GPX5

GPX5
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	2I3Y
Identifiers
Aliases	GPX5 , HEL-S-75p, glutathione peroxidase 5, GPx-5, EGLP, GSHPx-5
External IDs	OMIM: 603435 MGI: 104886 HomoloGene: 1155 GeneCards: GPX5
Gene location (Human)
Chr.	Chromosome 6 (human)
End	28,534,955 bp
Gene location (Mouse)
Chr.	Chromosome 13 (mouse)
End	21,476,901 bp
RNA expression pattern
	Top expressed in
	superior frontal gyrus; ; prefrontal cortex; ; islet of Langerhans; ; prostate; ; canal of the cervix; ; blood; ; human musculoskeletal system; ; muscle of leg; ; gastrocnemius muscle; ; hypothalamus;
	Top expressed in
	morula; ; entorhinal cortex; ; white adipose tissue; ; epidermis; ; adrenal gland; ; exocrine gland; ; hepatobiliary system; ; liver; ; gonad; ; testicle;
	More reference expression data
	n/a
Gene ontology
Molecular function	oxidoreductase activity ; peroxidase activity ; glutathione peroxidase activity ;
Cellular component	sperm plasma membrane ; extracellular region ; extracellular space ;
Biological process	cellular oxidant detoxification ; response to oxidative stress ; lipid metabolism ; cellular response to oxidative stress ;
	Sources:Amigo / QuickGO
Orthologs
	2880
	14780
	ENSG00000257770 ; ENSG00000224586
	ENSMUSG00000004344
	O75715
	P21765
	NM_001509 ; NM_003996
	NM_010343
	NP_001500 ; NP_003987
	NP_034473
	Wikidata
View/Edit Human	View/Edit Mouse

Last updated March 04, 2023

Glutathione peroxidase 5 (GPx-5), also known as epididymal secretory glutathione peroxidase is an enzyme that in humans is encoded by the GPX5 gene.^[5]^[6]

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.^[5]

Related Research Articles

<span class="mw-page-title-main">Glutathione peroxidase</span> Enzyme family protecting the organism from oxidative damages

Glutathione peroxidase (GPx) is the general name of an enzyme family with peroxidase activity whose main biological role is to protect the organism from oxidative damage. The biochemical function of glutathione peroxidase is to reduce lipid hydroperoxides to their corresponding alcohols and to reduce free hydrogen peroxide to water.

In molecular biology a selenoprotein is any protein that includes a selenocysteine amino acid residue. Among functionally characterized selenoproteins are five glutathione peroxidases (GPX) and three thioredoxin reductases, (TrxR/TXNRD) which both contain only one Sec. Selenoprotein P is the most common selenoprotein found in the plasma. It is unusual because in humans it contains 10 Sec residues, which are split into two domains, a longer N-terminal domain that contains 1 Sec, and a shorter C-terminal domain that contains 9 Sec. The longer N-terminal domain is likely an enzymatic domain, and the shorter C-terminal domain is likely a means of safely transporting the very reactive selenium atom throughout the body.

Glutathione peroxidase 1, also known as GPx1, is an enzyme that in humans is encoded by the GPX1 gene on chromosome 3. This gene encodes a member of the glutathione peroxidase family. Glutathione peroxidase functions in the detoxification of hydrogen peroxide, and is one of the most important antioxidant enzymes in humans.

<span class="mw-page-title-main">Glutathione S-transferase A1</span> Protein-coding gene in the species Homo sapiens

Glutathione S-transferase A1 is an enzyme that in humans is encoded by the GSTA1 gene.

Glutathione peroxidase 4, also known as GPX4, is an enzyme that in humans is encoded by the GPX4 gene. GPX4 is a phospholipid hydroperoxidase that protects cells against membrane lipid peroxidation.

Glutathione S-transferase A2 is an enzyme that in humans is encoded by the GSTA2 gene.

Actin, gamma-enteric smooth muscle is a protein that in humans is encoded by the ACTG2 gene.

Glutathione peroxidase 2 is an enzyme that in humans is encoded by the GPX2 gene.

Cysteine-rich secretory protein 3 is a cysteine-rich secretory protein that in humans is encoded by the CRISP3 gene.

WAP four-disulfide core domain protein 2 - also known as Human Epididymis Protein 4 (HE4) - is a protein that in humans is encoded by the WFDC2 gene.

PGDS protein is a protein that in humans is encoded by the HPGDS gene.

Spermatid nuclear transition protein 1 is a protein that in humans is encoded by the TNP1 gene.

Cystatin-8 is a protein that in humans is encoded by the CST8 gene.

Glutathione peroxidase 7 is an enzyme that in humans is encoded by the GPX7 gene.

Selenoprotein W is a protein that in humans is encoded by the SEPW1 gene.

Cysteine-rich secretory protein 1 is a cysteine-rich secretory protein that in humans is encoded by the CRISP1 gene.

Microsomal glutathione S-transferase 2 is an enzyme that in humans is encoded by the MGST2 gene.

Eppin is a protein that in humans is encoded by the SPINLW1 gene.

Glutathione peroxidase 3 (GPx-3), also known as plasma glutathione peroxidase (GPx-P) or extracellular glutathione peroxidase is an enzyme that in humans is encoded by the GPX3 gene.

Glutathione peroxidase 6 (GPx-6) is an enzyme that in humans is encoded by the GPX6 gene.

References

1 2 3 ENSG00000224586 GRCh38: Ensembl release 89: ENSG00000257770, ENSG00000224586 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000004344 - Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
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. doi:10.1042/bj3330005. 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. Bibcode:2003Natur.425..805M. 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. doi:10.1042/bj2850863. 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. S2CID 8103049.
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. Bibcode:2002PNAS...9916899M. 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. S2CID 20995200.
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. S2CID 7362454.
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.

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[refGRCh38Ensembl-1] 1 2 3 ENSG00000224586 GRCh38: Ensembl release 89: ENSG00000257770, ENSG00000224586 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000004344 - 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.

[entrez-5] 1 2 "Entrez Gene: glutathione peroxidase 5 (epididymal androgen-related protein)".

[pmid9639555-6] 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. doi:10.1042/bj3330005. PMC 1219548 . PMID 9639555.

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v t e Oxidoreductases: peroxidases (EC 1.11)
1.11.1.1-14	NADH peroxidase NADPH peroxidase Fatty-acid peroxidase 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

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Coenzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

GPX5

Related Research Articles

References

Further reading