Counteracts the innate antiviral activity of APOBEC3G. Forms a complex with host APOBEC3G thus preventing the entry of this lethally hypermutating enzyme into progeny virions. Functions as an adapter molecule, recruiting APOBEC3G to the ubiquitin-proteasome machinery. Targets APOBEC3G for degradation through the assembly with elongin BC complex, CUL5 and RBX1. Binds viral RNA and affects the stability of viral nucleoprotein core. May play a role in viral morphology (By similarity). Homomultimer; in vitro and presumably in vivo. Interacts with viral Pr55Gag precursor and host APOBEC3G. The interaction between Vif and APOBEC3G is species-specific, which may play a role in restricting the replication of SIV to their host. Forms an E3 ligase complex by interacting with host CUL5 and elongin BC complex (ELOB and ELOC) (By similarity). Seems to colocalize with intermediate filament vimentin. A fraction is associated with the cytoplasmic side of cellular membranes, presumably via the interaction with Pr55Gag precursor (By similarity). Expressed late during infection in a Rev-dependent manner. The BC-like-box motif mediates the interaction with elongin BC complex. The HCCH motif (H-x(5)-C-x(18)-C-x(5)-H) mediates the interaction with CUL5. Processed in virion by the viral protease. Highly phosphorylated on serine and threonine residues. Polyubiquitinated and degraded by the proteasome in the presence of APOBEC3G. Vif-defective viruses show catastrophic failure in reverse transcription due to APOBEC-induced mutations that initiate a DNA base repair pathway and compromise the structural integrity of the ssDNA. In the absence of Vif, the virion is morphologically abnormal. The 155 isolate is from a monkey imported from Kenya. Belongs to the primate lentivirus group Vif protein family.