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J. Biol. Chem., Vol. 266, Issue 16, 10050-10053, Jun, 1991
KE Hill, RS Lloyd, JG Yang, R Read and RF Burk
Selenoprotein P is a plasma protein recently purified and characterized as
containing 7.5 +/- 1.0 selenium atoms/molecule as selenocysteine. In rats
maintained on a defined diet containing nutritionally adequate amounts of
selenate as the sole selenium source, over half the selenium in plasma is
accounted for by selenoprotein P. Its cDNA has been cloned from a rat liver
library and sequenced. The sequence is highly unusual, containing 10 TGA
codons in its open reading frame prior to the TAA termination codon. TGA
designates selenocysteine in other selenoproteins, and limited peptide
sequencing that included the amino acids encoded by two of the TGA codons
verified that they correspond to selenocysteine. The deduced 366-amino acid
sequence is histidine- and cysteine-rich and contains 9 of its
selenocysteines in the terminal 122 amino acids. Comparison of the deduced
amino acid sequence of selenoprotein P with those of other selenoprotein
reveals no significant similarities. Selenoprotein P represents a new class
of selenoproteins and is the first protein described with more than 1
selenocysteine in a single polypeptide chain. The primary structure of
selenoprotein P suggests that it might be responsible for some of the
antioxidant properties of selenium.
The cDNA for rat selenoprotein P contains 10 TGA codons in the open reading frame
Department of Medicine, Vanderbilt University School of Medicine, Nashville, Tennessee 37232.
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