PRDX4

Protein-coding gene in the species Homo sapiens
PRDX4
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

2PN8, 3TJB, 3TJF, 3TJG, 3TJJ, 3TJK, 3TKP, 3TKQ, 3TKR, 3TKS, 4RQX

Identifiers
AliasesPRDX4, AOE37-2, AOE372, HEL-S-97n, PRX-4, peroxiredoxin 4
External IDsOMIM: 300927; MGI: 1859815; HomoloGene: 4672; GeneCards: PRDX4; OMA:PRDX4 - orthologs
Gene location (Human)
X chromosome (human)
Chr.X chromosome (human)[1]
X chromosome (human)
Genomic location for PRDX4
Genomic location for PRDX4
BandXp22.11Start23,664,262 bp[1]
End23,686,397 bp[1]
Gene location (Mouse)
X chromosome (mouse)
Chr.X chromosome (mouse)[2]
X chromosome (mouse)
Genomic location for PRDX4
Genomic location for PRDX4
BandX F3|X 72.38 cMStart154,106,914 bp[2]
End154,123,750 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • body of pancreas

  • tibia

  • islet of Langerhans

  • parotid gland

  • stromal cell of endometrium

  • liver

  • periodontal fiber

  • right lobe of liver

  • corpus epididymis

  • seminal vesicula
Top expressed in
  • saccule

  • otic placode

  • external carotid artery

  • dermis

  • endocardial cushion

  • maxillary prominence

  • vas deferens

  • cumulus cell

  • internal carotid artery

  • seminiferous tubule
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
SpeciesHumanMouse
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 MbChr X: 154.11 – 154.12 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/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

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000123131 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000025289 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ 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.
  6. ^ a b "Entrez Gene: PRDX4 peroxiredoxin 4".

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.
  • v
  • t
  • e
  • 2pn8: Crystal structure of human peroxiredoxin 4 (thioredoxin peroxidase)
    2pn8: Crystal structure of human peroxiredoxin 4 (thioredoxin peroxidase)


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