The double-stranded RNA (dsRNA)-activated protein kinase (PKR), which is one of the products of interferon (IFN)-stimulated genes, participates in the biological actions of IFN such as antiviral effects and immune response. In the present study, we identified the primary structure of porcine PKR proteins by cDNA cloning. Porcine PKR protein consisted of 537 amino acids and had two dsRNA-binding domains similarly existing in PKR proteins of other species. The treatment with IFN-alpha induced the expression of PKR 3.9-fold in a porcine kidney cell line, LLC-PK1. The same results were obtained when the cells were treated with poly(I)-poly(C), but treatment with either IFN-gamma or LPS did not induce this gene in LLC-PK1 cells. These results suggest similarity of the regulatory mechanisms in the PKR gene among mammalian species.