PRDX3

PRDX3
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 5JCG
Identifiers
Aliases	PRDX3, AOP-1, AOP1, HBC189, MER5, PRO1748, SP-22, prx-III, peroxiredoxin 3, SCAR32, PPPCD
External IDs	OMIM: 604769; MGI: 88034; HomoloGene: 4944; GeneCards: PRDX3; OMA:PRDX3 - orthologs
Gene location (Human) Chr. Chromosome 10 (human) Band 10q26.11 Start 119,167,720 bp End 119,178,812 bp
Gene location (Mouse) Chr. Chromosome 19 (mouse) Band 19 D3|19 56.52 cM Start 60,852,489 bp End 60,862,994 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in right adrenal cortex left adrenal gland left adrenal cortex right ventricle biceps brachii Skeletal muscle tissue of biceps brachii oocyte islet of Langerhans gastrocnemius muscle secondary oocyte Top expressed in adrenal gland digastric muscle right ventricle temporal muscle right kidney soleus muscle sternocleidomastoid muscle myocardium of ventricle brown adipose tissue triceps brachii muscle More reference expression data BioGPS More reference expression data
Gene ontology Molecular function peroxidase activity cysteine-type endopeptidase inhibitor activity involved in apoptotic process kinase binding protein C-terminus binding protein binding antioxidant activity alkyl hydroperoxide reductase activity peroxiredoxin activity oxidoreductase activity protein kinase binding thioredoxin peroxidase activity identical protein binding Cellular component cytosol myelin sheath mitochondrial matrix mitochondrion IkappaB kinase complex cytoplasm endosome early endosome protein-containing complex Biological process myeloid cell differentiation peptidyl-cysteine oxidation mitochondrion organization negative regulation of apoptotic process response to oxidative stress regulation of mitochondrial membrane potential cellular response to reactive oxygen species response to lipopolysaccharide maternal placenta development positive regulation of NF-kappaB transcription factor activity positive regulation of cell population proliferation hydrogen peroxide catabolic process response to hydrogen peroxide negative regulation of kinase activity negative regulation of cysteine-type endopeptidase activity involved in apoptotic process cellular oxidant detoxification cell redox homeostasis apoptotic process cellular response to oxidative stress Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 10935 11757 Ensembl ENSG00000165672 ENSMUSG00000024997 UniProt P30048 P20108 RefSeq (mRNA) NM_001302272 NM_006793 NM_014098 NM_007452 RefSeq (protein) NP_001289201 NP_006784 NP_031478 Location (UCSC) Chr 10: 119.17 – 119.18 Mb Chr 19: 60.85 – 60.86 Mb PubMed search
Wikidata
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Thioredoxin-dependent peroxide reductase, mitochondrial is an enzyme that in humans is encoded by the PRDX3 gene. It is a member of the peroxiredoxin family of antioxidant enzymes.

Function

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.

Interactions

PRDX3 has been shown to interact with MAP3K13.

Clinical significance

It has been demonstrated that serum peroxiredoxin 3 can be a valuable biomarker for the diagnosis and assessment of hepatocellular carcinoma It has been shown that peroxiredoxin proteins protect MCF-7 breast cancer cells against doxorubicin-mediated toxicity. 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.

Further reading

• Hochstrasser DF, Frutiger S, Paquet N, Bairoch A, Ravier F, Pasquali C, Sanchez JC, Tissot JD, Bjellqvist B, Vargas R (1992). "Human liver protein map: a reference database established by microsequencing and gel comparison". Electrophoresis. 13 (12): 992–1001. doi:10.1002/elps.11501301201. PMID 1286669. S2CID 23518983.
• Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
• Shih SF, Wu YH, Hung CH, Yang HY, Lin JY (2001). "Abrin triggers cell death by inactivating a thiol-specific antioxidant protein". J. Biol. Chem. 276 (24): 21870–7. doi:10.1074/jbc.M100571200. PMID 11285261.
• Suzuki H, Fukunishi Y, Kagawa I, Saito R, Oda H, Endo T, Kondo S, Bono H, Okazaki Y, Hayashizaki Y (2001). "Protein-protein interaction panel using mouse full-length cDNAs". Genome Res. 11 (10): 1758–65. doi:10.1101/gr.180101. PMC 311163. PMID 11591653.
• Kim SH, Fountoulakis M, Cairns N, Lubec G (2001). "Protein levels of human peroxiredoxin subtypes in brains of patients with Alzheimer's disease and Down Syndrome". Protein Expression in Down Syndrome Brain. pp. 223–35. doi:10.1007/978-3-7091-6262-0_18. ISBN 978-3-211-83704-7. PMID 11771746. {{cite book}}: |journal= ignored (help)
• Rabilloud T, Heller M, Gasnier F, Luche S, Rey C, Aebersold R, Benahmed M, Louisot P, Lunardi J (2002). "Proteomics analysis of cellular response to oxidative stress. Evidence for in vivo overoxidation of peroxiredoxins at their active site". J. Biol. Chem. 277 (22): 19396–401. doi:10.1074/jbc.M106585200. PMID 11904290.
• Wonsey DR, Zeller KI, Dang CV (2002). "The c-Myc target gene PRDX3 is required for mitochondrial homeostasis and neoplastic transformation". Proc. Natl. Acad. Sci. U.S.A. 99 (10): 6649–54. Bibcode:2002PNAS...99.6649W. doi:10.1073/pnas.102523299. PMC 124457. PMID 12011429.
• 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.
• Masaki M, Ikeda A, Shiraki E, Oka S, Kawasaki T (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.
• Choi JH, Kim TN, Kim S, Baek SH, Kim JH, Lee SR, Kim JR (2003). "Overexpression of mitochondrial thioredoxin reductase and peroxiredoxin III in hepatocellular carcinomas". Anticancer Res. 22 (6A): 3331–5. PMID 12530083.
• Krapfenbauer K, Engidawork E, Cairns N, Fountoulakis M, Lubec G (2003). "Aberrant expression of peroxiredoxin subtypes in neurodegenerative disorders". Brain Res. 967 (1–2): 152–60. doi:10.1016/S0006-8993(02)04243-9. PMID 12650976. S2CID 854144.
• Chang TS, Cho CS, Park S, Yu S, Kang SW, Rhee SG (2004). "Peroxiredoxin III, a mitochondrion-specific peroxidase, regulates apoptotic signaling by mitochondria". J. Biol. Chem. 279 (40): 41975–84. doi:10.1074/jbc.M407707200. PMID 15280382.
• Liu L, Yang C, Yuan J, Chen X, Xu J, Wei Y, Yang J, Lin G, Yu L (2005). "RPK118, a PX domain-containing protein, interacts with peroxiredoxin-3 through pseudo-kinase domains". Mol. Cells. 19 (1): 39–45. doi:10.1016/S1016-8478(23)13134-7. PMID 15750338.