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Database: UniProt/SWISS-PROT
Entry: PARK7_CHICK
LinkDB: PARK7_CHICK
Original site: PARK7_CHICK 
ID   PARK7_CHICK             Reviewed;         189 AA.
AC   Q8UW59;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   05-DEC-2018, entry version 91.
DE   RecName: Full=Protein/nucleic acid deglycase DJ-1 {ECO:0000250|UniProtKB:Q99497};
DE            EC=3.1.2.- {ECO:0000250|UniProtKB:Q99497};
DE            EC=3.5.1.- {ECO:0000250|UniProtKB:Q99497};
DE            EC=3.5.1.124 {ECO:0000250|UniProtKB:Q99497};
DE   AltName: Full=Maillard deglycase {ECO:0000250|UniProtKB:Q99497};
DE   AltName: Full=Parkinson disease protein 7 homolog {ECO:0000305};
DE   AltName: Full=Parkinsonism-associated deglycase {ECO:0000250|UniProtKB:Q99497};
DE   AltName: Full=Protein DJ-1 {ECO:0000250|UniProtKB:Q99497};
DE            Short=DJ-1;
DE   Flags: Precursor;
GN   Name=PARK7 {ECO:0000250|UniProtKB:Q99497};
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes;
OC   Phasianidae; Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=15976810; DOI=10.1038/sj.cdd.4401704;
RA   Shinbo Y., Niki T., Taira T., Ooe H., Takahashi-Niki K., Maita C.,
RA   Seino C., Iguchi-Ariga S.M.M., Ariga H.;
RT   "Proper SUMO-1 conjugation is essential to DJ-1 to exert its full
RT   activities.";
RL   Cell Death Differ. 13:96-108(2006).
CC   -!- FUNCTION: Protein and nucleotide deglycase that catalyzes the
CC       deglycation of the Maillard adducts formed between amino groups of
CC       proteins or nucleotides and reactive carbonyl groups of glyoxals.
CC       Thus, functions as a protein deglycase that repairs
CC       methylglyoxal- and glyoxal-glycated proteins, and releases
CC       repaired proteins and lactate or glycolate, respectively.
CC       Deglycates cysteine, arginine and lysine residues in proteins, and
CC       thus reactivates these proteins by reversing glycation by
CC       glyoxals. Acts on early glycation intermediates (hemithioacetals
CC       and aminocarbinols), preventing the formation of advanced
CC       glycation endproducts (AGE) that cause irreversible damage. Also
CC       functions as a nucleotide deglycase able to repair glycated
CC       guanine in the free nucleotide pool (GTP, GDP, GMP, dGTP) and in
CC       DNA and RNA. Is thus involved in a major nucleotide repair system
CC       named guanine glycation repair (GG repair), dedicated to reversing
CC       methylglyoxal and glyoxal damage via nucleotide sanitization and
CC       direct nucleic acid repair. Also displays an apparent glyoxalase
CC       activity that in fact reflects its deglycase activity. Plays an
CC       important role in cell protection against oxidative stress and
CC       cell death acting as oxidative stress sensor and redox-sensitive
CC       chaperone and protease. It is involved in neuroprotective
CC       mechanisms as well as cell growth and transformation. Its
CC       involvement in protein repair could also explain other unrelated
CC       functions. Eliminates hydrogen peroxide and protects cells against
CC       hydrogen peroxide-induced cell death. Required for correct
CC       mitochondrial morphology and function as well as for autophagy of
CC       dysfunctional mitochondria. Regulates astrocyte inflammatory
CC       responses, may modulate lipid rafts-dependent endocytosis in
CC       astrocytes and neuronal cells. Binds to a number of mRNAs
CC       containing multiple copies of GG or CC motifs and partially
CC       inhibits their translation but dissociates following oxidative
CC       stress. Metal-binding protein able to bind copper as well as toxic
CC       mercury ions, enhances the cell protection mechanism against
CC       induced metal toxicity (By similarity).
CC       {ECO:0000250|UniProtKB:Q99497, ECO:0000250|UniProtKB:Q99LX0}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N(omega)-(1-hydroxy-2-oxopropyl)-L-arginyl-
CC         [protein] = H(+) + L-arginyl-[protein] + lactate;
CC         Xref=Rhea:RHEA:49548, Rhea:RHEA-COMP:10532, Rhea:RHEA-
CC         COMP:12428, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:24996, ChEBI:CHEBI:29965, ChEBI:CHEBI:131708;
CC         EC=3.5.1.124; Evidence={ECO:0000250|UniProtKB:Q99497};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N(6)-(1-hydroxy-2-oxopropyl)-L-lysyl-[protein] =
CC         H(+) + L-lysyl-[protein] + lactate; Xref=Rhea:RHEA:49552,
CC         Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:12429, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:29969,
CC         ChEBI:CHEBI:131709; EC=3.5.1.124;
CC         Evidence={ECO:0000250|UniProtKB:Q99497};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + S-(1-hydroxy-2-oxopropyl)-L-cysteinyl-[protein] =
CC         H(+) + L-cysteinyl-[protein] + lactate; Xref=Rhea:RHEA:49556,
CC         Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:12430, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:29950,
CC         ChEBI:CHEBI:131710; EC=3.5.1.124;
CC         Evidence={ECO:0000250|UniProtKB:Q99497};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N(omega)-(1-hydroxy-2-oxoethyl)-L-arginyl-[protein]
CC         = glycolate + H(+) + L-arginyl-[protein]; Xref=Rhea:RHEA:57188,
CC         Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:14844, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:29965,
CC         ChEBI:CHEBI:141553; EC=3.5.1.124;
CC         Evidence={ECO:0000250|UniProtKB:Q99497};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N(6)-(1-hydroxy-2-oxoethyl)-L-lysyl-[protein] =
CC         glycolate + H(+) + L-lysyl-[protein]; Xref=Rhea:RHEA:57192,
CC         Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:14845, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:29969,
CC         ChEBI:CHEBI:141554; EC=3.5.1.124;
CC         Evidence={ECO:0000250|UniProtKB:Q99497};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + S-(1-hydroxy-2-oxoethyl)-L-cysteinyl-[protein] =
CC         glycolate + H(+) + L-cysteinyl-[protein]; Xref=Rhea:RHEA:57196,
CC         Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:14846, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:29950,
CC         ChEBI:CHEBI:141555; EC=3.5.1.124;
CC         Evidence={ECO:0000250|UniProtKB:Q99497};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-dGTP = dGTP + H(+) +
CC         lactate; Xref=Rhea:RHEA:57244, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:61429,
CC         ChEBI:CHEBI:141569; Evidence={ECO:0000250|UniProtKB:Q99497};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-GTP = GTP + H(+) +
CC         lactate; Xref=Rhea:RHEA:57256, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:37565,
CC         ChEBI:CHEBI:141570; Evidence={ECO:0000250|UniProtKB:Q99497};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-GDP = GDP + H(+) +
CC         lactate; Xref=Rhea:RHEA:57260, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:58189,
CC         ChEBI:CHEBI:141573; Evidence={ECO:0000250|UniProtKB:Q99497};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-GMP = GMP + H(+) +
CC         lactate; Xref=Rhea:RHEA:57268, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:58115,
CC         ChEBI:CHEBI:141575; Evidence={ECO:0000250|UniProtKB:Q99497};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N(2)-(1-hydroxy-2-oxoethyl)-dGTP = dGTP + glycolate
CC         + H(+); Xref=Rhea:RHEA:57248, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:61429,
CC         ChEBI:CHEBI:141572; Evidence={ECO:0000250|UniProtKB:Q99497};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N(2)-(1-hydroxy-2-oxoethyl)-GTP = glycolate + GTP +
CC         H(+); Xref=Rhea:RHEA:57252, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:37565,
CC         ChEBI:CHEBI:141571; Evidence={ECO:0000250|UniProtKB:Q99497};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N(2)-(1-hydroxy-2-oxoethyl)-GDP = GDP + glycolate +
CC         H(+); Xref=Rhea:RHEA:57264, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:58189,
CC         ChEBI:CHEBI:141574; Evidence={ECO:0000250|UniProtKB:Q99497};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N(2)-(1-hydroxy-2-oxoethyl)-GMP = glycolate + GMP +
CC         H(+); Xref=Rhea:RHEA:57304, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:58115,
CC         ChEBI:CHEBI:141576; Evidence={ECO:0000250|UniProtKB:Q99497};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an N(2)-(1-hydroxy-2-oxopropyl)-guanosine in RNA + H2O =
CC         a guanosine in RNA + H(+) + lactate; Xref=Rhea:RHEA:57288,
CC         Rhea:RHEA-COMP:14855, Rhea:RHEA-COMP:14858, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:74269,
CC         ChEBI:CHEBI:141580; Evidence={ECO:0000250|UniProtKB:Q99497};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an N(2)-(1-hydroxy-2-oxopropyl)-2'-deoxyguanosine in DNA
CC         + H2O = a 2'-deoxyguanosine in DNA + H(+) + lactate;
CC         Xref=Rhea:RHEA:57300, Rhea:RHEA-COMP:11367, Rhea:RHEA-
CC         COMP:14856, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:24996, ChEBI:CHEBI:85445, ChEBI:CHEBI:141578;
CC         Evidence={ECO:0000250|UniProtKB:Q99497};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an N(2)-(1-hydroxy-2-oxoethyl)-guanosine in RNA + H2O = a
CC         guanosine in RNA + glycolate + H(+); Xref=Rhea:RHEA:57292,
CC         Rhea:RHEA-COMP:14855, Rhea:RHEA-COMP:14859, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:74269,
CC         ChEBI:CHEBI:141581; Evidence={ECO:0000250|UniProtKB:Q99497};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an N(2)-(1-hydroxy-2-oxoethyl)-2'-deoxyguanosine in DNA +
CC         H2O = a 2'-deoxyguanosine in DNA + glycolate + H(+);
CC         Xref=Rhea:RHEA:57296, Rhea:RHEA-COMP:11367, Rhea:RHEA-
CC         COMP:14857, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29805, ChEBI:CHEBI:85445, ChEBI:CHEBI:141579;
CC         Evidence={ECO:0000250|UniProtKB:Q99497};
CC   -!- COFACTOR:
CC       Note=Deglycase activity does not require glutathione as a
CC       cofactor, however, glycated glutathione constitutes a PARK7
CC       substrate. {ECO:0000250|UniProtKB:Q99497};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q99497}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane
CC       {ECO:0000250|UniProtKB:O88767}; Lipid-anchor
CC       {ECO:0000250|UniProtKB:O88767}. Cytoplasm
CC       {ECO:0000250|UniProtKB:Q99497}. Nucleus
CC       {ECO:0000250|UniProtKB:Q99497}. Membrane raft
CC       {ECO:0000250|UniProtKB:O88767}. Mitochondrion
CC       {ECO:0000250|UniProtKB:Q99497}.
CC   -!- PTM: Sumoylated on Lys-130; which is essential for cell-growth
CC       promoting activity and transforming activity.
CC       {ECO:0000250|UniProtKB:Q99497}.
CC   -!- PTM: Undergoes cleavage of a C-terminal peptide and subsequent
CC       activation of protease activity in response to oxidative stress.
CC       {ECO:0000250|UniProtKB:Q99497}.
CC   -!- SIMILARITY: Belongs to the peptidase C56 family. {ECO:0000305}.
CC   -!- CAUTION: Glyoxylase activity previously reported may reflect in
CC       fact its deglycase activity. {ECO:0000250|UniProtKB:Q99497}.
CC   -!- CAUTION: The protein deglycation activity has been ascribed to a
CC       TRIS buffer artifact by a publication, which has then been
CC       rebutted by clear biochemical experiments showing that PARK7 is a
CC       bona fide deglycase. Deglycase activity is even strengthened by a
CC       novel article that reports nucleotide deglycation activity.
CC       {ECO:0000250|UniProtKB:Q99497}.
DR   EMBL; AB076264; BAB79527.1; -; mRNA.
DR   RefSeq; NP_989916.1; NM_204585.1.
DR   UniGene; Gga.3836; -.
DR   ProteinModelPortal; Q8UW59; -.
DR   SMR; Q8UW59; -.
DR   BioGrid; 675570; 1.
DR   STRING; 9031.ENSGALP00000000741; -.
DR   MEROPS; C56.971; -.
DR   PaxDb; Q8UW59; -.
DR   PRIDE; Q8UW59; -.
DR   GeneID; 395277; -.
DR   KEGG; gga:395277; -.
DR   CTD; 11315; -.
DR   eggNOG; KOG2764; Eukaryota.
DR   eggNOG; COG0693; LUCA.
DR   HOGENOM; HOG000063194; -.
DR   HOVERGEN; HBG053511; -.
DR   InParanoid; Q8UW59; -.
DR   KO; K05687; -.
DR   PhylomeDB; Q8UW59; -.
DR   PRO; PR:Q8UW59; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; ISS:AgBase.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:AgBase.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0098793; C:presynapse; IEA:GOC.
DR   GO; GO:0003729; F:mRNA binding; ISS:UniProtKB.
DR   GO; GO:0008233; F:peptidase activity; ISS:UniProtKB.
DR   GO; GO:0036524; F:protein deglycase activity; IBA:GO_Central.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR   GO; GO:0008344; P:adult locomotory behavior; ISS:AgBase.
DR   GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR   GO; GO:0070301; P:cellular response to hydrogen peroxide; ISS:UniProtKB.
DR   GO; GO:0034599; P:cellular response to oxidative stress; ISS:UniProtKB.
DR   GO; GO:0006281; P:DNA repair; ISS:UniProtKB.
DR   GO; GO:0051583; P:dopamine uptake involved in synaptic transmission; ISS:AgBase.
DR   GO; GO:0042593; P:glucose homeostasis; ISS:UniProtKB.
DR   GO; GO:0106044; P:guanine deglycation; ISS:UniProtKB.
DR   GO; GO:0106046; P:guanine deglycation, glyoxal removal; ISS:UniProtKB.
DR   GO; GO:0106045; P:guanine deglycation, methylglyoxal removal; ISS:UniProtKB.
DR   GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR   GO; GO:0030073; P:insulin secretion; ISS:UniProtKB.
DR   GO; GO:0060548; P:negative regulation of cell death; ISS:UniProtKB.
DR   GO; GO:1903427; P:negative regulation of reactive oxygen species biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0002866; P:positive regulation of acute inflammatory response to antigenic stimulus; ISS:UniProtKB.
DR   GO; GO:0033864; P:positive regulation of NAD(P)H oxidase activity; ISS:UniProtKB.
DR   GO; GO:2000277; P:positive regulation of oxidative phosphorylation uncoupler activity; ISS:UniProtKB.
DR   GO; GO:0036529; P:protein deglycation, glyoxal removal; IBA:GO_Central.
DR   GO; GO:0006517; P:protein deglycosylation; ISS:UniProtKB.
DR   GO; GO:0050821; P:protein stabilization; ISS:UniProtKB.
DR   GO; GO:0043523; P:regulation of neuron apoptotic process; ISS:UniProtKB.
DR   GO; GO:0042542; P:response to hydrogen peroxide; ISS:AgBase.
DR   GO; GO:0007338; P:single fertilization; IEA:UniProtKB-KW.
DR   GO; GO:0001963; P:synaptic transmission, dopaminergic; ISS:AgBase.
DR   Gene3D; 3.40.50.880; -; 1.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR006287; DJ-1.
DR   InterPro; IPR002818; DJ-1/PfpI.
DR   Pfam; PF01965; DJ-1_PfpI; 1.
DR   SUPFAM; SSF52317; SSF52317; 1.
DR   TIGRFAMs; TIGR01383; not_thiJ; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Autophagy; Cell membrane; Chaperone; Complete proteome;
KW   Copper; Cytoplasm; Fertilization; Hydrolase; Inflammatory response;
KW   Isopeptide bond; Lipoprotein; Membrane; Mitochondrion; Nucleus;
KW   Oxidation; Palmitate; Phosphoprotein; Protease; Reference proteome;
KW   RNA-binding; Stress response; Tumor suppressor; Ubl conjugation;
KW   Zymogen.
FT   CHAIN         1      ?       Protein/nucleic acid deglycase DJ-1.
FT                                /FTId=PRO_0000252486.
FT   PROPEP        ?    189       Removed in mature form.
FT                                /FTId=PRO_0000405562.
FT   ACT_SITE    106    106       Nucleophile.
FT                                {ECO:0000250|UniProtKB:Q99497}.
FT   ACT_SITE    126    126       {ECO:0000250|UniProtKB:Q99497}.
FT   MOD_RES      67     67       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:Q99497}.
FT   MOD_RES     106    106       Cysteine sulfinic acid (-SO2H);
FT                                alternate.
FT                                {ECO:0000250|UniProtKB:Q99497}.
FT   MOD_RES     148    148       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q99LX0}.
FT   MOD_RES     182    182       N6-succinyllysine.
FT                                {ECO:0000250|UniProtKB:Q99LX0}.
FT   LIPID        46     46       S-palmitoyl cysteine.
FT                                {ECO:0000250|UniProtKB:Q99497}.
FT   LIPID        53     53       S-palmitoyl cysteine.
FT                                {ECO:0000250|UniProtKB:Q99497}.
FT   LIPID       106    106       S-palmitoyl cysteine; alternate.
FT                                {ECO:0000250|UniProtKB:Q99497}.
FT   CROSSLNK    130    130       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO).
FT                                {ECO:0000250|UniProtKB:Q99497}.
SQ   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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