GenomeNet

Database: UniProt/SWISS-PROT
Entry: PARK7_MOUSE
LinkDB: PARK7_MOUSE
Original site: PARK7_MOUSE 
ID   PARK7_MOUSE             Reviewed;         189 AA.
AC   Q99LX0; O88306; Q3THB9; Q3U509;
DT   07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   05-DEC-2018, entry version 146.
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:0000305};
DE            Short=DJ-1;
DE   Flags: Precursor;
GN   Name=Park7 {ECO:0000312|MGI:MGI:2135637};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Kidney;
RX   PubMed=11223268; DOI=10.1016/S0378-1119(00)00590-4;
RA   Taira T., Takahashi K., Kitagawa R., Iguchi-Ariga S.M.M., Ariga H.;
RT   "Molecular cloning of human and mouse DJ-1 genes and identification of
RT   Sp1-dependent activation of the human DJ-1 promoter.";
RL   Gene 263:285-292(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=BALB/cJ, and NOD; TISSUE=Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PROTEIN SEQUENCE OF 13-27; 63-89 AND 99-122, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RC   TISSUE=Hippocampus;
RA   Lubec G., Klug S.;
RL   Submitted (MAR-2007) to UniProtKB.
RN   [6]
RP   INDUCTION.
RX   PubMed=14749723; DOI=10.1038/sj.embor.7400074;
RA   Taira T., Saito Y., Niki T., Iguchi-Ariga S.M., Takahashi K.,
RA   Ariga H.;
RT   "DJ-1 has a role in antioxidative stress to prevent cell death.";
RL   EMBO Rep. 5:213-218(2004).
RN   [7]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=15784737; DOI=10.1073/pnas.0501282102;
RA   Kim R.H., Smith P.D., Aleyasin H., Hayley S., Mount M.P., Pownall S.,
RA   Wakeham A., You-Ten A.J., Kalia S.K., Horne P., Westaway D.,
RA   Lozano A.M., Anisman H., Park D.S., Mak T.W.;
RT   "Hypersensitivity of DJ-1-deficient mice to 1-methyl-4-phenyl-1,2,3,6-
RT   tetrahydropyrindine (MPTP) and oxidative stress.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:5215-5220(2005).
RN   [8]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=17015834; DOI=10.1073/pnas.0607260103;
RA   Clements C.M., McNally R.S., Conti B.J., Mak T.W., Ting J.P.;
RT   "DJ-1, a cancer- and Parkinson's disease-associated protein,
RT   stabilizes the antioxidant transcriptional master regulator Nrf2.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15091-15096(2006).
RN   [9]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF CYS-46; CYS-53 AND
RP   CYS-106.
RX   PubMed=17766438; DOI=10.1073/pnas.0703219104;
RA   Andres-Mateos E., Perier C., Zhang L., Blanchard-Fillion B.,
RA   Greco T.M., Thomas B., Ko H.S., Sasaki M., Ischiropoulos H.,
RA   Przedborski S., Dawson T.M., Dawson V.L.;
RT   "DJ-1 gene deletion reveals that DJ-1 is an atypical peroxiredoxin-
RT   like peroxidase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:14807-14812(2007).
RN   [10]
RP   FUNCTION.
RX   PubMed=19276172; DOI=10.1096/fj.08-125153;
RA   Waak J., Weber S.S., Waldenmaier A., Gorner K., Alunni-Fabbroni M.,
RA   Schell H., Vogt-Weisenhorn D., Pham T.T., Reumers V., Baekelandt V.,
RA   Wurst W., Kahle P.J.;
RT   "Regulation of astrocyte inflammatory responses by the Parkinson's
RT   disease-associated gene DJ-1.";
RL   FASEB J. 23:2478-2489(2009).
RN   [11]
RP   FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=20800516; DOI=10.1016/j.bcmd.2010.07.014;
RA   Xu X., Martin F., Friedman J.S.;
RT   "The familial Parkinson's disease gene DJ-1 (PARK7) is expressed in
RT   red cells and plays a role in protection against oxidative damage.";
RL   Blood Cells Mol. Dis. 45:227-232(2010).
RN   [12]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and
RT   expression.";
RL   Cell 143:1174-1189(2010).
RN   [13]
RP   INTERACTION WITH BBS1; CLCF1; MTERF AND OTUD7B.
RX   PubMed=21097510; DOI=10.1074/jbc.M110.147371;
RA   McNally R.S., Davis B.K., Clements C.M., Accavitti-Loper M.A.,
RA   Mak T.W., Ting J.P.;
RT   "DJ-1 enhances cell survival through the binding of cezanne, a
RT   negative regulator of NF-{kappa}B.";
RL   J. Biol. Chem. 286:4098-4106(2011).
RN   [14]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=21068725; DOI=10.1038/nature09536;
RA   Guzman J.N., Sanchez-Padilla J., Wokosin D., Kondapalli J., Ilijic E.,
RA   Schumacker P.T., Surmeier D.J.;
RT   "Oxidant stress evoked by pacemaking in dopaminergic neurons is
RT   attenuated by DJ-1.";
RL   Nature 468:696-700(2010).
RN   [15]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=20186336; DOI=10.1371/journal.pone.0009367;
RA   Krebiehl G., Ruckerbauer S., Burbulla L.F., Kieper N., Maurer B.,
RA   Waak J., Wolburg H., Gizatullina Z., Gellerich F.N., Woitalla D.,
RA   Riess O., Kahle P.J., Proikas-Cezanne T., Kruger R.;
RT   "Reduced basal autophagy and impaired mitochondrial dynamics due to
RT   loss of Parkinson's disease-associated protein DJ-1.";
RL   PLoS ONE 5:E9367-E9367(2010).
RN   [16]
RP   FUNCTION, AND CAUTION.
RX   PubMed=22523093; DOI=10.1093/hmg/dds155;
RA   Lee J.Y., Song J., Kwon K., Jang S., Kim C., Baek K., Kim J., Park C.;
RT   "Human DJ-1 and its homologs are novel glyoxalases.";
RL   Hum. Mol. Genet. 21:3215-3225(2012).
RN   [17]
RP   FUNCTION, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=22611253; DOI=10.1093/jmcb/mjs025;
RA   Jain D., Jain R., Eberhard D., Eglinger J., Bugliani M., Piemonti L.,
RA   Marchetti P., Lammert E.;
RT   "Age- and diet-dependent requirement of DJ-1 for glucose homeostasis
RT   in mice with implications for human type 2 diabetes.";
RL   J. Mol. Cell Biol. 4:221-230(2012).
RN   [18]
RP   FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX   PubMed=23847046; DOI=10.1093/hmg/ddt332;
RA   Kim K.S., Kim J.S., Park J.Y., Suh Y.H., Jou I., Joe E.H., Park S.M.;
RT   "DJ-1 associates with lipid rafts by palmitoylation and regulates
RT   lipid rafts-dependent endocytosis in astrocytes.";
RL   Hum. Mol. Genet. 22:4805-4817(2013).
RN   [19]
RP   FUNCTION.
RX   PubMed=23792957; DOI=10.1074/jbc.M113.482091;
RA   Bjorkblom B., Adilbayeva A., Maple-Grodem J., Piston D., Okvist M.,
RA   Xu X.M., Brede C., Larsen J.P., Moller S.G.;
RT   "Parkinson disease protein DJ-1 binds metals and protects against
RT   metal-induced cytotoxicity.";
RL   J. Biol. Chem. 288:22809-22820(2013).
RN   [20]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-148, SUCCINYLATION [LARGE
RP   SCALE ANALYSIS] AT LYS-182, AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA   Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
RA   Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT   "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT   pathways.";
RL   Mol. Cell 50:919-930(2013).
RN   [21]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH NCF1.
RX   PubMed=26021615; DOI=10.1038/cr.2015.63;
RA   Liu W., Wu H., Chen L., Wen Y., Kong X., Gao W.Q.;
RT   "Park7 interacts with p47(phox) to direct NADPH oxidase-dependent ROS
RT   production and protect against sepsis.";
RL   Cell Res. 25:691-706(2015).
RN   [22]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=26422139; DOI=10.1371/journal.pone.0138535;
RA   Jain D., Weber G., Eberhard D., Mehana A.E., Eglinger J., Welters A.,
RA   Bartosinska B., Jeruschke K., Weiss J., Paeth G., Ariga H.,
RA   Seufert J., Lammert E.;
RT   "DJ-1 Protects Pancreatic Beta Cells from Cytokine- and
RT   Streptozotocin-Mediated Cell Death.";
RL   PLoS ONE 10:E0138535-E0138535(2015).
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 (By similarity). Also displays an
CC       apparent glyoxalase activity that in fact reflects its deglycase
CC       activity (PubMed:22523093). Plays an important role in cell
CC       protection against oxidative stress and cell death acting as
CC       oxidative stress sensor and redox-sensitive chaperone and
CC       protease; functions probably related to its primary function
CC       (PubMed:15784737, PubMed:17015834, PubMed:20800516,
CC       PubMed:21068725). It is involved in neuroprotective mechanisms
CC       like the stabilization of NFE2L2 and PINK1 proteins, male
CC       fertility as a positive regulator of androgen signaling pathway as
CC       well as cell growth and transformation through, for instance, the
CC       modulation of NF-kappa-B signaling pathway (PubMed:17015834,
CC       PubMed:21097510). Eliminates hydrogen peroxide and protects cells
CC       against hydrogen peroxide-induced cell death (PubMed:17766438).
CC       Required for correct mitochondrial morphology and function as well
CC       as for autophagy of dysfunctional mitochondria (PubMed:20186336).
CC       Plays a role in regulating expression or stability of the
CC       mitochondrial uncoupling proteins SLC25A14 and SLC25A27 in
CC       dopaminergic neurons of the substantia nigra pars compacta and
CC       attenuates the oxidative stress induced by calcium entry into the
CC       neurons via L-type channels during pacemaking (PubMed:21068725).
CC       Regulates astrocyte inflammatory responses, may modulate lipid
CC       rafts-dependent endocytosis in astrocytes and neuronal cells
CC       (PubMed:23847046, PubMed:19276172). In pancreatic islets, involved
CC       in the maintenance of mitochondrial reactive oxygen species (ROS)
CC       levels and glucose homeostasis in an age- and diet dependent
CC       manner (PubMed:22611253). Protects pancreatic beta cells from cell
CC       death induced by inflammatory and cytotoxic setting
CC       (PubMed:26422139). Binds to a number of mRNAs containing multiple
CC       copies of GG or CC motifs and partially inhibits their translation
CC       but dissociates following oxidative stress (By similarity). Metal-
CC       binding protein able to bind copper as well as toxic mercury ions,
CC       enhances the cell protection mechanism against induced metal
CC       toxicity (PubMed:23792957). In macrophages, interacts with the
CC       NADPH oxidase subunit NCF1 to direct NADPH oxidase-dependent ROS
CC       production, and protects against sepsis (PubMed:26021615).
CC       {ECO:0000250|UniProtKB:Q99497, ECO:0000269|PubMed:15784737,
CC       ECO:0000269|PubMed:17015834, ECO:0000269|PubMed:17766438,
CC       ECO:0000269|PubMed:19276172, ECO:0000269|PubMed:20186336,
CC       ECO:0000269|PubMed:20800516, ECO:0000269|PubMed:21068725,
CC       ECO:0000269|PubMed:22523093, ECO:0000269|PubMed:22611253,
CC       ECO:0000269|PubMed:23792957, ECO:0000269|PubMed:23847046,
CC       ECO:0000269|PubMed:26021615, ECO:0000269|PubMed:26422139}.
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. Binds EFCAB6/DJBP and PIAS2. Part of a ternary
CC       complex containing PARK7, EFCAB6/DJBP and AR. Binds to HIPK1 (By
CC       similarity). Interacts (via N-terminus) with OTUD7B
CC       (PubMed:21097510). Interacts with BBS1, CLCF1 and MTERF
CC       (PubMed:21097510). Interacts (via C-terminus) with NCF1; the
CC       interaction is enhanced by LPS and modulates NCF1 phosphorylation
CC       and membrane translocation (PubMed:26021615).
CC       {ECO:0000250|UniProtKB:Q99497, ECO:0000269|PubMed:21097510,
CC       ECO:0000269|PubMed:26021615}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23847046};
CC       Lipid-anchor {ECO:0000269|PubMed:23847046}. Cytoplasm
CC       {ECO:0000250|UniProtKB:Q99497}. Membrane raft
CC       {ECO:0000269|PubMed:23847046}. Nucleus
CC       {ECO:0000250|UniProtKB:Q99497}. Mitochondrion
CC       {ECO:0000250|UniProtKB:Q99497}. Note=Under normal conditions,
CC       located predominantly in the cytoplasm and, to a lesser extent, in
CC       the nucleus and mitochondrion. Translocates to the mitochondrion
CC       and subsequently to the nucleus in response to oxidative stress
CC       and exerts an increased cytoprotective effect against oxidative
CC       damage (By similarity). Membrane raft localization in astrocytes
CC       and neuronal cells requires palmitoylation (PubMed:23847046).
CC       {ECO:0000250|UniProtKB:Q99497, ECO:0000269|PubMed:23847046}.
CC   -!- TISSUE SPECIFICITY: Expressed in erythroblasts and in mature red
CC       blood cells from peripheral blood (at protein level)
CC       (PubMed:20800516). In pancreas, expression is higher in islets
CC       than surrounding exocrine tissues (PubMed:22611253).
CC       {ECO:0000269|PubMed:20800516, ECO:0000269|PubMed:22611253}.
CC   -!- DEVELOPMENTAL STAGE: Expression increases during erythroid
CC       development (at protein level) (PubMed:20800516). In pancreatic
CC       islets, expression increases during aging (PubMed:22611253).
CC       {ECO:0000269|PubMed:20800516, ECO:0000269|PubMed:22611253}.
CC   -!- INDUCTION: By hydrogen peroxide. {ECO:0000269|PubMed:14749723}.
CC   -!- PTM: Sumoylated on Lys-130 by PIAS2 or PIAS4; which is essential
CC       for cell-growth 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   -!- DISRUPTION PHENOTYPE: Increased sensitivity of embryonic cortical
CC       neurons to oxidative stress. Age-dependent increase in
CC       mitochondrial hydrogen peroxide production and reduced
CC       mitochondrial aconitase activity. Down-regulation of Slc25a14 and
CC       Slc25a27, compromised calcium-induced uncoupling and increased
CC       oxidation of mitochondrial matrix proteins specifically in the
CC       dopaminergic neurons of the substantia nigra pars compacta.
CC       Reduced N2el2 protein expression. Impaired mitochondrial function
CC       and morphology with reduced autophagy leading to accumulation of
CC       defective mitochondria. Targeted knockouts in astrocytes exhibit
CC       augmented LPS-induced CRK/p38 phosphorylation and signaling, they
CC       don't stimulate TLR4 endocytosis upon LPS stimulation. Knockout
CC       animals present increased bacterial burdens, reduced local and
CC       systemic inflammation, macrophage paralysis and impaired induction
CC       of proinflammatory cytokines, such as IL6 and TNF, under the
CC       condition of sepsis (PubMed:26021615). Mutants from 12 weeks old,
CC       but not younger, show higher levels of reactive oxygen species
CC       (ROS) and mitochondrial fragmentation in pancreatic islets. They
CC       have lower levels of plasma insulin after glucose challenge,
CC       display glucose intolerance and have reduced beta-cell area.
CC       Younger mutants kept on a high fat diet also show lower levels of
CC       plasma insulin, display glucose intolerance and have reduced beta-
CC       cell area (PubMed:22611253). Animals become diabetic upon multiple
CC       low doses of streptozotocin with reduced insulin concentrations,
CC       higher fasting blood glucose concentrations and higher rates of
CC       beta cell apoptosis compared to wild type (PubMed:26422139).
CC       {ECO:0000269|PubMed:15784737, ECO:0000269|PubMed:17015834,
CC       ECO:0000269|PubMed:17766438, ECO:0000269|PubMed:20186336,
CC       ECO:0000269|PubMed:21068725, ECO:0000269|PubMed:22611253,
CC       ECO:0000269|PubMed:23847046, ECO:0000269|PubMed:26021615,
CC       ECO:0000269|PubMed:26422139}.
CC   -!- SIMILARITY: Belongs to the peptidase C56 family. {ECO:0000305}.
CC   -!- CAUTION: Glyoxylase activity previously reported may reflect in
CC       fact its deglycase activity (PubMed:22523093).
CC       {ECO:0000250|UniProtKB:Q99497, ECO:0000269|PubMed:22523093}.
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; AB015652; BAA29063.2; -; mRNA.
DR   EMBL; AK146368; BAE27118.1; -; mRNA.
DR   EMBL; AK153948; BAE32271.1; -; mRNA.
DR   EMBL; AK168341; BAE40278.1; -; mRNA.
DR   EMBL; AL607084; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC002187; AAH02187.1; -; mRNA.
DR   CCDS; CCDS18975.1; -.
DR   RefSeq; NP_065594.2; NM_020569.3.
DR   UniGene; Mm.277349; -.
DR   ProteinModelPortal; Q99LX0; -.
DR   SMR; Q99LX0; -.
DR   BioGrid; 208257; 19.
DR   IntAct; Q99LX0; 27.
DR   MINT; Q99LX0; -.
DR   STRING; 10090.ENSMUSP00000030805; -.
DR   MEROPS; C56.002; -.
DR   iPTMnet; Q99LX0; -.
DR   PhosphoSitePlus; Q99LX0; -.
DR   SwissPalm; Q99LX0; -.
DR   REPRODUCTION-2DPAGE; Q99LX0; -.
DR   UCD-2DPAGE; Q99LX0; -.
DR   EPD; Q99LX0; -.
DR   MaxQB; Q99LX0; -.
DR   PaxDb; Q99LX0; -.
DR   PeptideAtlas; Q99LX0; -.
DR   PRIDE; Q99LX0; -.
DR   TopDownProteomics; Q99LX0; -.
DR   Ensembl; ENSMUST00000030805; ENSMUSP00000030805; ENSMUSG00000028964.
DR   Ensembl; ENSMUST00000105673; ENSMUSP00000101298; ENSMUSG00000028964.
DR   Ensembl; ENSMUST00000105674; ENSMUSP00000101299; ENSMUSG00000028964.
DR   Ensembl; ENSMUST00000105675; ENSMUSP00000101300; ENSMUSG00000028964.
DR   GeneID; 57320; -.
DR   KEGG; mmu:57320; -.
DR   UCSC; uc008vxz.2; mouse.
DR   CTD; 11315; -.
DR   MGI; MGI:2135637; Park7.
DR   eggNOG; KOG2764; Eukaryota.
DR   eggNOG; COG0693; LUCA.
DR   GeneTree; ENSGT00390000001231; -.
DR   HOGENOM; HOG000063194; -.
DR   HOVERGEN; HBG053511; -.
DR   InParanoid; Q99LX0; -.
DR   KO; K05687; -.
DR   OMA; CYPGFEK; -.
DR   OrthoDB; EOG091G12NS; -.
DR   PhylomeDB; Q99LX0; -.
DR   TreeFam; TF300119; -.
DR   Reactome; R-MMU-3899300; SUMOylation of transcription cofactors.
DR   PRO; PR:Q99LX0; -.
DR   Proteomes; UP000000589; Chromosome 4.
DR   Bgee; ENSMUSG00000028964; Expressed in 293 organ(s), highest expression level in triceps surae.
DR   ExpressionAtlas; Q99LX0; baseline and differential.
DR   Genevisible; Q99LX0; MM.
DR   GO; GO:0030424; C:axon; ISO:MGI.
DR   GO; GO:0044297; C:cell body; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0000785; C:chromatin; ISO:MGI.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR   GO; GO:0045121; C:membrane raft; ISO:MGI.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0005759; C:mitochondrial matrix; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0005747; C:mitochondrial respiratory chain complex I; IEA:Ensembl.
DR   GO; GO:0005739; C:mitochondrion; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0043005; C:neuron projection; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016605; C:PML body; ISO:MGI.
DR   GO; GO:0098793; C:presynapse; IEA:GOC.
DR   GO; GO:0061827; C:sperm head; ISO:MGI.
DR   GO; GO:0050681; F:androgen receptor binding; ISO:MGI.
DR   GO; GO:0005507; F:copper ion binding; ISS:UniProtKB.
DR   GO; GO:1903135; F:cupric ion binding; ISO:MGI.
DR   GO; GO:1903136; F:cuprous ion binding; ISO:MGI.
DR   GO; GO:0019955; F:cytokine binding; ISO:MGI.
DR   GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0019900; F:kinase binding; ISO:MGI.
DR   GO; GO:0036478; F:L-dopa decarboxylase activator activity; ISO:MGI.
DR   GO; GO:0045340; F:mercury ion binding; ISS:UniProtKB.
DR   GO; GO:0003729; F:mRNA binding; ISS:UniProtKB.
DR   GO; GO:0016684; F:oxidoreductase activity, acting on peroxide as acceptor; ISO:MGI.
DR   GO; GO:0008233; F:peptidase activity; ISS:UniProtKB.
DR   GO; GO:0051920; F:peroxiredoxin activity; IMP:MGI.
DR   GO; GO:0036524; F:protein deglycase activity; ISO:MGI.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR   GO; GO:0070491; F:repressing transcription factor binding; ISO:MGI.
DR   GO; GO:0003723; F:RNA binding; TAS:MGI.
DR   GO; GO:0097110; F:scaffold protein binding; ISO:MGI.
DR   GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR   GO; GO:0044388; F:small protein activating enzyme binding; ISO:MGI.
DR   GO; GO:0016532; F:superoxide dismutase copper chaperone activity; ISO:MGI.
DR   GO; GO:0003713; F:transcription coactivator activity; ISO:MGI.
DR   GO; GO:0008134; F:transcription factor binding; ISO:MGI.
DR   GO; GO:0036470; F:tyrosine 3-monooxygenase activator activity; ISO:MGI.
DR   GO; GO:0044390; F:ubiquitin-like protein conjugating enzyme binding; ISO:MGI.
DR   GO; GO:1990381; F:ubiquitin-specific protease binding; ISO:MGI.
DR   GO; GO:0008344; P:adult locomotory behavior; IMP:MGI.
DR   GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR   GO; GO:0008283; P:cell proliferation; TAS:MGI.
DR   GO; GO:0036471; P:cellular response to glyoxal; IMP:ParkinsonsUK-UCL.
DR   GO; GO:0070301; P:cellular response to hydrogen peroxide; IMP:UniProtKB.
DR   GO; GO:0034599; P:cellular response to oxidative stress; IMP:UniProtKB.
DR   GO; GO:0034614; P:cellular response to reactive oxygen species; IMP:MGI.
DR   GO; GO:0010273; P:detoxification of copper ion; IMP:UniProtKB.
DR   GO; GO:0050787; P:detoxification of mercury ion; IMP:UniProtKB.
DR   GO; GO:0006281; P:DNA repair; ISS:UniProtKB.
DR   GO; GO:0051583; P:dopamine uptake involved in synaptic transmission; IMP:MGI.
DR   GO; GO:0018323; P:enzyme active site formation via L-cysteine sulfinic acid; IMP:ParkinsonsUK-UCL.
DR   GO; GO:0042593; P:glucose homeostasis; IMP:UniProtKB.
DR   GO; GO:0036531; P:glutathione deglycation; ISO:MGI.
DR   GO; GO:0046295; P:glycolate biosynthetic process; IDA:ParkinsonsUK-UCL.
DR   GO; GO:1903189; P:glyoxal metabolic process; IDA:ParkinsonsUK-UCL.
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:0042743; P:hydrogen peroxide metabolic process; IMP:MGI.
DR   GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR   GO; GO:0030073; P:insulin secretion; IMP:UniProtKB.
DR   GO; GO:0019249; P:lactate biosynthetic process; ISO:MGI.
DR   GO; GO:0051899; P:membrane depolarization; IMP:MGI.
DR   GO; GO:0060081; P:membrane hyperpolarization; IMP:MGI.
DR   GO; GO:0007005; P:mitochondrion organization; IMP:UniProtKB.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IMP:ParkinsonsUK-UCL.
DR   GO; GO:0060548; P:negative regulation of cell death; IMP:UniProtKB.
DR   GO; GO:2001268; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway; ISO:MGI.
DR   GO; GO:1902236; P:negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway; IMP:ParkinsonsUK-UCL.
DR   GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; ISO:MGI.
DR   GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI.
DR   GO; GO:1903206; P:negative regulation of hydrogen peroxide-induced cell death; ISO:MGI.
DR   GO; GO:1903208; P:negative regulation of hydrogen peroxide-induced neuron death; IMP:ParkinsonsUK-UCL.
DR   GO; GO:1903384; P:negative regulation of hydrogen peroxide-induced neuron intrinsic apoptotic signaling pathway; IMP:ParkinsonsUK-UCL.
DR   GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISO:MGI.
DR   GO; GO:1901215; P:negative regulation of neuron death; ISO:MGI.
DR   GO; GO:1905259; P:negative regulation of nitrosative stress-induced intrinsic apoptotic signaling pathway; ISO:MGI.
DR   GO; GO:1904782; P:negative regulation of NMDA glutamate receptor activity; ISO:MGI.
DR   GO; GO:1903202; P:negative regulation of oxidative stress-induced cell death; ISO:MGI.
DR   GO; GO:1903204; P:negative regulation of oxidative stress-induced neuron death; IMP:ParkinsonsUK-UCL.
DR   GO; GO:1903377; P:negative regulation of oxidative stress-induced neuron intrinsic apoptotic signaling pathway; ISO:MGI.
DR   GO; GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; ISO:MGI.
DR   GO; GO:1901984; P:negative regulation of protein acetylation; ISO:MGI.
DR   GO; GO:0032091; P:negative regulation of protein binding; ISS:UniProtKB.
DR   GO; GO:0042177; P:negative regulation of protein catabolic process; IMP:ParkinsonsUK-UCL.
DR   GO; GO:0046826; P:negative regulation of protein export from nucleus; ISO:MGI.
DR   GO; GO:1903094; P:negative regulation of protein K48-linked deubiquitination; ISO:MGI.
DR   GO; GO:0006469; P:negative regulation of protein kinase activity; ISO:MGI.
DR   GO; GO:0001933; P:negative regulation of protein phosphorylation; ISO:MGI.
DR   GO; GO:0033234; P:negative regulation of protein sumoylation; ISO:MGI.
DR   GO; GO:0031397; P:negative regulation of protein ubiquitination; IMP:ParkinsonsUK-UCL.
DR   GO; GO:1903427; P:negative regulation of reactive oxygen species biosynthetic process; IMP:UniProtKB.
DR   GO; GO:1903122; P:negative regulation of TRAIL-activated apoptotic signaling pathway; ISO:MGI.
DR   GO; GO:0051444; P:negative regulation of ubiquitin-protein transferase activity; ISO:MGI.
DR   GO; GO:2000157; P:negative regulation of ubiquitin-specific protease activity; ISO:MGI.
DR   GO; GO:0036527; P:peptidyl-arginine deglycation; ISO:MGI.
DR   GO; GO:0036526; P:peptidyl-cysteine deglycation; ISO:MGI.
DR   GO; GO:0036528; P:peptidyl-lysine deglycation; ISO:MGI.
DR   GO; GO:0002866; P:positive regulation of acute inflammatory response to antigenic stimulus; IMP:UniProtKB.
DR   GO; GO:2000825; P:positive regulation of androgen receptor activity; ISO:MGI.
DR   GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; ISO:MGI.
DR   GO; GO:1903181; P:positive regulation of dopamine biosynthetic process; ISO:MGI.
DR   GO; GO:1905516; P:positive regulation of fertilization; ISO:MGI.
DR   GO; GO:0010628; P:positive regulation of gene expression; IMP:ParkinsonsUK-UCL.
DR   GO; GO:0032757; P:positive regulation of interleukin-8 production; ISO:MGI.
DR   GO; GO:1903197; P:positive regulation of L-dopa biosynthetic process; ISO:MGI.
DR   GO; GO:1903200; P:positive regulation of L-dopa decarboxylase activity; ISO:MGI.
DR   GO; GO:1902958; P:positive regulation of mitochondrial electron transport, NADH to ubiquinone; IMP:ParkinsonsUK-UCL.
DR   GO; GO:0033864; P:positive regulation of NAD(P)H oxidase activity; IMP:UniProtKB.
DR   GO; GO:2000277; P:positive regulation of oxidative phosphorylation uncoupler activity; IMP:UniProtKB.
DR   GO; GO:1902177; P:positive regulation of oxidative stress-induced intrinsic apoptotic signaling pathway; IMP:MGI.
DR   GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; ISO:MGI.
DR   GO; GO:0090073; P:positive regulation of protein homodimerization activity; ISO:MGI.
DR   GO; GO:1900182; P:positive regulation of protein localization to nucleus; ISO:MGI.
DR   GO; GO:1903168; P:positive regulation of pyrroline-5-carboxylate reductase activity; ISO:MGI.
DR   GO; GO:1903428; P:positive regulation of reactive oxygen species biosynthetic process; IDA:MGI.
DR   GO; GO:1901671; P:positive regulation of superoxide dismutase activity; ISO:MGI.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:ParkinsonsUK-UCL.
DR   GO; GO:2000679; P:positive regulation of transcription regulatory region DNA binding; ISO:MGI.
DR   GO; GO:1903178; P:positive regulation of tyrosine 3-monooxygenase activity; ISO:MGI.
DR   GO; GO:0036529; P:protein deglycation, glyoxal removal; ISO:MGI.
DR   GO; GO:0006517; P:protein deglycosylation; ISS:UniProtKB.
DR   GO; GO:0050821; P:protein stabilization; IMP:UniProtKB.
DR   GO; GO:0060765; P:regulation of androgen receptor signaling pathway; ISO:MGI.
DR   GO; GO:0050727; P:regulation of inflammatory response; IMP:UniProtKB.
DR   GO; GO:0051881; P:regulation of mitochondrial membrane potential; ISO:MGI.
DR   GO; GO:0043523; P:regulation of neuron apoptotic process; ISS:UniProtKB.
DR   GO; GO:0042542; P:response to hydrogen peroxide; IDA:MGI.
DR   GO; GO:0006979; P:response to oxidative stress; ISO:MGI.
DR   GO; GO:0007338; P:single fertilization; IEA:UniProtKB-KW.
DR   GO; GO:0001963; P:synaptic transmission, dopaminergic; IMP:MGI.
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   1: Evidence at protein level;
KW   Acetylation; Autophagy; Cell membrane; Chaperone; Complete proteome;
KW   Copper; Cytoplasm; Direct protein sequencing; DNA damage; DNA repair;
KW   Fertilization; Hydrolase; Inflammatory response; Isopeptide bond;
KW   Lipoprotein; Membrane; Mitochondrion; Nucleus; Oxidation; Palmitate;
KW   Phosphoprotein; Protease; Reference proteome; RNA-binding;
KW   Stress response; Tumor suppressor; Ubl conjugation; Zymogen.
FT   INIT_MET      1      1       Removed. {ECO:0000250|UniProtKB:Q99497}.
FT   CHAIN         2      ?       Protein/nucleic acid deglycase DJ-1.
FT                                /FTId=PRO_0000157850.
FT   PROPEP        ?    189       Removed in mature form.
FT                                /FTId=PRO_0000405560.
FT   ACT_SITE    106    106       Nucleophile.
FT                                {ECO:0000250|UniProtKB:Q99497}.
FT   ACT_SITE    126    126       {ECO:0000250|UniProtKB:Q99497}.
FT   MOD_RES       2      2       N-acetylalanine.
FT                                {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:0000244|PubMed:23806337}.
FT   MOD_RES     182    182       N6-succinyllysine.
FT                                {ECO:0000244|PubMed:23806337}.
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}.
FT   MUTAGEN      46     46       C->A: Sulfinic acid detected following
FT                                treatment with hydrogen peroxide.
FT                                {ECO:0000269|PubMed:17766438}.
FT   MUTAGEN      53     53       C->A: Sulfinic acid detected following
FT                                treatment with hydrogen peroxide.
FT                                {ECO:0000269|PubMed:17766438}.
FT   MUTAGEN     106    106       C->A: No sulfinic acid detected following
FT                                treatment with hydrogen peroxide.
FT                                {ECO:0000269|PubMed:17766438}.
FT   CONFLICT    127    127       P -> T (in Ref. 2; BAE40278).
FT                                {ECO:0000305}.
SQ   SEQUENCE   189 AA;  20021 MW;  877C825CCA07468F CRC64;
     MASKRALVIL AKGAEEMETV IPVDVMRRAG IKVTVAGLAG KDPVQCSRDV MICPDTSLED
     AKTQGPYDVV VLPGGNLGAQ NLSESPMVKE ILKEQESRKG LIAAICAGPT ALLAHEVGFG
     CKVTTHPLAK DKMMNGSHYS YSESRVEKDG LILTSRGPGT SFEFALAIVE ALVGKDMANQ
     VKAPLVLKD
//
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