Thioredoxin-related transmembrane protein 1 (TMX1)
The protein contains 280 amino acids for an estimated molecular weight of 31791 Da.
May participate in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyze dithiol-disulfide exchange reactions. (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.
- 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.
This protein is predicted to be membranous by TOPCONS.
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The reference OMIM entry for this protein is 610527
Thioredoxin domain-containing protein 1; txndc1
Transmembrane trx-related protein; tmx
DESCRIPTION
TXNDC1 is a thioredoxin (TXN; see 187700)-related protein with disulfide reductase activity (Matsuo et al., 2001).CLONING
Using gene trap screening of cDNA from a TGF-beta (TGFB; 190180)-treated human lung adenocarcinoma cell line, followed by 5-prime RACE, Akiyama et al. (2000) isolated a partial TXNDC1 cDNA. Using this fragment for further screening of the cDNA library, Matsuo et al. (2001) isolated full-length TXNDC1. The deduced 280-amino acid protein has a predicted molecular mass of 31.8 kD and contains an N-terminal signal sequence, a TRX-like domain with an active site sequence CPAC, and a transmembrane domain. Northern blot analysis detected a 2.5-kb transcript in all tissues examined, with highest expression in kidney, liver, placenta, and lung. Confocal microscopy of intact HEK293 cells expressing TXNDC1 and Western analysis of subcellular fractions localized TXNDC1 primarily in the microsomal fraction in an endoplasmic reticulum (ER)-like staining pattern characterized by a diffuse network-like labeling of the cytoplasm and nuclear rim.GENE FUNCTION
Using recombinant TXNDC1 catalytic domain expressed in E. coli, Matsuo et al. (2001) showed that TXNDC1 had dose-dependent insulin (INS; 176730) disulfide reducing activity. Using doxycycline-regulated TXNDC1 expression in HEK293 cells treated with reagents known to induce ER stress, namely, thapsigargin, calcium ionophore A23187, or brefeldin A (BFA), Matsuo et al. (2001) showed that TXNDC1 expression suppressed BFA-induced apoptosis. Mutation of the two TXNDC1 active site cysteine residues abolished both disulfide-reducing activity and suppression of BFA-induced apoptosis.MAPPING
The International Radiation Hybrid Mapping Consortium mapped the TXNDC1 gene to chromosome 14 (TMAP RH94716). ... 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
March 25, 2017: Additional information
No protein expression data in P. Mayeux work for TMX1
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 610527 was added.
Feb. 24, 2016: Protein entry updated
Automatic update: model status changed