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 27-MAR-2024, entry version 176.
DE RecName: Full=Parkinson disease protein 7 homolog {ECO:0000305};
DE AltName: Full=Maillard deglycase {ECO:0000250|UniProtKB:Q99497};
DE AltName: Full=Parkinsonism-associated deglycase {ECO:0000250|UniProtKB:Q99497};
DE AltName: Full=Protein DJ-1 {ECO:0000305};
DE Short=DJ-1;
DE AltName: 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 Flags: Precursor;
GN Name=Park7 {ECO:0000312|MGI:MGI:2135637};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC 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 Sp1-
RT 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., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., 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., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., 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., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT 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 project:
RT 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 MASS
RP 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., 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., Lozano A.M.,
RA 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, stabilizes the
RT 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., Greco T.M.,
RA Thomas B., Ko H.S., Sasaki M., Ischiropoulos H., Przedborski S.,
RA Dawson T.M., Dawson V.L.;
RT "DJ-1 gene deletion reveals that DJ-1 is an atypical peroxiredoxin-like
RT 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 disease-
RT 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 red
RT 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, Pancreas,
RC 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 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., Mak T.W.,
RA Ting J.P.;
RT "DJ-1 enhances cell survival through the binding of cezanne, a negative
RT 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 attenuated
RT 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., Waak J.,
RA Wolburg H., Gizatullina Z., Gellerich F.N., Woitalla D., Riess O.,
RA Kahle P.J., Proikas-Cezanne T., Kruger R.;
RT "Reduced basal autophagy and impaired mitochondrial dynamics due to loss of
RT Parkinson's disease-associated protein DJ-1.";
RL PLoS ONE 5:E9367-E9367(2010).
RN [16]
RP PROTEOLYTIC CLEAVAGE, AND SUBCELLULAR LOCATION.
RX PubMed=22555455; DOI=10.1038/cdd.2012.55;
RA Robert G., Puissant A., Dufies M., Marchetti S., Jacquel A., Cluzeau T.,
RA Colosetti P., Belhacene N., Kahle P., Da Costa C.A., Luciano F.,
RA Checler F., Auberger P.;
RT "The caspase 6 derived N-terminal fragment of DJ-1 promotes apoptosis via
RT increased ROS production.";
RL Cell Death Differ. 19:1769-1778(2012).
RN [17]
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 [18]
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 in
RT mice with implications for human type 2 diabetes.";
RL J. Mol. Cell Biol. 4:221-230(2012).
RN [19]
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 lipid
RT rafts-dependent endocytosis in astrocytes.";
RL Hum. Mol. Genet. 22:4805-4817(2013).
RN [20]
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 metal-
RT induced cytotoxicity.";
RL J. Biol. Chem. 288:22809-22820(2013).
RN [21]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-148, SUCCINYLATION [LARGE SCALE
RP ANALYSIS] AT LYS-182, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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., Zhang Y.,
RA 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 [22]
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 [23]
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., Seufert J.,
RA Lammert E.;
RT "DJ-1 Protects Pancreatic Beta Cells from Cytokine- and Streptozotocin-
RT Mediated Cell Death.";
RL PLoS ONE 10:E0138535-E0138535(2015).
RN [24]
RP INTERACTION WITH NENF, AND SUBCELLULAR LOCATION.
RX PubMed=31536960; DOI=10.1016/j.isci.2019.08.057;
RA Moutaoufik M.T., Malty R., Amin S., Zhang Q., Phanse S., Gagarinova A.,
RA Zilocchi M., Hoell L., Minic Z., Gagarinova M., Aoki H., Stockwell J.,
RA Jessulat M., Goebels F., Broderick K., Scott N.E., Vlasblom J., Musso G.,
RA Prasad B., Lamantea E., Garavaglia B., Rajput A., Murayama K., Okazaki Y.,
RA Foster L.J., Bader G.D., Cayabyab F.S., Babu M.;
RT "Rewiring of the Human Mitochondrial Interactome during Neuronal
RT Reprogramming Reveals Regulators of the Respirasome and Neurogenesis.";
RL IScience 19:1114-1132(2019).
CC -!- FUNCTION: Multifunctional protein with controversial molecular function
CC which plays an important role in cell protection against oxidative
CC stress and cell death acting as oxidative stress sensor and redox-
CC sensitive chaperone and protease (PubMed:15784737, PubMed:17015834,
CC PubMed:20800516, PubMed:21068725). It is involved in neuroprotective
CC mechanisms like the stabilization of NFE2L2 and PINK1 proteins, male
CC fertility as a positive regulator of androgen signaling pathway as well
CC as cell growth and transformation through, for instance, the modulation
CC of NF-kappa-B signaling pathway (PubMed:17015834, PubMed:21097510). Has
CC been described as a 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. But
CC this function is rebuted by other works. As a protein deglycase,
CC repairs methylglyoxal- and glyoxal-glycated proteins, and releases
CC repaired proteins and lactate or glycolate, respectively. Deglycates
CC cysteine, arginine and lysine residues in proteins, and thus
CC reactivates these proteins by reversing glycation by glyoxals. Acts on
CC early glycation intermediates (hemithioacetals and aminocarbinols),
CC preventing the formation of advanced glycation endproducts (AGE) that
CC cause irreversible damage. Also functions as a nucleotide deglycase
CC able to repair glycated guanine in the free nucleotide pool (GTP, GDP,
CC GMP, dGTP) and in DNA and RNA. Is thus involved in a major nucleotide
CC repair system named guanine glycation repair (GG repair), dedicated to
CC reversing methylglyoxal and glyoxal damage via nucleotide sanitization
CC and direct nucleic acid repair. Protects histones from adduction by
CC methylglyoxal, controls the levels of methylglyoxal-derived argininine
CC modifications on chromatin. Able to remove the glycations and restore
CC histone 3, histone glycation disrupts both local and global chromatin
CC architecture by altering histone-DNA interactions as well as histone
CC acetylation and ubiquitination levels. Displays a very low glyoxalase
CC activity that may reflect its deglycase activity (PubMed:22523093).
CC Eliminates hydrogen peroxide and protects cells against hydrogen
CC peroxide-induced cell death (PubMed:17766438). Required for correct
CC mitochondrial morphology and function as well as for autophagy of
CC dysfunctional mitochondria (PubMed:20186336). Plays a role in
CC regulating expression or stability of the mitochondrial uncoupling
CC proteins SLC25A14 and SLC25A27 in dopaminergic neurons of the
CC substantia nigra pars compacta and attenuates the oxidative stress
CC induced by calcium entry into the neurons via L-type channels during
CC pacemaking (PubMed:21068725). Regulates astrocyte inflammatory
CC responses, may modulate lipid rafts-dependent endocytosis in astrocytes
CC and neuronal cells (PubMed:23847046, PubMed:19276172). In pancreatic
CC islets, involved in the maintenance of mitochondrial reactive oxygen
CC species (ROS) levels and glucose homeostasis in an age- and diet
CC dependent manner. Protects pancreatic beta cells from cell death
CC induced by inflammatory and cytotoxic setting (PubMed:26422139). Binds
CC to a number of mRNAs containing multiple copies of GG or CC motifs and
CC partially inhibits their translation but dissociates following
CC oxidative stress (By similarity). Metal-binding protein able to bind
CC copper as well as toxic mercury ions, enhances the cell protection
CC mechanism against induced metal toxicity (PubMed:23792957). In
CC macrophages, interacts with the NADPH oxidase subunit NCF1 to direct
CC NADPH oxidase-dependent ROS production, and protects against sepsis
CC (PubMed:26021615). {ECO:0000250|UniProtKB:Q99497,
CC ECO:0000269|PubMed:15784737, ECO:0000269|PubMed:17015834,
CC ECO:0000269|PubMed:17766438, ECO:0000269|PubMed:19276172,
CC ECO:0000269|PubMed:20186336, ECO:0000269|PubMed:20800516,
CC ECO:0000269|PubMed:21068725, ECO:0000269|PubMed:22523093,
CC ECO:0000269|PubMed:22611253, ECO:0000269|PubMed:23792957,
CC ECO:0000269|PubMed:23847046, ECO:0000269|PubMed:26021615,
CC ECO:0000269|PubMed:26422139}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(omega)-(1-hydroxy-2-oxopropyl)-L-arginyl-[protein] =
CC H(+) + L-arginyl-[protein] + lactate; Xref=Rhea:RHEA:49548,
CC Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:12428, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:29965,
CC ChEBI:CHEBI:131708; EC=3.5.1.124;
CC Evidence={ECO:0000250|UniProtKB:Q99497};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(6)-(1-hydroxy-2-oxopropyl)-L-lysyl-[protein] = H(+) +
CC L-lysyl-[protein] + lactate; Xref=Rhea:RHEA:49552, Rhea:RHEA-
CC 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] = H(+) +
CC L-cysteinyl-[protein] + lactate; Xref=Rhea:RHEA:49556, Rhea:RHEA-
CC 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, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:24996, ChEBI:CHEBI:61429, ChEBI:CHEBI:141569;
CC Evidence={ECO:0000250|UniProtKB:Q99497};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-GTP = GTP + H(+) + lactate;
CC Xref=Rhea:RHEA:57256, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:24996, ChEBI:CHEBI:37565, ChEBI:CHEBI:141570;
CC Evidence={ECO:0000250|UniProtKB:Q99497};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-GDP = GDP + H(+) + lactate;
CC Xref=Rhea:RHEA:57260, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:24996, ChEBI:CHEBI:58189, ChEBI:CHEBI:141573;
CC Evidence={ECO:0000250|UniProtKB:Q99497};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-GMP = GMP + H(+) + lactate;
CC Xref=Rhea:RHEA:57268, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:24996, ChEBI:CHEBI:58115, ChEBI:CHEBI:141575;
CC 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, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29805, ChEBI:CHEBI:61429, ChEBI:CHEBI:141572;
CC 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, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29805, ChEBI:CHEBI:37565, ChEBI:CHEBI:141571;
CC 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, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29805, ChEBI:CHEBI:58189, ChEBI:CHEBI:141574;
CC 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, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29805, ChEBI:CHEBI:58115, ChEBI:CHEBI:141576;
CC Evidence={ECO:0000250|UniProtKB:Q99497};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N(2)-(1-hydroxy-2-oxopropyl)-guanosine in RNA + H2O = a
CC guanosine in RNA + H(+) + lactate; Xref=Rhea:RHEA:57288, Rhea:RHEA-
CC 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 + H2O
CC = a 2'-deoxyguanosine in DNA + H(+) + lactate; Xref=Rhea:RHEA:57300,
CC Rhea:RHEA-COMP:11367, Rhea:RHEA-COMP:14856, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:85445,
CC ChEBI:CHEBI:141578; 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, Rhea:RHEA-
CC 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 + H2O
CC = a 2'-deoxyguanosine in DNA + glycolate + H(+);
CC Xref=Rhea:RHEA:57296, Rhea:RHEA-COMP:11367, Rhea:RHEA-COMP:14857,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805,
CC ChEBI:CHEBI:85445, ChEBI:CHEBI:141579;
CC Evidence={ECO:0000250|UniProtKB:Q99497};
CC -!- COFACTOR:
CC Note=Deglycase activity does not require glutathione as a cofactor,
CC however, glycated glutathione constitutes a PARK7 substrate.
CC {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 (PubMed:21097510).
CC Interacts with BBS1, CLCF1 and MTERF (PubMed:21097510). Interacts (via
CC C-terminus) with NCF1; the interaction is enhanced by LPS and modulates
CC NCF1 phosphorylation and membrane translocation (PubMed:26021615).
CC Interacts with NENF (PubMed:31536960). {ECO:0000250|UniProtKB:Q99497,
CC ECO:0000269|PubMed:21097510, ECO:0000269|PubMed:26021615,
CC ECO:0000269|PubMed:31536960}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23847046};
CC Lipid-anchor {ECO:0000269|PubMed:23847046}. Cytoplasm
CC {ECO:0000269|PubMed:22555455}. Membrane raft
CC {ECO:0000269|PubMed:23847046}. Nucleus {ECO:0000269|PubMed:22555455}.
CC Mitochondrion {ECO:0000269|PubMed:31536960}. Endoplasmic reticulum
CC {ECO:0000269|PubMed:31536960}. Note=Under normal conditions, located
CC predominantly in the cytoplasm and, to a lesser extent, in the nucleus
CC and mitochondrion. Translocates to the mitochondrion and subsequently
CC to the nucleus in response to oxidative stress and exerts an increased
CC cytoprotective effect against oxidative damage (By similarity).
CC Membrane raft localization in astrocytes and neuronal cells requires
CC palmitoylation (PubMed:23847046). {ECO:0000250|UniProtKB:Q99497,
CC ECO:0000269|PubMed:23847046}.
CC -!- TISSUE SPECIFICITY: Expressed in erythroblasts and in mature red blood
CC cells from peripheral blood (at protein level) (PubMed:20800516). In
CC pancreas, expression is higher in islets than surrounding exocrine
CC tissues (PubMed:22611253). {ECO:0000269|PubMed:20800516,
CC ECO:0000269|PubMed:22611253}.
CC -!- DEVELOPMENTAL STAGE: Expression increases during erythroid development
CC (at protein level) (PubMed:20800516). In pancreatic islets, expression
CC increases during aging (PubMed:22611253). {ECO:0000269|PubMed:20800516,
CC 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 for
CC 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 mitochondrial
CC hydrogen peroxide production and reduced mitochondrial aconitase
CC activity. Down-regulation of Slc25a14 and Slc25a27, compromised
CC calcium-induced uncoupling and increased oxidation of mitochondrial
CC matrix proteins specifically in the dopaminergic neurons of the
CC substantia nigra pars compacta. Reduced N2el2 protein expression.
CC Impaired mitochondrial function and morphology with reduced autophagy
CC leading to accumulation of defective mitochondria. Targeted knockouts
CC in astrocytes exhibit augmented LPS-induced CRK/p38 phosphorylation and
CC signaling, they don't stimulate TLR4 endocytosis upon LPS stimulation.
CC Knockout animals present increased bacterial burdens, reduced local and
CC systemic inflammation, macrophage paralysis and impaired induction of
CC pro-inflammatory cytokines, such as IL6 and TNF, under the condition of
CC sepsis (PubMed:26021615). Mutants from 12 weeks old, but not younger,
CC show higher levels of reactive oxygen species (ROS) and mitochondrial
CC fragmentation in pancreatic islets. They have lower levels of plasma
CC insulin after glucose challenge, display glucose intolerance and have
CC reduced beta-cell area. Younger mutants kept on a high fat diet also
CC show lower levels of plasma insulin, display glucose intolerance and
CC have reduced beta-cell area (PubMed:22611253). Animals become diabetic
CC upon multiple low doses of streptozotocin with reduced insulin
CC concentrations, higher fasting blood glucose concentrations and higher
CC rates of 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: Glyoxalase activity has been reported (PubMed:22523093). It
CC may however reflect its deglycase activity.
CC {ECO:0000250|UniProtKB:Q99497, ECO:0000269|PubMed:22523093}.
CC -!- CAUTION: The protein deglycation activity is controversial. It has been
CC ascribed to a TRIS buffer artifact by a publication and as a result of
CC the removal of methylglyoxal by glyoxalase activity that leads to a
CC subsequent decomposition of hemithioacetals and hemianimals due to the
CC shift in equilibrium position by another one. However, biochemical
CC experiments showing that PARK7 is a bona fide deglycase have been
CC performed. {ECO:0000250|UniProtKB:Q99497}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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 AlphaFoldDB; Q99LX0; -.
DR SMR; Q99LX0; -.
DR BioGRID; 208257; 53.
DR IntAct; Q99LX0; 25.
DR MINT; Q99LX0; -.
DR STRING; 10090.ENSMUSP00000101299; -.
DR MEROPS; C56.002; -.
DR GlyGen; Q99LX0; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q99LX0; -.
DR MetOSite; Q99LX0; -.
DR PhosphoSitePlus; Q99LX0; -.
DR SwissPalm; Q99LX0; -.
DR REPRODUCTION-2DPAGE; Q99LX0; -.
DR UCD-2DPAGE; Q99LX0; -.
DR CPTAC; non-CPTAC-3991; -.
DR EPD; Q99LX0; -.
DR jPOST; Q99LX0; -.
DR MaxQB; Q99LX0; -.
DR PaxDb; 10090-ENSMUSP00000030805; -.
DR PeptideAtlas; Q99LX0; -.
DR ProteomicsDB; 294387; -.
DR Pumba; Q99LX0; -.
DR TopDownProteomics; Q99LX0; -.
DR Antibodypedia; 1372; 988 antibodies from 51 providers.
DR DNASU; 57320; -.
DR Ensembl; ENSMUST00000030805.14; ENSMUSP00000030805.8; ENSMUSG00000028964.15.
DR Ensembl; ENSMUST00000105673.8; ENSMUSP00000101298.2; ENSMUSG00000028964.15.
DR Ensembl; ENSMUST00000105674.8; ENSMUSP00000101299.2; ENSMUSG00000028964.15.
DR Ensembl; ENSMUST00000105675.8; ENSMUSP00000101300.2; ENSMUSG00000028964.15.
DR GeneID; 57320; -.
DR KEGG; mmu:57320; -.
DR UCSC; uc008vxz.2; mouse.
DR AGR; MGI:2135637; -.
DR CTD; 11315; -.
DR MGI; MGI:2135637; Park7.
DR VEuPathDB; HostDB:ENSMUSG00000028964; -.
DR eggNOG; KOG2764; Eukaryota.
DR GeneTree; ENSGT00390000001231; -.
DR HOGENOM; CLU_000445_44_2_1; -.
DR InParanoid; Q99LX0; -.
DR OMA; KATCYPG; -.
DR OrthoDB; 1117759at2759; -.
DR PhylomeDB; Q99LX0; -.
DR TreeFam; TF300119; -.
DR Reactome; R-MMU-3899300; SUMOylation of transcription cofactors.
DR Reactome; R-MMU-9646399; Aggrephagy.
DR BioGRID-ORCS; 57320; 2 hits in 114 CRISPR screens.
DR ChiTaRS; Park7; mouse.
DR PRO; PR:Q99LX0; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q99LX0; Protein.
DR Bgee; ENSMUSG00000028964; Expressed in triceps brachii and 265 other cell types or tissues.
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:UniProtKB.
DR GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0043005; C:neuron projection; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
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: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:0140297; F:DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:1990422; F:glyoxalase (glycolic acid-forming) activity; ISS:UniProtKB.
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:0050681; F:nuclear androgen receptor binding; ISO:MGI.
DR GO; GO:0016684; F:oxidoreductase activity, acting on peroxide as acceptor; ISO:MGI.
DR GO; GO:0019826; F:oxygen sensor activity; IMP:ParkinsonsUK-UCL.
DR GO; GO:0008233; F:peptidase activity; ISS:UniProtKB.
DR GO; GO:0051920; F:peroxiredoxin activity; IMP:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex 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: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:0110095; P:cellular detoxification of aldehyde; ISS:UniProtKB.
DR GO; GO:0140041; P:cellular detoxification of methylglyoxal; ISS:UniProtKB.
DR GO; GO:0036471; P:cellular response to glyoxal; IMP:ParkinsonsUK-UCL.
DR GO; GO:0070301; P:cellular response to hydrogen peroxide; ISO:MGI.
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:0070994; P:detection of oxidative stress; IMP:ParkinsonsUK-UCL.
DR GO; GO:0010273; P:detoxification of copper ion; IMP:UniProtKB.
DR GO; GO:0061691; P:detoxification of hydrogen peroxide; ISO:MGI.
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: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:0061727; P:methylglyoxal catabolic process to lactate; ISS:UniProtKB.
DR GO; GO:0007005; P:mitochondrion organization; IMP:UniProtKB.
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:1903384; P:negative regulation of hydrogen peroxide-induced neuron intrinsic apoptotic signaling pathway; IMP:ParkinsonsUK-UCL.
DR GO; GO:1903751; P:negative regulation of intrinsic apoptotic signaling pathway in response to hydrogen peroxide; IMP:ParkinsonsUK-UCL.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISO:MGI.
DR GO; GO:1905259; P:negative regulation of nitrosative stress-induced intrinsic apoptotic signaling pathway; ISO:MGI.
DR GO; GO:1902176; P:negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway; IMP:ParkinsonsUK-UCL.
DR GO; GO:1903377; P:negative regulation of oxidative stress-induced neuron intrinsic apoptotic signaling pathway; IMP:ParkinsonsUK-UCL.
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: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:0014912; P:negative regulation of smooth muscle cell migration; ISO:MGI.
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; IC:ParkinsonsUK-UCL.
DR GO; GO:1904706; P:negative regulation of vascular associated smooth muscle cell proliferation; ISO:MGI.
DR GO; GO:0036527; P:peptidyl-arginine deglycation; ISS:UniProtKB.
DR GO; GO:0002866; P:positive regulation of acute inflammatory response to antigenic stimulus; IMP:UniProtKB.
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: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:1900182; P:positive regulation of protein localization to nucleus; ISO:MGI.
DR GO; GO:0031334; P:positive regulation of protein-containing complex assembly; ISO:MGI.
DR GO; GO:1903428; P:positive regulation of reactive oxygen species biosynthetic process; IDA:MGI.
DR GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:ParkinsonsUK-UCL.
DR GO; GO:0050821; P:protein stabilization; IMP:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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:1903376; P:regulation of oxidative stress-induced neuron intrinsic apoptotic signaling pathway; ISO:MGI.
DR GO; GO:0042542; P:response to hydrogen peroxide; IDA:MGI.
DR GO; GO:0006979; P:response to oxidative stress; IMP:UniProtKB.
DR GO; GO:0007338; P:single fertilization; IEA:UniProtKB-KW.
DR GO; GO:0001963; P:synaptic transmission, dopaminergic; IMP:MGI.
DR CDD; cd03135; GATase1_DJ-1; 1.
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 NCBIfam; TIGR01383; not_thiJ; 1.
DR PANTHER; PTHR48094:SF12; PARKINSON DISEASE PROTEIN 7 HOMOLOG; 1.
DR PANTHER; PTHR48094; PROTEIN/NUCLEIC ACID DEGLYCASE DJ-1-RELATED; 1.
DR Pfam; PF01965; DJ-1_PfpI; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
PE 1: Evidence at protein level;
KW Acetylation; Autophagy; Cell membrane; Chaperone; Copper; Cytoplasm;
KW Direct protein sequencing; DNA damage; DNA repair; Endoplasmic reticulum;
KW Fertilization; Hydrolase; Inflammatory response; Isopeptide bond;
KW Lipoprotein; Membrane; Mitochondrion; Nucleus; Oxidation; Palmitate;
KW Phosphoprotein; Protease; Reference proteome; RNA-binding; Stress response;
KW Tumor suppressor; Ubl conjugation; Zymogen.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q99497"
FT CHAIN 2..?
FT /note="Parkinson disease protein 7 homolog"
FT /id="PRO_0000157850"
FT PROPEP ?..189
FT /note="Removed in mature form"
FT /id="PRO_0000405560"
FT ACT_SITE 106
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q99497"
FT ACT_SITE 126
FT /evidence="ECO:0000250|UniProtKB:Q99497"
FT SITE 149..150
FT /note="Cleavage; by CASP6"
FT /evidence="ECO:0000269|PubMed:22555455"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q99497"
FT MOD_RES 67
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q99497"
FT MOD_RES 106
FT /note="Cysteine sulfinic acid (-SO2H); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99497"
FT MOD_RES 148
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 182
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT LIPID 46
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q99497"
FT LIPID 53
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q99497"
FT LIPID 106
FT /note="S-palmitoyl cysteine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99497"
FT CROSSLNK 130
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250|UniProtKB:Q99497"
FT MUTAGEN 46
FT /note="C->A: Sulfinic acid detected following treatment
FT with hydrogen peroxide."
FT /evidence="ECO:0000269|PubMed:17766438"
FT MUTAGEN 53
FT /note="C->A: Sulfinic acid detected following treatment
FT with hydrogen peroxide."
FT /evidence="ECO:0000269|PubMed:17766438"
FT MUTAGEN 106
FT /note="C->A: No sulfinic acid detected following treatment
FT with hydrogen peroxide."
FT /evidence="ECO:0000269|PubMed:17766438"
FT CONFLICT 127
FT /note="P -> T (in Ref. 2; BAE40278)"
FT /evidence="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
//
