| IED ID | IndEnz0002013102 |
| Enzyme Type ID | protease013102 |
| Protein Name |
Virion infectivity factor Vif SOR protein Cleaved into: p17; p7 |
| Gene Name | vif |
| Organism | Human immunodeficiency virus type 1 group M subtype B (isolate BRU/LAI) (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 BRU/LAI) (HIV-1) |
| Enzyme Sequence | MENRWQVMIVWQVDRMRIRTWKSLVKHHMYVSGKARGWFYRHHYESPHPRISSEVHIPLGDARLVITTYWGLHTGERDWHLGQGVSIEWRKKRYSTQVDPELADQLIHLYYFDCFSDSAIRKALLGHIVSPRCEYQAGHNKVGSLQYLALAALITPKKIKPPLPSVTKLTEDRWNKPQKTKGHRGSHTMNGH |
| Enzyme Length | 192 |
| Uniprot Accession Number | P69721 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Counteracts the innate antiviral activity of host APOBEC3F and APOBEC3G. Forms a complex with host APOBEC3F and APOBEC3G thus preventing the entry of these lethally hypermutating enzymes into progeny virions. Recruits an active E3 ubiquitin ligase complex composed of elongin BC, CUL5, and RBX2 to induce polyubiquitination of APOBEC3G and APOBEC3F. In turn, they are directed to the 26S proteasome for degradation. Vif interaction with APOBEC3G also blocks its cytidine deaminase activity in a proteasome-independent manner, suggesting a dual inhibitory mechanism. May interact directly with APOBEC3G mRNA in order to inhibit its translation. Seems to play a role in viral morphology by affecting the stability of the viral nucleoprotein core. Finally, Vif also contributes to the G2 cell cycle arrest observed in HIV infected cells. {ECO:0000255|HAMAP-Rule:MF_04081}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (3); Modified residue (5); Motif (2); Region (8); Site (1) |
| Keywords | AIDS;Host cell membrane;Host cytoplasm;Host membrane;Host-virus interaction;Membrane;Phosphoprotein;RNA-binding;Reference proteome;Ubl conjugation;Ubl conjugation pathway;Virion |
| Interact With | |
| Induction | INDUCTION: Expressed late during infection in a Rev-dependent manner. {ECO:0000255|HAMAP-Rule:MF_04081}. |
| Subcellular Location | SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04081}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04081}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_04081}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_04081}. Virion {ECO:0000255|HAMAP-Rule:MF_04081}. 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. {ECO:0000255|HAMAP-Rule:MF_04081}. |
| Modified Residue | MOD_RES 96; /note=Phosphothreonine; by host MAP4K1; /evidence=ECO:0000255|HAMAP-Rule:MF_04081; MOD_RES 144; /note=Phosphoserine; by host; /evidence=ECO:0000255|HAMAP-Rule:MF_04081; MOD_RES 155; /note=Phosphothreonine; by host; /evidence=ECO:0000255|HAMAP-Rule:MF_04081; MOD_RES 165; /note=Phosphoserine; by host MAP4K1; /evidence=ECO:0000255|HAMAP-Rule:MF_04081; MOD_RES 188; /note=Phosphothreonine; by host; /evidence=ECO:0000255|HAMAP-Rule:MF_04081 |
| Post Translational Modification | PTM: Processed in virion by the viral protease. {ECO:0000255|HAMAP-Rule:MF_04081}.; PTM: Highly phosphorylated on serine and threonine residues. {ECO:0000255|HAMAP-Rule:MF_04081}.; PTM: Polyubiquitinated and degraded by the proteasome in the presence of APOBEC3G. {ECO:0000255|HAMAP-Rule:MF_04081}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 12167863; 12368356; 12859895; 14557625; 14564014; 14672928; 14722068; 14747572; 15156567; 15367624; 15373943; 15383144; 15537645; 15574592; 15602725; 15611076; 15781449; 15989462; 16303161; 16460778; 16492778; 16501124; 16636053; 16731937; 17049578; 17067930; 17267497; 17272283; 17331040; 17522211; 17522216; 17598142; 17609216; 17660191; 17825339; 17898068; 17916373; 17977970; 18023836; 18082865; 18326044; 18366335; 18391217; 18414671; 18419775; 18499212; 18562529; 18596088; 18603011; 18619467; 18836454; 18842592; 19004939; 19036809; 19088851; 19105849; 19128510; 19297501; 19324886; 19357165; 19487726; 19535447; 19535450; 19588889; 19669862; 19826902; 19910370; 19939923; 19944180; 20147392; 20335268; 20463065; 20538015; 20592083; 20624919; 20686027; 20728451; 20809132; 20833716; 20971849; 21071676; 21149631; 21228271; 21270145; 21569376; 21571098; 21752914; 21763503; 21763507; 22013041; 22190036; 22190037; 22725134; 22767258; 22894923; 22970171; 23001005; 23080486; 23098073; 23175372; 23316055; 23417613; 23469063; 23576497; 23689841; 23707381; 23988114; 24146808; 24225024; 24390320; 24390335; 24402281; 24418540; 24422669; 24503066; 24522927; 25142588; 25275135; 25304135; 25411794; 25424878; 25490467; 25582776; 25590520; 25717111; 25855743; 25984970; 26105074; 26275799; 26537685; 26628363; 27297094; 27363431; 27758855; 27996044; 28131088; 28184007; 28336404; 28516844; 29263270; 29321323; 30851937; 31253590; 31257246; 31665623; 31792451; 31941780; 32292164; 32587092; 32847850; 32893454; 34425283; |
| Motif | MOTIF 108..139; /note=HCCH motif; /evidence=ECO:0000255|HAMAP-Rule:MF_04081; MOTIF 144..153; /note=BC-box-like motif; /evidence=ECO:0000255|HAMAP-Rule:MF_04081 |
| Gene Encoded By | |
| Mass | 22,513 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |