This entry is an approximately 100 residue region of selenoprotein-T, conserved from plants to humans. The protein binds to UDP-glucose:glycoprotein glucosyltransferase (UGTR), the endoplasmic reticulum (ER)-resident protein, which is known to be involved in the quality control of protein folding [1]. Selenium (Se) plays an essential role in cell survival and most of the effects of Se are probably mediated by selenoproteins, including selenoprotein T. However, despite its binding to UGTR and that its mRNA is up-regulated in extended asphyxia, the function of the protein and hence of this region of it is unknown [2]. Selenoprotein W contains selenium as selenocysteine in the primary protein structure and levels of this selenoprotein are affected by selenium [3]. [1]. 11278576. Association between the 15-kDa selenoprotein and UDP-glucose:glycoprotein glucosyltransferase in the endoplasmic reticulum of mammalian cells. Korotkov KV, Kumaraswamy E, Zhou Y, Hatfield DL, Gladyshev VN;. J Biol Chem. 2001;276:15330-15336. [2]. 17034973. Identification of novel genes expressed in hypoxic brain condition by fluorescence differential display. Ikematsu K, Tsuda R, Tsuruya S, Nakasono I;. Forensic Sci Int. 2007;169:168-172. [3]. 12405536. Selenoprotein W gene regulation by selenium in L8 cells. Gu QP, Ream W, Whanger PD;. Biometals 2002;15:411-420. [4]. 17503775. SelT, SelW, SelH, and Rdx12: genomics and molecular insights into the functions of selenoproteins of a novel thioredoxin-like family. Dikiy A, Novoselov SV, Fomenko DE, Sengupta A, Carlson BA, Cerny RL, Ginalski K, Grishin NV, Hatfield DL, Gladyshev VN;. Biochemistry. 2007;46:. TRUNCATED at 1650 bytes (from Pfam)
- Date:
- 2024-10-16