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P69721 (VIF_HV1BR) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 62. 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 BRU/LAI) (HIV-1) [Complete proteome]
Taxonomic identifier11686 [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 protein level

General annotation (Comments)

Function

Counteracts the innate antiviral activity of human 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 By similarity.

Subunit structure

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/ZINand 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 human CUL5 and elongin BC complex (TCEB1 and TCEB2). Interacts with host MDM2; this interaction targets Vif for degradation by the proteasome By similarity. Ref.2

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
   Technical termComplete proteome
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_0000043029
Chain1 – 150150p17 By similarity
PRO_0000043030
Chain151 – 19242p7 By similarity
PRO_0000043031

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
P69721 [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]"Nucleotide sequence of the AIDS virus, LAV."
Wain-Hobson S., Sonigo P., Danos O., Cole S., Alizon M.
Cell 40:9-17(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[2]"Identification of a host protein essential for assembly of immature HIV-1 capsids."
Zimmerman C., Klein K.C., Kiser P.K., Singh A.R., Firestein B.L., Riba S.C., Lingappa J.R.
Nature 415:88-92(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HUMAN ABCE1.
[3]"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
K02013 Genomic RNA. Translation: AAB59748.1.
A04321 Unassigned RNA. Translation: CAA00351.1.
RefSeqNP_057851.1. NC_001802.1.

3D structure databases

ProteinModelPortalP69721.
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_HV1BR
AccessionPrimary (citable) accession number: P69721
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 62 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