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P69721

- VIF_HV1BR

UniProt

P69721 - VIF_HV1BR

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Protein

Virion infectivity factor

Gene

vif

Organism
Human immunodeficiency virus type 1 group M subtype B (isolate BRU/LAI) (HIV-1)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

Functioni

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).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei150 – 1512Cleavage in virion (by viral protease)By similarity

GO - Molecular functioni

  1. RNA binding Source: UniProtKB-KW

GO - Biological processi

  1. viral life cycle Source: InterPro
Complete GO annotation...

Keywords - Biological processi

Host-virus interaction, Ubl conjugation pathway

Keywords - Ligandi

RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Virion infectivity factor
Short name:
Vif
Alternative name(s):
SOR protein
Cleaved into the following 2 chains:
Gene namesi
Name:vif
OrganismiHuman immunodeficiency virus type 1 group M subtype B (isolate BRU/LAI) (HIV-1)
Taxonomic identifieri11686 [NCBI]
Taxonomic lineageiVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeLentivirusPrimate lentivirus group
Virus hostiHomo sapiens (Human) [TaxID: 9606]
ProteomesiUP000007692: Genome

Subcellular locationi

Host cytoplasm By similarity. Host cell membrane By similarity; Peripheral membrane protein By similarity; 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).By similarity

GO - Cellular componenti

  1. host cell cytoplasm Source: UniProtKB-KW
  2. host cell plasma membrane Source: UniProtKB-KW
  3. membrane Source: UniProtKB-KW
  4. virion Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Host cell membrane, Host cytoplasm, Host membrane, Membrane, Virion

Pathology & Biotechi

Keywords - Diseasei

AIDS

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 192192Virion infectivity factorBy similarityPRO_0000043029Add
BLAST
Chaini1 – 150150p17By similarityPRO_0000043030Add
BLAST
Chaini151 – 19242p7By similarityPRO_0000043031Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei96 – 961Phosphothreonine; by host MAP4K1By similarity
Modified residuei144 – 1441Phosphoserine; by hostBy similarity
Modified residuei165 – 1651Phosphoserine; by host MAP4K1By similarity
Modified residuei188 – 1881Phosphothreonine; by hostBy similarity

Post-translational modificationi

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).By similarity
Polyubiquitinated and degraded by the proteasome in the presence of APOBEC3G.By similarity

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Expressioni

Inductioni

Expressed late during infection in a Rev-dependent manner.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi1205539. 56 interactions.

Structurei

3D structure databases

ProteinModelPortaliP69721.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni14 – 174Interaction with host APOBEC3F; F1-boxBy similarity
Regioni40 – 445Interaction with host APOBEC3G; G-boxBy similarity
Regioni54 – 7219Interaction with host APOBEC3F and APOBEC3G; FG-boxBy similarityAdd
BLAST
Regioni74 – 796Interaction with host APOBEC3F; F2-boxBy similarity
Regioni75 – 11440RNA-bindingSequence AnalysisAdd
BLAST
Regioni151 – 16414MultimerizationBy similarityAdd
BLAST
Regioni171 – 1722Membrane associationBy similarity

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi108 – 13932HCCH motifBy similarityAdd
BLAST
Motifi144 – 15310BC-box-like motif

Domaini

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

Sequence similaritiesi

Family and domain databases

InterProiIPR000475. Viral_infect.
[Graphical view]
PfamiPF00559. Vif. 1 hit.
[Graphical view]
PRINTSiPR00349. VIRIONINFFCT.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P69721-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MENRWQVMIV WQVDRMRIRT WKSLVKHHMY VSGKARGWFY RHHYESPHPR
60 70 80 90 100
ISSEVHIPLG DARLVITTYW GLHTGERDWH LGQGVSIEWR KKRYSTQVDP
110 120 130 140 150
ELADQLIHLY YFDCFSDSAI RKALLGHIVS PRCEYQAGHN KVGSLQYLAL
160 170 180 190
AALITPKKIK PPLPSVTKLT EDRWNKPQKT KGHRGSHTMN GH
Length:192
Mass (Da):22,513
Last modified:August 13, 1987 - v1
Checksum:iD22589F3955CBE40
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
K02013 Genomic RNA. Translation: AAB59748.1.
A04321 Unassigned RNA. Translation: CAA00351.1.
RefSeqiNP_057851.1. NC_001802.1.

Genome annotation databases

GeneIDi155459.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
K02013 Genomic RNA. Translation: AAB59748.1 .
A04321 Unassigned RNA. Translation: CAA00351.1 .
RefSeqi NP_057851.1. NC_001802.1.

3D structure databases

ProteinModelPortali P69721.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 1205539. 56 interactions.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 155459.

Family and domain databases

InterProi IPR000475. Viral_infect.
[Graphical view ]
Pfami PF00559. Vif. 1 hit.
[Graphical view ]
PRINTSi PR00349. VIRIONINFFCT.
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiVIF_HV1BR
AccessioniPrimary (citable) accession number: P69721
Secondary accession number(s): P03401
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: August 13, 1987
Last modified: October 29, 2014
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

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).

Keywords - Technical termi

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3