PARK7

PARK7
Наявні структури
PDB	Пошук ортологів: PDBe RCSB
Список кодів PDB
	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, 4ZGG, 4RKW, 4RKY, 4S0Z
Ідентифікатори
Символи	PARK7, DJ-1, DJ1, HEL-S-67p, Parkinsonism associated deglycase, GATD2
Зовнішні ІД	OMIM: 602533 MGI: 2135637 HomoloGene: 38295 GeneCards: PARK7
Пов'язані генетичні захворювання
	autosomal recessive early-onset Parkinson disease 7, young-onset Parkinson disease
Онтологія гена
Молекулярна функція	• signaling receptor binding; • GO:0019974 cytokine binding; • cupric ion binding; • transcription factor binding; • L-dopa decarboxylase activator activity; • GO:0070122 peptidase activity; • kinase binding; • tyrosine 3-monooxygenase activator activity; • enzyme binding; • mRNA binding; • protein homodimerization activity; • scaffold protein binding; • small protein activating enzyme binding; • single-stranded DNA binding; • ubiquitin-like protein conjugating enzyme binding; • GO:0001948, GO:0016582 protein binding; • peroxiredoxin activity; • double-stranded DNA binding; • copper ion binding; • mercury ion binding; • GO:0001105 transcription coactivator activity; • oxidoreductase activity, acting on peroxide as acceptor; • androgen receptor binding; • superoxide dismutase copper chaperone activity; • RNA binding; • identical protein binding; • ubiquitin-specific protease binding; • hydrolase activity; • cuprous ion binding; • cadherin binding; • protein deglycase activity; • GO:0032403 protein-containing complex binding;
Клітинна компонента	• цитоплазма; • гіалоплазма; • мембрана; • мітохондріальний міжмембранний простір; • мітохондрія; • neuron projection; • клітинне ядро; • mitochondrial respiratory chain complex I; • ендоплазматичний ретикулум; • membrane raft; • Хроматин; • екзосома; • клітинна мембрана; • мітохондріальний матрикс; • cell body; • PML body; • presynapse; • perinuclear region of cytoplasm; • аксон; • нуклеоплазма;
Біологічний процес	• GO:1904089 negative regulation of neuron apoptotic process; • positive regulation of transcription regulatory region DNA binding; • negative regulation of protein sumoylation; • negative regulation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway; • negative regulation of protein binding; • synaptic transmission, dopaminergic; • positive regulation of interleukin-8 production; • negative regulation of proteasomal ubiquitin-dependent protein catabolic process; • Ras protein signal transduction; • cellular response to glyoxal; • negative regulation of protein acetylation; • positive regulation of reactive oxygen species biosynthetic process; • positive regulation of oxidative phosphorylation uncoupler activity; • positive regulation of protein kinase B signaling; • GO:1903363 negative regulation of protein catabolic process; • adult locomotory behavior; • regulation of neuron apoptotic process; • negative regulation of extrinsic apoptotic signaling pathway; • negative regulation of cell death; • glycolate biosynthetic process; • positive regulation of protein homodimerization activity; • negative regulation of gene expression; • single fertilization; • positive regulation of peptidyl-serine phosphorylation; • positive regulation of mitochondrial electron transport, NADH to ubiquinone; • negative regulation of hydrogen peroxide-induced neuron intrinsic apoptotic signaling pathway; • negative regulation of oxidative stress-induced cell death; • inflammatory response; • negative regulation of oxidative stress-induced neuron intrinsic apoptotic signaling pathway; • regulation of supramolecular fiber organization; • negative regulation of neuron death; • GO:0033128 negative regulation of protein phosphorylation; • negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway; • negative regulation of protein kinase activity; • negative regulation of oxidative stress-induced neuron death; • membrane depolarization; • protein stabilization; • mitochondrion organization; • positive regulation of DNA-binding transcription factor activity; • negative regulation of death-inducing signaling complex assembly; • negative regulation of apoptotic process; • протеоліз; • negative regulation of protein K48-linked deubiquitination; • dopamine uptake involved in synaptic transmission; • positive regulation of tyrosine 3-monooxygenase activity; • positive regulation of L-dopa decarboxylase activity; • negative regulation of hydrogen peroxide-induced neuron death; • regulation of inflammatory response; • regulation of androgen receptor signaling pathway; • negative regulation of hydrogen peroxide-induced cell death; • positive regulation of autophagy of mitochondrion; • response to hydrogen peroxide; • detoxification of copper ion; • positive regulation of superoxide dismutase activity; • positive regulation of dopamine biosynthetic process; • positive regulation of protein localization to nucleus; • positive regulation of L-dopa biosynthetic process; • activation of protein kinase B activity; • membrane hyperpolarization; • detoxification of mercury ion; • negative regulation of TRAIL-activated apoptotic signaling pathway; • cellular oxidant detoxification; • negative regulation of ubiquitin-specific protease activity; • автофагія; • GO:0072353 cellular response to reactive oxygen species; • regulation of mitochondrial membrane potential; • negative regulation of protein ubiquitination; • hydrogen peroxide metabolic process; • GO:1901313 positive regulation of gene expression; • negative regulation of protein export from nucleus; • negative regulation of ubiquitin-protein transferase activity; • positive regulation of oxidative stress-induced intrinsic apoptotic signaling pathway; • cellular response to oxidative stress; • positive regulation of androgen receptor activity; • positive regulation of pyrroline-5-carboxylate reductase activity; • GO:0003257, GO:0010735, GO:1901228, GO:1900622, GO:1904488 positive regulation of transcription by RNA polymerase II; • cellular response to hydrogen peroxide; • methylglyoxal metabolic process; • lactate biosynthetic process; • peptidyl-cysteine deglycation; • peptidyl-arginine deglycation; • peptidyl-lysine deglycation; • protein deglycation, glyoxal removal; • protein deglycation, methylglyoxal removal; • glutathione deglycation; • glyoxal metabolic process; • negative regulation of nitrosative stress-induced intrinsic apoptotic signaling pathway; • positive regulation of acute inflammatory response to antigenic stimulus; • protein deglycosylation; • positive regulation of NAD(P)H oxidase activity; • GO:0100026 Репарація ДНК; • cellular response to DNA damage stimulus; • insulin secretion; • glucose homeostasis; • guanine deglycation; • guanine deglycation, methylglyoxal removal; • guanine deglycation, glyoxal removal; • negative regulation of reactive oxygen species biosynthetic process;
	Джерела:Amigo / QuickGO
Шаблон експресії
	Більше даних
Ортологи
	11315
	57320
	ENSG00000116288
	ENSMUSG00000028964
	Q99497
	Q99LX0
	NM_001123377; NM_007262
	NM_020569
	NP_001116849; NP_009193
	NP_065594
	Вікідані
Див./Ред. для людей	Див./Ред. для мишей

PARK7 (англ. Parkinsonism associated deglycase) – білок, який кодується однойменним геном, розташованим у людей на короткому плечі 1-ї хромосоми. ^[4] Довжина поліпептидного ланцюга білка становить 189 амінокислот, а молекулярна маса — 19 891^[5].

Послідовність амінокислот

10	20	30	40	50
MASKRALVIL	AKGAEEMETV	IPVDVMRRAG	IKVTVAGLAG	KDPVQCSRDV
VICPDASLED	AKKEGPYDVV	VLPGGNLGAQ	NLSESAAVKE	ILKEQENRKG
LIAAICAGPT	ALLAHEIGFG	SKVTTHPLAK	DKMMNGGHYT	YSENRVEKDG
LILTSRGPGT	SFEFALAIVE	ALNGKEVAAQ	VKAPLVLKD

A: Аланін

C: Цистеїн

D: Аспарагінова кислота

E: Глутамінова кислота

F: Фенілаланін

G: Гліцин

H: Гістидин

I: Ізолейцин

K: Лізин

L: Лейцин

M: Метіонін

N: Аспарагін

P: Пролін

Q: Глутамін

R: Аргінін

S: Серин

T: Треонін

V: Валін

Y: Тирозин

Кодований геном білок за функціями належить до шаперонів, гідролаз, протеаз. Задіяний у таких біологічних процесах як відповідь на стрес, запальна відповідь, автофагія, запліднення. Білок має сайт для зв'язування з іоном міді, РНК. Локалізований у клітинній мембрані, цитоплазмі, ядрі, мембрані, мітохондрії.

Література

The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 14: 2121—2127. 2004. PMID 15489334 DOI:10.1101/gr.2596504
Taira T., Takahashi K., Kitagawa R., Iguchi-Ariga S.M.M., Ariga H. (2001). Molecular cloning of human and mouse DJ-1 genes and identification of Sp1-dependent activation of the human DJ-1 promoter. Gene. 263: 285—292. PMID 11223268 DOI:10.1016/S0378-1119(00)00590-4
Shendelman S., Jonason A., Martinat C., Leete T., Abeliovich A. (2004). DJ-1 is a redox-dependent molecular chaperone that inhibits alpha-synuclein aggregate formation. PLoS Biol. 2: 1—10. PMID 15502874 DOI:10.1371/journal.pbio.0020362
Clements C.M., McNally R.S., Conti B.J., Mak T.W., Ting J.P. (2006). DJ-1, a cancer- and Parkinson's disease-associated protein, stabilizes the antioxidant transcriptional master regulator Nrf2. Proc. Natl. Acad. Sci. U.S.A. 103: 15091—15096. PMID 17015834 DOI:10.1073/pnas.0607260103
Junn E., Jang W.H., Zhao X., Jeong B.S., Mouradian M.M. (2009). Mitochondrial localization of DJ-1 leads to enhanced neuroprotection. J. Neurosci. Res. 87: 123—129. PMID 18711745 DOI:10.1002/jnr.21831
Chen J., Li L., Chin L.S. (2010). Parkinson disease protein DJ-1 converts from a zymogen to a protease by carboxyl-terminal cleavage. Hum. Mol. Genet. 19: 2395—2408. PMID 20304780 DOI:10.1093/hmg/ddq113