Antiviral protein which inhibits the replication of viruses by recruiting the cellular RNA degradation machineries to degrade the viral mRNAs. Binds to a ZAP-responsive element (ZRE) present in the target viral mRNA, recruits cellular poly(A)-specific ribonuclease PARN to remove the poly(A) tail, and the 3'-5' exoribonuclease complex exosome to degrade the RNA body from the 3'-end. It also recruits the decapping complex DCP1-DCP2 through RNA helicase p72 (DDX17) to remove the cap structure of the viral mRNA to initiate its degradation from the 5'-end. Its target viruses belong to families which include retroviridae: human immunodeficiency virus type 1 (HIV-1) and moloney and murine leukemia virus (MoMLV), filoviridae: ebola virus (EBOV) and marburg virus (MARV), togaviridae: sindbis virus (SINV) and Ross river virus (RRV). Specifically targets the multiply spliced but not unspliced or singly spliced HIV-1 mRNAs for degradation. Homodimer or homooligomer. Homooligomerization is essential for its antiviral activity. Interacts with EXOSC5. Interacts with EXOSC3, EXOSC7, DCP2 and DCP1A (By similarity). Interacts with PARN in an RNA-independent manner (By similarity). Interacts with XRN1 in an RNA-dependent manner (By similarity). Interacts (via N-terminal domain) with DHX30 (via N-terminus) in an RNA-independent manner. Interacts (via N-terminal domain) with DDX17 in an RNA-independent manner. Localizes in the cytoplasm at steady state, but shuttles between nucleus and cytoplasm in a XPO1-dependent manner. Expressed in the kidney and liver. By type I interferon (IFN) and viruses. The N-terminal domain is sufficient to bind to viral RNAs and promote their degradation. The second and fourth zinc fingers are involved in binding to specific viral RNAs. Contains a divergent PARP homology ADP-ribosyltransferase domain which lacks the structural requirements for NAD[+] binding. It is therefore inactive. Phosphorylation at Ser-274 is essential for sequential phosphorylation of Ser-270, Ser-266, Ser-262 and Ser-257 by GSK3-beta. Phosphorylation by GSK3-beta enhances its antiviral activity. Belongs to the ARTD/PARP family.