Selenoprotein W

Ick Young Kim, Daewon Jeong

Research output: Chapter in Book/Report/Conference proceedingChapter

1 Citation (Scopus)


In mammals and some bacteria, small molecular weight (∼10kDa) selenoprotein W (SelW) includes a single selenocysteine (Sec) residue in the Cys-X-X-Sec redox motif of the N-terminal region. It is expressed in a broad range of organisms, from mammals to bacteria. It is ubiquitously distributed in many tissues, and especially highly expressed in the skeletal muscle, heart and brain. Although many bacterial and frog SelW-like proteins contain Cys instead of Sec, it is highly conserved in many species of primates, domestic animals, rodents, amphibians, fish and bacteria. SelW is down- or up-regulated in response to oxidative stress, which suggests a redox function. SelW has Cys-X-X-Sec or Cys-X-X-Cys, both of which function as catalytic sites of redox proteins, such as thioredoxin, and allows reversible binding of glutathione to the Cys-37 residue of its protein. Moreover, since cells that overexpress SelW are resistant to exogenous oxidative stress, it is suggested that SelW may participate in an antioxidant function. However, the exact physiological function and enzymatic activity of SelW are largely unknown. This chapter will review what is currently known about SelW.

Original languageEnglish
Title of host publicationAdvanced Topics in Science and Technology in China
PublisherSpringer Science and Business Media Deutschland GmbH
Number of pages9
Publication statusPublished - 2012

Publication series

NameAdvanced Topics in Science and Technology in China
ISSN (Print)1995-6819
ISSN (Electronic)1995-6827

Bibliographical note

Publisher Copyright:
© Zhejiang University Press, Hangzhou and Springer-Verlag Berlin Heidelberg 2011.


  • Exogenous oxidative stress
  • Keshan disease
  • SelW mRNA
  • Selenium concentration
  • White muscle disease

ASJC Scopus subject areas

  • General Chemical Engineering
  • General Engineering
  • General


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