Peptidylprolyl Isomerase Like Protein 2 (PPIL2)

PPIL2 is a member of the cyclophilin family of peptidylprolyl isomerases. The cyclophilins are a highly conserved ubiquitous family, members of which play an important role in protein folding, immunosuppression by cyclosporin A, and infection of HIV-1 virions. This protein interacts with the proteinase inhibitor eglin c and is localized in the nucleus. Multiple transcript variants encoding different isoforms have been found for this gene.

The protein has a calculated molecular mass of about 60 kD. PPIL2 contains sequences characteristic of the cyclophilin family, but it lacks several highly conserved residues. It has a unique 288-amino acid N terminus and a unique 109-amino acid C terminus. Northern blot analysis detected ubiquitous expression of 3.0- and 4.4-kb transcripts.