Park7
entrez
117287
canonical
uniprot
O88767
canonical
ensembl
ENSRNOG00000018289
resolver
ensembl
ENSRNOG00060003529
resolver
ensembl
ENSRNOG00065011489
resolver
ensp
ENSRNOP00000072068
resolver
ensp
ENSRNOP00000074942
resolver
ensp
ENSRNOP00060004213
resolver
ensp
ENSRNOP00065014300
resolver
enst
ENSRNOT00000087402
resolver
enst
ENSRNOT00000091206
resolver
enst
ENSRNOT00060005789
resolver
enst
ENSRNOT00065018694
resolver
genesymbol
Park7
resolver
genesymbol_syn
Cap1
resolver
genesymbol_syn
RGD1560648
resolver
uniprot
A0A0G2K9C2
resolver
uniprot
Q5BKC3
resolver
uniprot_entry
A0A0G2K9C2_RAT
resolver
uniprot_entry
PARK7_RAT
resolver
uniprot_entry
Q5BKC3_RAT
resolver
amino_acid_sequence
MASKRALVILAKGAEEMETVIPVDIMRRAGIKVTVAGLAGKDPVQCSRDVVICPDTSLEEAKTQGPYDVVVLPGGNLGAQNLSESALVKEILKEQENRKGLIAAICAGPTALLAHEVGFGCKVTSHPLAKDKMMNGSHYSYSESRVEKDGLILTSRGPGTSFEFALAIVEALSGKDMANQVKAPLVLKD
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: 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). {ECO:0000250|UniProtKB:Q99497, ECO:0000250|UniProtKB:Q99LX0}.
uniprot
proteins
mass_dalton
19974
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
10022524
uniprot
proteins
pubmed
23847046
uniprot
proteins
pubmed
31250274
uniprot
proteins
pubmed
31536960
uniprot
proteins
pubmed
9733139
uniprot
proteins
pubmed
9792810
uniprot
proteins
sequence_length
189
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q99LX0}; Lipid-anchor {ECO:0000250|UniProtKB:Q99LX0}. Cytoplasm {ECO:0000269|PubMed:10022524}. Membrane raft {ECO:0000269|PubMed:23847046}. Nucleus {ECO:0000269|PubMed:10022524}. 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