PRDX4

PRDX4
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	2PN8, 3TJB, 3TJF, 3TJG, 3TJJ, 3TJK, 3TKP, 3TKQ, 3TKR, 3TKS, 4RQX
Identifiers
Aliases	PRDX4, AOE37-2, AOE372, HEL-S-97n, PRX-4, peroxiredoxin 4
External IDs	OMIM: 300927; MGI: 1859815; HomoloGene: 4672; GeneCards: PRDX4; OMA:PRDX4 - orthologs
Gene location (Human)
Chr.	X chromosome (human)
End	23,686,397 bp
Gene location (Mouse)
Chr.	X chromosome (mouse)
End	154,123,750 bp
RNA expression pattern
	Top expressed in
	body of pancreas; ; tibia; ; islet of Langerhans; ; parotid gland; ; stromal cell of endometrium; ; beta cell; ; gonad; ; right testis; ; left testis; ; cartilage tissue;
	Top expressed in
	saccule; ; otic placode; ; otic vesicle; ; external carotid artery; ; dermis; ; endocardial cushion; ; maxillary prominence; ; Gonadal ridge; ; vas deferens; ; cumulus cell;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	protein homodimerization activity; peroxidase activity; thioredoxin peroxidase activity; antioxidant activity; protein binding; peroxiredoxin activity; oxidoreductase activity;
Cellular component	cytoplasm; cytosol; smooth endoplasmic reticulum; endoplasmic reticulum; mitochondrion; extracellular exosome; nucleus; extracellular space; secretory granule lumen; ficolin-1-rich granule lumen; extracellular region;
Biological process	male gonad development; 4-hydroxyproline metabolic process; extracellular matrix organization; I-kappaB phosphorylation; protein maturation by protein folding; cell redox homeostasis; reactive oxygen species metabolic process; spermatogenesis; negative regulation of male germ cell proliferation; cellular oxidant detoxification; neutrophil degranulation; response to oxidative stress; hydrogen peroxide catabolic process;
	Sources:Amigo / QuickGO
Orthologs
	10549
	53381
	ENSG00000123131
	ENSMUSG00000025289
	Q13162
	O08807
	NM_006406
	NM_016764; NM_001313711
	NP_006397
	NP_001300640; NP_058044
	Wikidata
View/Edit Human	View/Edit Mouse

Peroxiredoxin-4 is a protein that in humans is encoded by the PRDX4 gene.^[5]^[6] It is a member of the peroxiredoxin family of antioxidant enzymes.

Function

The protein encoded by this gene is an antioxidant enzyme of the peroxiredoxin family. The protein is localized to the cytoplasm. Peroxidases of the peroxiredoxin family reduce hydrogen peroxide and alkyl hydroperoxides to water and alcohol with the use of reducing equivalents derived from thiol-containing donor molecules. This protein has been found to play a regulatory role in the activation of the transcription factor NF-kappaB.^[6]

Interactions

PRDX4 has been shown to interact with Peroxiredoxin 1.^[5]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000123131 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000025289 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ ^a ^b Jin DY, Chae HZ, Rhee SG, Jeang KT (Jan 1998). "Regulatory role for a novel human thioredoxin peroxidase in NF-kappaB activation". J. Biol. Chem. 272 (49): 30952–61. doi:10.1074/jbc.272.49.30952. PMID 9388242.
^ ^a ^b "Entrez Gene: PRDX4 peroxiredoxin 4".

Sasagawa I, Matsuki S, Suzuki Y, Iuchi Y, Tohya K, Kimura M, Nakada T, Fujii J (2001). "Possible involvement of the membrane-bound form of peroxiredoxin 4 in acrosome formation during spermiogenesis of rats". Eur. J. Biochem. 268 (10): 3053–61. doi:10.1046/j.1432-1327.2001.02200.x. PMID 11358524.
Wagner E, Luche S, Penna L, Chevallet M, Van Dorsselaer A, Leize-Wagner E, Rabilloud T (2002). "A method for detection of overoxidation of cysteines: peroxiredoxins are oxidized in vivo at the active-site cysteine during oxidative stress". Biochem. J. 366 (Pt 3): 777–85. doi:10.1042/BJ20020525. PMC 1222825. PMID 12059788.
Shen C, Nathan C (2002). "Nonredundant antioxidant defense by multiple two-cysteine peroxiredoxins in human prostate cancer cells". Mol. Med. 8 (2): 95–102. doi:10.1007/BF03402079. PMC 2039972. PMID 12080185.
Leonard D, Ajuh P, Lamond AI, Legerski RJ (2003). "hLodestar/HuF2 interacts with CDC5L and is involved in pre-mRNA splicing". Biochem. Biophys. Res. Commun. 308 (4): 793–801. CiteSeerX 10.1.1.539.8359. doi:10.1016/S0006-291X(03)01486-4. PMID 12927788.
Ahmed M, Forsberg J, Bergsten P (2005). "Protein profiling of human pancreatic islets by two-dimensional gel electrophoresis and mass spectrometry". J. Proteome Res. 4 (3): 931–40. doi:10.1021/pr050024a. PMID 15952740.
Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
Guo D, Han J, Adam BL, Colburn NH, Wang MH, Dong Z, Eizirik DL, She JX, Wang CY (2005). "Proteomic analysis of SUMO4 substrates in HEK293 cells under serum starvation-induced stress". Biochem. Biophys. Res. Commun. 337 (4): 1308–18. doi:10.1016/j.bbrc.2005.09.191. PMID 16236267.
Giguère P, Turcotte ME, Hamelin E, Parent A, Brisson J, Laroche G, Labrecque P, Dupuis G, Parent JL (2007). "Peroxiredoxin-4 interacts with and regulates the thromboxane A(2) receptor". FEBS Lett. 581 (20): 3863–8. doi:10.1016/j.febslet.2007.07.011. PMID 17644091.