IFP 35 is an interferon-induced leucine zipper protein that undergoes interferon-regulated cellular redistribution.

We have isolated a new human cDNA, named IFP 35, whose expression is regulated by interferons (IFN). Induction of IFP 35 mRNA in HeLa cells by IFN is due, at least in part, to increased transcription. In response to IFN treatment, the expression of IFP 35 mRNA is seen in a wide range of different cell types, including fibroblasts, macrophages, and epithelial cells. The cDNA sequence encodes a 282-amino acid protein with a deduced molecular mass of 31,130 Da. In vitro translation of mRNA obtained by both in vitro transcription and hybrid selection resulted in the synthesis of a 35-kDa protein. Antisera raised against IFP 35 recognized a protein with an apparent molecular mass of 35 kDa in HeLa cells. Amino acid sequence analysis revealed a leucine zipper motif in an alpha-helical configuration at the extreme amino terminus of IFP 35. Notable IFP 35 is a unique novel leucine zipper protein in that it lacks a basic domain critical for DNA binding. IFP 35 can specifically form homodimers in vitro. Western blot analysis of fractionated cell extracts indicates increased nuclear localization following IFN treatment.