Glutaredoxin-1 (GLRX)
The protein contains 106 amino acids for an estimated molecular weight of 11776 Da.
Has a glutathione-disulfide oxidoreductase activity in the presence of NADPH and glutathione reductase. Reduces low molecular weight disulfides and proteins. (updated: March 4, 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.
- 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:rs4767 |
Biological Process
Cell redox homeostasis
Nucleobase-containing small molecule interconversion
Nucleobase-containing small molecule metabolic process
Positive regulation of membrane potential
Positive regulation of sodium ion transmembrane transporter activity
Protein deglutathionylation
Small molecule metabolic process
The reference OMIM entry for this protein is 600443
Glutaredoxin; glrx
Grx
Thioltransferase
CLONING
Glutaredoxin is a glutathione (GSH)-dependent hydrogen donor for ribonucleotide reductase and also catalyzes glutathione-disulfide oxidoreduction reactions in the presence of NADPH and glutathione reductase. Padilla et al. (1995) purified a human placental glutaredoxin to homogeneity and showed that its amino acid sequence was similar to that of other known mammalian glutaredoxins (about 80% identity), with some important differences. A cDNA that encodes the entire GRX open reading frame (ORF) and flanking sequences was isolated from a human spleen cDNA library. Glutaredoxin is a small protein of 12 kD.MAPPING
Using a genomic clone for fluorescence in situ hybridization, Padilla et al. (1996) mapped the GLRX gene to 5q14. This localization was in agreement with that arrived at by somatic cell hybrid analysis.GENE FUNCTION
Raghavachari et al. (2001) investigated how the expression of thioltransferase (TTase), a critical thiol repair and dethiolating enzyme, is regulated in human lens epithelial cells under oxidative stress. They also examined whether depleting the primary cellular antioxidant glutathione in these cells has any influence on TTase expression under the same conditions. They found a transient increase in TTase mRNA after 5 minutes of H(2)O(2) treatment. Upregulation reached a maximum of 80% above normal by 10 minutes and gradually decreased as the cells detoxified the oxidant. They found that manipulation of cellular GSH resulted in minimal changes in TTase expression. When cells depleted of GSH were subjected to oxidative stress, TTase expression was also strongly upregulated. Raghavachari et al. (2001) concluded that the upregulation of TTase expression in lens epithelial cells could be an adaptive response of the cells to combat oxidative stress and restore the vital functions of lens proteins and enzymes. They found that such regulation was independent of cellular GSH concentration. ... 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
June 20, 2017: Protein entry updated
Automatic update: comparative model was added.
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 600443 was added.
Jan. 28, 2016: Protein entry updated
Automatic update: model status changed
Jan. 24, 2016: Protein entry updated
Automatic update: model status changed