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Protein

Protein/nucleic acid deglycase DJ-1

Gene

Park7

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Protein and nucleotide deglycase that catalyzes the deglycation of the Maillard adducts formed between amino groups of proteins or nucleotides and reactive carbonyl groups of glyoxals. Thus, functions as a protein deglycase that repairs methylglyoxal- and glyoxal-glycated proteins, and releases repaired proteins and lactate or glycolate, respectively. Deglycates cysteine, arginine and lysine residues in proteins, and thus reactivates these proteins by reversing glycation by glyoxals. Acts on early glycation intermediates (hemithioacetals and aminocarbinols), preventing the formation of advanced glycation endproducts (AGE) that cause irreversible damage. Also functions as a nucleotide deglycase able to repair glycated guanine in the free nucleotide pool (GTP, GDP, GMP, dGTP) and in DNA and RNA. Is thus involved in a major nucleotide repair system named guanine glycation repair (GG repair), dedicated to reversing methylglyoxal and glyoxal damage via nucleotide sanitization and direct nucleic acid repair. Also displays an apparent glyoxalase activity that in fact reflects its deglycase activity. Plays an important role in cell protection against oxidative stress and cell death acting as oxidative stress sensor and redox-sensitive chaperone and protease; functions probably related to its primary function. It is involved in neuroprotective mechanisms like the stabilization of NFE2L2 and PINK1 proteins, male fertility as a positive regulator of androgen signaling pathway as well as cell growth and transformation through, for instance, the modulation of NF-kappa-B signaling pathway. Eliminates hydrogen peroxide and protects cells against hydrogen peroxide-induced cell death. Required for correct mitochondrial morphology and function as well as for autophagy of dysfunctional mitochondria. Plays a role in regulating expression or stability of the mitochondrial uncoupling proteins SLC25A14 and SLC25A27 in dopaminergic neurons of the substantia nigra pars compacta and attenuates the oxidative stress induced by calcium entry into the neurons via L-type channels during pacemaking. Regulates astrocyte inflammatory responses, may modulate lipid rafts-dependent endocytosis in astrocytes and neuronal cells (By similarity). In pancreatic islets, involved in the maintenance of mitochondrial reactive oxygen species (ROS) levels and glucose homeostasis in an age- and diet dependent manner. Protects pancreatic beta cells from cell death induced by inflammatory and cytotoxic setting (By similarity). Binds to a number of mRNAs containing multiple copies of GG or CC motifs and partially inhibits their translation but dissociates following oxidative stress. Metal-binding protein able to bind copper as well as toxic mercury ions, enhances the cell protection mechanism against induced metal toxicity (By similarity). In macrophages, interacts with the NADPH oxidase subunit NCF1 to direct NADPH oxidase-dependent ROS production, and protects against sepsis (By similarity).By similarity

Caution

Glyoxylase activity previously reported may reflect in fact its deglycase activity.By similarity
The protein deglycation activity has been ascribed to a TRIS buffer artifact by a publication, which has then been rebutted by clear biochemical experiments showing that PARK7 is a bona fide deglycase. Deglycase activity is even strengthened by a novel article that reports nucleotide deglycation activity.By similarity

Catalytic activityi

An N(omega)-(1-hydroxy-2-oxopropyl)-[protein]-L-arginine + H2O = a [protein]-L-arginine + (R)-lactate.By similarity
An N6-(1-hydroxy-2-oxopropyl)-[protein]-L-lysine + H2O = a [protein]-L-lysine + (R)-lactate.By similarity
An S-(1-hydroxy-2-oxopropyl)-[protein]-L-cysteine + H2O = a [protein]-L-cysteine + (R)-lactate.By similarity

Cofactori

Note: Deglycase activity does not require glutathione as a cofactor, however, glycated glutathione constitutes a PARK7 substrate.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei106NucleophileBy similarity1
Active sitei126By similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionChaperone, Hydrolase, Protease, RNA-binding
Biological processAutophagy, Fertilization, Inflammatory response, Stress response
LigandCopper

Protein family/group databases

MEROPSiC56.002

Names & Taxonomyi

Protein namesi
Recommended name:
Protein/nucleic acid deglycase DJ-1By similarity (EC:3.1.2.-By similarity, EC:3.5.1.-By similarity, EC:3.5.1.124By similarity)
Alternative name(s):
Contraception-associated protein 11 Publication
Short name:
Protein CAP1
Fertility protein SP221 Publication
Maillard deglycaseBy similarity
Parkinson disease protein 7 homologCurated
Parkinsonism-associated deglycaseBy similarity
Protein DJ-1By similarity
Short name:
DJ-1
Gene namesi
Name:Park7Imported
Synonyms:Cap1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 5

Organism-specific databases

RGDi621808 Park7

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Mitochondrion, Nucleus

Pathology & Biotechi

Keywords - Diseasei

Tumor suppressor

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
PropeptideiPRO_0000405561? – 189Removed in mature form
Initiator methionineiRemovedBy similarity
ChainiPRO_00001578512 – ?Protein/nucleic acid deglycase DJ-1

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1
Lipidationi46S-palmitoyl cysteineBy similarity1
Lipidationi53S-palmitoyl cysteineBy similarity1
Modified residuei67PhosphotyrosineBy similarity1
Modified residuei106Cysteine sulfinic acid (-SO2H); alternateBy similarity1
Lipidationi106S-palmitoyl cysteine; alternateBy similarity1
Cross-linki130Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Modified residuei148N6-acetyllysineBy similarity1
Modified residuei182N6-succinyllysineBy similarity1

Post-translational modificationi

Sumoylated on Lys-130 by PIAS2 or PIAS4; which is essential for cell-growth promoting activity and transforming activity.By similarity
Undergoes cleavage of a C-terminal peptide and subsequent activation of protease activity in response to oxidative stress.By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Lipoprotein, Oxidation, Palmitate, Phosphoprotein, Ubl conjugation, Zymogen

Proteomic databases

PaxDbiO88767
PRIDEiO88767

2D gel databases

World-2DPAGE0004:O88767

PTM databases

iPTMnetiO88767
PhosphoSitePlusiO88767

Expressioni

Tissue specificityi

Ubiquitous. Detected on epididymal sperm. Highly expressed in testis and prostate. Detected at lower levels in heart, lung, brain, liver, kidney, seminal vesicle, caput and corpus epididymis.1 Publication

Gene expression databases

BgeeiENSRNOG00000018289
ExpressionAtlasiO88767 baseline and differential
GenevisibleiO88767 RN

Interactioni

Subunit structurei

Homodimer. Binds EFCAB6/DJBP and PIAS2. Part of a ternary complex containing PARK7, EFCAB6/DJBP and AR. Interacts (via N-terminus) with OTUD7B. Interacts with BBS1, HIPK1, CLCF1 and MTERF. Forms a complex with PINK1 and PRKN (By similarity). Interacts (via C-terminus) with NCF1; the interaction is enhanced by LPS and modulates NCF1 phosphorylation and membrane translocation (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi250731, 76 interactors
IntActiO88767, 1 interactor
STRINGi10116.ENSRNOP00000024711

Structurei

3D structure databases

ProteinModelPortaliO88767
SMRiO88767
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase C56 family.Curated

Phylogenomic databases

eggNOGiKOG2764 Eukaryota
COG0693 LUCA
GeneTreeiENSGT00390000001231
HOGENOMiHOG000063194
HOVERGENiHBG053511
InParanoidiO88767
KOiK05687
OMAiMMNGSHY

Family and domain databases

Gene3Di3.40.50.880, 1 hit
InterProiView protein in InterPro
IPR029062 Class_I_gatase-like
IPR006287 DJ-1
IPR002818 DJ-1/PfpI
PfamiView protein in Pfam
PF01965 DJ-1_PfpI, 1 hit
SUPFAMiSSF52317 SSF52317, 1 hit
TIGRFAMsiTIGR01383 not_thiJ, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O88767-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASKRALVIL AKGAEEMETV IPVDIMRRAG IKVTVAGLAG KDPVQCSRDV
60 70 80 90 100
VICPDTSLEE AKTQGPYDVV VLPGGNLGAQ NLSESALVKE ILKEQENRKG
110 120 130 140 150
LIAAICAGPT ALLAHEVGFG CKVTSHPLAK DKMMNGSHYS YSESRVEKDG
160 170 180
LILTSRGPGT SFEFALAIVE ALSGKDMANQ VKAPLVLKD
Length:189
Mass (Da):19,974
Last modified:November 1, 1998 - v1
Checksum:i08AC2C37D62A9455
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ007291 mRNA Translation: CAA07434.1
AF157511 mRNA Translation: AAD43956.1
AF157512 mRNA Translation: AAD43957.1
PIRiJE0344
RefSeqiNP_001264179.1, NM_001277250.1
NP_001264180.1, NM_001277251.1
NP_001264181.1, NM_001277252.1
NP_001264182.1, NM_001277253.1
NP_476484.1, NM_057143.2
UniGeneiRn.30105

Genome annotation databases

EnsembliENSRNOT00000024711; ENSRNOP00000024711; ENSRNOG00000018289
ENSRNOT00000087402; ENSRNOP00000072068; ENSRNOG00000018289
GeneIDi117287
KEGGirno:117287
UCSCiRGD:621808 rat

Similar proteinsi

Entry informationi

Entry nameiPARK7_RAT
AccessioniPrimary (citable) accession number: O88767
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 7, 2004
Last sequence update: November 1, 1998
Last modified: May 23, 2018
This is version 135 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health