Detail Information for IndEnz0002013101
IED ID IndEnz0002013101
Enzyme Type ID protease013101
Protein Name Virion infectivity factor
Vif
Q protein
SOR protein
Gene Name vif
Organism Human immunodeficiency virus type 2 subtype A (isolate ST) (HIV-2)
Taxonomic Lineage Viruses Riboviria Pararnavirae Artverviricota Revtraviricetes Ortervirales Retroviridae Orthoretrovirinae Lentivirus Human immunodeficiency virus 2 HIV-2 subtype A Human immunodeficiency virus type 2 subtype A (isolate ST) (HIV-2)
Enzyme Sequence MEEGKRWIAVPTWRVPGRMERWHSLIKYLKYRTGDLEKVCYVPHHKVGWAWWTCSRVIFPLKGESHLEIQAYWNLTPEKGWLSSYSVRLTWYTEKFWTDVTPDCADSLIHSTYFSCFTAGEVRRAIRGEKLLSCCNYPQAHKYQVPSLQFLALVVVQQNGRPQRDNTTRKQWRRNYRRGLRVARQDGRSHKQRGSEPPAPRAYFPGVAKVLEILA
Enzyme Length 215
Uniprot Accession Number P20878
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number
Enzyme Function FUNCTION: 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). {ECO:0000250}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Chain (1); Modified residue (2); Motif (2); Region (1)
Keywords AIDS;Host cell membrane;Host cytoplasm;Host membrane;Host-virus interaction;Membrane;Phosphoprotein;Ubl conjugation;Ubl conjugation pathway;Virion
Interact With
Induction INDUCTION: Expressed late during infection in a Rev-dependent manner.
Subcellular Location SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000250}. Host cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Virion {ECO:0000250}. Note=In the cytoplasm, 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). {ECO:0000250}.
Modified Residue MOD_RES 98; /note=Phosphothreonine; by host MAP4K1; /evidence=ECO:0000250; MOD_RES 147; /note=Phosphoserine; by host; /evidence=ECO:0000250
Post Translational Modification PTM: Processed in virion by the viral protease. {ECO:0000250}.; PTM: Highly phosphorylated on serine and threonine residues. {ECO:0000250}.; PTM: Polyubiquitinated and degraded by the proteasome in the presence of APOBEC3G. {ECO:0000250}.
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif MOTIF 110..141; /note=HCCH motif; /evidence=ECO:0000250; MOTIF 147..156; /note=BC-box-like motif; /evidence=ECO:0000250
Gene Encoded By
Mass 25,355
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda