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Peroxiredoxin 3
Protein PRDX3 PDB 1zye.png
PDB rendering based on 1zye.
Available structures
PDB Ortholog search: PDBe, RCSB
Symbols PRDX3 ; AOP-1; AOP1; HBC189; MER5; PRO1748; SP-22; prx-III
External IDs OMIM604769 MGI88034 HomoloGene4944 GeneCards: PRDX3 Gene
EC number
RNA expression pattern
PBB GE PRDX3 201619 at tn.png
More reference expression data
Species Human Mouse
Entrez 10935 11757
Ensembl ENSG00000165672 ENSMUSG00000024997
UniProt P30048 P20108
RefSeq (mRNA) NM_006793 NM_007452
RefSeq (protein) NP_006784 NP_031478
Location (UCSC) Chr 10:
120.93 – 120.94 Mb
Chr 19:
60.86 – 60.87 Mb
PubMed search [1] [2]

Thioredoxin-dependent peroxide reductase, mitochondrial is an enzyme that in humans is encoded by the PRDX3 gene.[1][2][3]


This gene encodes a protein with antioxidant function and is localized in the mitochondrion. This gene shows significant nucleotide sequence similarity to the gene coding for the C22 subunit of Salmonella typhimurium alkylhydroperoxide reductase. Expression of this gene product in E. coli deficient in the C22-subunit gene rescued resistance of the bacteria to alkylhydroperoxide. The human and mouse genes are highly conserved, and they map to the regions syntenic between mouse and human chromosomes. Sequence comparisons with recently cloned mammalian homologues suggest that these genes consist of a family that is responsible for regulation of cellular proliferation, differentiation, and antioxidant functions. Two transcript variants encoding two different isoforms have been found for this gene.[3]


PRDX3 has been shown to interact with MAP3K13.[4]

Clinical significance[edit]

It has been demonstrated that serum peroxiredoxin 3 can be a valuable biomarker for the diagnosis and assessment of hepatocellular carcinoma[5] It has been shown that peroxiredoxin proteins protect MCF-7 breast cancer cells against doxorubicin-mediated toxicity.[6] Additionally, it has been shown that peroxiredoxin 3 is overexpressed in prostate cancer and promotes cancer cell survival by defending cells against the damages incurred by oxidative stress.[7]


  1. ^ Tsuji K, Copeland NG, Jenkins NA, Obinata M (May 1995). "Mammalian antioxidant protein complements alkylhydroperoxide reductase (ahpC) mutation in Escherichia coli". Biochem. J. 307 ( Pt 2) (2): 377–81. PMC 1136659. PMID 7733872. 
  2. ^ Watabe S, Hiroi T, Yamamoto Y, Fujioka Y, Hasegawa H, Yago N et al. (Dec 1997). "SP-22 is a thioredoxin-dependent peroxide reductase in mitochondria". Eur. J. Biochem. 249 (1): 52–60. doi:10.1111/j.1432-1033.1997.t01-1-00052.x. PMID 9363753. 
  3. ^ a b "Entrez Gene: PRDX3 peroxiredoxin 3". 
  4. ^ Masaki M, Ikeda A, Shiraki E, Oka S, Kawasaki T (Jan 2003). "Mixed lineage kinase LZK and antioxidant protein-1 activate NF-kappaB synergistically". Eur. J. Biochem. 270 (1): 76–83. doi:10.1046/j.1432-1033.2003.03363.x. PMID 12492477. 
  5. ^ Shi L, Wu LL, Yang JR, Chen XF, Zhang Y, Chen ZQ et al. (2014). "Serum peroxiredoxin3 is a useful biomarker for early diagnosis and assessemnt of prognosis of hepatocellular carcinoma in Chinese patients". Asian Pacific Journal of Cancer Prevention 15 (7). PMID 24815434. 
  6. ^ McDonald C, Muhlbauer J, Perlmutter G, Taparra K, Phelan SA (Jul 2014). "Peroxiredoxin proteins protect MCF-7 breast cancer cells from doxorubicin-induced toxicity". International Journal of Oncology 45 (1). doi:10.3892/ijo.2014.2398. PMID 24789097. 
  7. ^ Whitaker HC, Patel D, Howat WJ, Warren AY, Kay JD, Sangan T et al. (Aug 2013). "Peroxiredoxin-3 is overexpressed in prostate cancer and promotes cancer cell survival by protecting cells from oxidative stress". British Journal of Cancer 109 (4). doi:10.1038/bjc.2013.396. PMID 23880827. 

Further reading[edit]