COQ7_CAEEL
ID COQ7_CAEEL Reviewed; 187 AA.
AC P48376;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 150.
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=Clock abnormal protein 1 {ECO:0000312|WormBase:ZC395.2};
DE Short=Protein clk-1 {ECO:0000305};
DE AltName: Full=Ubiquinone biosynthesis monooxygenase COQ7 {ECO:0000255|HAMAP-Rule:MF_03194};
DE Flags: Precursor;
GN Name=clk-1 {ECO:0000255|HAMAP-Rule:MF_03194};
GN ORFNames=ZC395.2 {ECO:0000312|WormBase:ZC395.2};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, MUTAGENESIS OF GLU-148, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=9020081; DOI=10.1126/science.275.5302.980;
RA Ewbank J.J., Barnes T.M., Lakowski B., Lussier M., Bussey H., Hekimi S.;
RT "Structural and functional conservation of the Caenorhabditis elegans
RT timing gene clk-1.";
RL Science 275:980-983(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF 1-MET--ALA-12.
RX PubMed=25961505; DOI=10.1038/ncb3170;
RA Monaghan R.M., Barnes R.G., Fisher K., Andreou T., Rooney N., Poulin G.B.,
RA Whitmarsh A.J.;
RT "A nuclear role for the respiratory enzyme CLK-1 in regulating
RT mitochondrial stress responses and longevity.";
RL Nat. Cell Biol. 17:782-792(2015).
RN [4]
RP FUNCTION.
RX PubMed=30198021; DOI=10.26508/lsa.201800082;
RA Molenaars M., Janssens G.E., Santermans T., Lezzerini M., Jelier R.,
RA MacInnes A.W., Houtkooper R.H.;
RT "Mitochondrial ubiquinone-mediated longevity is marked by reduced
RT cytoplasmic mRNA translation.";
RL Life. Sci Alliance 1:0-0(2018).
CC -!- FUNCTION: Catalyzes the hydroxylation of 2-polyprenyl-3-methyl-6-
CC methoxy-1,4-benzoquinol (DMQH2) during ubiquinone biosynthesis (By
CC similarity). Has also a structural role in the COQ enzyme complex,
CC stabilizing other COQ polypeptides (By similarity). Involved in
CC lifespan determination in a ubiquinone-independent manner (By
CC similarity) (PubMed:9020081, PubMed:25961505). Plays a role in
CC modulating mitochondrial stress responses, acting in the nucleus,
CC perhaps via regulating gene expression, independent of its
CC characterized mitochondrial function in ubiquinone biosynthesis
CC (PubMed:25961505). Plays a role in modulating polyribosome formation
CC (PubMed:30198021). {ECO:0000255|HAMAP-Rule:MF_03194,
CC ECO:0000269|PubMed:25961505, ECO:0000269|PubMed:30198021,
CC ECO:0000269|PubMed:9020081}.
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.
CC {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 Mitochondrion {ECO:0000269|PubMed:25961505}. Nucleus
CC {ECO:0000269|PubMed:25961505}.
CC -!- DISRUPTION PHENOTYPE: Worms show deregulation timing of a wide range of
CC physiological processes. This leads to an average lengthening of the
CC worm's early cell cycles, the embryonic and postembryonic development,
CC and the period of rhythmic adult behaviors.
CC {ECO:0000269|PubMed:9020081}.
CC -!- SIMILARITY: Belongs to the COQ7 family. {ECO:0000255|HAMAP-
CC Rule:MF_03194}.
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DR EMBL; FO080775; CCD66658.1; -; Genomic_DNA.
DR PIR; T27545; T27545.
DR RefSeq; NP_498128.1; NM_065727.3.
DR AlphaFoldDB; P48376; -.
DR SMR; P48376; -.
DR STRING; 6239.ZC395.2; -.
DR EPD; P48376; -.
DR PaxDb; P48376; -.
DR PeptideAtlas; P48376; -.
DR EnsemblMetazoa; ZC395.2.1; ZC395.2.1; WBGene00000536.
DR GeneID; 175729; -.
DR KEGG; cel:CELE_ZC395.2; -.
DR UCSC; ZC395.2; c. elegans.
DR CTD; 175729; -.
DR WormBase; ZC395.2; CE01438; WBGene00000536; clk-1.
DR eggNOG; KOG4061; Eukaryota.
DR GeneTree; ENSGT00390000014520; -.
DR HOGENOM; CLU_071892_2_0_1; -.
DR InParanoid; P48376; -.
DR OMA; HYNDQVR; -.
DR OrthoDB; 1242061at2759; -.
DR PhylomeDB; P48376; -.
DR BioCyc; MetaCyc:MON-13880; -.
DR BRENDA; 1.14.99.60; 1045.
DR UniPathway; UPA00232; -.
DR PRO; PR:P48376; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00000536; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR GO; GO:0031314; C:extrinsic component of mitochondrial inner membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0005743; C:mitochondrial inner membrane; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:WormBase.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
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:0016709; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen; IEA:UniProtKB-UniRule.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:WormBase.
DR GO; GO:0030534; P:adult behavior; IMP:WormBase.
DR GO; GO:0045333; P:cellular respiration; TAS:WormBase.
DR GO; GO:0008340; P:determination of adult lifespan; IMP:UniProtKB.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; IMP:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:WormBase.
DR GO; GO:0006119; P:oxidative phosphorylation; IMP:WormBase.
DR GO; GO:0048520; P:positive regulation of behavior; IMP:WormBase.
DR GO; GO:0051094; P:positive regulation of developmental process; IMP:WormBase.
DR GO; GO:0010628; P:positive regulation of gene expression; IGI:UniProtKB.
DR GO; GO:0040010; P:positive regulation of growth rate; IMP:WormBase.
DR GO; GO:0061063; P:positive regulation of nematode larval development; IGI:UniProtKB.
DR GO; GO:1904808; P:positive regulation of protein oxidation; IGI:UniProtKB.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IMP:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:WormBase.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR GO; GO:2000377; P:regulation of reactive oxygen species metabolic process; IMP:WormBase.
DR GO; GO:0000003; P:reproduction; IMP:WormBase.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IMP:WormBase.
DR GO; GO:0006744; P:ubiquinone biosynthetic process; IDA:WormBase.
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 1: Evidence at protein level;
KW Iron; Membrane; Metal-binding; Mitochondrion; Mitochondrion inner membrane;
KW Monooxygenase; Nucleus; Oxidoreductase; Reference proteome; Repeat;
KW Transit peptide; Ubiquinone biosynthesis.
FT TRANSIT 1..8
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03194"
FT CHAIN 9..187
FT /note="5-demethoxyubiquinone hydroxylase, mitochondrial"
FT /id="PRO_0000079250"
FT REPEAT 28..99
FT /note="1"
FT REPEAT 100..187
FT /note="2"
FT REGION 28..187
FT /note="2 X approximate tandem repeats"
FT BINDING 30
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03194"
FT BINDING 60
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03194"
FT BINDING 60
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03194"
FT BINDING 63
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03194"
FT BINDING 112
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03194"
FT BINDING 148
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03194"
FT BINDING 148
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03194"
FT BINDING 151
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03194"
FT MUTAGEN 1..12
FT /note="Missing: Enhances nuclear localization. Unable to
FT contribute to the mitochondrial role in ubiquinone
FT biosynthesis. Modulates lifespan."
FT /evidence="ECO:0000269|PubMed:25961505"
FT MUTAGEN 148
FT /note="E->K: In e2519; Extension of life-span, longer and
FT more irregular defecation period."
FT /evidence="ECO:0000269|PubMed:9020081"
SQ SEQUENCE 187 AA; 20466 MW; 4EFF688778CE4151 CRC64;
MFRVITRGAH TAASRQALIE KIIRVDHAGE LGADRIYAGQ LAVLQGSSVG SVIKKMWDEE
KEHLDTMERL AAKHNVPHTV FSPVFSVAAY ALGVGSALLG KEGAMACTIA VEELIGQHYN
DQLKELLADD PETHKELLKI LTRLRDEELH HHDTGVEHDG MKAPAYSALK WIIQTGCKGA
IAIAEKI
