REFERENCES [1] IUCN (International Union for Conservation of Nature). (2017). IUCN Red List of Threatened Species. [online] Available at: https://www.iucnredlist.org/species/41754/50381766#geographic-range [Accessed 16 Nov. 2018]. [2] Jefferson, T.A. & Wang, J.Y. Revision of the taxonomy of finless porpoises (genus Neophocaena): The existence of two species. J Mar Anim Ecol. 2011;4:3-16. [3] En.wikipedia.org. (2017). Narrow-ridged finless porpoise. [online] Available at: https://en.wikipedia.org/wiki/Narrow-ridged_finless_porpoise [Accessed 16 Nov. 2018]. [4] Selenocysteine Biosynthesis [Internet]. YouTube. 2018 [cited 29 November 2018]. Available from: https://www.youtube.com/watch?v=GqEMsdeIVGo. [5] Lammi M, Qu C. Selenium-Related Transcriptional Regulation of Gene Expression. Int J Mol Sci. 2018;19(9):2665. [6] Lu J, Holmgren A. Selenoproteins. J Biol Chem. 2008;284(2):723-727. [7] Hatfield D, Gladyshev V. How Selenium Has Altered Our Understanding of the Genetic Code. Mol Cell Biol. 2002;22(11):3565-3576. [8] Fajardo D, Schlautman B, Steffan S, Polashock J, Vorsa N, Zalapa J. The American cranberry mitochondrial genome reveals the presence of selenocysteine (tRNA-Sec and SECIS) insertion machinery in land plants. Gene. 2014;536(2):336-343. [9] Mariotti M, Ridge P, Zhang Y, Lobanov A, Pringle T, Guigo R et al. Composition and Evolution of the Vertebrate and Mammalian Selenoproteomes. PLoS ONE. 2012;7(3):e33066. [10] Castellano S, Gladyshev VN., Guigó R. and Berry MJ. SelenoDB 1.0: a database of selenoprotein genes, proteins and SECIS elements. Nucleic Acids Res. 2008; 36: 339-343. [11] Blast.ncbi.nlm.nih.gov. BLAST: Basic Local Alignment Search Tool. [online] Available at: https://blast.ncbi.nlm.nih.gov/Blast.cgi [Accessed 15 Nov. 2018]. [12] Tcoffee.org. T-Coffee Home Page. [online] Available at: http://www.tcoffee.org/Projects/tcoffee/ [Accessed 15 Nov. 2018]. [13] Birney E, Clamp M, Durbin R. GeneWise and Genomewise. Genome Res. 2004;14(5):988-95. [14] Marco Mariotti, Alexei V. Lobanov, Roderic Guigo, and Vadim N. Gladyshev (2013) SECISearch3 and Seblastian: new tools for prediction of SECIS elements and selenoproteins. Nucleic Acids Res. First published online June 19, 2013. [15] Harding R, Pinkerton K. The lung. 2nd ed. Academic Press; 2014. [16] Labunskyy VM, Hatfield DL, Gladyshev VN. Selenoproteins: molecular pathways and physiological roles. Physiol Rev. 2014;94(3):739-77. [17] Brigelius-Flohé R, Maiorino M. Glutathione peroxidases. Biochim Biophys Acta - General Subjects [Internet]. 2013 [cited 28 November 2018];1830(5):3289-3303. Available from: https://www.ncbi.nlm.nih.gov/pubmed/23201771. [18] Corso C, Acco A. Glutathione system in animal model of solid tumors: From regulation to therapeutic target. Crit Rev Oncol Hematol [Internet]. 2018 [cited 28 November 2018];128:43-57. Available from: https://www.ncbi.nlm.nih.gov/pubmed/29958630. [19] Lu J, Holmgren A. Selenoproteins. J Biol Chem [Internet]. 2008 [cited 28 November 2018];284(2):723-727. Available from: https://www.sciencedirect.com/science/article/pii/S0304416512003406?via%3Dihub. [20] Lubos, E., J. Loscalzo & D.E. Handy. 2011. Glutathione peroxidase-1 in health and disease: from molecular mechanisms to therapeutic opportunities. Antioxid Redox Signal. 15: 1957–1997. [21] Krehl S, Loewinger M, Florian S, Kipp A, Banning A, Wessjohann L et al. Glutathione peroxidase-2 and selenium decreased inflammation and tumors in a mouse model of inflammation-associated carcinogenesis whereas sulforaphane effects differed with selenium supply. Carcinogenesis. 2011;33(3):620-628. [22] Brigelius-Flohé R, Kipp A. Physiological functions of GPx2 and its role in inflammation-triggered carcinogenesis. Ann N Y Acad Sci. 2012;1259(1):19-25. [23] Imai H, Matsuoka M, Kumagai T, Sakamoto T, Koumura T. Lipid Peroxidation-Dependent Cell Death Regulated by GPx4 and Ferroptosis. Curr Top Microbiol Immunol. 2016;403:143-170. [24] Flohé L. Selenium in mammalian spermiogenesis. J Biol Chem. 2007;388(10). [25] GPX5 glutathione peroxidase 5 [Homo sapiens (human)] - Gene - NCBI [Internet]. Ncbi.nlm.nih.gov. [cited 29 November 2018]. Available from: https://www.ncbi.nlm.nih.gov/gene/2880. [26] Kasaikina M, Fomenko D, Labunskyy V, Lachke S, Qiu W, Moncaster J et al. Roles of the 15-kDa Selenoprotein (Sep15) in Redox Homeostasis and Cataract Development Revealed by the Analysis of Sep 15 Knockout Mice. Journal of Biological Chemistry. 2011;286(38):33203-33212. [27]SELENOM selenoprotein M [Homo sapiens (human)] - Gene - NCBI [Internet]. Ncbi.nlm.nih.gov. [cited 29 November 2018]. Available from: https://www.ncbi.nlm.nih.gov/gene/140606. [28] Cox A, Tsomides A, Kim A, Saunders D, Hwang K, Evason K et al. Selenoprotein H is an essential regulator of redox homeostasis that cooperates with p53 in development and tumorigenesis. Proc Natl Acad Sci U S A. 2016;113(38):E5562-E5571. [29] SELENOI selenoprotein I [Homo sapiens (human)] - Gene - NCBI [Internet]. Ncbi.nlm.nih.gov. [cited 29 November 2018]. Available from: https://www.ncbi.nlm.nih.gov/gene/85465. [30] Shchedrina V, Everley R, Zhang Y, Gygi S, Hatfield D, Gladyshev V. Selenoprotein K Binds Multiprotein Complexes and Is Involved in the Regulation of Endoplasmic Reticulum Homeostasis. J Biol Chem. 2011;286(50):42937-42948. [31] SELENOK - Selenoprotein K - Homo sapiens (Human) - SELENOK gene & protein [Internet]. Uniprot.org. [cited 29 November 2018]. Available from: https://www.uniprot.org/uniprot/Q9Y6D0. [32] SELENON selenoprotein N [Homo sapiens (human)] - Gene - NCBI [Internet]. Ncbi.nlm.nih.gov. [cited 29 November 2018]. Available from: https://www.ncbi.nlm.nih.gov/gene/57190. [33] Han S, Lee B, Yim S, Gladyshev V, Lee S. Characterization of Mammalian Selenoprotein O: A Redox-Active Mitochondrial Protein. PLoS ONE. 2014;9(4):e95518. [34] Chadani H, Usui S, Inoue O, Kusayama T, Takashima S, Kato T et al. Endogenous Selenoprotein P, a Liver-Derived Secretory Protein, Mediates Myocardial Ischemia/Reperfusion Injury in Mice. Int J Mol Sci. 2018;19(3):878. [35] SELENOP selenoprotein P [Homo sapiens (human)] - Gene - NCBI [Internet]. Ncbi.nlm.nih.gov. [cited 29 November 2018]. Available from: https://www.ncbi.nlm.nih.gov/gene/6414. [36] Zhang X, Weissbach H. Origin and evolution of the protein-repairing enzymes methionine sulphoxide reductases.Biol Rev. 2008;83(3):249-257. [37] MSRB1 methionine sulfoxide reductase B1 [Homo sapiens (human)] - Gene - NCBI [Internet]. Ncbi.nlm.nih.gov. [cited 29 November 2018]. Available from: https://www.ncbi.nlm.nih.gov/gene/51734. [38] Kryukov G, Kumar R, Koc A, Sun Z, Gladyshev V. Selenoprotein R is a zinc-containing stereo-specific methionine sulfoxide reductase. Proc Natl Acad Sci U S A. 2002;99(7):4245-4250. [39] Pascual I, Larrayoz I, Campos M, Rodriguez I. Methionine sulfoxide reductase B2 is highly expressed in the retina and protects retinal pigmented epithelium cells from oxidative damage. Exp Eye Res. 2010;90(3):420-428. [40] MSRB2 - Methionine-R-sulfoxide reductase B2, mitochondrial precursor - Homo sapiens (Human) - MSRB2 gene & protein [Internet]. Uniprot.org. [cited 29 November 2018]. Available from: https://www.uniprot.org/uniprot/Q9Y3D2. [41] Kim H, Gladyshev V. Methionine Sulfoxide Reduction in Mammals: Characterization of Methionine-R-Sulfoxide Reductases. Mol Biol Cell. 2004;15(3):1055-1064. [42] MSRB3 methionine sulfoxide reductase B3 [Homo sapiens (human)] - Gene - NCBI [Internet]. Ncbi.nlm.nih.gov. [cited 29 November 2018]. Available from: https://www.ncbi.nlm.nih.gov/gene/253827. [43] Pascual I, Larrayoz I, Campos M, Rodriguez I. Methionine sulfoxide reductase B2 is highly expressed in the retina and protects retinal pigmented epithelium cells from oxidative damage. Exp Eye Res. 2010;90(3):420-428. [44] MSRA methionine sulfoxide reductase A [Homo sapiens (human)] - Gene - NCBI [Internet]. Ncbi.nlm.nih.gov. [cited 29 November 2018]. Available from: https://www.ncbi.nlm.nih.gov/gene/4482. [45] Kim C, Kim K. Selenate Prevents Adipogenesis through Induction of Selenoprotein S and Attenuation of Endoplasmic Reticulum Stress. Molecules. 2018;23(11):2882. [46] Hamieh A, Cartier D, Abid H, Calas A, Burel C, Bucharles C et al. Selenoprotein T is a novel OST subunit that regulates UPR signaling and hormone secretion. EMBO rep. 2017;18(11):1935-1946. [47] SELENOT selenoprotein T [Homo sapiens (human)] - Gene - NCBI [Internet]. Ncbi.nlm.nih.gov. [cited 29 November 2018]. Available from: https://www.ncbi.nlm.nih.gov/gene/51714. [48] Sattar H, Yang J, Zhao X, Cai J, Liu Q, Ishfaq M et al. Selenoprotein-U (SelU) knockdown triggers autophagy through PI3K–Akt–mTOR pathway inhibition in rooster Sertoli cells. Metallomics. 2018;10(7):929-940. [49] ELENOU selenoprotein U [Gallus gallus (chicken)] - Gene - NCBI [Internet]. Ncbi.nlm.nih.gov. [cited 29 November 2018]. Available from: https://www.ncbi.nlm.nih.gov/gene/423625. [50] SELENOW selenoprotein W [Homo sapiens (human)] - Gene - NCBI [Internet]. Ncbi.nlm.nih.gov. [cited 29 November 2018]. Available from: https://www.ncbi.nlm.nih.gov/gene/6415. [51] Saccoccia F, Angelucci F, Boumis G, Carotti D, Desiato G, Miele A et al. Thioredoxin Reductase and its Inhibitors. Curr Protein Pept Sci. 2014;15(6):621-646. [52] MUSTACICH D, POWIS G. Thioredoxin reductase. Biochem J. 2000;346(1):1-8. [53] Cadenas C, Franckenstein D, Schmidt M, Gehrmann M, Hermes M, Geppert B et al. Role of thioredoxin reductase 1 and thioredoxin interacting protein in prognosis of breast cancer. Breast Cancer Res. 2010;12(3). [54] XNRD2 thioredoxin reductase 2 [Homo sapiens (human)] - Gene - NCBI [Internet]. Ncbi.nlm.nih.gov. [cited 29 November 2018]. Available from: https://www.ncbi.nlm.nih.gov/gene/10587. [55] TXNRD2 - Thioredoxin reductase 2, mitochondrial precursor - Homo sapiens (Human) - TXNRD2 gene & protein [Internet]. Uniprot.org. [cited 29 November 2018]. Available from: https://www.uniprot.org/uniprot/Q9NNW7. [56] TXNRD3 thioredoxin reductase 3 [Homo sapiens (human)] - Gene - NCBI [Internet]. Ncbi.nlm.nih.gov. [cited 29 November 2018]. Available from: https://www.ncbi.nlm.nih.gov/gene/114112. [57] TXNRD3 - Thioredoxin reductase 3 - Homo sapiens (Human) - TXNRD3 gene & protein [Internet]. Uniprot.org. [cited 29 November 2018]. Available from: https://www.uniprot.org/uniprot/Q86VQ6. [58] Sherrer R, O’Donoghue P, Söll D. Characterization and evolutionary history of an archaeal kinase involved in selenocysteinyl-tRNA formation. Nucleic Acids Res. 2008;36(4):1247-1259. [59] NCBI CDD Conserved Protein Domain RRM1_SECp43 [Internet]. Ncbi.nlm.nih.gov. [cited 29 November 2018]. Available from: https://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=241054. [60] Chapple C, Guigó R. Relaxation of Selective Constraints Causes Independent Selenoprotein Extinction in Insect Genomes. PLoS ONE. 2008;3(8):e2968. [61] Ganichkin O, Xu X, Carlson B, Mix H, Hatfield D, Gladyshev V et al. Structure and Catalytic Mechanism of Eukaryotic Selenocysteine Synthase. J Biol Chem. 2007;283(9):5849-5865. [62] Simonović M, Puppala A. On elongation factor eEFSec, its role and mechanism during selenium incorporation into nascent selenoproteins. Biochim Biophys Acta. 2018;1862(11):2463-2472. [63] SEPHS1 selenophosphate synthetase 1 [Homo sapiens (human)] - Gene - NCBI [Internet]. Ncbi.nlm.nih.gov. [cited 29 November 2018]. Available from: https://www.ncbi.nlm.nih.gov/gene/22929. [64] Gentschew L, Bishop K, Han D, Morgan A, Fraser A, Lam W et al. Selenium, Selenoprotein Genes and Crohn’s Disease in a Case-Control Population from Auckland, New Zealand. Nutrients. 2012;4(9):1247-1259. [65] SEPHS1 - Selenide, water dikinase 1 - Homo sapiens (Human) - SEPHS1 gene & protein [Internet]. Uniprot.org. [cited 29 November 2018]. Available from: https://www.uniprot.org/uniprot/P49903. [66] Kossinova O, Malygin A, Krol A, Karpova G. The SBP2 protein central to selenoprotein synthesis contacts the human ribosome at expansion segment 7L of the 28S rRNA. RNA. 2014;20(7):1046-1056. [67] Labunskyy V, Hatfield D, Gladyshev V. Selenoproteins: Molecular Pathways and Physiological Roles. Physiol Rev. 2014;94(3):739-777. [68] SEPHS1 - Selenide, water dikinase 1 - Homo sapiens (Human) - SEPHS1 gene & protein [Internet]. Uniprot.org. [cited 29 November 2018]. Available from: https://www.uniprot.org/uniprot/P49903.