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Protein/nucleic acid deglycase DJ-1 (EC 3.1.2.-) (EC 3.5.1.-) (EC 3.5.1.124) (Maillard deglycase) (Parkinson disease protein 7 homolog) (Parkinsonism-associated deglycase) (Protein DJ-1) (DJ-1)

 PARK7_CHICK             Reviewed;         189 AA.
Q8UW59;
17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
01-MAR-2002, sequence version 1.
10-OCT-2018, entry version 89.
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=3.5.1.124 {ECO:0000250|UniProtKB:Q99497};
AltName: Full=Maillard deglycase {ECO:0000250|UniProtKB:Q99497};
AltName: Full=Parkinson disease protein 7 homolog {ECO:0000305};
AltName: Full=Parkinsonism-associated deglycase {ECO:0000250|UniProtKB:Q99497};
AltName: Full=Protein DJ-1 {ECO:0000250|UniProtKB:Q99497};
Short=DJ-1;
Flags: Precursor;
Name=PARK7 {ECO:0000250|UniProtKB:Q99497};
Gallus gallus (Chicken).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes;
Phasianidae; Phasianinae; Gallus.
NCBI_TaxID=9031;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=15976810; DOI=10.1038/sj.cdd.4401704;
Shinbo Y., Niki T., Taira T., Ooe H., Takahashi-Niki K., Maita C.,
Seino C., Iguchi-Ariga S.M.M., Ariga H.;
"Proper SUMO-1 conjugation is essential to DJ-1 to exert its full
activities.";
Cell Death Differ. 13:96-108(2006).
-!- 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. It is involved in neuroprotective
mechanisms as well as cell growth and transformation. Its
involvement in protein repair could also explain other unrelated
functions. 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. Regulates astrocyte inflammatory
responses, may modulate lipid rafts-dependent endocytosis in
astrocytes and neuronal cells. 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).
{ECO:0000250|UniProtKB:Q99497, ECO:0000250|UniProtKB:Q99LX0}.
-!- CATALYTIC ACTIVITY: An N(omega)-(1-hydroxy-2-oxopropyl)-[protein]-
L-arginine + H(2)O = a [protein]-L-arginine + lactate.
{ECO:0000250|UniProtKB:Q99497}.
-!- CATALYTIC ACTIVITY: An N(6)-(1-hydroxy-2-oxopropyl)-[protein]-L-
lysine + H(2)O = a [protein]-L-lysine + lactate.
{ECO:0000250|UniProtKB:Q99497}.
-!- CATALYTIC ACTIVITY: An S-(1-hydroxy-2-oxopropyl)-[protein]-L-
cysteine + H(2)O = a [protein]-L-cysteine + lactate.
{ECO:0000250|UniProtKB:Q99497}.
-!- CATALYTIC ACTIVITY: An N(omega)-(1-hydroxy-2-oxoethyl)-[protein]-
L-arginine + H(2)O = a [protein]-L-arginine + glycolate.
{ECO:0000250|UniProtKB:Q99497}.
-!- CATALYTIC ACTIVITY: An N(6)-(1-hydroxy-2-oxoethyl)-[protein]-L-
lysine + H(2)O = a [protein]-L-lysine + glycolate.
{ECO:0000250|UniProtKB:Q99497}.
-!- CATALYTIC ACTIVITY: An S-(1-hydroxy-2-oxoethyl)-[protein]-L-
cysteine + H(2)O = a [protein]-L-cysteine + glycolate.
{ECO:0000250|UniProtKB:Q99497}.
-!- CATALYTIC ACTIVITY: N(2)-(1-hydroxy-2-oxopropyl)-dGTP + H(2)O =
dGTP + lactate. {ECO:0000250|UniProtKB:Q99497}.
-!- CATALYTIC ACTIVITY: N(2)-(1-hydroxy-2-oxopropyl)-GTP + H(2)O = GTP
+ lactate. {ECO:0000250|UniProtKB:Q99497}.
-!- CATALYTIC ACTIVITY: N(2)-(1-hydroxy-2-oxopropyl)-GDP + H(2)O = GDP
+ lactate. {ECO:0000250|UniProtKB:Q99497}.
-!- CATALYTIC ACTIVITY: N(2)-(1-hydroxy-2-oxopropyl)-GMP + H(2)O = GMP
+ lactate. {ECO:0000250|UniProtKB:Q99497}.
-!- CATALYTIC ACTIVITY: N(2)-(1-hydroxy-2-oxoethyl)-dGTP + H(2)O =
dGTP + glycolate. {ECO:0000250|UniProtKB:Q99497}.
-!- CATALYTIC ACTIVITY: N(2)-(1-hydroxy-2-oxoethyl)-GTP + H(2)O = GTP
+ glycolate. {ECO:0000250|UniProtKB:Q99497}.
-!- CATALYTIC ACTIVITY: N(2)-(1-hydroxy-2-oxoethyl)-GDP + H(2)O = GDP
+ glycolate. {ECO:0000250|UniProtKB:Q99497}.
-!- CATALYTIC ACTIVITY: N(2)-(1-hydroxy-2-oxoethyl)-GMP + H(2)O = GMP
+ glycolate. {ECO:0000250|UniProtKB:Q99497}.
-!- CATALYTIC ACTIVITY: An N(2)-(1-hydroxy-2-oxopropyl)-guanosine in
RNA + H(2)O = a guanosine in RNA + lactate.
{ECO:0000250|UniProtKB:Q99497}.
-!- CATALYTIC ACTIVITY: An N(2)-(1-hydroxy-2-oxopropyl)-2'-
deoxyguanosine in DNA + H(2)O = a 2'-deoxyguanosine in RNA +
lactate. {ECO:0000250|UniProtKB:Q99497}.
-!- CATALYTIC ACTIVITY: An N(2)-(1-hydroxy-2-oxoethyl)-guanosine in
RNA + H(2)O = a guanosine in RNA + glycolate.
{ECO:0000250|UniProtKB:Q99497}.
-!- CATALYTIC ACTIVITY: An N(2)-(1-hydroxy-2-oxoethyl)-2'-
deoxyguanosine in DNA + H(2)O = a 2'-deoxyguanosine in RNA +
glycolate. {ECO:0000250|UniProtKB:Q99497}.
-!- COFACTOR:
Note=Deglycase activity does not require glutathione as a
cofactor, however, glycated glutathione constitutes a PARK7
substrate. {ECO:0000250|UniProtKB:Q99497};
-!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q99497}.
-!- SUBCELLULAR LOCATION: Cell membrane
{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}.
-!- PTM: Sumoylated on Lys-130; which is essential for cell-growth
promoting activity and transforming activity.
{ECO:0000250|UniProtKB:Q99497}.
-!- PTM: Undergoes cleavage of a C-terminal peptide and subsequent
activation of protease activity in response to oxidative stress.
{ECO:0000250|UniProtKB:Q99497}.
-!- SIMILARITY: Belongs to the peptidase C56 family. {ECO:0000305}.
-!- CAUTION: Glyoxylase activity previously reported may reflect in
fact 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.
{ECO:0000250|UniProtKB:Q99497}.
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EMBL; AB076264; BAB79527.1; -; mRNA.
RefSeq; NP_989916.1; NM_204585.1.
UniGene; Gga.3836; -.
ProteinModelPortal; Q8UW59; -.
SMR; Q8UW59; -.
BioGrid; 675570; 1.
STRING; 9031.ENSGALP00000000741; -.
MEROPS; C56.971; -.
PaxDb; Q8UW59; -.
PRIDE; Q8UW59; -.
GeneID; 395277; -.
KEGG; gga:395277; -.
CTD; 11315; -.
eggNOG; KOG2764; Eukaryota.
eggNOG; COG0693; LUCA.
HOGENOM; HOG000063194; -.
HOVERGEN; HBG053511; -.
InParanoid; Q8UW59; -.
KO; K05687; -.
PhylomeDB; Q8UW59; -.
PRO; PR:Q8UW59; -.
Proteomes; UP000000539; Unplaced.
GO; GO:0005737; C:cytoplasm; ISS:AgBase.
GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; ISS:AgBase.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0098793; C:presynapse; IEA:GOC.
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:0008344; P:adult locomotory behavior; ISS:AgBase.
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:0006281; P:DNA repair; ISS:UniProtKB.
GO; GO:0051583; P:dopamine uptake involved in synaptic transmission; ISS:AgBase.
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:0060548; P:negative regulation of cell death; 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:0043523; P:regulation of neuron apoptotic process; ISS:UniProtKB.
GO; GO:0042542; P:response to hydrogen peroxide; ISS:AgBase.
GO; GO:0007338; P:single fertilization; IEA:UniProtKB-KW.
GO; GO:0001963; P:synaptic transmission, dopaminergic; ISS:AgBase.
Gene3D; 3.40.50.880; -; 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.
2: Evidence at transcript level;
Acetylation; Autophagy; Cell membrane; Chaperone; Complete proteome;
Copper; Cytoplasm; 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.
/FTId=PRO_0000252486.
PROPEP ? 189 Removed in mature form.
/FTId=PRO_0000405562.
ACT_SITE 106 106 Nucleophile.
{ECO:0000250|UniProtKB:Q99497}.
ACT_SITE 126 126 {ECO:0000250|UniProtKB:Q99497}.
MOD_RES 67 67 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q99497}.
MOD_RES 106 106 Cysteine sulfinic acid (-SO2H);
alternate.
{ECO:0000250|UniProtKB:Q99497}.
MOD_RES 148 148 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q99LX0}.
MOD_RES 182 182 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q99LX0}.
LIPID 46 46 S-palmitoyl cysteine.
{ECO:0000250|UniProtKB:Q99497}.
LIPID 53 53 S-palmitoyl cysteine.
{ECO:0000250|UniProtKB:Q99497}.
LIPID 106 106 S-palmitoyl cysteine; alternate.
{ECO:0000250|UniProtKB:Q99497}.
CROSSLNK 130 130 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000250|UniProtKB:Q99497}.
SEQUENCE 189 AA; 19943 MW; A39FE229D97DB942 CRC64;
MASKRALVIL AKGAEEMETV IPTDVMRRAG IKVTVAGLTG KEPVQCSRDV LICPDASLED
ARKEGPYDVI VLPGGNLGAQ NLSESAAVKD ILKDQESRKG LIAAICAGPT ALLAHGIGFG
SKVITHPLAK DKMMNGAHYC YSESRVEKDG NILTSRGPGT SFEFGLAIVE ALMGKEVAEQ
VKAPLILKD


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