Selenoprotein F (SEP15)
The protein contains 162 amino acids for an estimated molecular weight of 17790 Da.
May be involved in redox reactions associated with the formation of disulfide bonds (By similarity). May contribute to the quality control of protein folding in the endoplasmic reticulum (PubMed:24415556). May regulate protein folding by enhancing the catalytic activity of UGGT1/UGCGL1 and UGGT2/UGCGL2 (PubMed:24415556). (updated: Oct. 16, 2019)
Protein identification was indicated in the following studies:
- 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.
- 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.
(right-click above to access to more options from the contextual menu)
The reference OMIM entry for this protein is 606254
Selenoprotein, 15-kd
Sep15
Nutritional and biochemical studies have implicated selenium in immunologic and other biologic processes. In mammals, selenium is found not as a cofactor but as a selenocysteine residue, sometimes termed the twenty-first amino acid, encoded by UGA. In order for the UGA codon to be translated correctly, rather than as a stop codon, a stem-loop structure called a selenocysteine insertion sequence, or SECIS, element in the 3-prime untranslated region (UTR) of selenoprotein mRNA is essential.
CLONING
By culturing a T-cell line in the presence of selenium, SDS-PAGE analysis, biochemical purification of a 15-kD protein, micropeptide sequence analysis, and EST database searching, Gladyshev et al. (1998) obtained a cDNA encoding SEP15. The deduced 162-amino acid protein has an N-terminal signal peptide. SEP15 mRNA contains a SECIS element in its 3-prime UTR. Using Northern blot analysis, Kumaraswamy et al. (2000) detected high expression of a 1.3-kb SEP15 transcript in prostate, liver, brain, kidney, and testis; expression was low in skeletal muscle, mammary gland, and trachea. They noted that selenium supplementation trials had shown reduced cancer incidence in prostate and liver, where SEP15 was highly expressed.MOLECULAR GENETICS
Kumaraswamy et al. (2000) found that an A-to-G polymorphism at position 1125 in the SECIS of SEP15 results in increased responses to selenium in terms of luciferase activity.GENE STRUCTURE
Kumaraswamy et al. (2000) determined that the SEP15 gene contains 5 exons, with the TGA codon for sec located in exon 3, and spans 51 kb.MAPPING
By analysis of ESTs corresponding to the SEP15 gene, Gladyshev et al. (1998) mapped the SEP15 gene to 1p31, a region frequently deleted or altered in cancer. ... More on the omim web site
Oct. 27, 2019: Protein entry updated
Automatic update: Entry updated from uniprot information.
Feb. 5, 2018: Protein entry updated
Automatic update: Entry updated from uniprot information.
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 25, 2017: Additional information
No protein expression data in P. Mayeux work for SEP15
March 15, 2016: Protein entry updated
Automatic update: OMIM entry 606254 was added.