Peptidyl-prolyl cis-trans isomerase-like 3 (PPIL3)

Peptidyl-prolyl cis-trans isomerase-like 3 (PPIL3) is a member of the cyclophilin family of peptidyl-prolyl isomerases, enzymes that catalyze the cis-trans isomerization of proline imide bonds in peptides and proteins[1][3][4]. This protein can function both as a catalyst for protein folding and as a molecular chaperone. PPIL3 directly interacts with the viral protein Apoptin in tumor cells, regulating Apoptin's cytoplasmic localization and, thereby, its apoptosis-inducing function in cancer cells[1]. Like other cyclophilins, PPIL3 may also play roles in pre-mRNA splicing, and its gene is alternatively spliced to produce different isoforms. Cyclophilin J (CYPJ), a synonym for PPIL3, is upregulated in certain cancers and has been proposed as a biomarker and potential therapeutic target[1][2]. The protein binds the immunosuppressant cyclosporine, though the physiological and clinical relevance of this interaction for PPIL3 specifically is not fully established[2].

Other names

Cyclophilin JCyPJCYPJPPIaseRotamase PPIL3Peptidylprolyl cis-trans isomerase-like protein 3Cyclophilin-like protein PPIL3Cyclophilin-like protein 3PPIase-like protein 3

Inhibition of isomerase activity (cyclosporine and derivatives)