Zinc finger CCCH-type antiviral protein 1 (ZC3HAV1)

Zinc finger CCCH-type antiviral protein 1 (ZC3HAV1), also known as zinc finger antiviral protein (ZAP) and PARP13, is an interferon-inducible RNA-binding protein that restricts the replication of a broad range of RNA and DNA viruses by binding specific viral RNAs and directing their degradation[1][2][3][4]. ZC3HAV1 contains four N-terminal CCCH-type zinc finger motifs that directly recognize target viral RNAs—often sequences rich in CpG dinucleotides—and recruits cellular degradation machinery, including exoribonuclease complexes, decapping complexes, and cofactors[1][2][3]. Alternative splicing produces at least two main isoforms: ZAP-S (short) and ZAP-L (long), the latter containing a C-terminal PARP-like domain (which is enzymatically inactive)[2][3]. ZC3HAV1 is upregulated in response to interferon signaling during viral infection and enhances interferon and pro-inflammatory cytokine production, contributing to innate immune responses[1][2][3]. While essential for viral restriction and immune modulation, ZC3HAV1 is not currently a direct therapeutic target of any approved drugs, nor is it established as a clinical biomarker. Viruses can evolve to evade ZC3HAV1 by lowering CpG content or, in some cases, expressing antagonistic proteins[2][3].

Other names

Zinc finger antiviral proteinZAPPARP13ARTD13Zinc finger CCCH domain-containing protein 2Zinc finger CCCH-type containing, antiviral 1ZC3HDC2PRO1677ZC3H2FLB6421FLJ13288MGC48898ADP-ribosyltransferase diphtheria toxin-like 13Inactive poly [ADP-ribose] polymerase 13

viral mRNA recognition and degradation