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P12504

- VIF_HV1N5

UniProt

P12504 - VIF_HV1N5

Protein

Virion infectivity factor

Gene

vif

Organism
Human immunodeficiency virus type 1 group M subtype B (isolate NY5) (HIV-1)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 96 (01 Oct 2014)
      Sequence version 1 (01 Oct 1989)
      Previous versions | rss
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    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)

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. RNA binding Source: UniProtKB-KW

    GO - Biological processi

    1. viral life cycle Source: InterPro

    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 NY5) (HIV-1)
    Taxonomic identifieri11698 [NCBI]
    Taxonomic lineageiVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeLentivirusPrimate lentivirus group
    Virus hostiHomo sapiens (Human) [TaxID: 9606]

    Subcellular locationi

    Host cytoplasm. Host cell membrane; Peripheral membrane protein; Cytoplasmic side. Virion
    Note: 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.

    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

    Keywords - Cellular componenti

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

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi5 – 62WQ → AA: 44% loss of viral infectivity. 1 Publication
    Mutagenesisi12 – 132QV → AA: No effect on viral infectivity. 1 Publication
    Mutagenesisi16 – 183MRI → AAA: 29% loss of viral infectivity. 1 Publication
    Mutagenesisi23 – 242RL → AA: 14% loss of viral infectivity. 1 Publication
    Mutagenesisi29 – 313MYI → AAV: 59% loss of viral infectivity. 1 Publication
    Mutagenesisi33 – 342RK → AA: 35% loss of viral infectivity. 1 Publication
    Mutagenesisi38 – 403WFY → AAA: 94% loss of viral infectivity. 1 Publication
    Mutagenesisi43 – 442HY → AA: 95% loss of viral infectivity. 1 Publication
    Mutagenesisi53 – 542SE → AA: 39% loss of viral infectivity. 1 Publication
    Mutagenesisi58 – 592PL → AA: 45% loss of viral infectivity. 1 Publication
    Mutagenesisi69 – 702YW → AA: 97% loss of viral infectivity. 1 Publication
    Mutagenesisi73 – 742HT → AA: No effect onviral infectivity. 1 Publication
    Mutagenesisi80 – 812HL → AA: 19% loss of viral infectivity. 1 Publication
    Mutagenesisi86 – 872SI → AA: 42% loss of viral infectivity. 1 Publication
    Mutagenesisi90 – 923RKK → AAA: No effect on viral infectivity. 1 Publication
    Mutagenesisi97 – 982QV → AA: 27% loss of viral infectivity. 1 Publication
    Mutagenesisi105 – 1073QLI → AAV: 98% loss of viral infectivity. 1 Publication
    Mutagenesisi108 – 1081H → L: Complete loss of interaction with CUL5. 2 Publications
    Mutagenesisi111 – 1122YF → AA: 93% loss of viral infectivity. 1 Publication
    Mutagenesisi114 – 1141C → S: 98% loss of viral infectivity. Complete loss of interaction with CUL5. 4 Publications
    Mutagenesisi121 – 1233RNT → AAA: 35% increase of viral infectivity. 1 Publication
    Mutagenesisi127 – 1282RI → AA: 10% loss of viral infectivity. 1 Publication
    Mutagenesisi133 – 1331C → S: 95% loss of viral infectivity. Complete loss of interaction with CUL5. 4 Publications
    Mutagenesisi135 – 1362YQ → AA: 73% loss of viral infectivity. 1 Publication
    Mutagenesisi139 – 1391H → L: Complete loss of interaction with CUL5. 2 Publications
    Mutagenesisi140 – 1412NK → AA: 68% loss of viral infectivity. 1 Publication
    Mutagenesisi144 – 1463SLQ → AAA: 93% loss of viral infectivity. 2 Publications
    Mutagenesisi144 – 1441S → A: 25% loss of interaction with CUL5y. 2 Publications
    Mutagenesisi145 – 1451L → A: Complete loss of interaction with CUL5. 2 Publications
    Mutagenesisi146 – 1461Q → A: 90% loss of interaction with CUL5. 2 Publications
    Mutagenesisi147 – 1482YL → AA: 40% loss of viral infectivity. 2 Publications
    Mutagenesisi147 – 1471Y → A: 40% loss of interaction with CUL5. 2 Publications
    Mutagenesisi148 – 1481L → A: 35% loss of interaction with CUL5. 2 Publications
    Mutagenesisi149 – 1513ALA → RKS: Complete loss of processing between p17 and p7. Complete loss of replication. 2 Publications
    Mutagenesisi149 – 1491A → G: 75% loss of CUL5 binding activity. 2 Publications
    Mutagenesisi150 – 1501L → A: 90% loss of CUL5 binding activity. 2 Publications
    Mutagenesisi151 – 1511A → E: No effect on processing between p17 and p7. 1 Publication
    Mutagenesisi151 – 1511A → N: Slightly increased processing between p17 and p7. 1 Publication
    Mutagenesisi151 – 1511A → P: Increased processing between p17 and p7. 1 Publication
    Mutagenesisi151 – 1511A → Y: Partial loss of processing between p17 and p7. 1 Publication
    Mutagenesisi156 – 1583PKQ → AAA: No effect on viral infectivity. 1 Publication
    Mutagenesisi157 – 1571K → A: No effect viral infectivity. 2 Publications
    Mutagenesisi158 – 1603QIK → AAA: 9% loss of viral infectivity. 1 Publication
    Mutagenesisi160 – 1601K → A: 33% loss of viral infectivity. 1 Publication
    Mutagenesisi161 – 1644PPLP → APLA: 88% loss of viral infectivity. 1 Publication
    Mutagenesisi161 – 1633PPL → AAA: 97% loss of viral infectivity. 1 Publication
    Mutagenesisi161 – 1611P → A: 27% loss of viral infectivity. 1 Publication
    Mutagenesisi162 – 1621P → A: No effect viral infectivity. 1 Publication
    Mutagenesisi163 – 1631L → A: 26% loss of viral infectivity. 1 Publication
    Mutagenesisi164 – 1641P → A: 63% loss of viral infectivity. 1 Publication
    Mutagenesisi165 – 1651S → A: 67% loss of viral infectivity. 2 Publications
    Mutagenesisi166 – 1661V → A: 20% loss of viral infectivity. 2 Publications
    Mutagenesisi169 – 1702LT → AA: 42% loss of viral infectivity. 1 Publication
    Mutagenesisi180 – 1812TK → AA: 5% loss of viral infectivity. 1 Publication
    Mutagenesisi189 – 1902MN → AA: 4% loss of viral infectivity. 1 Publication

    Keywords - Diseasei

    AIDS

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 192192Virion infectivity factorPRO_0000042762Add
    BLAST
    Chaini1 – 150150Virion infectivity factor p17PRO_0000042763Add
    BLAST
    Chaini151 – 19242Virion infectivity factor p7PRO_0000042764Add
    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.
    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.1 Publication
    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.1 Publication

    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

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    AMBRA1Q9C0C75EBI-779991,EBI-2512975From a different organism.
    CBFBQ139515EBI-779991,EBI-718750From a different organism.
    CUL2Q136175EBI-779991,EBI-456179From a different organism.
    CUL5Q930345EBI-779991,EBI-1057139From a different organism.
    DCAF11Q8TEB13EBI-779991,EBI-2213388From a different organism.
    DNAJC7Q996153EBI-779991,EBI-357552From a different organism.
    GPS2Q132272EBI-779991,EBI-713355From a different organism.
    HCKP086313EBI-779991,EBI-346340From a different organism.
    HDAC3O153792EBI-779991,EBI-607682From a different organism.
    MAPK6Q166592EBI-779991,EBI-1384105From a different organism.
    PSME3P612892EBI-779991,EBI-355546From a different organism.
    RNF216Q9NWF9-34EBI-779991,EBI-723337From a different organism.
    RNF7Q9UBF64EBI-779991,EBI-398632From a different organism.
    SQSTM1Q135012EBI-779991,EBI-307104From a different organism.
    STUB1Q9UNE72EBI-779991,EBI-357085From a different organism.
    TCEB1Q153695EBI-779991,EBI-301231From a different organism.
    TCEB2Q153705EBI-779991,EBI-301238From a different organism.
    UBL4AP114412EBI-779991,EBI-356983From a different organism.
    UBR2Q8IWV83EBI-779991,EBI-1237260From a different organism.

    Protein-protein interaction databases

    DIPiDIP-36069N.
    IntActiP12504. 29 interactions.

    Structurei

    Secondary structure

    1
    192
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 139
    Helixi15 – 3016
    Turni34 – 374
    Beta strandi39 – 413
    Turni43 – 453
    Beta strandi51 – 599
    Beta strandi62 – 698
    Beta strandi73 – 753
    Beta strandi83 – 919
    Beta strandi94 – 974
    Helixi100 – 10910
    Helixi119 – 1257
    Helixi136 – 1383
    Helixi145 – 15410
    Helixi166 – 1694

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2MA9NMR-A143-174[»]
    3DCGX-ray2.40E/F139-176[»]
    4N9FX-ray3.301/2/7/G/M/S/b/d/j/p/q/v1-176[»]
    ProteinModelPortaliP12504.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP12504.

    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 – 16414MultimerizationAdd
    BLAST
    Regioni171 – 1722Membrane association

    Motif

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

    Domaini

    The BC-like-box motif mediates the interaction with elongin BC complex.
    The HCCH motif (H-x(5)-C-x(18)-C-x(5)-H) mediates the interaction with CUL5.

    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.

    P12504-1 [UniParc]FASTAAdd to Basket

    « Hide

    MENRWQVMIV WQVDRMRINT WKRLVKHHMY ISRKAKDWFY RHHYESTNPK    50
    ISSEVHIPLG DAKLVITTYW GLHTGERDWH LGQGVSIEWR KKRYSTQVDP 100
    DLADQLIHLH YFDCFSESAI RNTILGRIVS PRCEYQAGHN KVGSLQYLAL 150
    AALIKPKQIK PPLPSVRKLT EDRWNKPQKT KGHRGSHTMN GH 192
    Length:192
    Mass (Da):22,699
    Last modified:October 1, 1989 - v1
    Checksum:i2830B3233E8ECD16
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti90 – 934RKKR → KKRK in strain: Clinical isolate; from an asymptomatic patient; Vif is mislocalized to the nucleus and non functional.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M19921 Genomic RNA. Translation: AAA44989.1.
    M38431 Genomic RNA. Translation: AAB04038.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M19921 Genomic RNA. Translation: AAA44989.1 .
    M38431 Genomic RNA. Translation: AAB04038.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2MA9 NMR - A 143-174 [» ]
    3DCG X-ray 2.40 E/F 139-176 [» ]
    4N9F X-ray 3.30 1/2/7/G/M/S/b/d/j/p/q/v 1-176 [» ]
    ProteinModelPortali P12504.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-36069N.
    IntActi P12504. 29 interactions.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P12504.

    Family and domain databases

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

    Publicationsi

    1. Buckler C.E., Buckler-White A.J., Willey R.L., McCoy J.
      Submitted (JUN-1988) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
      Strain: Clone pNL4-3.
    2. Theodore T., Buckler-White A.J.
      Submitted (OCT-1992) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    3. "Expression of human immunodeficiency virus type 1 vif and vpr mRNAs is Rev-dependent and regulated by splicing."
      Schwartz S., Felber B.K., Pavlakis G.N.
      Virology 183:677-686(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    4. "Role of vif during packing of the core of HIV-1."
      Hoglund S., Ohagen A., Lawrence K., Gabuzda D.
      Virology 201:349-355(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: ROLE IN VIRION MORPHOLOGY.
    5. "Mutational analysis of the human immunodeficiency virus type 1 Vif protein."
      Simon J.H., Sheehy A.M., Carpenter E.A., Fouchier R.A., Malim M.H.
      J. Virol. 73:2675-2681(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF 5-TRP-GLN-6; 12-GLN-VAL-13; 16-MET--ILE-18; 23-ARG-LEU-24; 29-MET--ILE-31; 33-ARG-LYS-34; 38-TRP--TYR-40; 43-HIS-TYR-44; 53-SER-GLU-54; 58-PRO-LEU-59; 69-TYR-TRP-70; 73-HIS-THR-74; 80-HIS-LEU-81; 86-SER-ILE-87; 90-ARG--LYS-92; 97-GLN-VAL-98; 105-GLN--ILE-107; 111-TYR-PHE-112; CYS-114; 121-ARG--THR-123; 127-ARG-ILE-128; CYS-133; 135-TYR-GLN-136; 140-ASN-LYS-141; 144-SER--GLN-146; 147-TYR-LEU-148; 156-PRO--GLN-158; LYS-157; 158-GLN--LYS-160; 161-PRO--LEU-164; SER-165; VAL-166; 169-LEU-THR-170; 180-THR-LYS-181 AND 189-MET-ASN-190.
    6. "The multimerization of human immunodeficiency virus type I Vif protein: a requirement for Vif function in the viral life cycle."
      Yang S., Sun Y., Zhang H.
      J. Biol. Chem. 276:4889-4893(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: MULTIMERIZATION.
    7. "Human immunodeficiency virus type 1 Vif protein is packaged into the nucleoprotein complex through an interaction with viral genomic RNA."
      Khan M.A., Aberham C., Kao S., Akari H., Gorelick R., Bour S., Strebel K.
      J. Virol. 75:7252-7265(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NUCLEOPROTEIN.
    8. "The tyrosine kinase Hck is an inhibitor of HIV-1 replication counteracted by the viral vif protein."
      Hassaine G., Courcoul M., Bessou G., Barthalay Y., Picard C., Olive D., Collette Y., Vigne R., Decroly E.
      J. Biol. Chem. 276:16885-16893(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HUMAN HCK.
    9. "Intravirion processing of the human immunodeficiency virus type 1 Vif protein by the viral protease may be correlated with Vif function."
      Khan M.A., Akari H., Kao S., Aberham C., Davis D., Buckler-White A., Strebel K.
      J. Virol. 76:9112-9123(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-9 AND 151-162, CLEAVAGE BY VIRAL PROTEASE, MUTAGENESIS OF 149-ALA--ALA-151.
    10. "The human immunodeficiency virus type 1 Vif protein reduces intracellular expression and inhibits packaging of APOBEC3G (CEM15), a cellular inhibitor of virus infectivity."
      Kao S., Khan M.A., Miyagi E., Plishka R., Buckler-White A., Strebel K.
      J. Virol. 77:11398-11407(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    11. "The role of Vif during HIV-1 infection: interaction with novel host cellular factors."
      Lake J.A., Carr J., Feng F., Mundy L., Burrell C., Li P.
      J. Clin. Virol. 26:143-152(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HUMAN SAT.
    12. "HIV-1 Vif protein binds the editing enzyme APOBEC3G and induces its degradation."
      Marin M., Rose K.M., Kozak S.L., Kabat D.
      Nat. Med. 9:1398-1403(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HUMAN APOBEC3G.
    13. "Phosphorylation of a novel SOCS-box regulates assembly of the HIV-1 Vif-Cul5 complex that promotes APOBEC3G degradation."
      Mehle A., Goncalves J., Santa-Marta M., McPike M., Gabuzda D.
      Genes Dev. 18:2861-2866(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HUMAN CUL5 AND ELONGIN BC COMPLEX, MUTAGENESIS OF SER-144; LEU-145; GLN-146; TYR-147; LEU-148; ALA-149 AND LEU-150.
    14. "Vif overcomes the innate antiviral activity of APOBEC3G by promoting its degradation in the ubiquitin-proteasome pathway."
      Mehle A., Strack B., Ancuta P., Zhang C., McPike M., Gabuzda D.
      J. Biol. Chem. 279:7792-7798(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HUMAN APOBEC3G, MUTAGENESIS OF CYS-114 AND CYS-133.
    15. "Ring finger protein ZIN interacts with human immunodeficiency virus type 1 Vif."
      Feng F., Davis A., Lake J.A., Carr J., Xia W., Burrell C., Li P.
      J. Virol. 78:10574-10581(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HUMAN UBCE7IP1.
    16. "Primate lentiviral virion infectivity factors are substrate receptors that assemble with cullin 5-E3 ligase through a HCCH motif to suppress APOBEC3G."
      Luo K., Xiao Z., Ehrlich E., Yu Y., Liu B., Zheng S., Yu X.-F.
      Proc. Natl. Acad. Sci. U.S.A. 102:11444-11449(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HUMAN CUL5, MUTAGENESIS OF HIS-108; CYS-114; CYS-133 AND HIS-139.
    17. "Nuclear localization of HIV type 1 Vif isolated from a long-term asymptomatic individual and potential role in virus attenuation."
      Farrow M.A., Somasundaran M., Zhang C., Gabuzda D., Sullivan J.L., Greenough T.C.
      AIDS Res. Hum. Retroviruses 21:565-574(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT 90-LYS--LYS-93.
      Strain: Clinical Isolate.
    18. "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_HV1N5
    AccessioniPrimary (citable) accession number: P12504
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1989
    Last sequence update: October 1, 1989
    Last modified: October 1, 2014
    This is version 96 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.
    The infectious clone pNL4-3 is a chimeric provirus that consists of DNA from HIV isolates NY5 (5' half) and BRU (3' half).
    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

    3D-structure, Direct protein sequencing

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3