PRDX4

From Wikipedia, the free encyclopedia

Peroxiredoxin 4

PDB rendering based on 2pn8.

Available structures: 2pn8

Identifiers

Symbol(s)

PRDX4; AOE37-2

External IDs

OMIM: 606506 MGI: 1859815 HomoloGene: 4672

Gene ontology
Molecular Function:	• thioredoxin peroxidase activity • oxidoreductase activity • peroxiredoxin activity
Cellular Component:	• mitochondrion
Biological Process:	• I-kappaB phosphorylation

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_006406 (mRNA)
NP_006397 (protein)

NM_016764 (mRNA)
NP_058044 (protein)

Location

Chr X: 23.59 - 23.61 Mb

Chr X: 150.66 - 150.68 Mb

Pubmed search

[1]

[2]

Peroxiredoxin 4, also known as PRDX4, is a human gene.^[1]

The protein encoded by this gene is an antioxidant enzyme and belongs to 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.^[1]

[edit] References

^ ^a ^b Entrez Gene: PRDX4 peroxiredoxin 4.

[edit] Further reading

Jin DY, Chae HZ, Rhee SG, Jeang KT (1998). "Regulatory role for a novel human thioredoxin peroxidase in NF-kappaB activation.". J. Biol. Chem. 272 (49): 30952–61. PMID 9388242.
Sasagawa I, Matsuki S, Suzuki Y, et al. (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. PMID 11358524.
Wagner E, Luche S, Penna L, et al. (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. 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. PMID 12080185.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
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. PMID 12927788.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMID 15489334.
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, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network.". Nature 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
Guo D, Han J, Adam BL, et al. (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, et al. (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.