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P69722

- VIF_HV112

UniProt

P69722 - VIF_HV112

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Protein
Virion infectivity factor
Gene
vif
Organism
Human immunodeficiency virus type 1 group M subtype B (isolate PCV12) (HIV-1)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at transcript leveli

Functioni

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.

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 PCV12) (HIV-1)
Taxonomic identifieri11679 [NCBI]
Taxonomic lineageiVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeLentivirusPrimate lentivirus group
Virus hostiHomo sapiens (Human) [TaxID: 9606]

Subcellular locationi

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.

GO - Cellular componenti

  1. host cell cytoplasm Source: UniProtKB-SubCell
  2. host cell plasma membrane Source: UniProtKB-SubCell
  3. membrane Source: UniProtKB-KW
  4. virion Source: UniProtKB-SubCell
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 factor By similarity
PRO_0000043023Add
BLAST
Chaini1 – 150150p17 By similarity
PRO_0000043024Add
BLAST
Chaini151 – 19242p7 By similarity
PRO_0000043025Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei96 – 961Phosphothreonine; by host MAP4K1 By similarity
Modified residuei144 – 1441Phosphoserine; by host By similarity
Modified residuei165 – 1651Phosphoserine; by host MAP4K1 By similarity
Modified residuei188 – 1881Phosphothreonine; by host By 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.
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 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.

Protein-protein interaction databases

BioGridi1205539. 56 interactions.

Structurei

3D structure databases

ProteinModelPortaliP69722.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni14 – 174Interaction with host APOBEC3F; F1-box By similarity
Regioni40 – 445Interaction with host APOBEC3G; G-box By similarity
Regioni54 – 7219Interaction with host APOBEC3F and APOBEC3G; FG-box By similarity
Add
BLAST
Regioni74 – 796Interaction with host APOBEC3F; F2-box By similarity
Regioni75 – 11440RNA-binding Reviewed prediction
Add
BLAST
Regioni151 – 16414Multimerization By similarity
Add
BLAST
Regioni171 – 1722Membrane association By similarity

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi108 – 13932HCCH motif By similarity
Add
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.

P69722-1 [UniParc]FASTAAdd to Basket

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MENRWQVMIV WQVDRMRIRT WKSLVKHHMY VSGKARGWFY RHHYESPHPR    50
ISSEVHIPLG DARLVITTYW GLHTGERDWH LGQGVSIEWR KKRYSTQVDP 100
ELADQLIHLY YFDCFSDSAI RKALLGHIVS PRCEYQAGHN KVGSLQYLAL 150
AALITPKKIK PPLPSVTKLT EDRWNKPQKT KGHRGSHTMN GH 192
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
M11840 Genomic RNA. Translation: AAA44997.1.
PIRiA04002. ASLJS3.
RefSeqiNP_057851.1. NC_001802.1.

Genome annotation databases

GeneIDi155459.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M11840 Genomic RNA. Translation: AAA44997.1 .
PIRi A04002. ASLJS3.
RefSeqi NP_057851.1. NC_001802.1.

3D structure databases

ProteinModelPortali P69722.
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. "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.

Entry informationi

Entry nameiVIF_HV112
AccessioniPrimary (citable) accession number: P69722
Secondary accession number(s): P03401
Entry historyi
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 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).

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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