F6LXF0 · F6LXF0_9HIV1
- ProteinVirion infectivity factor
- Genevif
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids192 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score4/5
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.
Miscellaneous
HIV-1 lineages are divided in three main groups, M (for Major), O (for Outlier), and N (for New, or Non-M, Non-O). The vast majority of strains found worldwide belong to the group M. Group O seems to be endemic to and largely confined to Cameroon and neighboring countries in West Central Africa, where these viruses represent a small minority of HIV-1 strains. The group N is represented by a limited number of isolates from Cameroonian persons. The group M is further subdivided in 9 clades or subtypes (A to D, F to H, J and K).
Required for replication in 'nonpermissive' cells, including primary T-cells, macrophages and certain T-cell lines, but is dispensable for replication in 'permissive' cell lines, such as 293T cells. In nonpermissive cells, Vif-defective viruses can produce virions, but they fail to complete reverse transcription and cannot successfully infect new cells.
Vif-defective viruses show catastrophic failure in reverse transcription due to APOBEC-induced mutations that initiate a DNA base repair pathway and compromise the structural integrity of the ssDNA. In the absence of Vif, the virion is morphologically abnormal.
Features
Showing features for site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 150-151 | Cleavage in virion (by viral protease) | ||||
Sequence: LT |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | host cell cytoplasm | |
Cellular Component | host cell plasma membrane | |
Cellular Component | plasma membrane | |
Cellular Component | virion component | |
Molecular Function | RNA binding | |
Biological Process | viral life cycle |
Keywords
- Molecular function
- Biological process
Names & Taxonomy
Protein names
- Recommended nameVirion infectivity factor
- Short namesVif
- Alternative names
- Cleaved into 2 chains
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageViruses > Riboviria > Pararnavirae > Artverviricota > Revtraviricetes > Ortervirales > Retroviridae > Orthoretrovirinae > Lentivirus
- Virus hosts
Accessions
- Primary accessionF6LXF0
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Peripheral membrane protein
Host cell membrane ; Peripheral membrane protein
Membrane ; Peripheral membrane protein
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.
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_5023410929 | 1-150 | p17 | |||
Sequence: MENRWQVMIVWQVDRMRIRTWKSLVKHHMYISKKAKGWFYRHHYESTHPRISSEVHIPLGEAGLAVTTYWGLHTGERDWHLGQGVSIEWRQGRYRTQIDPGLADQLIHIYYFDCFSESAIRKAILGHKISPRCNYQAGHNKVGSLQYLAL | ||||||
Chain | PRO_5023410930 | 1-192 | Virion infectivity factor | |||
Sequence: MENRWQVMIVWQVDRMRIRTWKSLVKHHMYISKKAKGWFYRHHYESTHPRISSEVHIPLGEAGLAVTTYWGLHTGERDWHLGQGVSIEWRQGRYRTQIDPGLADQLIHIYYFDCFSESAIRKAILGHKISPRCNYQAGHNKVGSLQYLALTALVAPKKTKPPLPSVKKLVEDRWNKPQETRGHRGSHTMNGH | ||||||
Modified residue | 96 | Phosphothreonine; by host MAP4K1 | ||||
Sequence: T | ||||||
Modified residue | 144 | Phosphoserine; by host | ||||
Sequence: S | ||||||
Chain | PRO_5023410928 | 151-192 | p7 | |||
Sequence: TALVAPKKTKPPLPSVKKLVEDRWNKPQETRGHRGSHTMNGH | ||||||
Modified residue | 165 | Phosphoserine; by host MAP4K1 | ||||
Sequence: S | ||||||
Modified residue | 188 | Phosphothreonine; by host | ||||
Sequence: T |
Post-translational modification
Highly phosphorylated on serine and threonine residues.
Polyubiquitinated and degraded by the proteasome in the presence of APOBEC3G.
Processed in virion by the viral protease.
Keywords
- PTM
Expression
Induction
Expressed late during infection in a Rev-dependent manner.
Interaction
Subunit
Homomultimer; in vitro and presumably in vivo. Interacts with viral RNA and Pr55Gag precursor; these interactions mediate Vif incorporation into the virion. Interacts with the viral reverse transcriptase. Interacts with human APOBEC3F and APOBEC3G. Interacts with host UBCE7IP1 isoform 3/ZIN and possibly with SAT. Interacts with host tyrosine kinases HCK and FYN; these interactions may decrease level of phosphorylated APOBEC3G incorporation into virions. Interacts with host ABCE1; this interaction may play a role in protecting viral RNA from damage during viral assembly. Forms an E3 ligase complex by interacting with host CUL5 and elongin BC complex (ELOB and ELOC). Interacts with host MDM2; this interaction targets Vif for degradation by the proteasome.
Structure
Family & Domains
Features
Showing features for region, motif, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 14-17 | Interaction with host APOBEC3F; F1-box | ||||
Sequence: DRMR | ||||||
Region | 40-44 | Interaction with host APOBEC3G; G-box | ||||
Sequence: YRHHY | ||||||
Region | 54-72 | Interaction with host APOBEC3F and APOBEC3G; FG-box | ||||
Sequence: EVHIPLGEAGLAVTTYWGL | ||||||
Region | 74-79 | Interaction with host APOBEC3F; F2-box | ||||
Sequence: TGERDW | ||||||
Region | 75-114 | RNA-binding | ||||
Sequence: GERDWHLGQGVSIEWRQGRYRTQIDPGLADQLIHIYYFDC | ||||||
Motif | 108-139 | HCCH motif | ||||
Sequence: HIYYFDCFSESAIRKAILGHKISPRCNYQAGH | ||||||
Motif | 144-153 | BC-box-like motif | ||||
Sequence: SLQYLALTAL | ||||||
Region | 151-164 | Multimerization | ||||
Sequence: TALVAPKKTKPPLP | ||||||
Region | 171-172 | Membrane association | ||||
Sequence: ED | ||||||
Compositional bias | 171-186 | Basic and acidic residues | ||||
Sequence: EDRWNKPQETRGHRGS | ||||||
Region | 171-192 | Disordered | ||||
Sequence: EDRWNKPQETRGHRGSHTMNGH |
Domain
The BC-like-box motif mediates the interaction with elongin BC complex.
The HCCH motif (H-x5-C-x18-C-x5-H) mediates the interaction with CUL5.
Sequence similarities
Belongs to the primate lentivirus group Vif protein family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length192
- Mass (Da)22,443
- Last updated2011-07-27 v1
- Checksum9F174585D9ED3197
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 171-186 | Basic and acidic residues | ||||
Sequence: EDRWNKPQETRGHRGS |