Thioredoxin reductase-like selenoprotein T (SELENOT)
The protein contains 195 amino acids for an estimated molecular weight of 22324 Da.
Selenoprotein with thioredoxin reductase-like oxidoreductase activity (By similarity). Protects dopaminergic neurons against oxidative stress ans cell death (PubMed:26866473). Involved in ADCYAP1/PACAP-induced calcium mobilization and neuroendocrine secretion (By similarity). Plays a role in fibroblast anchorage and redox regulation (By similarity). In gastric smooth muscle, modulates the contraction processes through the regulation of calcium release and MYLK activation (By similarity). In pancreatic islets, involved in the control of glucose homeostasis, contributes to prolonged ADCYAP1/PACAP-induced insulin secretion (By similarity). (updated: June 20, 2018)
Protein identification was indicated in the following studies:
- D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
- 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.
This protein is predicted to be membranous by TOPCONS.
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No binding partner found
Biological Process
Cell redox homeostasis
Cellular oxidant detoxification
Glucose homeostasis
Insulin secretion involved in cellular response to glucose stimulus
Pancreas development
Positive regulation of cytosolic calcium ion concentration
Positive regulation of growth hormone secretion
Response to glucose
Selenocysteine incorporation
The reference OMIM entry for this protein is 607912
Selenoprotein t
Selt
DESCRIPTION
Selenoproteins, such as SELT, contain the rare twenty-first amino acid, selenocysteine (sec). These proteins lack common amino acid sequence motifs, but the 3-prime untranslated regions of selenoprotein genes have a common stem-loop structure, the sec insertion sequence (SECIS), that is necessary for the recognition of UGA as a sec codon rather than as a stop signal (summary by Kryukov et al., 1999).CLONING
By searching databases for sequences harboring putative SECIS elements, Kryukov et al. (1999) identified an EST containing SELT. The deduced 163-amino acid SELT protein has a calculated molecular mass of about 19 kD. The selenocysteine residue, sec17, is encoded by TGA and is located in the N-terminal portion of the protein. The SECIS element is located 509 nucleotides downstream of the sec17 codon. Sec17 is preceded by a conserved cys14 in a putative redox center, CxxU, similar to that found in several redox active proteins. Kryukov et al. (1999) identified sequences homologous to SELT in several animal and plant genomes, although in some the sec residue was replaced with cys. EST database analysis suggested that SELT is expressed at low levels in a broad range of human tissues and organs. Kryukov et al. (2003) reported that the full-length SELT protein contains 182 amino acids. The sec residue is at position 36, just upstream of an alpha helix. Using Northern blot and PCR analyses, Dikiy et al. (2007) detected Selt expression in all mouse tissues examined, with highest expression in kidney, followed by brain, heart, thymus, and testis. Western blot analysis detected highest expression in testis and kidney.GENE STRUCTURE
Kryukov et al. (2003) reported that the SELT gene contains 6 exons.MAPPING
Kryukov et al. (2003) reported that the SELT gene maps to chromosome 3q24. ... More on the omim web site
Oct. 20, 2018: Protein entry updated
Automatic update: OMIM entry 607912 was added.
Oct. 19, 2018: Additional information
Initial protein addition to the database. This entry was referenced in Bryk and co-workers. (2017).