| IED ID | IndEnz0002013332 |
| Enzyme Type ID | protease013332 |
| Protein Name |
Virion infectivity factor Vif SOR protein Cleaved into: p17; p7 Fragment |
| Gene Name | vif |
| Organism | Human immunodeficiency virus type 1 group M subtype B (isolate SC) (HIV-1) |
| Taxonomic Lineage | Viruses Riboviria Pararnavirae Artverviricota Revtraviricetes Ortervirales Retroviridae Orthoretrovirinae Lentivirus Human immunodeficiency virus 1 HIV-1 unknown group Human immunodeficiency virus type 1 group M subtype B (isolate SC) (HIV-1) |
| Enzyme Sequence | GVSIEWTKKRYSTQVDPDLADRLIHLYYFDCFSESAIRNAILGALVSGRCEYQAGHNKVGSLQYLALTALITPKKTKPPLPSVRKLTEDRWNKPQKTKGHRGSHTMNGH |
| Enzyme Length | 109 |
| Uniprot Accession Number | P05899 |
| 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. Interacts with host ABCE1, which seems to be involved in lentiviruses capsid formation and displays RNase L inhibitor activity. This interaction may play a role in protecting viral RNA from damage during viral assembly. May interact with host SAT, which is a regulator of polyamine cell level. This interaction may be relevant since polyamines affect viral RNA properties (By similarity). {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (3); Compositional bias (1); Modified residue (4); Motif (2); Non-terminal residue (1); Region (4); Site (1) |
| Keywords | AIDS;Host cell membrane;Host cytoplasm;Host membrane;Host-virus interaction;Membrane;Phosphoprotein;RNA-binding;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. Incorporated in virions at a ratio of approximately 7 to 20 molecules per virion (By similarity). {ECO:0000250}. |
| Modified Residue | MOD_RES 13; /note=Phosphothreonine; by host MAP4K1; /evidence=ECO:0000250; MOD_RES 61; /note=Phosphoserine; by host; /evidence=ECO:0000250; MOD_RES 82; /note=Phosphoserine; by host MAP4K1; /evidence=ECO:0000250; MOD_RES 105; /note=Phosphothreonine; 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. Thr-13 and Ser-82 are phosphorylated by the mitogen activated kinase MAP4K1. As the HIV-1 replication can be activated by stress and mitogens, these phosphorylations could be involved in this process. Ser-61 phosphorylation may inhibit elongin BC complex binding (By similarity). {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 25..56; /note=HCCH motif; /evidence=ECO:0000250; MOTIF 61..70; /note=BC-box-like motif; /evidence=ECO:0000250 |
| Gene Encoded By | |
| Mass | 12,308 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |