Selenoprotein expression and function-selenoprotein W.
Selenoprotein W (SeW) is a small selenoprotein (85 to 88 amino acids) first identified in sheep suffering from selenium deficiency. The levels are highest in muscle, heart (except rodents) spleen and brain. The deduced amino acid sequence has been obtained for mice, rats, monkeys, humans, sheep, pigs, fish and chickens. The sequences of SeW are identical in rats and mice as well as monkeys and humans. In all eight species of animals cysteine is present at residue number 9 and selenocysteine at residue number 13. Residue number 37 is cysteine in six species of animal with fish and chickens as the exceptions. Of those examined, the rodent SeW is the only one containing four cysteines whereas the others contain only two cysteines. Glutathionylaltion has been shown for SeW from rats and monkeys but has not been confirmed for this selenoprotein from the other six animals. The biological function of SeW has not been definitely identified. Evidence has been obtained that it can serve as an antioxidant, responds to stress, involved in cell immunity, specific target for methylmercury, and has thioredoxin-like function.
Whanger
P D
PD
Department of Environmental and Molecular Toxicology, Oregon State University, Corvallis, OR 97330, USA. phil.whanger@oregonstate.edu
D000595:Amino Acid Sequence; D000818:Animals; D006801:Humans; D053858:Metabolic Networks and Pathways / Q000502:physiology; D008969:Molecular Sequence Data; D051151:Selenoprotein W / Q000235:genetics* / Q000378:metabolism / Q000502:physiology*; D051140:Selenoproteins / Q000235:genetics* / Q000378:metabolism / Q000502:physiology*; D017386:Sequence Homology, Amino Acid
D051151:Selenoprotein W; D051140:Selenoproteins