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 |