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Protein

Virion infectivity factor

Gene

vif

Organism
Simian immunodeficiency virus AGM.tantalus (SIV-agm.tan) (Simian immunodeficiency virus African green monkey tantalus)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein 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 (By similarity).By similarity

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Host-virus interaction, Ubl conjugation pathway

Names & Taxonomyi

Protein namesi
Recommended name:
Virion infectivity factor
Short name:
Vif
Alternative name(s):
Q protein
SOR protein
Gene namesi
Name:vif
OrganismiSimian immunodeficiency virus AGM.tantalus (SIV-agm.tan) (Simian immunodeficiency virus African green monkey tantalus)
Taxonomic identifieri349692 [NCBI]
Taxonomic lineageiVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeLentivirusPrimate lentivirus group
Virus hostiChlorocebus tantalus (Tantalus monkey) (Cercopithecus tantalus) [TaxID: 60712]

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi111 – 1111H → L: Complete loss of interaction with CUL5. 1 Publication
Mutagenesisi117 – 1171C → S: Complete loss of interaction with CUL5. 1 Publication
Mutagenesisi135 – 1351C → S: Complete loss of interaction with CUL5. 1 Publication
Mutagenesisi141 – 1411H → L: Complete loss of interaction with CUL5. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 238238Virion infectivity factorPRO_0000085335Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei99 – 991Phosphothreonine; by hostBy similarity
Modified residuei152 – 1521Phosphoserine; by hostBy similarity

Post-translational modificationi

Processed in virion by the viral protease.By similarity
Highly phosphorylated on serines and threonines residues.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 and host APOBEC3G. The interaction between Vif and APOBEC3G is species-specific, which may play a role in restricting the replication of SIV to their host. Forms an E3 ligase complex by interacting with host CUL5 and elongin BC complex (TCEB1 and TCEB2) (By similarity).By similarity

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni159 – 17517MultimerizationBy similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi111 – 14636HCCH motifBy similarityAdd
BLAST
Motifi152 – 16110BC-box-like motifBy similarity

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.

P89905-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEREKLWVTR LTWRVSGEHI DKWKGIVKYH MRNRLQDWTY LMHYQCGWAW
60 70 80 90 100
YTCSRFLIPL GGEGKIVVDC YWHLTPEQGW LSTYAVAISF ENWQNTYKTE
110 120 130 140 150
VTPDVADHMI HCHYFPCFTD RAIQQAIRGE SFLWCTYKEG HVAENHWGQV
160 170 180 190 200
RSLQFLALTV YTDFLRNGRR KRFQGKKTRM VRNLGSQQGA VGRMIKRHGS
210 220 230
RTQSGSTTPF WERTPLPSME LLSGRRGKEW GTNDRKGL
Length:238
Mass (Da):28,169
Last modified:May 1, 1997 - v1
Checksum:i0E15A107E0627762
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U58991 Genomic DNA. Translation: AAC57053.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U58991 Genomic DNA. Translation: AAC57053.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

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

Entry informationi

Entry nameiVIF_SIVTA
AccessioniPrimary (citable) accession number: P89905
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: May 1, 1997
Last modified: April 1, 2015
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Miscellaneous

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.

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.