GPX5

Available structures

Ortholog search: PDBe RCSB

List of PDB id codes
2I3Y

Identifiers

Aliases

GPX5, HEL-S-75p, glutathione peroxidase 5

External IDs

MGI: 104886 HomoloGene: 1155 GeneCards: GPX5

Gene ontology
Molecular function	• oxidoreductase activity • peroxidase activity • glutathione peroxidase activity
Cellular component	• extracellular fluid • sperm plasma membrane • extracellular region
Biological process	• cellular oxidant detoxification • cellular response to oxidative stress • oxidation-reduction process • response to oxidative stress • lipid metabolic process • response to reactive oxygen species
Sources:Amigo / QuickGO

Orthologs

Species

Human

Mouse

Entrez


2880


14780

Ensembl


n/a


ENSMUSG00000004344

UniProt


O75715


P21765

RefSeq (mRNA)


NM_001509 NM_003996


NM_010343

RefSeq (protein)


NP_001500.1 NP_003987.2


NP_034473.2

Location (UCSC)

Chr 6: 28.53 – 28.53 Mb

Chr 13: 21.29 – 21.29 Mb

PubMed search

^[1]

^[2]

Wikidata

View/Edit Human

View/Edit Mouse

Glutathione peroxidase 5 (GPx-5), also known as epididymal secretory glutathione peroxidase is an enzyme that in humans is encoded by the GPX5 gene.^[3]^[4]

GPx-5 belongs to the glutathione peroxidase family. It is specifically expressed in the epididymis in the mammalian male reproductive tract, and is androgen-regulated. Unlike mRNAs for other characterized glutathione peroxidases, this mRNA does not contain a selenocysteine (UGA) codon. Thus, the encoded protein is selenium-independent, and has been proposed to play a role in protecting the membranes of spermatozoa from the damaging effects of lipid peroxidation and/or preventing premature acrosome reaction. Alternatively spliced transcript variants encoding different isoforms have been described for this gene.^[3]

References

↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
1 2 "Entrez Gene: glutathione peroxidase 5 (epididymal androgen-related protein)".
↑ Hall L, Williams K, Perry AC, Frayne J, Jury JA (July 1998). "The majority of human glutathione peroxidase type 5 (GPX5) transcripts are incorrectly spliced: implications for the role of GPX5 in the male reproductive tract". Biochem. J. 333 (1): 5–9. PMC 1219548. PMID 9639555.

Talmud PJ, Drenos F, Shah S, et al. (2009). "Gene-centric association signals for lipids and apolipoproteins identified via the HumanCVD BeadChip.". Am. J. Hum. Genet. 85 (5): 628–42. doi:10.1016/j.ajhg.2009.10.014. PMC 2775832. PMID 19913121.
Mungall AJ, Palmer SA, Sims SK, et al. (2003). "The DNA sequence and analysis of human chromosome 6.". Nature. 425 (6960): 805–11. doi:10.1038/nature02055. PMID 14574404.
Perry AC, Jones R, Niang LS, et al. (1992). "Genetic evidence for an androgen-regulated epididymal secretory glutathione peroxidase whose transcript does not contain a selenocysteine codon.". Biochem. J. 285 (3): 863–70. PMC 1132876. PMID 1386734.
Richard MJ, Guiraud P, Didier C, et al. (2001). "Human immunodeficiency virus type 1 Tat protein impairs selenoglutathione peroxidase expression and activity by a mechanism independent of cellular selenium uptake: consequences on cellular resistance to UV-A radiation.". Arch. Biochem. Biophys. 386 (2): 213–20. doi:10.1006/abbi.2000.2197. PMID 11368344.
Opalenik SR, Ding Q, Mallery SR, Thompson JA (1998). "Glutathione depletion associated with the HIV-1 TAT protein mediates the extracellular appearance of acidic fibroblast growth factor.". Arch. Biochem. Biophys. 351 (1): 17–26. doi:10.1006/abbi.1997.0566. PMID 9501919.
Hartley JL, Temple GF, Brasch MA (2000). "DNA cloning using in vitro site-specific recombination.". Genome Res. 10 (11): 1788–95. doi:10.1101/gr.143000. PMC 310948. PMID 11076863.
Rejraji H, Vernet P, Drevet JR (2002). "GPX5 is present in the mouse caput and cauda epididymidis lumen at three different locations.". Mol. Reprod. Dev. 63 (1): 96–103. doi:10.1002/mrd.10136. PMID 12211066.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
Choi J, Liu RM, Kundu RK, et al. (2000). "Molecular mechanism of decreased glutathione content in human immunodeficiency virus type 1 Tat-transgenic mice.". J. Biol. Chem. 275 (5): 3693–8. doi:10.1074/jbc.275.5.3693. PMID 10652368.
Kimura K, Wakamatsu A, Suzuki Y, et al. (2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes.". Genome Res. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC 1356129. PMID 16344560.
Strausberg RL, Feingold EA, Grouse LH, et al. (2002). "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. PMC 139241. PMID 12477932.
Vernet P, Faure J, Dufaure JP, Drevet JR (1997). "Tissue and developmental distribution, dependence upon testicular factors and attachment to spermatozoa of GPX5, a murine epididymis-specific glutathione peroxidase.". Mol. Reprod. Dev. 47 (1): 87–98. doi:10.1002/(SICI)1098-2795(199705)47:1<87::AID-MRD12>3.0.CO;2-X. PMID 9110319.
Price TO, Ercal N, Nakaoke R, Banks WA (2005). "HIV-1 viral proteins gp120 and Tat induce oxidative stress in brain endothelial cells.". Brain Res. 1045 (1-2): 57–63. doi:10.1016/j.brainres.2005.03.031. PMID 15910762.
Williams K, Frayne J, Hall L (1998). "Expression of extracellular glutathione peroxidase type 5 (GPX5) in the rat male reproductive tract.". Mol. Hum. Reprod. 4 (9): 841–8. doi:10.1093/molehr/4.9.841. PMID 9783843.
Bailey SD, Xie C, Do R, et al. (2010). "Variation at the NFATC2 locus increases the risk of thiazolidinedione-induced edema in the Diabetes REduction Assessment with ramipril and rosiglitazone Medication (DREAM) study.". Diabetes Care. 33 (10): 2250–3. doi:10.2337/dc10-0452. PMC 2945168. PMID 20628086.
Moyer AM, Sun Z, Batzler AJ, et al. (2010). "Glutathione pathway genetic polymorphisms and lung cancer survival after platinum-based chemotherapy.". Cancer Epidemiol. Biomarkers Prev. 19 (3): 811–21. doi:10.1158/1055-9965.EPI-09-0871. PMC 2837367. PMID 20200426.

Oxidoreductases: peroxidases (EC 1.11)

1.11.1.1-14	Catalase Cytochrome c peroxidase Eosinophil peroxidase Glutathione peroxidase GPX 1 2 3 4 5 6 7 8 Horseradish peroxidase Lactoperoxidase Myeloperoxidase Thyroid peroxidase Deiodinase Iodothyronine deiodinase Iodotyrosine deiodinase

1.11.1.15 (peroxiredoxin)	1 2 3 4 5 6

Enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list)

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GPX5

References

Further reading