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) Band Xp22.11 Start 23,664,262 bp End 23,686,397 bp
Gene location (Mouse) Chr. X chromosome (mouse) Band X F3|X 72.38 cM Start 154,106,914 bp End 154,123,750 bp
RNA expression pattern Bgee Human Mouse (ortholog) 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 BioGPS 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 Species Human Mouse Entrez 10549 53381 Ensembl ENSG00000123131 ENSMUSG00000025289 UniProt Q13162 O08807 RefSeq (mRNA) NM_006406 NM_016764 NM_001313711 RefSeq (protein) NP_006397 NP_001300640 NP_058044 Location (UCSC) Chr X: 23.66 – 23.69 Mb Chr X: 154.11 – 154.12 Mb PubMed search
Wikidata
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Peroxiredoxin-4 is a protein that in humans is encoded by the PRDX4 gene. 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.

Interactions

PRDX4 has been shown to interact with Peroxiredoxin 1.

Further reading

• 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.