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Protein/nucleic acid deglycase DJ-1 (EC 3.1.2.-) (EC 3.5.1.-) (EC (Contraception-associated protein 1) (Maillard deglycase) (Parkinson disease protein 7 homolog) (Parkinsonism-associated deglycase) (Protein DJ-1) (DJ-1) [Cleaved into: Protein/nucleic acid deglycase DJ-1, N-terminally processed]

 PARK7_MESAU             Reviewed;         189 AA.
17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
01-OCT-2003, sequence version 1.
16-JAN-2019, entry version 73.
RecName: Full=Protein/nucleic acid deglycase DJ-1 {ECO:0000250|UniProtKB:Q99497};
EC=3.1.2.- {ECO:0000250|UniProtKB:Q99497};
EC=3.5.1.- {ECO:0000250|UniProtKB:Q99497};
EC= {ECO:0000250|UniProtKB:Q99497};
AltName: Full=Contraception-associated protein 1 {ECO:0000305};
AltName: Full=Maillard deglycase {ECO:0000250|UniProtKB:Q99497};
AltName: Full=Parkinson disease protein 7 homolog;
AltName: Full=Parkinsonism-associated deglycase {ECO:0000250|UniProtKB:Q99497};
AltName: Full=Protein DJ-1 {ECO:0000250|UniProtKB:Q99497};
RecName: Full=Protein/nucleic acid deglycase DJ-1, N-terminally processed;
Flags: Precursor;
Name=PARK7; Synonyms=CAP1;
Mesocricetus auratus (Golden hamster).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Cricetidae; Cricetinae; Mesocricetus.
PubMed=15112332; DOI=10.1002/mrd.20085;
Siva A.B., Sundareswaran V.R., Yeung C.-H., Cooper T.G., Shivaji S.;
"Hamster contraception associated protein 1 (CAP1).";
Mol. Reprod. Dev. 68:373-383(2004).
PubMed=20400973; DOI=10.1038/aja.2010.19;
Kameshwari D.B., Bhande S., Sundaram C.S., Kota V., Siva A.B.,
Shivaji S.;
"Glucose-regulated protein precursor (GRP78) and tumor rejection
antigen (GP96) are unique to hamster caput epididymal spermatozoa.";
Asian J. Androl. 12:344-355(2010).
-!- FUNCTION: Protein and nucleotide deglycase that catalyzes the
deglycation of the Maillard adducts formed between amino groups of
proteins or nucleotides and reactive carbonyl groups of glyoxals.
Thus, functions as a protein deglycase that repairs
methylglyoxal- and glyoxal-glycated proteins, and releases
repaired proteins and lactate or glycolate, respectively.
Deglycates cysteine, arginine and lysine residues in proteins, and
thus reactivates these proteins by reversing glycation by
glyoxals. Acts on early glycation intermediates (hemithioacetals
and aminocarbinols), preventing the formation of advanced
glycation endproducts (AGE) that cause irreversible damage. Also
functions as a nucleotide deglycase able to repair glycated
guanine in the free nucleotide pool (GTP, GDP, GMP, dGTP) and in
DNA and RNA. Is thus involved in a major nucleotide repair system
named guanine glycation repair (GG repair), dedicated to reversing
methylglyoxal and glyoxal damage via nucleotide sanitization and
direct nucleic acid repair. Also displays an apparent glyoxalase
activity that in fact reflects its deglycase activity. Plays an
important role in cell protection against oxidative stress and
cell death acting as oxidative stress sensor and redox-sensitive
chaperone and protease; functions probably related to its primary
function. It is involved in neuroprotective mechanisms like the
stabilization of NFE2L2 and PINK1 proteins, male fertility as a
positive regulator of androgen signaling pathway as well as cell
growth and transformation through, for instance, the modulation of
NF-kappa-B signaling pathway. Eliminates hydrogen peroxide and
protects cells against hydrogen peroxide-induced cell death.
Required for correct mitochondrial morphology and function as well
as for autophagy of dysfunctional mitochondria. Plays a role in
regulating expression or stability of the mitochondrial uncoupling
proteins SLC25A14 and SLC25A27 in dopaminergic neurons of the
substantia nigra pars compacta and attenuates the oxidative stress
induced by calcium entry into the neurons via L-type channels
during pacemaking. Regulates astrocyte inflammatory responses, may
modulate lipid rafts-dependent endocytosis in astrocytes and
neuronal cells (By similarity). In pancreatic islets, involved in
the maintenance of mitochondrial reactive oxygen species (ROS)
levels and glucose homeostasis in an age- and diet dependent
manner. Protects pancreatic beta cells from cell death induced by
inflammatory and cytotoxic setting (By similarity). Binds to a
number of mRNAs containing multiple copies of GG or CC motifs and
partially inhibits their translation but dissociates following
oxidative stress. Metal-binding protein able to bind copper as
well as toxic mercury ions, enhances the cell protection mechanism
against induced metal toxicity (By similarity). In macrophages,
interacts with the NADPH oxidase subunit NCF1 to direct NADPH
oxidase-dependent ROS production, and protects against sepsis (By
similarity). {ECO:0000250|UniProtKB:Q99497,
Reaction=H2O + N(omega)-(1-hydroxy-2-oxopropyl)-L-arginyl-
[protein] = H(+) + L-arginyl-[protein] + lactate;
Xref=Rhea:RHEA:49548, Rhea:RHEA-COMP:10532, Rhea:RHEA-
COMP:12428, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
ChEBI:CHEBI:24996, ChEBI:CHEBI:29965, ChEBI:CHEBI:131708;
EC=; Evidence={ECO:0000250|UniProtKB:Q99497};
Reaction=H2O + N(6)-(1-hydroxy-2-oxopropyl)-L-lysyl-[protein] =
H(+) + L-lysyl-[protein] + lactate; Xref=Rhea:RHEA:49552,
Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:12429, ChEBI:CHEBI:15377,
ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:29969,
ChEBI:CHEBI:131709; EC=;
Reaction=H2O + S-(1-hydroxy-2-oxopropyl)-L-cysteinyl-[protein] =
H(+) + L-cysteinyl-[protein] + lactate; Xref=Rhea:RHEA:49556,
Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:12430, ChEBI:CHEBI:15377,
ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:29950,
ChEBI:CHEBI:131710; EC=;
Reaction=H2O + N(omega)-(1-hydroxy-2-oxoethyl)-L-arginyl-[protein]
= glycolate + H(+) + L-arginyl-[protein]; Xref=Rhea:RHEA:57188,
Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:14844, ChEBI:CHEBI:15377,
ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:29965,
ChEBI:CHEBI:141553; EC=;
Reaction=H2O + N(6)-(1-hydroxy-2-oxoethyl)-L-lysyl-[protein] =
glycolate + H(+) + L-lysyl-[protein]; Xref=Rhea:RHEA:57192,
Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:14845, ChEBI:CHEBI:15377,
ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:29969,
ChEBI:CHEBI:141554; EC=;
Reaction=H2O + S-(1-hydroxy-2-oxoethyl)-L-cysteinyl-[protein] =
glycolate + H(+) + L-cysteinyl-[protein]; Xref=Rhea:RHEA:57196,
Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:14846, ChEBI:CHEBI:15377,
ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:29950,
ChEBI:CHEBI:141555; EC=;
Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-dGTP = dGTP + H(+) +
lactate; Xref=Rhea:RHEA:57244, ChEBI:CHEBI:15377,
ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:61429,
ChEBI:CHEBI:141569; Evidence={ECO:0000250|UniProtKB:Q99497};
Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-GTP = GTP + H(+) +
lactate; Xref=Rhea:RHEA:57256, ChEBI:CHEBI:15377,
ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:37565,
ChEBI:CHEBI:141570; Evidence={ECO:0000250|UniProtKB:Q99497};
Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-GDP = GDP + H(+) +
lactate; Xref=Rhea:RHEA:57260, ChEBI:CHEBI:15377,
ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:58189,
ChEBI:CHEBI:141573; Evidence={ECO:0000250|UniProtKB:Q99497};
Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-GMP = GMP + H(+) +
lactate; Xref=Rhea:RHEA:57268, ChEBI:CHEBI:15377,
ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:58115,
ChEBI:CHEBI:141575; Evidence={ECO:0000250|UniProtKB:Q99497};
Reaction=H2O + N(2)-(1-hydroxy-2-oxoethyl)-dGTP = dGTP + glycolate
+ H(+); Xref=Rhea:RHEA:57248, ChEBI:CHEBI:15377,
ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:61429,
ChEBI:CHEBI:141572; Evidence={ECO:0000250|UniProtKB:Q99497};
Reaction=H2O + N(2)-(1-hydroxy-2-oxoethyl)-GTP = glycolate + GTP +
H(+); Xref=Rhea:RHEA:57252, ChEBI:CHEBI:15377,
ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:37565,
ChEBI:CHEBI:141571; Evidence={ECO:0000250|UniProtKB:Q99497};
Reaction=H2O + N(2)-(1-hydroxy-2-oxoethyl)-GDP = GDP + glycolate +
H(+); Xref=Rhea:RHEA:57264, ChEBI:CHEBI:15377,
ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:58189,
ChEBI:CHEBI:141574; Evidence={ECO:0000250|UniProtKB:Q99497};
Reaction=H2O + N(2)-(1-hydroxy-2-oxoethyl)-GMP = glycolate + GMP +
H(+); Xref=Rhea:RHEA:57304, ChEBI:CHEBI:15377,
ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:58115,
ChEBI:CHEBI:141576; Evidence={ECO:0000250|UniProtKB:Q99497};
Reaction=an N(2)-(1-hydroxy-2-oxopropyl)-guanosine in RNA + H2O =
a guanosine in RNA + H(+) + lactate; Xref=Rhea:RHEA:57288,
Rhea:RHEA-COMP:14855, Rhea:RHEA-COMP:14858, ChEBI:CHEBI:15377,
ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:74269,
ChEBI:CHEBI:141580; Evidence={ECO:0000250|UniProtKB:Q99497};
Reaction=an N(2)-(1-hydroxy-2-oxopropyl)-2'-deoxyguanosine in DNA
+ H2O = a 2'-deoxyguanosine in DNA + H(+) + lactate;
Xref=Rhea:RHEA:57300, Rhea:RHEA-COMP:11367, Rhea:RHEA-
COMP:14856, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
ChEBI:CHEBI:24996, ChEBI:CHEBI:85445, ChEBI:CHEBI:141578;
Reaction=an N(2)-(1-hydroxy-2-oxoethyl)-guanosine in RNA + H2O = a
guanosine in RNA + glycolate + H(+); Xref=Rhea:RHEA:57292,
Rhea:RHEA-COMP:14855, Rhea:RHEA-COMP:14859, ChEBI:CHEBI:15377,
ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:74269,
ChEBI:CHEBI:141581; Evidence={ECO:0000250|UniProtKB:Q99497};
Reaction=an N(2)-(1-hydroxy-2-oxoethyl)-2'-deoxyguanosine in DNA +
H2O = a 2'-deoxyguanosine in DNA + glycolate + H(+);
Xref=Rhea:RHEA:57296, Rhea:RHEA-COMP:11367, Rhea:RHEA-
COMP:14857, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
ChEBI:CHEBI:29805, ChEBI:CHEBI:85445, ChEBI:CHEBI:141579;
Note=Deglycase activity does not require glutathione as a
cofactor, however, glycated glutathione constitutes a PARK7
substrate. {ECO:0000250|UniProtKB:Q99497};
-!- SUBUNIT: Homodimer. Binds EFCAB6/DJBP and PIAS2. Part of a ternary
complex containing PARK7, EFCAB6/DJBP and AR. Interacts (via N-
terminus) with OTUD7B. Interacts with BBS1, HIPK1, CLCF1 and
MTERF. Forms a complex with PINK1 and PRKN (By similarity).
Interacts (via C-terminus) with NCF1; the interaction is enhanced
by LPS and modulates NCF1 phosphorylation and membrane
translocation (By similarity). {ECO:0000250|UniProtKB:Q99497,
{ECO:0000250|UniProtKB:O88767}; Lipid-anchor
{ECO:0000250|UniProtKB:O88767}. Cytoplasm
{ECO:0000250|UniProtKB:Q99497}. Nucleus
{ECO:0000250|UniProtKB:Q99497}. Membrane raft
{ECO:0000250|UniProtKB:O88767}. Mitochondrion
{ECO:0000250|UniProtKB:Q99497}. Note=Under normal conditions,
located predominantly in the cytoplasm and, to a lesser extent, in
the nucleus and mitochondrion. Translocates to the mitochondrion
and subsequently to the nucleus in response to oxidative stress
and exerts an increased cytoprotective effect against oxidative
damage. Membrane raft localization in astrocytes and neuronal
cells requires palmitoylation. {ECO:0000250|UniProtKB:Q99497}.
-!- TISSUE SPECIFICITY: Detected in liver, heart, spleen and testis
(at protein level). Detected in liver, heart, spleen, kidney,
epididymidis, vas deferens, sperm cells and testis.
-!- PTM: Sumoylated on Lys-130 by PIAS2 or PIAS4; which is essential
for cell-growth promoting activity and transforming activity.
-!- PTM: Undergoes cleavage of a C-terminal peptide and subsequent
activation of protease activity in response to oxidative stress.
-!- SIMILARITY: Belongs to the peptidase C56 family. {ECO:0000305}.
-!- CAUTION: Glyoxylase activity previously reported may reflect its
deglycase activity. {ECO:0000250|UniProtKB:Q99497}.
-!- CAUTION: The protein deglycation activity has been ascribed to a
TRIS buffer artifact by a publication, which has then been
rebutted by clear biochemical experiments showing that PARK7 is a
bona fide deglycase. Deglycase activity is even strengthened by a
novel article that reports nucleotide deglycation activity.
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
EMBL; AJ431372; CAD24072.2; -; mRNA.
RefSeq; NP_001268568.1; NM_001281639.1.
ProteinModelPortal; Q7TQ35; -.
SMR; Q7TQ35; -.
MEROPS; C56.971; -.
PRIDE; Q7TQ35; -.
GeneID; 101826467; -.
CTD; 11315; -.
HOVERGEN; HBG053511; -.
Proteomes; UP000189706; Genome assembly.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; ISS:UniProtKB.
GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0005507; F:copper ion binding; ISS:UniProtKB.
GO; GO:0045340; F:mercury ion binding; ISS:UniProtKB.
GO; GO:0003729; F:mRNA binding; ISS:UniProtKB.
GO; GO:0008233; F:peptidase activity; ISS:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
GO; GO:0070301; P:cellular response to hydrogen peroxide; ISS:UniProtKB.
GO; GO:0034599; P:cellular response to oxidative stress; ISS:UniProtKB.
GO; GO:0010273; P:detoxification of copper ion; ISS:UniProtKB.
GO; GO:0050787; P:detoxification of mercury ion; ISS:UniProtKB.
GO; GO:0006281; P:DNA repair; ISS:UniProtKB.
GO; GO:0042593; P:glucose homeostasis; ISS:UniProtKB.
GO; GO:0106044; P:guanine deglycation; ISS:UniProtKB.
GO; GO:0106046; P:guanine deglycation, glyoxal removal; ISS:UniProtKB.
GO; GO:0106045; P:guanine deglycation, methylglyoxal removal; ISS:UniProtKB.
GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
GO; GO:0030073; P:insulin secretion; ISS:UniProtKB.
GO; GO:0007005; P:mitochondrion organization; ISS:UniProtKB.
GO; GO:0060548; P:negative regulation of cell death; ISS:UniProtKB.
GO; GO:0032091; P:negative regulation of protein binding; ISS:UniProtKB.
GO; GO:1903427; P:negative regulation of reactive oxygen species biosynthetic process; ISS:UniProtKB.
GO; GO:0002866; P:positive regulation of acute inflammatory response to antigenic stimulus; ISS:UniProtKB.
GO; GO:0033864; P:positive regulation of NAD(P)H oxidase activity; ISS:UniProtKB.
GO; GO:2000277; P:positive regulation of oxidative phosphorylation uncoupler activity; ISS:UniProtKB.
GO; GO:0006517; P:protein deglycosylation; ISS:UniProtKB.
GO; GO:0050821; P:protein stabilization; ISS:UniProtKB.
GO; GO:0050727; P:regulation of inflammatory response; ISS:UniProtKB.
GO; GO:0043523; P:regulation of neuron apoptotic process; ISS:UniProtKB.
GO; GO:0007338; P:single fertilization; IEA:UniProtKB-KW.
Gene3D;; -; 1.
InterPro; IPR029062; Class_I_gatase-like.
InterPro; IPR006287; DJ-1.
InterPro; IPR002818; DJ-1/PfpI.
Pfam; PF01965; DJ-1_PfpI; 1.
SUPFAM; SSF52317; SSF52317; 1.
TIGRFAMs; TIGR01383; not_thiJ; 1.
1: Evidence at protein level;
Acetylation; Autophagy; Cell membrane; Chaperone; Complete proteome;
Copper; Cytoplasm; Direct protein sequencing; Fertilization;
Hydrolase; Inflammatory response; Isopeptide bond; Lipoprotein;
Membrane; Mitochondrion; Nucleus; Oxidation; Palmitate;
Phosphoprotein; Protease; Reference proteome; RNA-binding;
Stress response; Tumor suppressor; Ubl conjugation; Zymogen.
CHAIN 1 ? Protein/nucleic acid deglycase DJ-1.
INIT_MET 1 1 Removed; alternate.
CHAIN 2 ? Protein/nucleic acid deglycase DJ-1, N-
terminally processed.
PROPEP ? 189 Removed in mature form.
ACT_SITE 106 106 Nucleophile.
ACT_SITE 126 126 {ECO:0000250|UniProtKB:Q99497}.
MOD_RES 2 2 N-acetylalanine; in Protein/nucleic acid
deglycase DJ-1, N-terminally processed.
MOD_RES 67 67 Phosphotyrosine.
MOD_RES 106 106 Cysteine sulfinic acid (-SO2H);
MOD_RES 148 148 N6-acetyllysine.
MOD_RES 182 182 N6-succinyllysine.
LIPID 46 46 S-palmitoyl cysteine.
LIPID 53 53 S-palmitoyl cysteine.
LIPID 106 106 S-palmitoyl cysteine; alternate.
CROSSLNK 130 130 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
SEQUENCE 189 AA; 19915 MW; D9106615AEDD9ABE CRC64;

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