Glutathione S-transferase Mu 3 (GSTM3)
The protein contains 225 amino acids for an estimated molecular weight of 26560 Da.
Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. May govern uptake and detoxification of both endogenous compounds and xenobiotics at the testis and brain blood barriers. (updated: Sept. 12, 2018)
Protein identification was indicated in the following studies:
- 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.
- 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.
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:rs7483 |
No binding partner found
Biological Process
Cellular detoxification of nitrogen compound
Establishment of blood-nerve barrier
Glutathione derivative biosynthetic process
Glutathione metabolic process
Nitrobenzene metabolic process
Response to estrogen
Xenobiotic catabolic process
Cellular Component
Cytoplasm
Cytosol
Extracellular exosome
Intercellular bridge
Nucleus
Sperm fibrous sheath
The reference OMIM entry for this protein is 138390
Glutathione s-transferase, mu-3; gstm3
Glutathione s-transferase m3
Brain gst; gstb
Glutathione s-transferase 5; gst5
DESCRIPTION
The glutathione S-transferases (GST; 2.5.1.18) are a family of enzymes responsible for the metabolism of a broad range of xenobiotics and carcinogens. The GSTs form a superfamily whose dimeric proteins are encoded by several multigene families. See GSTM1 (138350) for additional background.CLONING
In brain extracts, Van Cong et al. (1984) observed a novel GST band (GST5, or GSTM3) which is probably controlled by an independent gene. By immunoblotting, Campbell et al. (1990) identified GSTM3, a mu-class GST with an isoelectric point of 5.2. GSTM1 is prevalent in testis and found in cerebral cortex but not liver. Campbell et al. (1990) detected GSTM3 in all 13 testes and 28 brain samples tested, including those from individuals devoid of GSTM1 because of a GSTM1 gene deletion. These authors cloned GSTM3 cDNAs from human brain and testis cDNA libraries. The predicted 225-amino acid protein shares 72% sequence similarity with GSTM1.MAPPING
Gough et al. (1994) used oligonucleotide primers specific for exons 4 and 5 sequences to amplify a unique 199-bp fragment in the human GSTM3 gene. Using this fragment for the analysis of DNA from a panel of somatic cell hybrids, they assigned the GSTM3 locus to chromosome 1p. Pearson et al. (1993) isolated a YAC clone containing all 5 GSTM genes, GSTM1-5; using this clone, they mapped all of these genes to 1p13.3 by fluorescence in situ hybridization.MOLECULAR GENETICS
Inskip et al. (1995) demonstrated allelism in the GSTM3 gene using PCR with specific primers to exon 6 and exon 7. Sequencing showed the mutant GSTM3*B allele to have a 3-bp deletion in intron 6 with a frequency of 0.158. GSTM3*B was significantly associated with the GSTM1*A allele at the closely linked GSTM1 locus (138350). ... More on the omim web site
June 30, 2020: Protein entry updated
Automatic update: OMIM entry 138390 was added.
Oct. 19, 2018: Additional information
Initial protein addition to the database. This entry was referenced in Bryk and co-workers. (2017).