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Database: UniProt/SWISS-PROT
Entry: PARK7_RAT
LinkDB: PARK7_RAT
Original site: PARK7_RAT 
ID   PARK7_RAT               Reviewed;         189 AA.
AC   O88767;
DT   07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   07-NOV-2018, entry version 138.
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=Contraception-associated protein 1 {ECO:0000303|PubMed:9792810};
DE            Short=Protein CAP1;
DE   AltName: Full=Fertility protein SP22 {ECO:0000303|PubMed:9733139};
DE   AltName: Full=Maillard deglycase {ECO:0000250|UniProtKB:Q99497};
DE   AltName: Full=Parkinson disease protein 7 homolog {ECO:0000305};
DE   AltName: Full=Parkinsonism-associated deglycase {ECO:0000250|UniProtKB:Q99497};
DE   AltName: Full=Protein DJ-1 {ECO:0000250|UniProtKB:Q99497};
DE            Short=DJ-1;
DE   Flags: Precursor;
GN   Name=Park7 {ECO:0000312|RGD:621808}; Synonyms=Cap1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 13-29 AND 65-74, AND
RP   TISSUE SPECIFICITY.
RC   TISSUE=Testis;
RX   PubMed=9792810; DOI=10.1006/bbrc.1998.9512;
RA   Wagenfeld A., Gromoll J., Cooper T.G.;
RT   "Molecular cloning and expression of rat contraception associated
RT   protein 1 (CAP1), a protein putatively involved in fertilization.";
RL   Biochem. Biophys. Res. Commun. 251:545-549(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Sprague-Dawley; TISSUE=Testis;
RX   PubMed=9733139;
RA   Welch J.E., Barbee R.R., Roberts N.L., Suarez J.D., Klinefelter G.R.;
RT   "SP22: a novel fertility protein from a highly conserved gene
RT   family.";
RL   J. Androl. 19:385-393(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Sprague-Dawley; TISSUE=Testis;
RA   Welch J.E., Barbee R.R., Roberts N.L., Suarez J.D., Klinefelter G.R.;
RL   Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   PROTEIN SEQUENCE OF 27-45, ASSOCIATION WITH AN RNA-BINDING COMPLEX,
RP   AND SUBCELLULAR LOCATION.
RX   PubMed=10022524;
RX   DOI=10.1002/(SICI)1097-4644(19990301)72:3<435::AID-JCB12>3.3.CO;2-8;
RA   Hod Y., Pentyala S.N., Whyard T.C., El-Maghrabi M.R.;
RT   "Identification and characterization of a novel protein that regulates
RT   RNA-protein interaction.";
RL   J. Cell. Biochem. 72:435-444(1999).
RN   [5]
RP   PROTEIN SEQUENCE OF 33-48; 63-89; 100-122; 133-145 AND 157-175, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=Sprague-Dawley; TISSUE=Brain, Hippocampus, and Spinal cord;
RA   Lubec G., Afjehi-Sadat L., Chen W.-Q., Kang S.U.;
RL   Submitted (JUL-2007) to UniProtKB.
RN   [6]
RP   SUBCELLULAR LOCATION.
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).
CC   -!- FUNCTION: Protein and nucleotide deglycase that catalyzes the
CC       deglycation of the Maillard adducts formed between amino groups of
CC       proteins or nucleotides and reactive carbonyl groups of glyoxals.
CC       Thus, functions as a protein deglycase that repairs
CC       methylglyoxal- and glyoxal-glycated proteins, and releases
CC       repaired proteins and lactate or glycolate, respectively.
CC       Deglycates cysteine, arginine and lysine residues in proteins, and
CC       thus reactivates these proteins by reversing glycation by
CC       glyoxals. Acts on early glycation intermediates (hemithioacetals
CC       and aminocarbinols), preventing the formation of advanced
CC       glycation endproducts (AGE) that cause irreversible damage. Also
CC       functions as a nucleotide deglycase able to repair glycated
CC       guanine in the free nucleotide pool (GTP, GDP, GMP, dGTP) and in
CC       DNA and RNA. Is thus involved in a major nucleotide repair system
CC       named guanine glycation repair (GG repair), dedicated to reversing
CC       methylglyoxal and glyoxal damage via nucleotide sanitization and
CC       direct nucleic acid repair. Also displays an apparent glyoxalase
CC       activity that in fact reflects its deglycase activity. Plays an
CC       important role in cell protection against oxidative stress and
CC       cell death acting as oxidative stress sensor and redox-sensitive
CC       chaperone and protease; functions probably related to its primary
CC       function. It is involved in neuroprotective mechanisms like the
CC       stabilization of NFE2L2 and PINK1 proteins, male fertility as a
CC       positive regulator of androgen signaling pathway as well as cell
CC       growth and transformation through, for instance, the modulation of
CC       NF-kappa-B signaling pathway. Eliminates hydrogen peroxide and
CC       protects cells against hydrogen peroxide-induced cell death.
CC       Required for correct mitochondrial morphology and function as well
CC       as for autophagy of dysfunctional mitochondria. 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
CC       during pacemaking. Regulates astrocyte inflammatory responses, may
CC       modulate lipid rafts-dependent endocytosis in astrocytes and
CC       neuronal cells (By similarity). In pancreatic islets, involved in
CC       the maintenance of mitochondrial reactive oxygen species (ROS)
CC       levels and glucose homeostasis in an age- and diet dependent
CC       manner. Protects pancreatic beta cells from cell death induced by
CC       inflammatory and cytotoxic setting (By similarity). Binds to a
CC       number of mRNAs containing multiple copies of GG or CC motifs and
CC       partially inhibits their translation but dissociates following
CC       oxidative stress. Metal-binding protein able to bind copper as
CC       well as toxic mercury ions, enhances the cell protection mechanism
CC       against induced metal toxicity (By similarity). In macrophages,
CC       interacts with the NADPH oxidase subunit NCF1 to direct NADPH
CC       oxidase-dependent ROS production, and protects against sepsis (By
CC       similarity). {ECO:0000250|UniProtKB:Q99497,
CC       ECO:0000250|UniProtKB:Q99LX0}.
CC   -!- CATALYTIC ACTIVITY: An N(omega)-(1-hydroxy-2-oxopropyl)-[protein]-
CC       L-arginine + H(2)O = a [protein]-L-arginine + lactate.
CC       {ECO:0000250|UniProtKB:Q99497}.
CC   -!- CATALYTIC ACTIVITY: An N(6)-(1-hydroxy-2-oxopropyl)-[protein]-L-
CC       lysine + H(2)O = a [protein]-L-lysine + lactate.
CC       {ECO:0000250|UniProtKB:Q99497}.
CC   -!- CATALYTIC ACTIVITY: An S-(1-hydroxy-2-oxopropyl)-[protein]-L-
CC       cysteine + H(2)O = a [protein]-L-cysteine + lactate.
CC       {ECO:0000250|UniProtKB:Q99497}.
CC   -!- CATALYTIC ACTIVITY: An N(omega)-(1-hydroxy-2-oxoethyl)-[protein]-
CC       L-arginine + H(2)O = a [protein]-L-arginine + glycolate.
CC       {ECO:0000250|UniProtKB:Q99497}.
CC   -!- CATALYTIC ACTIVITY: An N(6)-(1-hydroxy-2-oxoethyl)-[protein]-L-
CC       lysine + H(2)O = a [protein]-L-lysine + glycolate.
CC       {ECO:0000250|UniProtKB:Q99497}.
CC   -!- CATALYTIC ACTIVITY: An S-(1-hydroxy-2-oxoethyl)-[protein]-L-
CC       cysteine + H(2)O = a [protein]-L-cysteine + glycolate.
CC       {ECO:0000250|UniProtKB:Q99497}.
CC   -!- CATALYTIC ACTIVITY: N(2)-(1-hydroxy-2-oxopropyl)-dGTP + H(2)O =
CC       dGTP + lactate. {ECO:0000250|UniProtKB:Q99497}.
CC   -!- CATALYTIC ACTIVITY: N(2)-(1-hydroxy-2-oxopropyl)-GTP + H(2)O = GTP
CC       + lactate. {ECO:0000250|UniProtKB:Q99497}.
CC   -!- CATALYTIC ACTIVITY: N(2)-(1-hydroxy-2-oxopropyl)-GDP + H(2)O = GDP
CC       + lactate. {ECO:0000250|UniProtKB:Q99497}.
CC   -!- CATALYTIC ACTIVITY: N(2)-(1-hydroxy-2-oxopropyl)-GMP + H(2)O = GMP
CC       + lactate. {ECO:0000250|UniProtKB:Q99497}.
CC   -!- CATALYTIC ACTIVITY: N(2)-(1-hydroxy-2-oxoethyl)-dGTP + H(2)O =
CC       dGTP + glycolate. {ECO:0000250|UniProtKB:Q99497}.
CC   -!- CATALYTIC ACTIVITY: N(2)-(1-hydroxy-2-oxoethyl)-GTP + H(2)O = GTP
CC       + glycolate. {ECO:0000250|UniProtKB:Q99497}.
CC   -!- CATALYTIC ACTIVITY: N(2)-(1-hydroxy-2-oxoethyl)-GDP + H(2)O = GDP
CC       + glycolate. {ECO:0000250|UniProtKB:Q99497}.
CC   -!- CATALYTIC ACTIVITY: N(2)-(1-hydroxy-2-oxoethyl)-GMP + H(2)O = GMP
CC       + glycolate. {ECO:0000250|UniProtKB:Q99497}.
CC   -!- CATALYTIC ACTIVITY: An N(2)-(1-hydroxy-2-oxopropyl)-guanosine in
CC       RNA + H(2)O = a guanosine in RNA + lactate.
CC       {ECO:0000250|UniProtKB:Q99497}.
CC   -!- CATALYTIC ACTIVITY: An N(2)-(1-hydroxy-2-oxopropyl)-2'-
CC       deoxyguanosine in DNA + H(2)O = a 2'-deoxyguanosine in RNA +
CC       lactate. {ECO:0000250|UniProtKB:Q99497}.
CC   -!- CATALYTIC ACTIVITY: An N(2)-(1-hydroxy-2-oxoethyl)-guanosine in
CC       RNA + H(2)O = a guanosine in RNA + glycolate.
CC       {ECO:0000250|UniProtKB:Q99497}.
CC   -!- CATALYTIC ACTIVITY: An N(2)-(1-hydroxy-2-oxoethyl)-2'-
CC       deoxyguanosine in DNA + H(2)O = a 2'-deoxyguanosine in RNA +
CC       glycolate. {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. Interacts (via N-
CC       terminus) with OTUD7B. Interacts with BBS1, HIPK1, CLCF1 and
CC       MTERF. Forms a complex with PINK1 and PRKN (By similarity).
CC       Interacts (via C-terminus) with NCF1; the interaction is enhanced
CC       by LPS and modulates NCF1 phosphorylation and membrane
CC       translocation (By similarity). {ECO:0000250|UniProtKB:Q99497,
CC       ECO:0000250|UniProtKB:Q99LX0}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane
CC       {ECO:0000250|UniProtKB:Q99LX0}; Lipid-anchor
CC       {ECO:0000250|UniProtKB:Q99LX0}. Cytoplasm
CC       {ECO:0000269|PubMed:10022524}. Membrane raft
CC       {ECO:0000269|PubMed:23847046}. Nucleus
CC       {ECO:0000269|PubMed:10022524}. 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: Ubiquitous. Detected on epididymal sperm.
CC       Highly expressed in testis and prostate. Detected at lower levels
CC       in heart, lung, brain, liver, kidney, seminal vesicle, caput and
CC       corpus epididymis. {ECO:0000269|PubMed:9792810}.
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   -!- SIMILARITY: Belongs to the peptidase C56 family. {ECO:0000305}.
CC   -!- CAUTION: Glyoxylase activity previously reported may reflect in
CC       fact its deglycase activity. {ECO:0000250|UniProtKB:Q99497}.
CC   -!- CAUTION: The protein deglycation activity has been ascribed to a
CC       TRIS buffer artifact by a publication, which has then been
CC       rebutted by clear biochemical experiments showing that PARK7 is a
CC       bona fide deglycase. Deglycase activity is even strengthened by a
CC       novel article that reports nucleotide deglycation activity.
CC       {ECO:0000250|UniProtKB:Q99497}.
DR   EMBL; AJ007291; CAA07434.1; -; mRNA.
DR   EMBL; AF157511; AAD43956.1; -; mRNA.
DR   EMBL; AF157512; AAD43957.1; -; mRNA.
DR   PIR; JE0344; JE0344.
DR   RefSeq; NP_001264179.1; NM_001277250.1.
DR   RefSeq; NP_001264180.1; NM_001277251.1.
DR   RefSeq; NP_001264181.1; NM_001277252.1.
DR   RefSeq; NP_001264182.1; NM_001277253.1.
DR   RefSeq; NP_476484.1; NM_057143.2.
DR   UniGene; Rn.30105; -.
DR   ProteinModelPortal; O88767; -.
DR   SMR; O88767; -.
DR   BioGrid; 250731; 76.
DR   IntAct; O88767; 1.
DR   STRING; 10116.ENSRNOP00000024711; -.
DR   MEROPS; C56.002; -.
DR   iPTMnet; O88767; -.
DR   PhosphoSitePlus; O88767; -.
DR   World-2DPAGE; 0004:O88767; -.
DR   PaxDb; O88767; -.
DR   PRIDE; O88767; -.
DR   Ensembl; ENSRNOT00000024711; ENSRNOP00000024711; ENSRNOG00000018289.
DR   Ensembl; ENSRNOT00000087402; ENSRNOP00000072068; ENSRNOG00000018289.
DR   GeneID; 117287; -.
DR   KEGG; rno:117287; -.
DR   UCSC; RGD:621808; rat.
DR   CTD; 11315; -.
DR   RGD; 621808; Park7.
DR   eggNOG; KOG2764; Eukaryota.
DR   eggNOG; COG0693; LUCA.
DR   GeneTree; ENSGT00390000001231; -.
DR   HOGENOM; HOG000063194; -.
DR   HOVERGEN; HBG053511; -.
DR   InParanoid; O88767; -.
DR   KO; K05687; -.
DR   OMA; CYPGFEK; -.
DR   Reactome; R-RNO-3899300; SUMOylation of transcription cofactors.
DR   PRO; PR:O88767; -.
DR   Proteomes; UP000002494; Chromosome 5.
DR   Bgee; ENSRNOG00000018289; Expressed in 10 organ(s), highest expression level in skeletal muscle tissue.
DR   ExpressionAtlas; O88767; baseline and differential.
DR   Genevisible; O88767; RN.
DR   GO; GO:0030424; C:axon; IDA:RGD.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IDA:RGD.
DR   GO; GO:0070062; C:extracellular exosome; ISS:ParkinsonsUK-UCL.
DR   GO; GO:0045121; C:membrane raft; IDA:RGD.
DR   GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:RGD.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016605; C:PML body; ISS:ParkinsonsUK-UCL.
DR   GO; GO:0061827; C:sperm head; IDA:RGD.
DR   GO; GO:0050681; F:androgen receptor binding; ISS:ParkinsonsUK-UCL.
DR   GO; GO:0005507; F:copper ion binding; ISS:UniProtKB.
DR   GO; GO:1903135; F:cupric ion binding; ISS:ParkinsonsUK-UCL.
DR   GO; GO:1903136; F:cuprous ion binding; ISS:ParkinsonsUK-UCL.
DR   GO; GO:0019955; F:cytokine binding; ISS:ParkinsonsUK-UCL.
DR   GO; GO:0036478; F:L-dopa decarboxylase activator activity; ISS:ParkinsonsUK-UCL.
DR   GO; GO:0045340; F:mercury ion binding; ISS:UniProtKB.
DR   GO; GO:0003729; F:mRNA binding; ISS:UniProtKB.
DR   GO; GO:0008233; F:peptidase activity; ISS:UniProtKB.
DR   GO; GO:0036524; F:protein deglycase activity; IBA:GO_Central.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR   GO; GO:0070491; F:repressing transcription factor binding; ISS:ParkinsonsUK-UCL.
DR   GO; GO:0097110; F:scaffold protein binding; ISS:ParkinsonsUK-UCL.
DR   GO; GO:0005102; F:signaling receptor binding; ISS:ParkinsonsUK-UCL.
DR   GO; GO:0044388; F:small protein activating enzyme binding; ISS:ParkinsonsUK-UCL.
DR   GO; GO:0016532; F:superoxide dismutase copper chaperone activity; ISS:ParkinsonsUK-UCL.
DR   GO; GO:0003713; F:transcription coactivator activity; ISS:ParkinsonsUK-UCL.
DR   GO; GO:0008134; F:transcription factor binding; ISS:ParkinsonsUK-UCL.
DR   GO; GO:0036470; F:tyrosine 3-monooxygenase activator activity; ISS:ParkinsonsUK-UCL.
DR   GO; GO:0044390; F:ubiquitin-like protein conjugating enzyme binding; ISS:ParkinsonsUK-UCL.
DR   GO; GO:0007568; P:aging; IEP:RGD.
DR   GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR   GO; GO:0036471; P:cellular response to glyoxal; ISS:ParkinsonsUK-UCL.
DR   GO; GO:0070301; P:cellular response to hydrogen peroxide; ISS:UniProtKB.
DR   GO; GO:0071222; P:cellular response to lipopolysaccharide; IEP:RGD.
DR   GO; GO:0034599; P:cellular response to oxidative stress; ISS:UniProtKB.
DR   GO; GO:0010273; P:detoxification of copper ion; ISS:UniProtKB.
DR   GO; GO:0050787; P:detoxification of mercury ion; ISS:UniProtKB.
DR   GO; GO:0006281; P:DNA repair; ISS:UniProtKB.
DR   GO; GO:0009566; P:fertilization; TAS:ParkinsonsUK-UCL.
DR   GO; GO:0042593; P:glucose homeostasis; ISS:UniProtKB.
DR   GO; GO:0046295; P:glycolate biosynthetic process; ISS: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; ISS:ParkinsonsUK-UCL.
DR   GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR   GO; GO:0030073; P:insulin secretion; ISS:UniProtKB.
DR   GO; GO:0060135; P:maternal process involved in female pregnancy; IEP:RGD.
DR   GO; GO:0007005; P:mitochondrion organization; ISS:UniProtKB.
DR   GO; GO:0060548; P:negative regulation of cell death; ISS:UniProtKB.
DR   GO; GO:2001268; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway; ISS:ParkinsonsUK-UCL.
DR   GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; ISS:ParkinsonsUK-UCL.
DR   GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISS:ParkinsonsUK-UCL.
DR   GO; GO:1901215; P:negative regulation of neuron death; IMP:RGD.
DR   GO; GO:1904782; P:negative regulation of NMDA glutamate receptor activity; IMP:RGD.
DR   GO; GO:1903377; P:negative regulation of oxidative stress-induced neuron intrinsic apoptotic signaling pathway; ISS:ParkinsonsUK-UCL.
DR   GO; GO:1901984; P:negative regulation of protein acetylation; ISS:ParkinsonsUK-UCL.
DR   GO; GO:0032091; P:negative regulation of protein binding; ISS:UniProtKB.
DR   GO; GO:0046826; P:negative regulation of protein export from nucleus; ISS:ParkinsonsUK-UCL.
DR   GO; GO:1903094; P:negative regulation of protein K48-linked deubiquitination; ISS:ParkinsonsUK-UCL.
DR   GO; GO:0006469; P:negative regulation of protein kinase activity; ISS:ParkinsonsUK-UCL.
DR   GO; GO:0001933; P:negative regulation of protein phosphorylation; ISS:ParkinsonsUK-UCL.
DR   GO; GO:0033234; P:negative regulation of protein sumoylation; ISS:ParkinsonsUK-UCL.
DR   GO; GO:0031397; P:negative regulation of protein ubiquitination; ISS:ParkinsonsUK-UCL.
DR   GO; GO:1903427; P:negative regulation of reactive oxygen species biosynthetic process; ISS:UniProtKB.
DR   GO; GO:1903122; P:negative regulation of TRAIL-activated apoptotic signaling pathway; ISS:ParkinsonsUK-UCL.
DR   GO; GO:2000157; P:negative regulation of ubiquitin-specific protease activity; ISS:ParkinsonsUK-UCL.
DR   GO; GO:0002866; P:positive regulation of acute inflammatory response to antigenic stimulus; ISS:UniProtKB.
DR   GO; GO:2000825; P:positive regulation of androgen receptor activity; ISS:ParkinsonsUK-UCL.
DR   GO; GO:1903181; P:positive regulation of dopamine biosynthetic process; ISS:ParkinsonsUK-UCL.
DR   GO; GO:1905516; P:positive regulation of fertilization; IMP:RGD.
DR   GO; GO:0032757; P:positive regulation of interleukin-8 production; ISS:ParkinsonsUK-UCL.
DR   GO; GO:1903197; P:positive regulation of L-dopa biosynthetic process; ISS:ParkinsonsUK-UCL.
DR   GO; GO:1903200; P:positive regulation of L-dopa decarboxylase activity; ISS:ParkinsonsUK-UCL.
DR   GO; GO:1902958; P:positive regulation of mitochondrial electron transport, NADH to ubiquinone; ISS:ParkinsonsUK-UCL.
DR   GO; GO:0033864; P:positive regulation of NAD(P)H oxidase activity; ISS:UniProtKB.
DR   GO; GO:2000277; P:positive regulation of oxidative phosphorylation uncoupler activity; ISS:UniProtKB.
DR   GO; GO:0090073; P:positive regulation of protein homodimerization activity; ISS:ParkinsonsUK-UCL.
DR   GO; GO:1900182; P:positive regulation of protein localization to nucleus; ISS:ParkinsonsUK-UCL.
DR   GO; GO:1903168; P:positive regulation of pyrroline-5-carboxylate reductase activity; ISS:ParkinsonsUK-UCL.
DR   GO; GO:1901671; P:positive regulation of superoxide dismutase activity; ISS:ParkinsonsUK-UCL.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:ParkinsonsUK-UCL.
DR   GO; GO:1903178; P:positive regulation of tyrosine 3-monooxygenase activity; ISS:ParkinsonsUK-UCL.
DR   GO; GO:0036529; P:protein deglycation, glyoxal removal; IBA:GO_Central.
DR   GO; GO:0006517; P:protein deglycosylation; ISS:UniProtKB.
DR   GO; GO:0050821; P:protein stabilization; ISS:UniProtKB.
DR   GO; GO:0060765; P:regulation of androgen receptor signaling pathway; ISS:ParkinsonsUK-UCL.
DR   GO; GO:0050727; P:regulation of inflammatory response; ISS:UniProtKB.
DR   GO; GO:0051881; P:regulation of mitochondrial membrane potential; ISS:ParkinsonsUK-UCL.
DR   GO; GO:0043523; P:regulation of neuron apoptotic process; ISS:UniProtKB.
DR   GO; GO:0042493; P:response to drug; IEP:RGD.
DR   GO; GO:0006979; P:response to oxidative stress; IMP:RGD.
DR   GO; GO:0007338; P:single fertilization; IEA:UniProtKB-KW.
DR   GO; GO:0007283; P:spermatogenesis; IEP:RGD.
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; Fertilization;
KW   Hydrolase; Inflammatory response; Isopeptide bond; Lipoprotein;
KW   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_0000157851.
FT   PROPEP        ?    189       Removed in mature form.
FT                                /FTId=PRO_0000405561.
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:0000250|UniProtKB:Q99LX0}.
FT   MOD_RES     182    182       N6-succinyllysine.
FT                                {ECO:0000250|UniProtKB:Q99LX0}.
FT   LIPID        46     46       S-palmitoyl cysteine.
FT                                {ECO:0000250|UniProtKB:Q99497}.
FT   LIPID        53     53       S-palmitoyl cysteine.
FT                                {ECO:0000250|UniProtKB:Q99497}.
FT   LIPID       106    106       S-palmitoyl cysteine; alternate.
FT                                {ECO:0000250|UniProtKB:Q99497}.
FT   CROSSLNK    130    130       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO).
FT                                {ECO:0000250|UniProtKB:Q99497}.
SQ   SEQUENCE   189 AA;  19974 MW;  08AC2C37D62A9455 CRC64;
     MASKRALVIL AKGAEEMETV IPVDIMRRAG IKVTVAGLAG KDPVQCSRDV VICPDTSLEE
     AKTQGPYDVV VLPGGNLGAQ NLSESALVKE ILKEQENRKG LIAAICAGPT ALLAHEVGFG
     CKVTSHPLAK DKMMNGSHYS YSESRVEKDG LILTSRGPGT SFEFALAIVE ALSGKDMANQ
     VKAPLVLKD
//
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