GENTAUR Molecular Products.

 PARK7_CHICK             Reviewed;         189 AA.
 Q8UW59;
 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
 01-MAR-2002, sequence version 1.
 22-NOV-2017, entry version 88.
 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 + (R)-lactate.
     {ECO:0000250|UniProtKB:Q99497}.
 -!- CATALYTIC ACTIVITY: An N(6)-(1-hydroxy-2-oxopropyl)-[protein]-L-
     lysine + H(2)O = a [protein]-L-lysine + (R)-lactate.
     {ECO:0000250|UniProtKB:Q99497}.
 -!- CATALYTIC ACTIVITY: An S-(1-hydroxy-2-oxopropyl)-[protein]-L-
     cysteine + H(2)O = a [protein]-L-cysteine + (R)-lactate.
     {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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