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The Apoliprotein B mRNA-editing, enzyme-catalytic, polypeptide-like (APOBEC) 3 is a multi-isoform member of the cytidine deaminase family of enzymes that act on monomeric nucleoside and nucleotide substrates. Similar to TRIM5-a which targets incoming retroviral capsids, APOBEC3 plays a major role in cellular defense against retroviral infection as at least two isoforms, APOBEC3G and to a lesser extent APOBEC3F, can be incorporated HIV-1 virions and induce hypermutation in the newly synthesized viral DNA and thus destabilize the viral genome. This innate mechanism of retroviral resistance is counteracted by the HIV-1 Vif protein by inducing the ubiquitization and degradation of APOBEC3G; a single amino acid substitution (D128K) blocks APOBEC3G depletion without affecting its inhibitory activity.
A3G; APOBEC3G; APOBEC-related cytidine deaminase; APOBEC-related protein; APOBEC-related protein 9; apolipoprotein B editing enzyme catalytic polypeptide-like 3G; apolipoprotein B mRNA editing enzyme catalytic polypeptide like 3G; apolipoprotein B mRNA editing enzyme catalytic subunit 3G; apolipoprotein B mRNA editing enzyme cytidine deaminase; apolipoprotein B mRNA editing enzyme, catalytic polypeptide-like 3G; apolipoprotein B mRNA-editing enzyme catalytic polypeptide 3G; ARCD; ARP9; ARP-9; ASGPR2; ASGP-R2; bK150C2.7; CEM15; CEM-15; CLEC4H2; Deoxycytidine deaminase; dJ494G10.1; DNA dC->dU editing enzyme; DNA dC->dU-editing enzyme APOBEC-3G; FLJ12740; HBXBP; HL-2; MDS019; OTTHUMP00000028911; phorbolin-like protein MDS019
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