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Protein

Protein deglycase DJ-1

Gene

Park7

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Protein deglycase that repairs methylglyoxal- and glyoxal-glycated amino acids and proteins, and releases repaired proteins and lactate or glycolate, respectively. Deglycates cysteines, arginines and lysines 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). 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. Its involvement in protein repair could also explain other unrelated functions. 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. 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

Cofactori

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei106 – 1061NucleophileBy similarity
Active sitei126 – 1261By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chaperone, Hydrolase, Protease

Keywords - Biological processi

Autophagy, Fertilization, Inflammatory response, Stress response

Keywords - Ligandi

Copper, RNA-binding

Protein family/group databases

MEROPSiC56.002.

Names & Taxonomyi

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

Organism-specific databases

RGDi621808. Park7.

Subcellular locationi

  • Cell membrane By similarity; Lipid-anchor By similarity
  • Cytoplasm 1 Publication
  • Membrane raft 1 Publication
  • Nucleus 1 Publication
  • Mitochondrion By similarity

  • Note: Under normal conditions, located predominantly in the cytoplasm and, to a lesser extent, in the nucleus and mitochondrion. Translocates to the mitochondrion and subsequently to the nucleus in response to oxidative stress and exerts an increased cytoprotective effect against oxidative damage (By similarity). Membrane raft localization in astrocytes and neuronal cells requires palmitoylation (PubMed:23847046).By similarity1 Publication

GO - Cellular componenti

  • axon Source: RGD
  • cytoplasm Source: UniProtKB
  • cytosol Source: RGD
  • extracellular exosome Source: ParkinsonsUK-UCL
  • membrane raft Source: UniProtKB-SubCell
  • mitochondrion Source: UniProtKB
  • nucleus Source: UniProtKB
  • plasma membrane Source: UniProtKB-SubCell
  • PML body Source: ParkinsonsUK-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Mitochondrion, Nucleus

Pathology & Biotechi

Keywords - Diseasei

Tumor suppressor

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei? – 189Removed in mature formPRO_0000405561
Initiator methionineiRemovedBy similarity
Chaini2 – ?Protein deglycase DJ-1PRO_0000157851

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Lipidationi46 – 461S-palmitoyl cysteineBy similarity
Lipidationi53 – 531S-palmitoyl cysteineBy similarity
Modified residuei67 – 671PhosphotyrosineBy similarity
Modified residuei106 – 1061Cysteine sulfinic acid (-SO2H); alternateBy similarity
Lipidationi106 – 1061S-palmitoyl cysteine; alternateBy similarity
Cross-linki130 – 130Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Modified residuei148 – 1481N6-acetyllysineBy similarity
Modified residuei182 – 1821N6-succinyllysineBy similarity

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.
PhosphoSiteiO88767.

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

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 PARK2.By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi250731. 76 interactions.
IntActiO88767. 1 interaction.
MINTiMINT-4577505.
STRINGi10116.ENSRNOP00000024711.

Structurei

3D structure databases

ProteinModelPortaliO88767.
SMRiO88767. Positions 1-189.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase C56 family.Curated

Phylogenomic databases

eggNOGiKOG2764. Eukaryota.
COG0693. LUCA.
GeneTreeiENSGT00390000001231.
HOGENOMiHOG000063194.
HOVERGENiHBG053511.
InParanoidiO88767.
KOiK05687.
OMAiAICAAPY.
OrthoDBiEOG7CVPZX.

Family and domain databases

Gene3Di3.40.50.880. 1 hit.
InterProiIPR029062. Class_I_gatase-like.
IPR002818. DJ-1/PfpI.
IPR006287. DJ1.
[Graphical view]
PfamiPF01965. DJ-1_PfpI. 1 hit.
[Graphical view]
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.

Cross-referencesi

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.

3D structure databases

ProteinModelPortaliO88767.
SMRiO88767. Positions 1-189.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi250731. 76 interactions.
IntActiO88767. 1 interaction.
MINTiMINT-4577505.
STRINGi10116.ENSRNOP00000024711.

Protein family/group databases

MEROPSiC56.002.

PTM databases

iPTMnetiO88767.
PhosphoSiteiO88767.

2D gel databases

World-2DPAGE0004:O88767.

Proteomic databases

PaxDbiO88767.
PRIDEiO88767.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi11315.
RGDi621808. Park7.

Phylogenomic databases

eggNOGiKOG2764. Eukaryota.
COG0693. LUCA.
GeneTreeiENSGT00390000001231.
HOGENOMiHOG000063194.
HOVERGENiHBG053511.
InParanoidiO88767.
KOiK05687.
OMAiAICAAPY.
OrthoDBiEOG7CVPZX.

Miscellaneous databases

PROiO88767.

Gene expression databases

ExpressionAtlasiO88767. baseline and differential.
GenevisibleiO88767. RN.

Family and domain databases

Gene3Di3.40.50.880. 1 hit.
InterProiIPR029062. Class_I_gatase-like.
IPR002818. DJ-1/PfpI.
IPR006287. DJ1.
[Graphical view]
PfamiPF01965. DJ-1_PfpI. 1 hit.
[Graphical view]
SUPFAMiSSF52317. SSF52317. 1 hit.
TIGRFAMsiTIGR01383. not_thiJ. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Molecular cloning and expression of rat contraception associated protein 1 (CAP1), a protein putatively involved in fertilization."
    Wagenfeld A., Gromoll J., Cooper T.G.
    Biochem. Biophys. Res. Commun. 251:545-549(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 13-29 AND 65-74, TISSUE SPECIFICITY.
    Tissue: Testis.
  2. "SP22: a novel fertility protein from a highly conserved gene family."
    Welch J.E., Barbee R.R., Roberts N.L., Suarez J.D., Klinefelter G.R.
    J. Androl. 19:385-393(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Testis.
  3. Welch J.E., Barbee R.R., Roberts N.L., Suarez J.D., Klinefelter G.R.
    Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Testis.
  4. "Identification and characterization of a novel protein that regulates RNA-protein interaction."
    Hod Y., Pentyala S.N., Whyard T.C., El-Maghrabi M.R.
    J. Cell. Biochem. 72:435-444(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 27-45, ASSOCIATION WITH AN RNA-BINDING COMPLEX, SUBCELLULAR LOCATION.
  5. Lubec G., Afjehi-Sadat L., Chen W.-Q., Kang S.U.
    Submitted (JUL-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 33-48; 63-89; 100-122; 133-145 AND 157-175, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Brain, Hippocampus and Spinal cord.
  6. "DJ-1 associates with lipid rafts by palmitoylation and regulates lipid rafts-dependent endocytosis in astrocytes."
    Kim K.S., Kim J.S., Park J.Y., Suh Y.H., Jou I., Joe E.H., Park S.M.
    Hum. Mol. Genet. 22:4805-4817(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.

Entry informationi

Entry nameiPARK7_RAT
AccessioniPrimary (citable) accession number: O88767
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 7, 2004
Last sequence update: November 1, 1998
Last modified: July 6, 2016
This is version 120 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.