Glutathione S-transferase omega-1 (GSTO1)
The protein contains 241 amino acids for an estimated molecular weight of 27566 Da.
Exhibits glutathione-dependent thiol transferase and dehydroascorbate reductase activities. Has S-(phenacyl)glutathione reductase activity. Has also glutathione S-transferase activity. Participates in the biotransformation of inorganic arsenic and reduces monomethylarsonic acid (MMA) and dimethylarsonic acid. (updated: April 1, 2015)
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.
- Lange and co-workers. (2014) Annotating N termini for the human proteome project: N termini and Nα-acetylation status differentiate stable cleaved protein species from degradation remnants in the human erythrocyte proteome. J Proteome Res. 13(4), 2028-2044.
- 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.
- D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
- Chu and co-workers. (2018) Quantitative mass spectrometry of human reticulocytes reveal proteome-wide modifications during maturation. Br J Haematol. 180(1), 118-133.
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:rs45529437 | |
| dbSNP:rs11509436 | |
| allele GSTO1*C | |
| dbSNP:rs11509438 | |
| dbSNP:rs11509439 |
Biological Process
Cellular response to arsenic-containing substance
Glutathione derivative biosynthetic process
Glutathione metabolic process
Interleukin-12-mediated signaling pathway
L-ascorbic acid metabolic process
Methylation
Negative regulation of ryanodine-sensitive calcium-release channel activity
Oxidation-reduction process
Positive regulation of ryanodine-sensitive calcium-release channel activity
Positive regulation of skeletal muscle contraction by regulation of release of sequestered calcium ion
Regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion
Regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum
Small molecule metabolic process
Toxin catabolic process
Xenobiotic catabolic process
Xenobiotic metabolic process
The reference OMIM entry for this protein is 605482
Glutathione s-transferase, omega-1; gsto1
DESCRIPTION
The glutathione S-transferases (GST; EC 2.5.1.18) are a family of enzymes responsible for the metabolism of a broad range of xenobiotics and carcinogens (Mannervik, 1985). This enzyme catalyzes the reaction of glutathione with a wide variety of organic compounds to form thioethers, a reaction that is sometimes a first step in a detoxification process leading to mercapturic acid formation. Based on amino acid sequence similarities and antibody cross-reactivities, the mammalian cytosolic GSTs are divided into several classes, including alpha (e.g., 138359), mu (e.g., 138350), kappa (602321), theta (e.g., 600436), pi (134660), omega, and zeta (603758). In addition, there is a class of microsomal GSTs (e.g., 138330).CLONING
By searching an EST database for homologies with GSTZ1 (603758), Board et al. (2000) identified a cDNA encoding GSTO1, the first member of the omega GST class. The deduced 241-amino acid protein has over 70% identity with the rodent omega GST sequences. Of the previously defined GST classes, the omega GSTS are most similar to the zeta class. The omega class GSTs possess a 19- to 20-residue N-terminal extension, not observed in other GSTs, that abuts the C terminus to form a novel structural unit. Northern blot analysis revealed ubiquitous expression of a 0.8-kb GSTO1 transcript, with highest expression in liver, skeletal muscle, and heart, and lowest expression in brain, placenta, and lung. Board et al. (2000) noted that the ubiquitous expression of GSTO1 contrasts with the tissue-specific expression typical of many GSTs. Western blot analysis of cytosolic extracts and recombinant protein showed that GSTO1 is expressed as a 31-kD protein in its monomeric form.BIOCHEMICAL FEATURES
- Cystral Structure Crystal structure analysis of GSTO1 by Board et al. (2000) demonstrated that GSTO1 has an N-terminal thioredoxin-like domain consisting of a central 4-stranded beta sheet flanked on one side by 2 alpha helices and on the other by a 3-10 helix. The C terminus is composed of 7 alpha helices and makes several H bonds with the N-terminal domain. GSTO1 forms a dimer and adopts the typical GST tertiary structure.GENE FUNCTION
Functional analyses by Board et al. (2000) showed that GSTO1 lacks activity with most GST substrates but exhibits glutathione-dependent thiol transferase and dehydroascorbate reductase activity characteristic of the glutaredoxins (e.g., GLRX, 600443). Whitbread et al. (2003) stated that GSTO1 also reduces monomethylarsonic acid to monomethylarsonous acid, which is the rate-limiting step in the biotransformation of inorganic arsenic. Kim et al. (2012) found that the Gsto1a and Gsto1b isoforms of Drosophila Gsto1 had distinct physiologic activities. Gsto1b protected flies against oxidative stress, whereas Gsto1a increased mitochondrial ATPase synthase complex assembly and activity by glutathionylation of the ATP synthase beta subunit (ATP5B; 102910). Overexpression of Gsto1a partially reversed the phenotype of parkin (PARK2; 602544) mutant files, including degeneration of dopaminergic neurons and muscle, cellular tubulin (see 602529) accumulation, and endoplasmic reticulum stress. Kim et al. (2012) concluded that Drosophila Gsto1 plays a protective role in parkin mutants by regulating mitochondrial ATP synthase activity.GENE STRUCTURE
Whitbread et al. (2003) determined that the GSTO1 gene contains 6 exons and spans 12.5 kb.MAPPING
... More on the omim web site
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
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 605482 was added.
Jan. 28, 2016: Protein entry updated
Automatic update: model status changed
Jan. 24, 2016: Protein entry updated
Automatic update: model status changed