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P12504

- VIF_HV1N5

UniProt

P12504 - VIF_HV1N5

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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

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. 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 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-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

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. 1 Publication
Mutagenesisi111 – 1122YF → AA: 93% loss of viral infectivity. 1 Publication
Mutagenesisi114 – 1141C → S: 98% loss of viral infectivity. Complete loss of interaction with CUL5. 3 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. 3 Publications
Mutagenesisi135 – 1362YQ → AA: 73% loss of viral infectivity. 1 Publication
Mutagenesisi139 – 1391H → L: Complete loss of interaction with CUL5. 1 Publication
Mutagenesisi140 – 1412NK → AA: 68% loss of viral infectivity. 1 Publication
Mutagenesisi144 – 1463SLQ → AAA: 93% loss of viral infectivity. 1 Publication
Mutagenesisi144 – 1441S → A: 25% loss of interaction with CUL5y. 1 Publication
Mutagenesisi145 – 1451L → A: Complete loss of interaction with CUL5. 1 Publication
Mutagenesisi146 – 1461Q → A: 90% loss of interaction with CUL5. 1 Publication
Mutagenesisi147 – 1482YL → AA: 40% loss of viral infectivity. 1 Publication
Mutagenesisi147 – 1471Y → A: 40% loss of interaction with CUL5. 1 Publication
Mutagenesisi148 – 1481L → A: 35% loss of interaction with CUL5. 1 Publication
Mutagenesisi149 – 1513ALA → RKS: Complete loss of processing between p17 and p7. Complete loss of replication. 1 Publication
Mutagenesisi149 – 1491A → G: 75% loss of CUL5 binding activity. 1 Publication
Mutagenesisi150 – 1501L → A: 90% loss of CUL5 binding activity. 1 Publication
Mutagenesisi151 – 1511A → E: No effect on processing between p17 and p7.
Mutagenesisi151 – 1511A → N: Slightly increased processing between p17 and p7.
Mutagenesisi151 – 1511A → P: Increased processing between p17 and p7.
Mutagenesisi151 – 1511A → Y: Partial loss of processing between p17 and p7.
Mutagenesisi156 – 1583PKQ → AAA: No effect on viral infectivity. 1 Publication
Mutagenesisi157 – 1571K → A: No effect viral infectivity. 1 Publication
Mutagenesisi158 – 1603QIK → AAA: 9% loss of viral infectivity. 1 Publication
Mutagenesisi160 – 1601K → A: 33% loss of viral infectivity.
Mutagenesisi161 – 1644PPLP → APLA: 88% loss of viral infectivity. 1 Publication
Mutagenesisi161 – 1633PPL → AAA: 97% loss of viral infectivity.
Mutagenesisi161 – 1611P → A: 27% loss of viral infectivity.
Mutagenesisi162 – 1621P → A: No effect viral infectivity.
Mutagenesisi163 – 1631L → A: 26% loss of viral infectivity.
Mutagenesisi164 – 1641P → A: 63% loss of viral infectivity.
Mutagenesisi165 – 1651S → A: 67% loss of viral infectivity. 1 Publication
Mutagenesisi166 – 1661V → A: 20% loss of viral infectivity. 1 Publication
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 – 139Combined sources
Helixi15 – 3016Combined sources
Turni34 – 374Combined sources
Beta strandi39 – 413Combined sources
Turni43 – 453Combined sources
Beta strandi51 – 599Combined sources
Beta strandi62 – 698Combined sources
Beta strandi73 – 753Combined sources
Beta strandi83 – 919Combined sources
Beta strandi94 – 974Combined sources
Helixi100 – 10910Combined sources
Helixi119 – 1257Combined sources
Helixi136 – 1383Combined sources
Helixi145 – 15410Combined sources
Helixi166 – 1694Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

        10         20         30         40         50
MENRWQVMIV WQVDRMRINT WKRLVKHHMY ISRKAKDWFY RHHYESTNPK
60 70 80 90 100
ISSEVHIPLG DAKLVITTYW GLHTGERDWH LGQGVSIEWR KKRYSTQVDP
110 120 130 140 150
DLADQLIHLH YFDCFSESAI RNTILGRIVS PRCEYQAGHN KVGSLQYLAL
160 170 180 190
AALIKPKQIK PPLPSVRKLT EDRWNKPQKT KGHRGSHTMN GH
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:
EMBLi
GenBanki
DDBJi
Links Updated
M19921 Genomic RNA. Translation: AAA44989.1.
M38431 Genomic RNA. Translation: AAB04038.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M19921 Genomic RNA. Translation: AAA44989.1 .
M38431 Genomic RNA. Translation: AAB04038.1 .

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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: November 26, 2014
This is version 98 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