like_SF.
DR InterPro; IPR011566; Ubq_synth_Coq7.
DR PANTHER; PTHR11237; PTHR11237; 1.
DR Pfam; PF03232; COQ7; 1.
DR SUPFAM; SSF47240; SSF47240; 1.
PE 2: Evidence at transcript level;
KW Iron; Membrane; Metal-binding; Mitochondrion; Mitochondrion inner membrane;
KW Monooxygenase; Oxidoreductase; Reference proteome; Repeat;
KW Ubiquinone biosynthesis.
FT CHAIN <1..179
FT /note="5-demethoxyubiquinone hydroxylase, mitochondrial"
FT /id="PRO_0000079253"
FT REPEAT 10..91
FT /note="1"
FT REPEAT 92..179
FT /note="2"
FT REGION 10..179
FT /note="2 X approximate tandem repeats"
FT BINDING 22
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03194"
FT BINDING 52
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03194"
FT BINDING 52
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03194"
FT BINDING 55
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03194"
FT BINDING 104
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03194"
FT BINDING 140
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03194"
FT BINDING 140
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03194"
FT BINDING 143
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03194"
FT NON_TER 1
SQ SEQUENCE 179 AA; 20140 MW; DB671199542F7922 CRC64;
MTLDNINRAA VDRIIRVDHA GEYGANRIYA GQMAVLGRTS VGPVIQKMWD QEKNHLKKFN
ELMVAFRVRP TVLMPLWNVA GFALGAGTAL LGKEGGMACT VAVEESIAHH YNNQIRMLME
EDAEKYEELL QVIKQFRDEE LEHHDTGLEH DAELAPAYTL LKRLIQAGCS AAIYLSERF
