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 03-AUG-2022, entry version 155.
DE RecName: Full=Parkinson disease protein 7 homolog {ECO:0000305};
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=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 {ECO:0000312|RGD:621808}; Synonyms=Cap1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 13-29 AND 65-74, AND TISSUE
RP 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 protein 1
RT (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 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, AND
RP SUBCELLULAR LOCATION.
RX PubMed=10022524;
RX DOI=10.1002/(sici)1097-4644(19990301)72:3<435::aid-jcb12>3.0.co;2-h;
RA Hod Y., Pentyala S.N., Whyard T.C., El-Maghrabi M.R.;
RT "Identification and characterization of a novel protein that regulates RNA-
RT 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 lipid
RT rafts-dependent endocytosis in astrocytes.";
RL Hum. Mol. Genet. 22:4805-4817(2013).
RN [7]
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).
RN [8]
RP DISRUPTION PHENOTYPE.
RX PubMed=31250274; DOI=10.1007/s12031-019-01358-0;
RA Kyser T.L., Dourson A.J., McGuire J.L., Hemmerle A.M., Williams M.T.,
RA Seroogy K.B.;
RT "Characterization of Motor and Non-Motor Behavioral Alterations in the Dj-1
RT (PARK7) Knockout Rat.";
RL J. Mol. Neurosci. 69:298-311(2019).
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. Thus,
CC functions as a protein deglycase that 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. Also displays an apparent glyoxalase activity that
CC in fact reflects its deglycase activity. Plays an important role in
CC cell protection against oxidative stress and cell death acting as
CC oxidative stress sensor and redox-sensitive chaperone and protease;
CC functions probably related to its primary function. It is involved in
CC neuroprotective mechanisms like the stabilization of NFE2L2 and PINK1
CC proteins, male fertility as a positive regulator of androgen signaling
CC pathway as well as cell growth and transformation through, for
CC instance, the modulation of NF-kappa-B signaling pathway. Eliminates
CC hydrogen peroxide and protects cells against hydrogen peroxide-induced
CC cell death. Required for correct mitochondrial morphology and function
CC as well 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 during
CC pacemaking. Regulates astrocyte inflammatory responses, may modulate
CC lipid rafts-dependent endocytosis in astrocytes and neuronal cells (By
CC similarity). In pancreatic islets, involved in the maintenance of
CC mitochondrial reactive oxygen species (ROS) levels and glucose
CC homeostasis in an age- and diet dependent manner. Protects pancreatic
CC beta cells from cell death induced by inflammatory and cytotoxic
CC setting (By similarity). Binds to a number of mRNAs containing multiple
CC copies of GG or CC motifs and partially inhibits their translation but
CC dissociates following oxidative stress. Metal-binding protein able to
CC bind copper as well as toxic mercury ions, enhances the cell protection
CC mechanism against induced metal toxicity (By similarity). In
CC macrophages, interacts with the NADPH oxidase subunit NCF1 to direct
CC NADPH oxidase-dependent ROS production, and protects against sepsis (By
CC similarity). {ECO:0000250|UniProtKB:Q99497,
CC 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 (PubMed:31536960). {ECO:0000250|UniProtKB:Q99497,
CC ECO:0000250|UniProtKB:Q99LX0, ECO:0000269|PubMed:31536960}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q99LX0};
CC Lipid-anchor {ECO:0000250|UniProtKB:Q99LX0}. Cytoplasm
CC {ECO:0000269|PubMed:10022524}. Membrane raft
CC {ECO:0000269|PubMed:23847046}. Nucleus {ECO:0000269|PubMed:10022524}.
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: Ubiquitous. Detected on epididymal sperm. Highly
CC expressed in testis and prostate. Detected at lower levels in heart,
CC lung, brain, liver, kidney, seminal vesicle, caput and corpus
CC epididymis. {ECO:0000269|PubMed:9792810}.
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: Mutants rear and groom less, they have a shorter
CC stride length than their wild-type counterparts, but take more forelimb
CC and hindlimb steps. They display deficits in short-term spatial memory
CC as early as 4.5 months of age during place preference testing, as well
CC as impaired coping strategies in the forced swim test.
CC {ECO:0000269|PubMed:31250274}.
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; 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 AlphaFoldDB; O88767; -.
DR SMR; O88767; -.
DR BioGRID; 250731; 92.
DR IntAct; O88767; 2.
DR MINT; O88767; -.
DR STRING; 10116.ENSRNOP00000024711; -.
DR MEROPS; C56.002; -.
DR iPTMnet; O88767; -.
DR PhosphoSitePlus; O88767; -.
DR World-2DPAGE; 0004:O88767; -.
DR jPOST; O88767; -.
DR PaxDb; O88767; -.
DR PRIDE; O88767; -.
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 GeneTree; ENSGT00390000001231; -.
DR HOGENOM; CLU_000445_44_2_1; -.
DR InParanoid; O88767; -.
DR OMA; TSYPAMK; -.
DR Reactome; R-RNO-3899300; SUMOylation of transcription cofactors.
DR Reactome; R-RNO-9646399; Aggrephagy.
DR PRO; PR:O88767; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000018289; Expressed in skeletal muscle tissue and 19 other tissues.
DR ExpressionAtlas; O88767; baseline and differential.
DR Genevisible; O88767; RN.
DR GO; GO:0030424; C:axon; IDA:RGD.
DR GO; GO:0044297; C:cell body; ISO:RGD.
DR GO; GO:0000785; C:chromatin; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; ISS:ParkinsonsUK-UCL.
DR GO; GO:0045121; C:membrane raft; IDA:RGD.
DR GO; GO:0005758; C:mitochondrial intermembrane space; ISO:RGD.
DR GO; GO:0005759; C:mitochondrial matrix; ISO:RGD.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0043005; C:neuron projection; ISO:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016605; C:PML body; ISS:ParkinsonsUK-UCL.
DR GO; GO:0098793; C:presynapse; IEA:GOC.
DR GO; GO:0061827; C:sperm head; IDA:RGD.
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:0140297; F:DNA-binding transcription factor binding; ISS:ParkinsonsUK-UCL.
DR GO; GO:0019899; F:enzyme binding; ISO:RGD.
DR GO; GO:1990422; F:glyoxalase (glycolic acid-forming) activity; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0019900; F:kinase binding; ISO:RGD.
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:0050681; F:nuclear androgen receptor binding; ISS:ParkinsonsUK-UCL.
DR GO; GO:0016684; F:oxidoreductase activity, acting on peroxide as acceptor; ISO:RGD.
DR GO; GO:0019826; F:oxygen sensor activity; ISO:RGD.
DR GO; GO:0008233; F:peptidase activity; ISS:UniProtKB.
DR GO; GO:0051920; F:peroxiredoxin activity; ISO:RGD.
DR GO; GO:0036524; F:protein deglycase activity; ISO:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:RGD.
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: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:1990381; F:ubiquitin-specific protease binding; ISO:RGD.
DR GO; GO:0008344; P:adult locomotory behavior; ISO:RGD.
DR GO; GO:0007568; P:aging; IEP:RGD.
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; ISS:ParkinsonsUK-UCL.
DR GO; GO:0070301; P:cellular response to hydrogen peroxide; ISS:UniProtKB.
DR GO; GO:0071456; P:cellular response to hypoxia; IEP:RGD.
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:0034614; P:cellular response to reactive oxygen species; ISO:RGD.
DR GO; GO:0070994; P:detection of oxidative stress; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0009566; P:fertilization; TAS:ParkinsonsUK-UCL.
DR GO; GO:0042593; P:glucose homeostasis; ISS:UniProtKB.
DR GO; GO:0036531; P:glutathione deglycation; ISO:RGD.
DR GO; GO:0046295; P:glycolate biosynthetic process; ISS:ParkinsonsUK-UCL.
DR GO; GO:1903189; P:glyoxal metabolic process; ISO:RGD.
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; 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:0019249; P:lactate biosynthetic process; ISO:RGD.
DR GO; GO:0060135; P:maternal process involved in female pregnancy; IEP:RGD.
DR GO; GO:0051899; P:membrane depolarization; ISO:RGD.
DR GO; GO:0060081; P:membrane hyperpolarization; ISO:RGD.
DR GO; GO:0061727; P:methylglyoxal catabolic process to lactate; ISS:UniProtKB.
DR GO; GO:0009438; P:methylglyoxal metabolic process; ISO:RGD.
DR GO; GO:0007005; P:mitochondrion organization; ISS:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:RGD.
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:1902236; P:negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway; ISO:RGD.
DR GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; ISS:ParkinsonsUK-UCL.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:RGD.
DR GO; GO:1903206; P:negative regulation of hydrogen peroxide-induced cell death; ISO:RGD.
DR GO; GO:1903208; P:negative regulation of hydrogen peroxide-induced neuron death; ISO:RGD.
DR GO; GO:1903384; P:negative regulation of hydrogen peroxide-induced neuron intrinsic apoptotic signaling pathway; ISO:RGD.
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:1905259; P:negative regulation of nitrosative stress-induced intrinsic apoptotic signaling pathway; ISO:RGD.
DR GO; GO:1904782; P:negative regulation of NMDA glutamate receptor activity; IMP:RGD.
DR GO; GO:1903202; P:negative regulation of oxidative stress-induced cell death; ISO:RGD.
DR GO; GO:1903204; P:negative regulation of oxidative stress-induced neuron death; ISO:RGD.
DR GO; GO:1903377; P:negative regulation of oxidative stress-induced neuron intrinsic apoptotic signaling pathway; ISS:ParkinsonsUK-UCL.
DR GO; GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; ISO:RGD.
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:0042177; P:negative regulation of protein catabolic process; ISO:RGD.
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:0014912; P:negative regulation of smooth muscle cell migration; IDA:RGD.
DR GO; GO:1903122; P:negative regulation of TRAIL-activated apoptotic signaling pathway; ISS:ParkinsonsUK-UCL.
DR GO; GO:0051444; P:negative regulation of ubiquitin-protein transferase activity; ISO:RGD.
DR GO; GO:2000157; P:negative regulation of ubiquitin-specific protease activity; ISS:ParkinsonsUK-UCL.
DR GO; GO:1904706; P:negative regulation of vascular associated smooth muscle cell proliferation; IDA:RGD.
DR GO; GO:0036527; P:peptidyl-arginine deglycation; ISS:UniProtKB.
DR GO; GO:0036526; P:peptidyl-cysteine deglycation; ISO:RGD.
DR GO; GO:0036528; P:peptidyl-lysine deglycation; ISO:RGD.
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:0051091; P:positive regulation of DNA-binding transcription factor activity; ISO:RGD.
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:0010628; P:positive regulation of gene expression; ISO: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:1902177; P:positive regulation of oxidative stress-induced intrinsic apoptotic signaling pathway; ISO:RGD.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; ISO:RGD.
DR GO; GO:1900182; P:positive regulation of protein localization to nucleus; ISS:ParkinsonsUK-UCL.
DR GO; GO:0031334; P:positive regulation of protein-containing complex assembly; ISS:ParkinsonsUK-UCL.
DR GO; GO:1903168; P:positive regulation of pyrroline-5-carboxylate reductase activity; ISS:ParkinsonsUK-UCL.
DR GO; GO:1903428; P:positive regulation of reactive oxygen species biosynthetic process; ISO:RGD.
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:2000679; P:positive regulation of transcription regulatory region DNA binding; ISO:RGD.
DR GO; GO:1903178; P:positive regulation of tyrosine 3-monooxygenase activity; ISS:ParkinsonsUK-UCL.
DR GO; GO:0036529; P:protein deglycation, glyoxal removal; ISO:RGD.
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; ISS:ParkinsonsUK-UCL.
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; ISS:ParkinsonsUK-UCL.
DR GO; GO:0043523; P:regulation of neuron apoptotic process; ISS:UniProtKB.
DR GO; GO:0042542; P:response to hydrogen peroxide; ISO:RGD.
DR GO; GO:0006979; P:response to oxidative stress; IMP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0007338; P:single fertilization; IEA:UniProtKB-KW.
DR GO; GO:0007283; P:spermatogenesis; IEP:RGD.
DR GO; GO:0001963; P:synaptic transmission, dopaminergic; ISO: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; Copper; Cytoplasm;
KW Direct protein sequencing; Endoplasmic reticulum; Fertilization; Hydrolase;
KW Inflammatory response; Isopeptide bond; Lipoprotein; Membrane;
KW Mitochondrion; Nucleus; Oxidation; Palmitate; Phosphoprotein; Protease;
KW Reference proteome; RNA-binding; Stress response; Tumor suppressor;
KW 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_0000157851"
FT PROPEP ?..189
FT /note="Removed in mature form"
FT /id="PRO_0000405561"
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; 19974 MW; 08AC2C37D62A9455 CRC64;
MASKRALVIL AKGAEEMETV IPVDIMRRAG IKVTVAGLAG KDPVQCSRDV VICPDTSLEE
AKTQGPYDVV VLPGGNLGAQ NLSESALVKE ILKEQENRKG LIAAICAGPT ALLAHEVGFG
CKVTSHPLAK DKMMNGSHYS YSESRVEKDG LILTSRGPGT SFEFALAIVE ALSGKDMANQ
VKAPLVLKD
