FKBP8 of 412 aas and   TMSs. It is a constitutively inactive PPiase, which becomes active when bound to calmodulin and calcium. It seems to act as a chaperone for BCL2, targets it to the mitochondria and modulates its phosphorylation state. The BCL2/FKBP8/calmodulin/calcium complex probably interferes with the binding of BCL2 to its targets. The active form of FKBP8 may therefore play a role in the regulation of apoptosis. It may be involved in the inhibition of viral infection by influenza A viruses (IAV) (Wang et al. 2017).