Peflin, a novel member of the five-EF-hand-protein family, is similar to the apoptosis-linked gene 2 (ALG-2) protein but possesses nonapeptide repeats in the N-terminal hydrophobic region.

The calpain small subunits of sorcin, grancalcin, and ALG-2 constitute a family of the Ca(2+)-binding proteins with five EF-hand-like motifs (penta-EF-hand domain or PEF domain) in their C-terminal regions and hydrophobic domains with variable lengths in their N-terminal regions. Searching the human DNA data base of expressed sequence tags (EST) revealed novel partial sequences similar to, but distinct from, the sequences of the previously known PEF proteins. We isolated a cDNA clone of near full length by 5'- and 3'-RACE (rapid amplification of cDNA end) methods and compared the predicted amino acid sequence (284 residues) of the novel EF-hand protein, named peflin, with those of known PEF proteins. The PEF domain of peflin is most similar to ALG-2 (40.9% identity) among the family, particularly in EF-1 (46.2%) and EF-3 (57.1%) regions. Peflin has a longer N-terminal hydrophobic domain than any other member of the family, and it contains nine nonapeptide (A/PPGGPYGGP) repeats. Western blot analysis demonstrated that peflin (30 kDa) was expressed in various nonadherent and adherent cultured human cell lines, including Jurkat, HL60, HeLa, and HT1080. Peflin may play basic roles in Ca(2+) signaling irrespective of cell types. Copyright 1999 Academic Press.