PIBF is synthesized during pregnancy in response to progesterone by progesterone receptor-positive T lymphocytes (mostly gamma-delta T cells). In the presence of PIBF, natural killer (NK) cells inhibit the release of perforin from storage granules and therefore fail to lyse target cells. In humans, the amount of cells that express PIBF is significantly higher in healthy pregnant women than in women at risk for premature pregnancy termination. Full-length PIBF is associated with the nucleus, whereas secretion of shorter forms is induced by activation of the cell. Research suggests that PIBF functions as a transcription factor in its full-length form, while smaller forms may act as cytokines. The PIBF gene encodes a deduced hydrophilic 757-amino acid alpha-helical protein with an N-terminal signal sequence, a leucine zipper motif, a basic zipper sequence, a PEST sequence, a nuclear localization signal, an endoplasmic reticulum membrane retention signal, and many presumeed N-glycosylation and phosphorylation sites.