CFLAR
Domain
The caspase domain lacks the active site residues involved in catalysis.
Function
Apoptosis regulator protein which may function as a crucial link between cell survival and cell death pathways in mammalian cells. Acts as an inhibitor of TNFRSF6 mediated apoptosis. A proteolytic fragment (p43) is likely retained in the death-inducing signaling complex (DISC) thereby blocking further recruitment and processing of caspase-8 at the complex. Full length and shorter isoforms have been shown either to induce apoptosis or to reduce TNFRSF-triggered apoptosis. Lacks enzymatic (caspase) activity.
Post-translational modifications
Proteolytically processed by CASP8 generating subunit p43 and p12.
Sequence Similarities
Belongs to the peptidase C14A family.
Tissue Specificity
Widely expressed. Higher expression in skeletal muscle, pancreas, heart, kidney, placenta, and peripheral blood leukocytes. Also detected in diverse cell lines. Isoform 8 is predominantly expressed in testis and skeletal muscle.
Alternative names
CASH, CASP8AP1, CLARP, MRIT, CFLAR, CASP8 and FADD-like apoptosis regulator, Caspase homolog, Caspase-eight-related protein, Caspase-like apoptosis regulatory protein, Cellular FLICE-like inhibitory protein, FADD-like antiapoptotic molecule 1, Inhibitor of FLICE, MACH-related inducer of toxicity, Usurpin, Casper, c-FLIP, FLAME-1, I-FLICE