P69722 (VIF_HV112) Reviewed, UniProtKB/Swiss-Prot
Last modified October 16, 2013. Version 59. History...
Names and origin
|Protein names||Recommended name:|
Virion infectivity factor
|Organism||Human immunodeficiency virus type 1 group M subtype B (isolate PCV12) (HIV-1)|
|Taxonomic identifier||11679 [NCBI]|
|Taxonomic lineage||Viruses › Retro-transcribing viruses › Retroviridae › Orthoretrovirinae › Lentivirus › Primate lentivirus group ›|
|Virus host||Homo sapiens (Human) [TaxID: 9606]|
|Sequence length||192 AA.|
|Sequence processing||The displayed sequence is further processed into a mature form.|
|Protein existence||Evidence at transcript level|
General annotation (Comments)
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.
Homomultimer; in vitro and presumably in vivo. Interacts with viral Pr55Gag precursor, human APOBEC3G, UBCE7IP1 isoform 3/ZIN, ABCE1 and possibly with SAT. Binds human HCK in vitro, but since this protein does not seem to be expressed in CD4+ cells, the significance of this interaction remains unclear. The interaction between Vif and APOBEC3G is species-specific, which may play a role in restricting the replication of HIV to humans. Forms an E3 ligase complex by interacting with human CUL5 and elongin BC complex (TCEB1 and TCEB2) By similarity.
Host cytoplasm By similarity. Host cell membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Virion By similarity. 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.
Expressed late during infection in a Rev-dependent manner.
The BC-like-box motif mediates the interaction with elongin BC complex By similarity.
The HCCH motif (H-x(5)-C-x(18)-C-x(5)-H) mediates the interaction with CUL5 By similarity.
Processed in virion by the viral protease By similarity.
Highly phosphorylated on serines and threonines residues. Thr-96 and Ser-165 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-144 phosphorylation may inhibit elongin BC complex binding By similarity.
Polyubiquitinated and degraded by the proteasome in the presence of APOBEC3G By similarity.
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.
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).
Belongs to the primate lentivirus group Vif protein family.
|Biological process||Host-virus interaction|
Ubl conjugation pathway
|Cellular component||Host cell membrane|
|Gene Ontology (GO)|
|Biological_process||modulation by virus of host morphology or physiology|
Inferred from electronic annotation. Source: UniProtKB-KWviral infectious cycle
Inferred from electronic annotation. Source: InterPro
|Cellular_component||host cell cytoplasm|
Inferred from electronic annotation. Source: UniProtKB-SubCellhost cell plasma membrane
Inferred from electronic annotation. Source: UniProtKB-SubCellmembrane
Inferred from electronic annotation. Source: UniProtKB-KWvirion
Inferred from electronic annotation. Source: UniProtKB-SubCell
Inferred from electronic annotation. Source: UniProtKB-KW
|Complete GO annotation...|
Sequence annotation (Features)
|Feature key||Position(s)||Length||Description||Graphical view||Feature identifier|
|Chain||1 – 192||192||Virion infectivity factor By similarity||PRO_0000043023|
|Chain||1 – 150||150||p17 By similarity||PRO_0000043024|
|Chain||151 – 192||42||p7 By similarity||PRO_0000043025|
|Region||14 – 17||4||Interaction with host APOBEC3F; F1-box By similarity|
|Region||40 – 44||5||Interaction with host APOBEC3G; G-box By similarity|
|Region||54 – 72||19||Interaction with host APOBEC3F and APOBEC3G; FG-box By similarity|
|Region||74 – 79||6||Interaction with host APOBEC3F; F2-box By similarity|
|Region||75 – 114||40||RNA-binding Potential|
|Region||151 – 164||14||Multimerization By similarity|
|Region||171 – 172||2||Membrane association By similarity|
|Motif||108 – 139||32||HCCH motif By similarity|
|Motif||144 – 153||10||BC-box-like motif|
|Site||150 – 151||2||Cleavage in virion (by viral protease) By similarity|
Amino acid modifications
|Modified residue||96||1||Phosphothreonine; by host MAP4K1 By similarity|
|Modified residue||144||1||Phosphoserine; by host By similarity|
|Modified residue||165||1||Phosphoserine; by host MAP4K1 By similarity|
|Modified residue||188||1||Phosphothreonine; by host By similarity|
|||"Three novel genes of human T-lymphotropic virus type III: immune reactivity of their products with sera from acquired immune deficiency syndrome patients."|
Arya S.K., Gallo R.C.
Proc. Natl. Acad. Sci. U.S.A. 83:2209-2213(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
|||"The viral infectivity factor (Vif) of HIV-1 unveiled."|
Rose K.M., Marin M., Kozak S.L., Kabat D.
Trends Mol. Med. 10:291-297(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
|+||Additional computationally mapped references.|
|M11840 Genomic RNA. Translation: AAA44997.1.|
|PIR||ASLJS3. A04002. |
|RefSeq||NP_057851.1. NC_001802.1. |
3D structure databases
Protocols and materials databases
Genome annotation databases
Family and domain databases
|InterPro||IPR000475. Viral_infect. |
|Pfam||PF00559. Vif. 1 hit. |
|PRINTS||PR00349. VIRIONINFFCT. |
|Accession||Primary (citable) accession number: P69722|
Secondary accession number(s): P03401
|Entry status||Reviewed (UniProtKB/Swiss-Prot)|
|Annotation program||Viral Protein Annotation Program|
Index of protein domains and families