
Mammalian ADARs. All ADARs are characterized by a C-terminal catalytic domain. In ADAR3, the deaminase domain is inactive. dsRBDs are required for recognizing double-stranded substrate RNA. ADAR1 has a nuclear localization signal (NLS) flanking its third dsRBD, and ADAR1p150 has an N-terminal nuclear export signal. Consequently, ADAR1 is manly cytoplasmic, while all other ADARs are primarily nuclear. A Zα domain can bind RNAs in Z-conformation in ADAR1p150, while the Zβ domain found in ADAR1p150 and p110 is degenerate.










