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P69722 (VIF_HV112) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Virion infectivity factor

Short name=Vif
Alternative name(s):
SOR protein

Cleaved into the following 2 chains:

  1. p17
  2. p7
Gene names
Name:vif
OrganismHuman immunodeficiency virus type 1 group M subtype B (isolate PCV12) (HIV-1)
Taxonomic identifier11679 [NCBI]
Taxonomic lineageVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeLentivirusPrimate lentivirus group
Virus hostHomo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length192 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

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.

Subunit structure

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.

Subcellular location

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.

Induction

Expressed late during infection in a Rev-dependent manner.

Domain

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.

Post-translational modification

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.

Miscellaneous

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).

Sequence similarities

Belongs to the primate lentivirus group Vif protein family.

Ontologies

Keywords
   Biological processHost-virus interaction
Ubl conjugation pathway
   Cellular componentHost cell membrane
Host cytoplasm
Host membrane
Membrane
Virion
   DiseaseAIDS
   LigandRNA-binding
   PTMPhosphoprotein
Ubl conjugation
Gene Ontology (GO)
   Biological_processviral life cycle

Inferred from electronic annotation. Source: InterPro

   Cellular_componenthost cell cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

host cell plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

membrane

Inferred from electronic annotation. Source: UniProtKB-KW

virion

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionRNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 192192Virion infectivity factor By similarity
PRO_0000043023
Chain1 – 150150p17 By similarity
PRO_0000043024
Chain151 – 19242p7 By similarity
PRO_0000043025

Regions

Region14 – 174Interaction with host APOBEC3F; F1-box By similarity
Region40 – 445Interaction with host APOBEC3G; G-box By similarity
Region54 – 7219Interaction with host APOBEC3F and APOBEC3G; FG-box By similarity
Region74 – 796Interaction with host APOBEC3F; F2-box By similarity
Region75 – 11440RNA-binding Potential
Region151 – 16414Multimerization By similarity
Region171 – 1722Membrane association By similarity
Motif108 – 13932HCCH motif By similarity
Motif144 – 15310BC-box-like motif

Sites

Site150 – 1512Cleavage in virion (by viral protease) By similarity

Amino acid modifications

Modified residue961Phosphothreonine; by host MAP4K1 By similarity
Modified residue1441Phosphoserine; by host By similarity
Modified residue1651Phosphoserine; by host MAP4K1 By similarity
Modified residue1881Phosphothreonine; by host By similarity

Sequences

Sequence LengthMass (Da)Tools
P69722 [UniParc].

Last modified August 13, 1987. Version 1.
Checksum: D22589F3955CBE40

FASTA19222,513
        10         20         30         40         50         60 
MENRWQVMIV WQVDRMRIRT WKSLVKHHMY VSGKARGWFY RHHYESPHPR ISSEVHIPLG 

        70         80         90        100        110        120 
DARLVITTYW GLHTGERDWH LGQGVSIEWR KKRYSTQVDP ELADQLIHLY YFDCFSDSAI 

       130        140        150        160        170        180 
RKALLGHIVS PRCEYQAGHN KVGSLQYLAL AALITPKKIK PPLPSVTKLT EDRWNKPQKT 

       190 
KGHRGSHTMN GH 

« Hide

References

[1]"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].
[2]"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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M11840 Genomic RNA. Translation: AAA44997.1.
PIRASLJS3. A04002.
RefSeqNP_057851.1. NC_001802.1.

3D structure databases

ProteinModelPortalP69722.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid1205539. 56 interactions.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID155459.

Family and domain databases

InterProIPR000475. Viral_infect.
[Graphical view]
PfamPF00559. Vif. 1 hit.
[Graphical view]
PRINTSPR00349. VIRIONINFFCT.
ProtoNetSearch...

Entry information

Entry nameVIF_HV112
AccessionPrimary (citable) accession number: P69722
Secondary accession number(s): P03401
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: August 13, 1987
Last modified: February 19, 2014
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families