Endoribonuclease that specifically cleaves inosine-containing RNAs: cleaves RNA at the second phosphodiester bond 3' to inosine. Active against both single-stranded and double-stranded RNAs. Has strong preference for single-stranded RNAs (ssRNAs) toward double-stranded RNAs (dsRNAs). Cleaves mRNAs and tRNAs containing inosine. Also able to cleave structure-specific dsRNA substrates containing the specific sites 5'-IIUI-3' and 5'-UIUU-3'. Inosine is present in a number of RNAs following editing; the function of inosine-specific endoribonuclease is still unclear: it could either play a regulatory role in edited RNAs, or be involved in antiviral response by removing the hyperedited long viral dsRNA genome that has undergone A-to-I editing. Binds branched DNA structures. Monomer. Interacts with PABPC1; the interaction is RNA-dependent and stimulates ENDOV activity. Relocalizes to cytoplasmic stress granules upon cellular stress where it colocalizes with PABPC1. Highest levels detected in liver with high levels also found in heart, kidney and testis. Expressed at low levels in brain. Was initially characterized as an endodeoxyribonuclease involved in DNA repair (PubMed:12853604). While it shows some weak endodeoxyribonuclease activity in vitro, such activity probably does not exist in vivo. Belongs to the endonuclease V family. Probable cloning artifact.