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Database: UniProt/SWISS-PROT
Entry: PARK7_DANRE
LinkDB: PARK7_DANRE
Original site: PARK7_DANRE 
ID   PARK7_DANRE             Reviewed;         189 AA.
AC   Q5XJ36;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   05-DEC-2018, entry version 100.
DE   RecName: Full=Protein/nucleic acid deglycase DJ-1 {ECO:0000250|UniProtKB:Q99497};
DE            EC=3.1.2.- {ECO:0000250|UniProtKB:Q99497};
DE            EC=3.5.1.- {ECO:0000250|UniProtKB:Q99497};
DE            EC=3.5.1.124 {ECO:0000250|UniProtKB:Q99497};
DE   AltName: Full=Maillard deglycase {ECO:0000250|UniProtKB:Q99497};
DE   AltName: Full=Parkinson disease protein 7 homolog {ECO:0000305};
DE   AltName: Full=Parkinsonism-associated deglycase {ECO:0000250|UniProtKB:Q99497};
DE   AltName: Full=Protein DJ-1zDJ-1 {ECO:0000250|UniProtKB:Q99497};
DE            Short=zDJ-1;
DE   Flags: Precursor;
GN   Name=park7 {ECO:0000312|EMBL:AAH83475.1};
GN   Synonyms=dj1 {ECO:0000312|EMBL:ABI64158.1}; ORFNames=zgc:103725;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Cyprinidae; Danio.
OX   NCBI_TaxID=7955;
RN   [1] {ECO:0000312|EMBL:ABI64158.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP   AND DEVELOPMENTAL STAGE.
RC   STRAIN=AB {ECO:0000312|EMBL:ABI64158.1};
RC   TISSUE=Brain {ECO:0000269|PubMed:16942755};
RX   PubMed=16942755; DOI=10.1016/j.brainres.2006.07.057;
RA   Bai Q., Mullett S.J., Garver J.A., Hinkle D.A., Burton E.A.;
RT   "Zebrafish DJ-1 is evolutionarily conserved and expressed in
RT   dopaminergic neurons.";
RL   Brain Res. 1113:33-44(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND
RP   DEVELOPMENTAL STAGE.
RX   PubMed=17166173; DOI=10.1111/j.1471-4159.2006.04291.x;
RA   Bretaud S., Allen C., Ingham P.W., Bandmann O.;
RT   "p53-dependent neuronal cell death in a DJ-1-deficient zebrafish model
RT   of Parkinson's disease.";
RL   J. Neurochem. 100:1626-1635(2007).
RN   [3] {ECO:0000312|EMBL:AAH83475.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=AB; TISSUE=Liver {ECO:0000312|EMBL:AAH83475.1};
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
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 (By
CC       similarity). Plays an important role in cell protection against
CC       oxidative stress and cell death acting as oxidative stress sensor
CC       and redox-sensitive chaperone and protease (PubMed:17166173). It
CC       is involved in neuroprotective mechanisms as well as cell growth
CC       and transformation. Its involvement in protein repair could also
CC       explain other unrelated functions. Eliminates hydrogen peroxide
CC       and 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. Regulates
CC       astrocyte inflammatory responses, may modulate lipid rafts-
CC       dependent endocytosis in astrocytes and neuronal cells. 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).
CC       {ECO:0000250|UniProtKB:Q99497, ECO:0000250|UniProtKB:Q99LX0,
CC       ECO:0000269|PubMed:17166173}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N(omega)-(1-hydroxy-2-oxopropyl)-L-arginyl-
CC         [protein] = H(+) + L-arginyl-[protein] + lactate;
CC         Xref=Rhea:RHEA:49548, Rhea:RHEA-COMP:10532, Rhea:RHEA-
CC         COMP:12428, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:24996, ChEBI:CHEBI:29965, ChEBI:CHEBI:131708;
CC         EC=3.5.1.124; Evidence={ECO:0000250|UniProtKB:Q99497};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N(6)-(1-hydroxy-2-oxopropyl)-L-lysyl-[protein] =
CC         H(+) + L-lysyl-[protein] + lactate; Xref=Rhea:RHEA:49552,
CC         Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:12429, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:29969,
CC         ChEBI:CHEBI:131709; EC=3.5.1.124;
CC         Evidence={ECO:0000250|UniProtKB:Q99497};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + S-(1-hydroxy-2-oxopropyl)-L-cysteinyl-[protein] =
CC         H(+) + L-cysteinyl-[protein] + lactate; Xref=Rhea:RHEA:49556,
CC         Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:12430, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:29950,
CC         ChEBI:CHEBI:131710; EC=3.5.1.124;
CC         Evidence={ECO:0000250|UniProtKB:Q99497};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N(omega)-(1-hydroxy-2-oxoethyl)-L-arginyl-[protein]
CC         = glycolate + H(+) + L-arginyl-[protein]; Xref=Rhea:RHEA:57188,
CC         Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:14844, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:29965,
CC         ChEBI:CHEBI:141553; EC=3.5.1.124;
CC         Evidence={ECO:0000250|UniProtKB:Q99497};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N(6)-(1-hydroxy-2-oxoethyl)-L-lysyl-[protein] =
CC         glycolate + H(+) + L-lysyl-[protein]; Xref=Rhea:RHEA:57192,
CC         Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:14845, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:29969,
CC         ChEBI:CHEBI:141554; EC=3.5.1.124;
CC         Evidence={ECO:0000250|UniProtKB:Q99497};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + S-(1-hydroxy-2-oxoethyl)-L-cysteinyl-[protein] =
CC         glycolate + H(+) + L-cysteinyl-[protein]; Xref=Rhea:RHEA:57196,
CC         Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:14846, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:29950,
CC         ChEBI:CHEBI:141555; EC=3.5.1.124;
CC         Evidence={ECO:0000250|UniProtKB:Q99497};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-dGTP = dGTP + H(+) +
CC         lactate; Xref=Rhea:RHEA:57244, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:61429,
CC         ChEBI:CHEBI:141569; Evidence={ECO:0000250|UniProtKB:Q99497};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-GTP = GTP + H(+) +
CC         lactate; Xref=Rhea:RHEA:57256, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:37565,
CC         ChEBI:CHEBI:141570; Evidence={ECO:0000250|UniProtKB:Q99497};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-GDP = GDP + H(+) +
CC         lactate; Xref=Rhea:RHEA:57260, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:58189,
CC         ChEBI:CHEBI:141573; Evidence={ECO:0000250|UniProtKB:Q99497};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-GMP = GMP + H(+) +
CC         lactate; Xref=Rhea:RHEA:57268, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:58115,
CC         ChEBI:CHEBI:141575; Evidence={ECO:0000250|UniProtKB:Q99497};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N(2)-(1-hydroxy-2-oxoethyl)-dGTP = dGTP + glycolate
CC         + H(+); Xref=Rhea:RHEA:57248, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:61429,
CC         ChEBI:CHEBI:141572; Evidence={ECO:0000250|UniProtKB:Q99497};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N(2)-(1-hydroxy-2-oxoethyl)-GTP = glycolate + GTP +
CC         H(+); Xref=Rhea:RHEA:57252, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:37565,
CC         ChEBI:CHEBI:141571; Evidence={ECO:0000250|UniProtKB:Q99497};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N(2)-(1-hydroxy-2-oxoethyl)-GDP = GDP + glycolate +
CC         H(+); Xref=Rhea:RHEA:57264, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:58189,
CC         ChEBI:CHEBI:141574; Evidence={ECO:0000250|UniProtKB:Q99497};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N(2)-(1-hydroxy-2-oxoethyl)-GMP = glycolate + GMP +
CC         H(+); Xref=Rhea:RHEA:57304, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:58115,
CC         ChEBI:CHEBI:141576; Evidence={ECO:0000250|UniProtKB:Q99497};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an N(2)-(1-hydroxy-2-oxopropyl)-guanosine in RNA + H2O =
CC         a guanosine in RNA + H(+) + lactate; Xref=Rhea:RHEA:57288,
CC         Rhea:RHEA-COMP:14855, Rhea:RHEA-COMP:14858, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:74269,
CC         ChEBI:CHEBI:141580; Evidence={ECO:0000250|UniProtKB:Q99497};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an N(2)-(1-hydroxy-2-oxopropyl)-2'-deoxyguanosine in DNA
CC         + H2O = a 2'-deoxyguanosine in DNA + H(+) + lactate;
CC         Xref=Rhea:RHEA:57300, Rhea:RHEA-COMP:11367, Rhea:RHEA-
CC         COMP:14856, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:24996, ChEBI:CHEBI:85445, ChEBI:CHEBI:141578;
CC         Evidence={ECO:0000250|UniProtKB:Q99497};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an N(2)-(1-hydroxy-2-oxoethyl)-guanosine in RNA + H2O = a
CC         guanosine in RNA + glycolate + H(+); Xref=Rhea:RHEA:57292,
CC         Rhea:RHEA-COMP:14855, Rhea:RHEA-COMP:14859, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:74269,
CC         ChEBI:CHEBI:141581; Evidence={ECO:0000250|UniProtKB:Q99497};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an N(2)-(1-hydroxy-2-oxoethyl)-2'-deoxyguanosine in DNA +
CC         H2O = a 2'-deoxyguanosine in DNA + glycolate + H(+);
CC         Xref=Rhea:RHEA:57296, Rhea:RHEA-COMP:11367, Rhea:RHEA-
CC         COMP:14857, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29805, ChEBI:CHEBI:85445, ChEBI:CHEBI:141579;
CC         Evidence={ECO:0000250|UniProtKB:Q99497};
CC   -!- COFACTOR:
CC       Note=Deglycase activity does not require glutathione as a
CC       cofactor, however, glycated glutathione constitutes a PARK7
CC       substrate. {ECO:0000250|UniProtKB:Q99497};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q99497}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane
CC       {ECO:0000250|UniProtKB:O88767}; Lipid-anchor
CC       {ECO:0000250|UniProtKB:O88767}. Cytoplasm
CC       {ECO:0000250|UniProtKB:Q99497}. Nucleus
CC       {ECO:0000250|UniProtKB:Q99497}. Membrane raft
CC       {ECO:0000250|UniProtKB:O88767}. 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. Detected in tau inclusions in brains from
CC       neurodegenerative disease patients. Membrane raft localization in
CC       astrocytes and neuronal cells requires palmitoylation.
CC       {ECO:0000250|UniProtKB:Q99497}.
CC   -!- TISSUE SPECIFICITY: Larval brain and gut from 96 hours post-
CC       fertilization (hpf). Ubiquitous in adult; most abundant in brain,
CC       eye, heart and muscle. Within brain, neuronal expression is
CC       widespread, particularly in the cerebellum, medullary reticular
CC       formation and diencephalon. Expressed in major forebrain and
CC       diencephalic dopaminergic cell groups.
CC       {ECO:0000269|PubMed:16942755, ECO:0000269|PubMed:17166173}.
CC   -!- DEVELOPMENTAL STAGE: Present from tailbud stage (10 hpf) through
CC       to adult. Levels increase from 24-120 hpf.
CC       {ECO:0000269|PubMed:16942755, ECO:0000269|PubMed:17166173}.
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:0000255}.
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; DQ882651; ABI64158.1; -; mRNA.
DR   EMBL; BC083475; AAH83475.1; -; mRNA.
DR   RefSeq; NP_001005938.1; NM_001005938.1.
DR   UniGene; Dr.85181; -.
DR   ProteinModelPortal; Q5XJ36; -.
DR   SMR; Q5XJ36; -.
DR   STRING; 7955.ENSDARP00000041530; -.
DR   MEROPS; C56.971; -.
DR   PaxDb; Q5XJ36; -.
DR   PRIDE; Q5XJ36; -.
DR   Ensembl; ENSDART00000182285; ENSDARP00000150435; ENSDARG00000116835.
DR   GeneID; 449674; -.
DR   KEGG; dre:449674; -.
DR   CTD; 11315; -.
DR   ZFIN; ZDB-GENE-041010-5; park7.
DR   eggNOG; KOG2764; Eukaryota.
DR   eggNOG; COG0693; LUCA.
DR   GeneTree; ENSGT00390000001231; -.
DR   HOGENOM; HOG000063194; -.
DR   HOVERGEN; HBG053511; -.
DR   InParanoid; Q5XJ36; -.
DR   KO; K05687; -.
DR   OMA; CYPGFEK; -.
DR   OrthoDB; EOG091G12NS; -.
DR   PhylomeDB; Q5XJ36; -.
DR   TreeFam; TF300119; -.
DR   Reactome; R-DRE-3899300; SUMOylation of transcription cofactors.
DR   PRO; PR:Q5XJ36; -.
DR   Proteomes; UP000000437; Chromosome 11.
DR   Bgee; ENSDARG00000034826; Expressed in 32 organ(s), highest expression level in muscle tissue.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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:0006914; P:autophagy; IEA:UniProtKB-KW.
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:0006281; P:DNA repair; ISS:UniProtKB.
DR   GO; GO:0042593; P:glucose homeostasis; ISS:UniProtKB.
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:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR   GO; GO:0030073; P:insulin secretion; ISS:UniProtKB.
DR   GO; GO:0060548; P:negative regulation of cell death; ISS:UniProtKB.
DR   GO; GO:1903427; P:negative regulation of reactive oxygen species biosynthetic process; ISS:UniProtKB.
DR   GO; GO:2000277; P:positive regulation of oxidative phosphorylation uncoupler activity; ISS:UniProtKB.
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:0043523; P:regulation of neuron apoptotic process; ISS:UniProtKB.
DR   GO; GO:0006979; P:response to oxidative stress; IMP:ZFIN.
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; Complete proteome;
KW   Copper; Cytoplasm; Fertilization; Hydrolase; Inflammatory response;
KW   Isopeptide bond; Lipoprotein; Membrane; Mitochondrion; Nucleus;
KW   Oxidation; Palmitate; Phosphoprotein; Protease; Reference proteome;
KW   RNA-binding; Stress response; Tumor suppressor; Ubl conjugation;
KW   Zymogen.
FT   CHAIN         1      ?       Protein/nucleic acid deglycase DJ-1.
FT                                /FTId=PRO_0000285970.
FT   PROPEP        ?    189       Removed in mature form.
FT                                /FTId=PRO_0000405563.
FT   ACT_SITE    106    106       Nucleophile.
FT                                {ECO:0000250|UniProtKB:Q99497}.
FT   ACT_SITE    126    126       {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                                {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. {ECO:0000250}.
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;  19764 MW;  F1C4F9F923FB2FF1 CRC64;
     MAGKRALVIL AKGAEEMETV IPVDVMRRAG IAVTVAGLAG KEPVQCSREV MICPDSSLED
     AHKQGPYDVV LLPGGLLGAQ NLSESPAVKE VLKDQEGRKG LIAAICAGPT ALLAHGIAYG
     STVTTHPGAK DKMMAGDHYK YSEARVQKDG NVITSRGPGT SFEFALTIVE ELMGAEVAAQ
     VKAPLILKD
//
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