Cloning and sequencing of the cDNA encoding a human testis phospholipid hydroperoxide glutathione peroxidase.
A human cDNA that encodes a polypeptide that has 94% deduced amino-acid sequence identity to porcine phospholipid hydroperoxide glutathione peroxidase was cloned from a testis library. The sequence shows preservation of the UGA selenocysteine codon, putative active-site Trp and Glu residues and a Tyr residue that is phosphorylated in the porcine protein. The 3'-UTR shows some conservation of sequences implicated in the insertion of selenocysteine at an opal codon in human glutathione peroxidase-1.
Esworthy
R S
RS
Department of Medical Oncology, City of Hope National Medical Center, Duarte, CA 9101.
Doan
K
K
Doroshow
J H
JH
Chu
F F
FF
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D001665:Binding Sites; D003001:Cloning, Molecular; D018076:DNA, Complementary; D005979:Glutathione Peroxidase / Q000235:genetics* / Q000378:metabolism; D006801:Humans; D008297:Male; D008969:Molecular Sequence Data; D000080662:Phospholipid Hydroperoxide Glutathione Peroxidase; D010766:Phosphorylation; D013737:Testis / Q000201:enzymology*
D018076:DNA, Complementary; D000080662:Phospholipid Hydroperoxide Glutathione Peroxidase; D005979:Glutathione Peroxidase