v5.1.0.3
Glycine data from LIS
Type | Domain |
Description | Ribonuclease L (RNase L) is a highly regulated, latent endoribonuclease (thus the 'L' in RNase L) and is widely expressed in most mammalian tissues. It is involved in the mediation of the antiviral and pro-apoptotic activities of the interferon-inducible 2-5A system, which blocks infections by certain types of viruses through cleavage of viral and cellular single-stranded RNA [ , ]. RNase L is unique in that it is composed of three major domains; N terminus regulatory ankyrin repeat domain (ARD), followed by a linker, a protein kinase (PK)-like domain and a C-terminal ribonuclease (RNase) domain. The RNase domain has homology with IRE1, also containing both a kinase and an endoribonuclease, that functions in the unfolded protein response (UPR) []. RNase L has been shown to have an impact on the pathogenesis of prostate cancer; the RNase L gene, RNASEL, has been identified as a strong candidate for the hereditary prostate cancer 1 (HPC1) allele [, , ]. The broad range of biological functions of RNase offers a possibility for RNase L as a therapeutic target.This entry represents the RNase domain of RNase L. |
Short Name | RNase-L_RNase |