| IED ID | IndEnz0002013368 |
| Enzyme Type ID | protease013368 |
| Protein Name |
Virion infectivity factor Vif Q protein SOR protein |
| Gene Name | vif |
| Organism | Simian immunodeficiency virus (isolate GB1) (SIV-mnd) (Simian immunodeficiency virus mandrill) |
| Taxonomic Lineage | Viruses Riboviria Pararnavirae Artverviricota Revtraviricetes Ortervirales Retroviridae Orthoretrovirinae Lentivirus Simian immunodeficiency virus (SIV) Simian immunodeficiency virus - mnd Simian immunodeficiency virus (isolate GB1) (SIV-mnd) (Simian immunodeficiency virus mandrill) |
| Enzyme Sequence | MERVERIVRLTWKVSSQRIEKWHWLVRRQMAWATANNEEGCWWLYPHFMAYNEWYTCSKVVIIINRDIRLIVRSYWHLQIEVGCLSTYAVSIEAVVRPPPFEKEWCTEITPEVADHLIHLHFYDCFMDSAVMKAIRGEEVLKVCRFPAGHKAQGVLSLQFLCLRVIYGPEER |
| Enzyme Length | 172 |
| Uniprot Accession Number | P22383 |
| 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) |
| Keywords | 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=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 107; /note=Phosphothreonine; by host; /evidence=ECO:0000250; MOD_RES 157; /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 119..150; /note=HCCH motif; /evidence=ECO:0000250; MOTIF 157..166; /note=BC-box-like motif; /evidence=ECO:0000250 |
| Gene Encoded By | |
| Mass | 20,499 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |