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Selenoprotein W is a protein that in humans is encoded by the SEPW1 gene.[5][6]
Function
This gene encodes a selenoprotein, which contains a selenocysteine (Sec) residue at its active site. The selenocysteine is encoded by the UGA codon that normally signals translation termination. The 3' UTR 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. This protein shows highest expression in skeletal muscle and heart, and may be involved in oxidation-reduction reactions. A retroprocessed pseudogene, SEPW1P, has been identified and mapped to chromosome 1p35-34.[6]
References
- ^ a b c GRCh38: Ensembl release 89: ENSG00000178980 – Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000041571 – Ensembl, May 2017
- ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ Gu QP, Beilstein MA, Vendeland SC, Lugade A, Ream W, Whanger PD (July 1997). "Conserved features of selenocysteine insertion sequence (SECIS) elements in selenoprotein W cDNAs from five species". Gene. 193 (2): 187–96. doi:10.1016/S0378-1119(97)00113-3. PMID 9256076.
- ^ a b "Entrez Gene: SEPW1 selenoprotein W, 1".
Further reading
- Whanger PD (December 2000). "Selenoprotein W: a review". Cellular and Molecular Life Sciences. 57 (13–14): 1846–52. doi:10.1007/PL00000666. PMID 11215511.
- Yeh JY, Beilstein MA, Andrews JS, Whanger PD (March 1995). "Tissue distribution and influence of selenium status on levels of selenoprotein W". FASEB Journal. 9 (5): 392–6. doi:10.1096/fasebj.9.5.7896009. PMID 7896009. S2CID 20754227.
- Smith JS, Tachibana I, Pohl U, Lee HK, Thanarajasingam U, Portier BP, Ueki K, Ramaswamy S, Billings SJ, Mohrenweiser HW, Louis DN, Jenkins RB (February 2000). "A transcript map of the chromosome 19q-arm glioma tumor suppressor region". Genomics. 64 (1): 44–50. doi:10.1006/geno.1999.6101. PMID 10708517.
- Kryukov GV, Castellano S, Novoselov SV, Lobanov AV, Zehtab O, Guigó R, Gladyshev VN (May 2003). "Characterization of mammalian selenoproteomes". Science. 300 (5624): 1439–43. Bibcode:2003Sci...300.1439K. doi:10.1126/science.1083516. PMID 12775843. S2CID 10363908.
- Bellingham J, Gregory-Evans K, Fox MF, Gregory-Evans CY (June 2003). "Gene structure and tissue expression of human selenoprotein W, SEPW1, and identification of a retroprocessed pseudogene, SEPW1P". Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression. 1627 (2–3): 140–6. doi:10.1016/s0167-4781(03)00078-2. PMID 12818432.
- Pagmantidis V, Bermano G, Villette S, Broom I, Arthur J, Hesketh J (January 2005). "Effects of Se-depletion on glutathione peroxidase and selenoprotein W gene expression in the colon". FEBS Letters. 579 (3): 792–6. Bibcode:2005FEBSL.579..792P. doi:10.1016/j.febslet.2004.12.042. PMID 15670848. S2CID 389992.
- Kim YJ, Chai YG, Ryu JC (May 2005). "Selenoprotein W as molecular target of methylmercury in human neuronal cells is down-regulated by GSH depletion". Biochemical and Biophysical Research Communications. 330 (4): 1095–102. doi:10.1016/j.bbrc.2005.03.080. PMID 15823556.
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