Park7
entrez
57320
canonical
uniprot
Q99LX0
canonical
ensembl
ENSMUSG00000028964
resolver
ensp
ENSMUSP00000030805
resolver
ensp
ENSMUSP00000101298
resolver
ensp
ENSMUSP00000101299
resolver
ensp
ENSMUSP00000101300
resolver
enst
ENSMUST00000030805
resolver
enst
ENSMUST00000105673
resolver
enst
ENSMUST00000105674
resolver
enst
ENSMUST00000105675
resolver
genesymbol
Park7
resolver
uniprot
O88306
resolver
uniprot
Q3THB9
resolver
uniprot
Q3U509
resolver
uniprot_entry
PARK7_MOUSE
resolver
uniprot_sec
O88306
resolver
uniprot_sec
Q3THB9
resolver
uniprot_sec
Q3U509
resolver
amino_acid_sequence
MASKRALVILAKGAEEMETVIPVDVMRRAGIKVTVAGLAGKDPVQCSRDVMICPDTSLEDAKTQGPYDVVVLPGGNLGAQNLSESPMVKEILKEQESRKGLIAAICAGPTALLAHEVGFGCKVTTHPLAKDKMMNGSHYSYSESRVEKDGLILTSRGPGTSFEFALAIVEALVGKDMANQVKAPLVLKD
uniprot
proteins
ec_number
3.1.2.-
uniprot
proteins
ec_number
3.5.1.-
uniprot
proteins
ec_number
3.5.1.124
uniprot
proteins
function
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:15784737, PubMed:17015834, PubMed:20800516, PubMed:21068725). 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:17015834, 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. But this function is rebuted by other works. 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. 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. Protects histones from adduction by methylglyoxal, controls the levels of methylglyoxal-derived argininine modifications on chromatin. 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. Displays a very low glyoxalase activity that may reflect its deglycase activity (PubMed:22523093). Eliminates hydrogen peroxide and protects cells against hydrogen peroxide-induced cell death (PubMed:17766438). Required for correct mitochondrial morphology and function as well as for autophagy of dysfunctional mitochondria (PubMed:20186336). 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:21068725). Regulates astrocyte inflammatory responses, may modulate lipid rafts-dependent endocytosis in astrocytes and neuronal cells (PubMed:19276172, 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 (PubMed:26422139). Binds to a number of mRNAs containing multiple copies of GG or CC motifs and partially inhibits their translation but dissociates following oxidative stress (By similarity). 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 (PubMed:26021615). {ECO:0000250|UniProtKB:Q99497, ECO:0000269|PubMed:15784737, ECO:0000269|PubMed:17015834, ECO:0000269|PubMed:17766438, ECO:0000269|PubMed:19276172, ECO:0000269|PubMed:20186336, ECO:0000269|PubMed:20800516, ECO:0000269|PubMed:21068725, ECO:0000269|PubMed:22523093, ECO:0000269|PubMed:22611253, ECO:0000269|PubMed:23792957, ECO:0000269|PubMed:23847046, ECO:0000269|PubMed:26021615, ECO:0000269|PubMed:26422139}.
uniprot
proteins
mass_dalton
20021
uniprot
proteins
mutagenesis
MUTAGEN 46; /note="C->A: Sulfinic acid detected following treatment with hydrogen peroxide."; /evidence="ECO:0000269|PubMed:17766438"; MUTAGEN 53; /note="C->A: Sulfinic acid detected following treatment with hydrogen peroxide."; /evidence="ECO:0000269|PubMed:17766438"; MUTAGEN 106; /note="C->A: No sulfinic acid detected following treatment with hydrogen peroxide."; /evidence="ECO:0000269|PubMed:17766438
uniprot
proteins
post_translational_modification
PTM: Sumoylated on Lys-130 by PIAS2 or PIAS4; which is essential for cell-growth promoting activity and transforming activity. {ECO:0000250|UniProtKB:Q99497}.; PTM: Undergoes cleavage of a C-terminal peptide and subsequent activation of protease activity in response to oxidative stress. {ECO:0000250|UniProtKB:Q99497}.
uniprot
proteins
protein_family
Peptidase C56 family
uniprot
proteins
pubmed
11223268
uniprot
proteins
pubmed
14749723
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15784737
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
17015834
uniprot
proteins
pubmed
17766438
uniprot
proteins
pubmed
19276172
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
20186336
uniprot
proteins
pubmed
20800516
uniprot
proteins
pubmed
21068725
uniprot
proteins
pubmed
21097510
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
22523093
uniprot
proteins
pubmed
22555455
uniprot
proteins
pubmed
22611253
uniprot
proteins
pubmed
23792957
uniprot
proteins
pubmed
23806337
uniprot
proteins
pubmed
23847046
uniprot
proteins
pubmed
26021615
uniprot
proteins
pubmed
26422139
uniprot
proteins
pubmed
31536960
uniprot
proteins
sequence_length
189
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23847046}; Lipid-anchor {ECO:0000269|PubMed:23847046}. Cytoplasm {ECO:0000269|PubMed:22555455}. Membrane raft {ECO:0000269|PubMed:23847046}. Nucleus {ECO:0000269|PubMed:22555455}. Mitochondrion {ECO:0000269|PubMed:31536960}. Endoplasmic reticulum {ECO:0000269|PubMed:31536960}. 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). {ECO:0000250|UniProtKB:Q99497, ECO:0000269|PubMed:23847046}.
uniprot
proteins