PARK7_BOVIN
ID PARK7_BOVIN Reviewed; 189 AA.
AC Q5E946; Q3ZC96;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 121.
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:0000250|UniProtKB:Q99497};
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;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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. 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. Has been described as a protein and
CC nucleotide deglycase that catalyzes the deglycation of the Maillard
CC adducts formed between amino groups of proteins or nucleotides and
CC reactive carbonyl groups of glyoxals. But this function is rebuted by
CC other works. As a protein deglycase, repairs methylglyoxal- and
CC glyoxal-glycated proteins, and releases repaired proteins and lactate
CC or glycolate, respectively. Deglycates cysteine, arginine and lysine
CC residues in proteins, and thus reactivates these proteins by reversing
CC glycation by glyoxals. Acts on early glycation intermediates
CC (hemithioacetals and aminocarbinols), preventing the formation of
CC advanced glycation endproducts (AGE) that cause irreversible damage.
CC Also functions as a nucleotide deglycase able to repair glycated
CC guanine in the free nucleotide pool (GTP, GDP, GMP, dGTP) and in DNA
CC and RNA. Is thus involved in a major nucleotide repair system named
CC guanine glycation repair (GG repair), dedicated to reversing
CC methylglyoxal and glyoxal damage via nucleotide sanitization and direct
CC nucleic acid repair. Protects histones from adduction by methylglyoxal,
CC controls the levels of methylglyoxal-derived argininine modifications
CC on chromatin. Able to remove the glycations and restore histone 3,
CC histone glycation disrupts both local and global chromatin architecture
CC by altering histone-DNA interactions as well as histone acetylation and
CC ubiquitination levels. Displays a very low glyoxalase activity that may
CC reflect its deglycase activity. Eliminates hydrogen peroxide and
CC protects cells against hydrogen peroxide-induced cell death. Required
CC for correct mitochondrial morphology and function as well as for
CC autophagy of dysfunctional mitochondria. Plays a role in regulating
CC expression or stability of the mitochondrial uncoupling proteins
CC SLC25A14 and SLC25A27 in dopaminergic neurons of the substantia nigra
CC pars compacta and attenuates the oxidative stress induced by calcium
CC entry into the neurons via L-type channels during pacemaking. Regulates
CC astrocyte inflammatory responses, may modulate lipid rafts-dependent
CC endocytosis in astrocytes and neuronal cells. In pancreatic islets,
CC involved in the maintenance of mitochondrial reactive oxygen species
CC (ROS) 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. Binds to a number of mRNAs
CC containing multiple copies of GG or CC motifs and partially inhibits
CC their translation but dissociates following oxidative stress. Metal-
CC binding protein able to bind copper as well as toxic mercury ions,
CC enhances the cell protection mechanism against induced metal toxicity.
CC In macrophages, interacts with the NADPH oxidase subunit NCF1 to direct
CC NADPH oxidase-dependent ROS production, and protects against sepsis.
CC {ECO:0000250|UniProtKB:Q99497, ECO:0000250|UniProtKB:Q99LX0}.
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. Interacts (via N-
CC terminus) with OTUD7B. Interacts with BBS1, HIPK1, CLCF1 and MTERF.
CC Forms a complex with PINK1 and PRKN (By similarity). Interacts (via C-
CC terminus) with NCF1; the interaction is enhanced by LPS and modulates
CC NCF1 phosphorylation and membrane translocation (By similarity).
CC Interacts with NENF (By similarity). {ECO:0000250|UniProtKB:Q99497,
CC ECO:0000250|UniProtKB:Q99LX0}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O88767};
CC Lipid-anchor {ECO:0000250|UniProtKB:O88767}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q99497}. Nucleus {ECO:0000250|UniProtKB:Q99497}.
CC Membrane raft {ECO:0000250|UniProtKB:O88767}. Mitochondrion
CC {ECO:0000250|UniProtKB:Q99497}. Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:Q99497}. 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. Membrane raft
CC localization in astrocytes and neuronal cells requires palmitoylation.
CC {ECO:0000250|UniProtKB:Q99497}.
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 -!- SIMILARITY: Belongs to the peptidase C56 family. {ECO:0000305}.
CC -!- CAUTION: Glyoxalase activity has been reported. It may however reflect
CC its deglycase activity. {ECO:0000250|UniProtKB:Q99497}.
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}.
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DR EMBL; BT021074; AAX09091.1; -; mRNA.
DR EMBL; BC102707; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; NP_001015572.1; NM_001015572.1.
DR RefSeq; XP_005217012.1; XM_005216955.3.
DR RefSeq; XP_005217013.1; XM_005216956.3.
DR AlphaFoldDB; Q5E946; -.
DR SMR; Q5E946; -.
DR STRING; 9913.ENSBTAP00000027339; -.
DR MEROPS; C56.971; -.
DR PaxDb; Q5E946; -.
DR PeptideAtlas; Q5E946; -.
DR PRIDE; Q5E946; -.
DR Ensembl; ENSBTAT00000027339; ENSBTAP00000027339; ENSBTAG00000020518.
DR GeneID; 511268; -.
DR KEGG; bta:511268; -.
DR CTD; 11315; -.
DR VEuPathDB; HostDB:ENSBTAG00000020518; -.
DR VGNC; VGNC:32586; PARK7.
DR eggNOG; KOG2764; Eukaryota.
DR GeneTree; ENSGT00390000001231; -.
DR HOGENOM; CLU_000445_44_2_1; -.
DR InParanoid; Q5E946; -.
DR OMA; TSYPAMK; -.
DR OrthoDB; 1165707at2759; -.
DR TreeFam; TF300119; -.
DR Proteomes; UP000009136; Chromosome 16.
DR Bgee; ENSBTAG00000020518; Expressed in temporal cortex and 101 other tissues.
DR GO; GO:0044297; C:cell body; IEA:Ensembl.
DR GO; GO:0000785; C:chromatin; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IEA:Ensembl.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:Ensembl.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0043005; C:neuron projection; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016605; C:PML body; IEA:Ensembl.
DR GO; GO:0098793; C:presynapse; IEA:GOC.
DR GO; GO:0005507; F:copper ion binding; ISS:UniProtKB.
DR GO; GO:1903135; F:cupric ion binding; IEA:Ensembl.
DR GO; GO:1903136; F:cuprous ion binding; IEA:Ensembl.
DR GO; GO:0019955; F:cytokine binding; IEA:Ensembl.
DR GO; GO:1990422; F:glyoxalase (glycolic acid-forming) activity; ISS:UniProtKB.
DR GO; GO:0019900; F:kinase binding; IEA:Ensembl.
DR GO; GO:0036478; F:L-dopa decarboxylase activator activity; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0016684; F:oxidoreductase activity, acting on peroxide as acceptor; IBA:GO_Central.
DR GO; GO:0019826; F:oxygen sensor activity; IEA:Ensembl.
DR GO; GO:0008233; F:peptidase activity; ISS:UniProtKB.
DR GO; GO:0051920; F:peroxiredoxin activity; IEA:Ensembl.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR GO; GO:0097110; F:scaffold protein binding; IEA:Ensembl.
DR GO; GO:0005102; F:signaling receptor binding; IEA:Ensembl.
DR GO; GO:0044388; F:small protein activating enzyme binding; IEA:Ensembl.
DR GO; GO:0016532; F:superoxide dismutase copper chaperone activity; IEA:Ensembl.
DR GO; GO:0003713; F:transcription coactivator activity; IEA:Ensembl.
DR GO; GO:0036470; F:tyrosine 3-monooxygenase activator activity; IEA:Ensembl.
DR GO; GO:0044390; F:ubiquitin-like protein conjugating enzyme binding; IEA:Ensembl.
DR GO; GO:1990381; F:ubiquitin-specific protease binding; IEA:Ensembl.
DR GO; GO:0008344; P:adult locomotory behavior; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0070301; P:cellular response to hydrogen peroxide; ISS:UniProtKB.
DR GO; GO:0034599; P:cellular response to oxidative stress; ISS:UniProtKB.
DR GO; GO:0070994; P:detection of oxidative stress; IEA:Ensembl.
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:0051583; P:dopamine uptake involved in synaptic transmission; IEA:Ensembl.
DR GO; GO:0042593; P:glucose homeostasis; ISS:UniProtKB.
DR GO; GO:0036531; P:glutathione deglycation; IEA:Ensembl.
DR GO; GO:0046295; P:glycolate biosynthetic process; IBA:GO_Central.
DR GO; GO:1903189; P:glyoxal metabolic process; IBA:GO_Central.
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:0016570; P:histone modification; ISS:UniProtKB.
DR GO; GO:0042743; P:hydrogen peroxide metabolic process; IEA:Ensembl.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR GO; GO:0030073; P:insulin secretion; ISS:UniProtKB.
DR GO; GO:0051899; P:membrane depolarization; IEA:Ensembl.
DR GO; GO:0060081; P:membrane hyperpolarization; IEA:Ensembl.
DR GO; GO:0061727; P:methylglyoxal catabolic process to lactate; ISS:UniProtKB.
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; IEA:Ensembl.
DR GO; GO:1902236; P:negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
DR GO; GO:1903384; P:negative regulation of hydrogen peroxide-induced neuron intrinsic apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:1901215; P:negative regulation of neuron death; IBA:GO_Central.
DR GO; GO:1905259; P:negative regulation of nitrosative stress-induced intrinsic apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; IEA:Ensembl.
DR GO; GO:1901984; P:negative regulation of protein acetylation; IEA:Ensembl.
DR GO; GO:0032091; P:negative regulation of protein binding; ISS:UniProtKB.
DR GO; GO:0046826; P:negative regulation of protein export from nucleus; IEA:Ensembl.
DR GO; GO:1903094; P:negative regulation of protein K48-linked deubiquitination; IEA:Ensembl.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; IEA:Ensembl.
DR GO; GO:0033234; P:negative regulation of protein sumoylation; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0051444; P:negative regulation of ubiquitin-protein transferase activity; IEA:Ensembl.
DR GO; GO:2000157; P:negative regulation of ubiquitin-specific protease activity; IEA:Ensembl.
DR GO; GO:0036527; P:peptidyl-arginine deglycation; ISS:UniProtKB.
DR GO; GO:0036526; P:peptidyl-cysteine deglycation; IEA:Ensembl.
DR GO; GO:0036528; P:peptidyl-lysine deglycation; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:1903181; P:positive regulation of dopamine biosynthetic process; IEA:Ensembl.
DR GO; GO:0032757; P:positive regulation of interleukin-8 production; IEA:Ensembl.
DR GO; GO:1903197; P:positive regulation of L-dopa biosynthetic process; IEA:Ensembl.
DR GO; GO:1902958; P:positive regulation of mitochondrial electron transport, NADH to ubiquinone; IEA:Ensembl.
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:1902177; P:positive regulation of oxidative stress-induced intrinsic apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IEA:Ensembl.
DR GO; GO:1900182; P:positive regulation of protein localization to nucleus; IEA:Ensembl.
DR GO; GO:0031334; P:positive regulation of protein-containing complex assembly; IEA:Ensembl.
DR GO; GO:1903168; P:positive regulation of pyrroline-5-carboxylate reductase activity; IEA:Ensembl.
DR GO; GO:1903428; P:positive regulation of reactive oxygen species biosynthetic process; IEA:Ensembl.
DR GO; GO:1901671; P:positive regulation of superoxide dismutase activity; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:2000679; P:positive regulation of transcription regulatory region DNA binding; IEA:Ensembl.
DR GO; GO:0036529; P:protein deglycation, glyoxal removal; IEA:Ensembl.
DR GO; GO:0036530; P:protein deglycation, methylglyoxal removal; ISS:UniProtKB.
DR GO; GO:0006517; P:protein deglycosylation; ISS:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; ISS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0060765; P:regulation of androgen receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0035065; P:regulation of histone acetylation; ISS:UniProtKB.
DR GO; GO:0033182; P:regulation of histone ubiquitination; ISS:UniProtKB.
DR GO; GO:0050727; P:regulation of inflammatory response; ISS:UniProtKB.
DR GO; GO:0051881; P:regulation of mitochondrial membrane potential; IEA:Ensembl.
DR GO; GO:0043523; P:regulation of neuron apoptotic process; ISS:UniProtKB.
DR GO; GO:0006979; P:response to oxidative stress; IBA:GO_Central.
DR GO; GO:0007338; P:single fertilization; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.880; -; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR006287; DJ-1.
DR InterPro; IPR002818; DJ-1/PfpI.
DR Pfam; PF01965; DJ-1_PfpI; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
DR TIGRFAMs; TIGR01383; not_thiJ; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Autophagy; Cell membrane; Chaperone; Copper; Cytoplasm;
KW Endoplasmic reticulum; Fertilization; Hydrolase; Inflammatory response;
KW Isopeptide bond; Lipoprotein; Membrane; Mitochondrion; Nucleus; Oxidation;
KW Palmitate; Phosphoprotein; Protease; Reference proteome; RNA-binding;
KW Stress response; 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_0000252485"
FT PROPEP ?..189
FT /note="Removed in mature form"
FT /id="PRO_0000405556"
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:0000250|UniProtKB:Q99LX0"
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:0000250|UniProtKB:Q99LX0"
FT MOD_RES 182
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99LX0"
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"
SQ SEQUENCE 189 AA; 20035 MW; C63FAA8D71056F2C CRC64;
MASKRALVIL AKGAEEMETV IPVDVMRRAG IKVTVAGLAG KDPVQCSRDV VICPDASLED
AKKEGPYDVV VLPGGNLGAQ NLSESAAVKE ILKEQEKRKG LIAAICAGPT ALLAHEIGFG
SKVTTHPLAK DKMMNGSHYS YSENRVEKDG LILTSRGPGT SFEFALKIVE VLVGKEVADQ
VKAPLVLKD
