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 03-AUG-2022, entry version 114.
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-1zDJ-1 {ECO:0000250|UniProtKB:Q99497};
DE Short=zDJ-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|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 Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1] {ECO:0000312|EMBL:ABI64158.1}
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP 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 dopaminergic
RT neurons.";
RL Brain Res. 1113:33-44(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP 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 of
RT 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: Multifunctional protein with controversial molecular function
CC which plays an important role in cell protection against oxidative
CC stress and cell death acting as oxidative stress sensor and redox-
CC sensitive chaperone and protease (PubMed:17166173). 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. Has been
CC described as a protein and nucleotide deglycase that catalyzes the
CC deglycation of the Maillard adducts formed between amino groups of
CC proteins or nucleotides and reactive carbonyl groups of glyoxals. But
CC this function is rebuted by other works. As a protein deglycase,
CC repairs methylglyoxal- and glyoxal-glycated proteins, and releases
CC repaired proteins and lactate or glycolate, respectively. Deglycates
CC cysteine, arginine and lysine residues in proteins, and thus
CC reactivates these proteins by reversing glycation by glyoxals. Acts on
CC early glycation intermediates (hemithioacetals and aminocarbinols),
CC preventing the formation of advanced glycation endproducts (AGE) that
CC cause irreversible damage. Also functions as a nucleotide deglycase
CC able to repair glycated guanine in the free nucleotide pool (GTP, GDP,
CC GMP, dGTP) and in DNA and RNA. Is thus involved in a major nucleotide
CC repair system named guanine glycation repair (GG repair), dedicated to
CC reversing methylglyoxal and glyoxal damage via nucleotide sanitization
CC and direct nucleic acid repair. Protects histones from adduction by
CC methylglyoxal, controls the levels of methylglyoxal-derived argininine
CC modifications on chromatin. Displays a very low glyoxalase activity
CC that may reflect its deglycase activity. It is involved in
CC neuroprotective mechanisms as well as cell growth and transformation.
CC Its involvement in protein repair could also explain other unrelated
CC functions. Eliminates hydrogen peroxide and protects cells against
CC hydrogen peroxide-induced cell death. Required for correct
CC mitochondrial morphology and function as well as for autophagy of
CC dysfunctional mitochondria. Regulates astrocyte inflammatory responses,
CC may modulate lipid rafts-dependent endocytosis in astrocytes and
CC neuronal cells. Binds to a number of mRNAs containing multiple copies
CC 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).
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-[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. {ECO:0000250|UniProtKB:Q99497}.
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. Detected in tau
CC inclusions in brains from neurodegenerative disease patients. Membrane
CC raft localization in astrocytes and neuronal cells requires
CC palmitoylation. {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, eye,
CC heart and muscle. Within brain, neuronal expression is widespread,
CC particularly in the cerebellum, medullary reticular formation and
CC diencephalon. Expressed in major forebrain and diencephalic
CC dopaminergic cell groups. {ECO:0000269|PubMed:16942755,
CC ECO:0000269|PubMed:17166173}.
CC -!- DEVELOPMENTAL STAGE: Present from tailbud stage (10 hpf) through to
CC adult. Levels increase from 24-120 hpf. {ECO:0000269|PubMed:16942755,
CC ECO:0000269|PubMed:17166173}.
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:0000255}.
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; DQ882651; ABI64158.1; -; mRNA.
DR EMBL; BC083475; AAH83475.1; -; mRNA.
DR RefSeq; NP_001005938.1; NM_001005938.1.
DR AlphaFoldDB; Q5XJ36; -.
DR SMR; Q5XJ36; -.
DR STRING; 7955.ENSDARP00000041530; -.
DR MEROPS; C56.971; -.
DR PaxDb; 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 GeneTree; ENSGT00390000001231; -.
DR HOGENOM; CLU_000445_44_2_1; -.
DR InParanoid; Q5XJ36; -.
DR OMA; TSYPAMK; -.
DR OrthoDB; 1165707at2759; -.
DR PhylomeDB; Q5XJ36; -.
DR TreeFam; TF300119; -.
DR Reactome; R-DRE-3899300; SUMOylation of transcription cofactors.
DR Reactome; R-DRE-9646399; Aggrephagy.
DR PRO; PR:Q5XJ36; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 11.
DR Bgee; ENSDARG00000116835; Expressed in muscle tissue and 40 other tissues.
DR GO; GO:0005737; C:cytoplasm; 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: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:1990422; F:glyoxalase (glycolic acid-forming) activity; ISS:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; ISS:UniProtKB.
DR GO; GO:0016684; F:oxidoreductase activity, acting on peroxide as acceptor; IBA:GO_Central.
DR GO; GO:0008233; F:peptidase activity; ISS:UniProtKB.
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: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: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:1901215; P:negative regulation of neuron death; IBA:GO_Central.
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: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: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; 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 CHAIN 1..?
FT /note="Parkinson disease protein 7 homolog"
FT /id="PRO_0000285970"
FT PROPEP ?..189
FT /note="Removed in mature form"
FT /id="PRO_0000405563"
FT ACT_SITE 106
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q99497"
FT ACT_SITE 126
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)"
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"
FT /evidence="ECO:0000250"
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; 19764 MW; F1C4F9F923FB2FF1 CRC64;
MAGKRALVIL AKGAEEMETV IPVDVMRRAG IAVTVAGLAG KEPVQCSREV MICPDSSLED
AHKQGPYDVV LLPGGLLGAQ NLSESPAVKE VLKDQEGRKG LIAAICAGPT ALLAHGIAYG
STVTTHPGAK DKMMAGDHYK YSEARVQKDG NVITSRGPGT SFEFALTIVE ELMGAEVAAQ
VKAPLILKD
