Virion infectivity factor - Human immunodeficiency virus type 1 group M subtype B (isolate PCV12) (HIV-1)

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P69722 (VIF_HV112) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 56. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Virion infectivity factor
Short name=Vif

Alternative name(s):
SOR protein

Cleaved into the following 2 chains:

Gene names

Name:

vif

Organism

Human immunodeficiency virus type 1 group M subtype B (isolate PCV12) (HIV-1)

Taxonomic identifier

11679 [NCBI]

Taxonomic lineage

Viruses › Retro-transcribing viruses › Retroviridae › Orthoretrovirinae › Lentivirus › Primate lentivirus group ›

Virus host

Homo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length	192 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 process	Host-virus interaction Ubl conjugation pathway
Cellular component	Host cell membrane Host cytoplasm Host membrane Membrane Virion
Disease	AIDS
Ligand	RNA-binding
PTM	Phosphoprotein Ubl conjugation
Gene Ontology (GO)
Biological_process	RNA-dependent DNA replication Traceable author statement. Source: Reactome entry into host cell Traceable author statement. Source: Reactome uncoating of virus Traceable author statement. Source: Reactome viral infectious cycle Inferred from electronic annotation. Source: InterPro virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytosol Traceable author statement. Source: Reactome host 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 nucleoplasm Traceable author statement. Source: Reactome virion Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	RNA binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 192

192

Virion infectivity factor By similarity

PRO_0000043023

Chain

1 – 150

150

p17 By similarity

PRO_0000043024

Chain

151 – 192

p7 By similarity

PRO_0000043025

Regions

Region

14 – 17

Interaction with host APOBEC3F; F1-box By similarity

Region

40 – 44

Interaction with host APOBEC3G; G-box By similarity

Region

54 – 72

Interaction with host APOBEC3F and APOBEC3G; FG-box By similarity

Region

74 – 79

Interaction with host APOBEC3F; F2-box By similarity

Region

75 – 114

RNA-binding Potential

Region

151 – 164

Multimerization By similarity

Region

171 – 172

Membrane association By similarity

Motif

108 – 139

HCCH motif By similarity

Motif

144 – 153

BC-box-like motif

Sites

Site

150 – 151

Cleavage in virion (by viral protease) By similarity

Amino acid modifications

Modified residue

Phosphothreonine; by host MAP4K1 By similarity

Modified residue

144

Phosphoserine; by host By similarity

Modified residue

165

Phosphoserine; by host MAP4K1 By similarity

Modified residue

188

Phosphothreonine; by host By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

P69722 [UniParc].

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

192

22,513

        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.
PIR	ASLJS3. A04002.
RefSeq	NP_057851.1. NC_001802.1.
3D structure databases
ProteinModelPortal	P69722.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	155459.
Enzyme and pathway databases
Reactome	REACT_116125. Disease.
Family and domain databases
InterPro	IPR000475. Viral_infect. [Graphical view]
Pfam	PF00559. Vif. 1 hit. [Graphical view]
PRINTS	PR00349. VIRIONINFFCT.
ProtoNet	Search...

Entry information

Entry name

VIF_HV112

Accession

Primary (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:	April 3, 2013
This is version 56 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Cleaved into the following 2 chains:

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents