At least two different types of proteins, NF-kappa B/KBF1 and HIV-EP1/PRDII-BF1/MBP-1, which are members of a family of rel oncoproteins and metal-finger proteins, respectively, bind to the human immunodeficiency virus type (HIV-1) enhancer. As a new member of a HIV-EP1 family that is expressed at a high level in T cells, we have isolated cDNA clones of HIV-EP2 by cross-hybridization with HIV-EP1 cDNA. HIV-EP2 protein consists of 1,833 amino acids and has a molecular weight of 211,000. HIV-EP2 protein is highly homologous with HIV-EP1/PRDII-BF1/MBP-1 in three regions. These three regions contain the potential nuclear localization signal followed by a Ser/Thr-rich region, the DNA-binding domain consisting of a metal-finger structure, and a cluster of acidic amino acids. The DNA-binding property of HIV-EP2 was similar to that of HIV-EP1. Northern blot analysis of HIV-EP2 mRNA indicated relatively high expression in the T cell line Molt-4 and in some tumor cell lines. Furthermore, like HIV-EP1, expression of HIV-EP2 mRNA was greatly induced by mitogen and phorbol ester treatment of Jurkat T cells, suggesting that HIV-EP2 acts in HIV production from latently infected T cells.