Peroxiredoxin-5, mitochondrial (PRDX5)
The protein contains 214 amino acids for an estimated molecular weight of 22086 Da.
Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events. (updated: Oct. 25, 2017)
Protein identification was indicated in the following studies:
- Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
- Hegedűs and co-workers. (2015) Inconsistencies in the red blood cell membrane proteome analysis: generation of a database for research and diagnostic applications. Database (Oxford) 1-8.
- Wilson and co-workers. (2016) Comparison of the Proteome of Adult and Cord Erythroid Cells, and Changes in the Proteome Following Reticulocyte Maturation. Mol Cell Proteomics. 15(6), 1938-1946.
- Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
Methods
The following articles were analysed to gather the proteome content of erythrocytes.
The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.
| Publication | Identification 1 | Uniprot mapping 2 | Not mapped / Obsolete | TrEMBL | Swiss-Prot |
|---|---|---|---|---|---|
| Goodman (2013) | 2289 (gene list) | 2278 | 53 | 20599 | 2269 |
| Lange (2014) | 1234 | 1234 | 7 | 28 | 1224 |
| Hegedus (2015) | 2638 | 2622 | 0 | 235 | 2387 |
| Wilson (2016) | 1658 | 1528 | 170 | 291 | 1068 |
| d'Alessandro (2017) | 1826 | 1817 | 2 | 0 | 1815 |
| Bryk (2017) | 2090 | 2060 | 10 | 108 | 1942 |
| Chu (2018) | 1853 | 1804 | 55 | 362 | 1387 |
1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry
The compilation of older studies can be retrieved from the Red Blood Cell Collection database.
The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.
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| Variant | Description |
|---|---|
| dbSNP:rs7938623 | |
| a breast cancer sample; somatic mutation |
Biological Process
Cell redox homeostasis
Cellular response to oxidative stress
Cellular response to reactive oxygen species
Hydrogen peroxide catabolic process
Inflammatory response
NADPH oxidation
Negative regulation of apoptotic process
Negative regulation of cysteine-type endopeptidase activity involved in apoptotic process
Negative regulation of oxidoreductase activity
Negative regulation of transcription by RNA polymerase III
Positive regulation of collagen biosynthetic process
Reactive nitrogen species metabolic process
Regulation of apoptosis involved in tissue homeostasis
Response to oxidative stress
Response to reactive oxygen species
Cellular Component
Cytoplasm
Cytoplasmic vesicle
Cytosol
Extracellular exosome
Extracellular space
Intracellular membrane-bounded organelle
Mitochondrial matrix
Mitochondrion
Nucleus
Obsolete cell
Perinuclear region of cytoplasm
Peroxisomal matrix
Peroxisome
Molecular Function
Antioxidant activity
Cysteine-type endopeptidase inhibitor activity involved in apoptotic process
Peroxidase activity
Peroxiredoxin activity
Peroxynitrite reductase activity
Protein dimerization activity
RNA polymerase III transcription regulatory region sequence-specific DNA binding
Signaling receptor binding
Thioredoxin peroxidase activity
The reference OMIM entry for this protein is 606583
Peroxiredoxin 5; prdx5
Antioxidant enzyme b166; aoeb166
DESCRIPTION
Incomplete reduction of atmospheric oxygen generates potent oxidizing agents, including reactive oxygen species (ROS) and their toxic byproducts. Sources of ROS include mitochondria and peroxisomes. Protection from ROS is mediated by nonenzymatic agents, such as vitamins; enzymes, such as catalase (CAT; 115500); and low molecular weight reducing agents, such as thioredoxin (TXN; 187700). PRDX5 is a member of the peroxiredoxin family and may play an antioxidant protective role in various tissues under nonpathologic conditions and during inflammatory processes.CLONING
By 2-dimensional electrophoresis of bronchoalveolar lavage (BAL) fluid and microsequence analysis to create an analytical map of BAL fluid proteins, Wattiez et al. (1999) identified a 17-kD protein with a pI of 6.9 that they termed B166. Using PCR amplification of lung cDNA with degenerate primers corresponding to the N terminus of B166, followed by 5-prime and 3-prime RACE, Knoops et al. (1999) isolated a cDNA encoding PRDX5, which they called antioxidant enzyme B166 (AOEB166). Sequence analysis predicted that the 214-amino acid protein is 90% identical to the rat sequence after the second methionine (in human, met53). PRDX5 displays mitochondrial presequence features and has 3 cysteines implicated in antioxidant activity and a C-terminal SQL peroxisomal targeting sequence. Northern blot analysis revealed ubiquitous expression of a 1.0-kb PRDX5 transcript in tissues and cell lines. Dot blot analysis indicated highest expression in thyroid gland, trachea, kidney, lung, adrenal gland, heart, and colon. Fluorescence microscopy demonstrated expression in mitochondria and peroxisomes. Rat Prdx5 expression was increased in lungs after the instillation of lipopolysaccharide. Functional analysis showed that PRDX5 has antioxidant activity equivalent to that of CAT. Knoops et al. (1999) noted that PRDX5 was the first peroxiredoxin to be associated with peroxisomes, and they suggested that it may play a protective role against ROS generated in these organelles.BIOCHEMICAL FEATURES
Declercq et al. (2001) reported the crystal structure of PRDX5 in its reduced form at 1.5-angstrom resolution. The structure revealed a thioredoxin-like domain and that PRDX5 does not form a dimer. The authors noted the presence of a benzoate ion, a hydroxyl radical scavenger, close to the active-site pocket.GENE FUNCTION
Wang et al. (2001) used PCR, Western blot, immunohistochemical, and in situ hybridization analyses to show that PRDX5 expression is increased in degenerative tendon compared with normal tendon. While PRDX5 was localized to fibroblasts in normal tendon, it was localized to fibroblasts and endothelial cells in degenerative tendon. Wang et al. (2002) mimicked osteoarthritis by exposing cultured human articular cartilage chondrocytes and cartilage explants to tumor necrosis factor-alpha (191160) and interleukin-1-beta (147720). Intracellular peroxide levels began to rise 3 hours after cytokine challenge. PRDX5 mRNA and protein levels increased at 12 hours, and the increase in PRDX5 expression correlated with reduced peroxide levels. Wang et al. (2002) concluded that PRDX5 plays a protective role against oxidative stress in human cartilage. Acting as a signal, hydrogen peroxide circumvents antioxidant defense by overoxidizing peroxiredoxins (Prxs), the enzymes that metabolize peroxides. Budanov et al. (2004) showed that sestrins, a famil ... More on the omim web site
Feb. 10, 2018: Protein entry updated
Automatic update: Entry updated from uniprot information.
Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated
Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated
Nov. 23, 2017: Protein entry updated
Automatic update: Uniprot description updated
June 20, 2017: Protein entry updated
Automatic update: comparative model was added.
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 606583 was added.