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selenoprotein

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Also known as Selenoproteins

In molecular biology, a selenoprotein is any protein that includes a selenocysteine (Sec, U, Se-Cys) amino acid residue. Among functionally characterized selenoproteins are five glutathione peroxidases (GPX) and three thioredoxin reductases, (TrxR/TXNRD) which both contain only one Sec. Selenoprotein P is the most common selenoprotein found in the plasma. It is unusual because in humans it contains 10 Sec residues, which are split into two domains, a longer N-terminal domain that contains 1 Sec, and a shorter C-terminal domain that contains 9 Sec. The longer N-terminal domain is likely an enzy

~17 min read

Article

22 sections
Contents
  • Species distribution
  • Production
  • Replacement by cysteine in mammals
  • Non-UAG (CUA) tRNA
  • Redox activity
  • Major families
  • Glutathione peroxidase
  • Thioredoxin reductase
  • Iodothyronine deiodinase
  • Selenophosphate synthetase
  • SelT, SelW, SelH, and Rdx12
  • Other families
  • Clinical significance
  • Related systems
  • Other types of selenium in proteins
  • Ligand selanoproteins
  • Random selenomethionine
  • Random selenocystine
  • Non-protein biomolecules
  • See also
  • References
  • Further reading

In molecular biology, a selenoprotein is any protein that includes a selenocysteine (Sec, U, Se-Cys) amino acid residue. Among functionally characterized selenoproteins are five glutathione peroxidases (GPX) and three thioredoxin reductases, (TrxR/TXNRD) which both contain only one Sec. Selenoprotein P is the most common selenoprotein found in the plasma. It is unusual because in humans it contains 10 Sec residues, which are split into two domains, a longer N-terminal domain that contains 1 Sec, and a shorter C-terminal domain that contains 9 Sec. The longer N-terminal domain is likely an enzymatic domain, and the shorter C-terminal domain is likely a means of safely transporting the very reactive selenium atom throughout the body.

== Species distribution ==

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