Apolipoprotein B mRNA editing enzyme catalytic polypeptide-like 3F (APOBEC3F)

Apolipoprotein B mRNA editing enzyme catalytic polypeptide-like 3F (APOBEC3F) is a zinc-dependent cytidine deaminase belonging to the APOBEC protein family, expressed mainly in hematopoietic cells. As an intrinsic antiviral restriction factor, APOBEC3F is packaged into retroviral particles during budding and acts during reverse transcription to deaminate cytosine residues to uracil on the negative strand of viral DNA, introducing G-to-A hypermutations that inactivate the virus, notably HIV-1[2][3][5]. This protein contains two cytidine deaminase (CDA) domains; only the C-terminal domain retains catalytic activity, while the N-terminal domain primarily mediates RNA binding[1][2]. APOBEC3F also restricts endogenous retroelements such as LINE-1 via deaminase-independent mechanisms. In the context of HIV-1 infection, the viral Vif protein counteracts APOBEC3F by targeting it for proteasomal degradation[5]. Dysregulation of APOBEC3F and related enzymes contributes to mutational burdens in cancer, underscoring its dual roles in immunity and genome stability[4].

Other names

DNA dC->dU-editing enzyme APOBEC-3FA3FARP8BK150C2.4.MRNAKA6Apolipoprotein B editing enzyme catalytic polypeptide-like 3FApolipoprotein B mRNA editing enzyme cytidine deaminaseInduced upon T-cell activation

Not applicable (no current clinical drugs specifically target APOBEC3F); hypothetical mechanisms would involve inhibition of its cytidine deaminase activity or enhancement of degradation by mimicking viral Vif action