Parkinson disease protein 7

Details

Name
Parkinson disease protein 7
Kind
protein
Synonyms
  • DJ-1
  • Maillard deglycase
  • Oncogene DJ1
  • Parkinsonism-associated deglycase
  • Protein DJ-1
  • Protein/nucleic acid deglycase DJ-1
Gene Name
PARK7
UniProtKB Entry
Q99497Swiss-Prot
Organism
Humans
NCBI Taxonomy ID
9606
Amino acid sequence
>lcl|BSEQ0010694|Parkinson disease protein 7
MASKRALVILAKGAEEMETVIPVDVMRRAGIKVTVAGLAGKDPVQCSRDVVICPDASLED
AKKEGPYDVVVLPGGNLGAQNLSESAAVKEILKEQENRKGLIAAICAGPTALLAHEIGFG
SKVTTHPLAKDKMMNGGHYTYSENRVEKDGLILTSRGPGTSFEFALAIVEALNGKEVAAQ
VKAPLVLKD
Number of residues
189
Molecular Weight
19890.88
Theoretical pI
6.78
GO Classification
Functions
cadherin binding / DNA-binding transcription factor binding / nuclear androgen receptor binding / oxygen sensor activity / protein deglycase activity / protein-containing complex binding / signaling receptor binding
Processes
cellular detoxification of aldehyde / cellular detoxification of methylglyoxal / detection of oxidative stress / detoxification of hydrogen peroxide / DNA repair / glucose homeostasis / glutathione deglycation / glyoxal metabolic process / guanine deglycation / guanine deglycation, glyoxal removal / guanine deglycation, methylglyoxal removal / insulin secretion / methylglyoxal catabolic process to lactate / methylglyoxal metabolic process / negative regulation of intrinsic apoptotic signaling pathway in response to hydrogen peroxide / negative regulation of nitrosative stress-induced intrinsic apoptotic signaling pathway / negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway / negative regulation of reactive oxygen species biosynthetic process / peptidyl-arginine deglycation / peptidyl-cysteine deglycation / peptidyl-lysine deglycation / positive regulation of acute inflammatory response to antigenic stimulus / positive regulation of autophagy of mitochondrion / positive regulation of DNA-binding transcription factor activity / positive regulation of NAD(P)H oxidase activity / positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / positive regulation of protein-containing complex assembly / positive regulation of reactive oxygen species metabolic process / positive regulation of transcription by RNA polymerase II / protein deglycation, glyoxal removal / protein deglycation, methylglyoxal removal / proteolysis / regulation of oxidative stress-induced neuron intrinsic apoptotic signaling pathway / regulation of supramolecular fiber organization / response to oxidative stress
Components
adherens junction / nucleoplasm / perinuclear region of cytoplasm / presynapse
General Function
Multifunctional protein with controversial molecular function which plays an important role in cell protection against oxidative stress and cell death acting as oxidative stress sensor and redox-sensitive chaperone and protease (PubMed:12796482, PubMed:17015834, PubMed:18711745, PubMed:19229105, PubMed:20304780, PubMed:25416785, PubMed:26995087, PubMed:28993701). 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 (PubMed:12612053, PubMed:14749723, PubMed:15502874, PubMed:17015834, PubMed:18711745, PubMed:21097510). Has been described as a 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 (PubMed:25416785, PubMed:28596309). But this function is rebuted by other works (PubMed:27903648, PubMed:31653696). As a protein deglycase, 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 (PubMed:25416785, PubMed:26995087, PubMed:28013050). 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 (PubMed:28596309). Protects histones from adduction by methylglyoxal, controls the levels of methylglyoxal-derived argininine modifications on chromatin (PubMed:30150385). Able to remove the glycations and restore histone 3, histone glycation disrupts both local and global chromatin architecture by altering histone-DNA interactions as well as histone acetylation and ubiquitination levels (PubMed:30150385, PubMed:30894531). Displays a very low glyoxalase activity that may reflect its deglycase activity (PubMed:22523093, PubMed:28993701, PubMed:31653696). Eliminates hydrogen peroxide and protects cells against hydrogen peroxide-induced cell death (PubMed:16390825). Required for correct mitochondrial morphology and function as well as for autophagy of dysfunctional mitochondria (PubMed:16632486, PubMed:19229105). 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 (PubMed:18711745). Regulates astrocyte inflammatory responses, may modulate lipid rafts-dependent endocytosis in astrocytes and neuronal cells (PubMed:23847046). 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 (PubMed:18626009). Metal-binding protein able to bind copper as well as toxic mercury ions, enhances the cell protection mechanism against induced metal toxicity (PubMed:23792957). In macrophages, interacts with the NADPH oxidase subunit NCF1 to direct NADPH oxidase-dependent ROS production, and protects against sepsis (By similarity)
Specific Function
Cadherin binding
Pfam Domain Function
Signal Regions
Not Available
Transmembrane Regions
Not Available
Cellular Location
Cell membrane
Gene sequence
>lcl|BSEQ0010695|Protein deglycase DJ-1 (PARK7)
ATGGCTTCCAAAAGAGCTCTGGTCATCCTGGCTAAAGGAGCAGAGGAAATGGAGACGGTC
ATCCCTGTAGATGTCATGAGGCGAGCTGGGATTAAGGTCACCGTTGCAGGCCTGGCTGGA
AAAGACCCAGTACAGTGTAGCCGTGATGTGGTCATTTGTCCTGATGCCAGCCTTGAAGAT
GCAAAAAAAGAGGGACCATATGATGTGGTGGTTCTACCAGGAGGTAATCTGGGCGCACAG
AATTTATCTGAGTCTGCTGCTGTGAAGGAGATACTGAAGGAGCAGGAAAACCGGAAGGGC
CTGATAGCCGCCATCTGTGCAGGTCCTACTGCTCTGTTGGCTCATGAAATAGGTTTTGGA
AGTAAAGTTACAACACACCCTCTTGCTAAAGACAAAATGATGAATGGAGGTCATTACACC
TACTCTGAGAATCGTGTGGAAAAAGACGGCCTGATTCTTACAAGCCGGGGGCCTGGGACC
AGCTTCGAGTTTGCGCTTGCAATTGTTGAAGCCCTGAATGGCAAGGAGGTGGCGGCTCAA
GTGAAGGCTCCACTTGTTCTTAAAGACTAG
Chromosome Location
1
Locus
1p36.23
External Identifiers
ResourceLink
UniProtKB IDQ99497
UniProtKB Entry NamePARK7_HUMAN
GenBank Protein ID30038760
GenBank Gene IDD61380
GeneCard IDPARK7
GenAtlas IDPARK7
HGNC IDHGNC:16369
PDB ID(s)1J42, 1P5F, 1PDV, 1PDW, 1PE0, 1Q2U, 1SOA, 1UCF, 2OR3, 2R1T, 2R1U, 2R1V, 2RK3, 2RK4, 2RK6, 3B36, 3B38, 3B3A, 3BWE, 3CY6, 3CYF, 3CZ9, 3CZA, 3EZG, 3F71, 3SF8, 4BTE, 4MNT, 4MTC, 4N0M, 4N12, 4OGF, 4OQ4, 4P2G, 4P34, 4P35, 4P36, 4RKW, 4RKY, 4S0Z, 4ZGG, 5IP5, 5SY6, 5SY9, 5SYA, 6AF5, 6AF7, 6AF9, 6AFA, 6AFB, 6AFC, 6AFD, 6AFE, 6AFF, 6AFG, 6AFH, 6AFI, 6AFJ, 6AFL, 6E5Z, 6M8Z, 7C62, 7PA2, 7PA3, 8PPW, 8PQ0
KEGG IDhsa:11315
NCBI Gene ID11315
General References
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  6. Takahashi K, Taira T, Niki T, Seino C, Iguchi-Ariga SM, Ariga H: DJ-1 positively regulates the androgen receptor by impairing the binding of PIASx alpha to the receptor. J Biol Chem. 2001 Oct 5;276(40):37556-63. Epub 2001 Jul 26. [Article]
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  8. Moore DJ, Zhang L, Dawson TM, Dawson VL: A missense mutation (L166P) in DJ-1, linked to familial Parkinson's disease, confers reduced protein stability and impairs homo-oligomerization. J Neurochem. 2003 Dec;87(6):1558-67. [Article]
  9. Niki T, Takahashi-Niki K, Taira T, Iguchi-Ariga SM, Ariga H: DJBP: a novel DJ-1-binding protein, negatively regulates the androgen receptor by recruiting histone deacetylase complex, and DJ-1 antagonizes this inhibition by abrogation of this complex. Mol Cancer Res. 2003 Feb;1(4):247-61. [Article]
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  16. Shinbo Y, Niki T, Taira T, Ooe H, Takahashi-Niki K, Maita C, Seino C, Iguchi-Ariga SM, Ariga H: Proper SUMO-1 conjugation is essential to DJ-1 to exert its full activities. Cell Death Differ. 2006 Jan;13(1):96-108. [Article]
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  18. Clements CM, McNally RS, Conti BJ, Mak TW, Ting JP: DJ-1, a cancer- and Parkinson's disease-associated protein, stabilizes the antioxidant transcriptional master regulator Nrf2. Proc Natl Acad Sci U S A. 2006 Oct 10;103(41):15091-6. Epub 2006 Oct 2. [Article]
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  40. Hering R, Strauss KM, Tao X, Bauer A, Woitalla D, Mietz EM, Petrovic S, Bauer P, Schaible W, Muller T, Schols L, Klein C, Berg D, Meyer PT, Schulz JB, Wollnik B, Tong L, Kruger R, Riess O: Novel homozygous p.E64D mutation in DJ1 in early onset Parkinson disease (PARK7). Hum Mutat. 2004 Oct;24(4):321-9. [Article]
  41. Gorner K, Holtorf E, Odoy S, Nuscher B, Yamamoto A, Regula JT, Beyer K, Haass C, Kahle PJ: Differential effects of Parkinson's disease-associated mutations on stability and folding of DJ-1. J Biol Chem. 2004 Feb 20;279(8):6943-51. Epub 2003 Nov 7. [Article]
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Associated Data

Drug Relations
DrugDrug groupPharmacological action?TypeActionsDetails
Copperapproved, investigationalunknowntargetDetails