Definition
Selenoprotein K (SelK) is encoded in one of the 25 selenium-containing protein genes in humans. It is present in most organisms in the animal kingdom including mammals, birds, reptiles, and fish, and its homologs also occur in other eukaryotes. It is a small protein of approximately 10 kDa located in the endoplasmic reticulum membrane and possibly involved in retrotranslocation of proteins from the endoplasmic reticulum. The exact function of SelK remains to be determined.
Introduction
Selenium (Se) is an essential micronutrient that plays important roles in human health, and its severe dietary deficiency is associated with various diseases such as Keshan disease, Kashin-Beck disease, and numerous other disorders including cancer and heart disease (Hatfield et al. 2012). The biological roles of selenium in health and development are exerted in large part through its presence in selenoproteins as selenocysteine (Sec, one-letter...
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
References
Al-Rifai MF, Moustafa ME (2012) Analysis of conserved structural features of selenoprotein. EJBMB 30(1):1–18
Chen CL, Shim MS, Chung J, Yoo HS, Ha JM, Kim JY, Choi J, Zang SL, Hou X, Carlson BA, Hatfield DL, Lee BJ (2006) G-rich, a Drosophila selenoprotein, is a Golgi-resident type III membrane protein. Biochem Biophys Res Commun 348(4):1296–1301
Du S, Zhou J, Jia Y, Huang K (2010) SelK is a novel ER stress-regulated protein and protects HepG2 cells from ER stress agent-induced apoptosis. Arch Biochem Biophys 502(2):137–143
Hatfield DL, Berry MJ, Gladyshev VN (2012) Selenium: its molecular biology and role in human health, 3rd edn. Springer, New York
Huang Z, Hoffmann FW, Norton RL, Hashimoto AC, Hoffmann PR (2011) Selenoprotein K is a novel target of m-calpain, and cleavage is regulated by Toll-like receptor-induced calpastatin in macrophages. J Biol Chem 286(40):34830–34838
Kryukov GV, Castellano S, Novoselov SV, Lobanov AV, Zehtab O, Guigó R, Gladyshev VN (2003) Characterization of mammalian selenoproteomes. Science 300(5624):1439–1443
Lu C, Qiu F, Zhou H, Peng Y, Hao W, Xu J, Yuan J, Wang S, Qiang B, Xu C, Peng X (2006) Identification and characterization of selenoprotein K: an antioxidant in cardiomyocytes. FEBS Lett 580(22):5189–5197
Shchedrina VA, Everley RA, Zhang Y, Gygi SP, Hatfield DL, Gladyshev VN (2011a) Selenoprotein K binds multiprotein complexes and is involved in the regulation of endoplasmic reticulum homeostasis. J Biol Chem 286(50):42937–42948
Shchedrina VA, Kabil H, Vorbruggen G, Lee BC, Turanov AA, Hirosawa-Takamori M, Kim HY, Harshman LG, Hatfield DL, Gladyshev VN (2011b) Analyses of fruit flies that do not express selenoproteins or express the mouse selenoprotein, methionine sulfoxide reductase B1, reveal a role of selenoproteins in stress resistance. J Biol Chem 286(34):29449–29461
Verma S, Hoffmann FW, Kumar M, Huang Z, Roe K, Nguyen-Wu E, Hashimoto AS, Hoffmann PR (2011) Selenoprotein K knockout mice exhibit deficient calcium flux in immune cells and impaired immune responses. J Immunol 186(4):2127–2137
Acknowledgments
The author thanks Dr. Dolph L. Hatfield, NCI, NIH, Bethesda, MD, USA and Dr.Vadim N. Gladyshev, Department of Medicine, Brigham and Women’s Hospital, Harvard Medical School, Boston, MA, USA for valuable comments on this chapter.
Author information
Authors and Affiliations
Corresponding author
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2013 Springer Science+Business Media New York
About this entry
Cite this entry
Moustafa, M.E. (2013). Selenoprotein K. In: Kretsinger, R.H., Uversky, V.N., Permyakov, E.A. (eds) Encyclopedia of Metalloproteins. Springer, New York, NY. https://doi.org/10.1007/978-1-4614-1533-6_499
Download citation
DOI: https://doi.org/10.1007/978-1-4614-1533-6_499
Publisher Name: Springer, New York, NY
Print ISBN: 978-1-4614-1532-9
Online ISBN: 978-1-4614-1533-6
eBook Packages: Biomedical and Life SciencesReference Module Biomedical and Life Sciences