Phosphatidylethanolamine Binding Protein 4 (PEBP4)

The phosphatidylethanolamine (PE)-binding proteins, including PEBP4, are an evolutionarily conserved family of proteins with pivotal biologic functions, such as lipid binding and inhibition of serine proteases. The deduced 227-amino acid protein has a calculated molecular mass of 25.7 kD and shares 45% identity with a putative murine homolog. PEBP4 contains a predicted PE-binding domain with a conserved asp-pro-asp-xaa-pro motif forming the predicted binding pocket. RT-PCR analysis detected PEBP4 expression in a variety of tumor cells and normal tissues. Northern blot analysis of human tissues detected a 1.2-kb transcript with high expression in testis, heart, skeletal muscle, and thyroid with weak expression in lung, liver, spinal cord, brain, adrenal gland, and bone marrow. Fluorescence confocal microscopy localized PEBP4 to lysosomes.