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Database: UniProt
Entry: VIF_HV2BE
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Original site: VIF_HV2BE 
ID   VIF_HV2BE               Reviewed;         215 AA.
AC   P18097;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 1.
DT   02-DEC-2020, entry version 90.
DE   RecName: Full=Virion infectivity factor;
DE            Short=Vif;
DE   AltName: Full=Q protein;
DE   AltName: Full=SOR protein;
GN   Name=vif;
OS   Human immunodeficiency virus type 2 subtype A (isolate BEN) (HIV-2).
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX   NCBI_TaxID=11714;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2353457; DOI=10.1016/0042-6822(90)90484-9;
RA   Kirchhoff F., Jentsch K., Bachmann B., Stuke A., Laloux C., Lueke W.,
RA   Stahl-Henning C., Schneider J., Nieselt K., Eigen M., Hunsmann G.;
RT   "A novel proviral clone of HIV-2: biological and phylogenetic relationship
RT   to other primate immunodeficiency viruses.";
RL   Virology 177:305-311(1990).
CC   -!- FUNCTION: Counteracts the innate antiviral activity of APOBEC3G. Forms
CC       a complex with host APOBEC3G thus preventing the entry of this lethally
CC       hypermutating enzyme into progeny virions. Functions as an adapter
CC       molecule, recruiting APOBEC3G to the ubiquitin-proteasome machinery.
CC       Targets APOBEC3G for degradation through the assembly with elongin BC
CC       complex, CUL5 and RBX1. Binds viral RNA and affects the stability of
CC       viral nucleoprotein core. May play a role in viral morphology (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homomultimer; in vitro and presumably in vivo. Interacts with
CC       viral Pr55Gag precursor and human APOBEC3G. The interaction between Vif
CC       and APOBEC3G is species-specific, which may play a role in restricting
CC       the replication of HIV to humans. Forms an E3 ligase complex by
CC       interacting with human CUL5 and elongin BC complex (ELOB and ELOC) (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000250}. Host cell membrane
CC       {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC       side {ECO:0000250}. Virion {ECO:0000250}. Note=In the cytoplasm, seems
CC       to colocalize with intermediate filament vimentin. A fraction is
CC       associated with the cytoplasmic side of cellular membranes, presumably
CC       via the interaction with Pr55Gag precursor (By similarity).
CC       {ECO:0000250}.
CC   -!- INDUCTION: Expressed late during infection in a Rev-dependent manner.
CC   -!- DOMAIN: The BC-like-box motif mediates the interaction with elongin BC
CC       complex. {ECO:0000250}.
CC   -!- DOMAIN: The HCCH motif (H-x(5)-C-x(18)-C-x(5)-H) mediates the
CC       interaction with CUL5. {ECO:0000250}.
CC   -!- PTM: Processed in virion by the viral protease. {ECO:0000250}.
CC   -!- PTM: Highly phosphorylated on serine and threonine residues.
CC       {ECO:0000250}.
CC   -!- PTM: Polyubiquitinated and degraded by the proteasome in the presence
CC       of APOBEC3G. {ECO:0000250}.
CC   -!- MISCELLANEOUS: Required for replication in 'nonpermissive' cells,
CC       including primary T-cells, macrophages and certain T-cell lines, but is
CC       dispensable for replication in 'permissive' cell lines, such as 293T
CC       cells. In nonpermissive cells, Vif-defective viruses can produce
CC       virions, but they fail to complete reverse transcription and cannot
CC       successfully infect new cells.
CC   -!- MISCELLANEOUS: Vif-defective viruses show catastrophic failure in
CC       reverse transcription due to APOBEC-induced mutations that initiate a
CC       DNA base repair pathway and compromise the structural integrity of the
CC       ssDNA. In the absence of Vif, the virion is morphologically abnormal.
CC   -!- MISCELLANEOUS: This isolate is from a German AIDS patient (with
CC       predominantly neurological complications) who was probably infected in
CC       Mali.
CC   -!- SIMILARITY: Belongs to the primate lentivirus group Vif protein family.
CC       {ECO:0000305}.
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DR   EMBL; M30502; AAB00738.1; -; Genomic_DNA.
DR   RefSeq; NP_056839.1; NC_001722.1.
DR   BioGRID; 1205548; 1.
DR   PRIDE; P18097; -.
DR   GeneID; 1724712; -.
DR   KEGG; vg:1724712; -.
DR   Proteomes; UP000002242; Genome.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0019012; C:virion; IEA:UniProtKB-SubCell.
DR   GO; GO:0019058; P:viral life cycle; IEA:InterPro.
DR   InterPro; IPR000475; Vif.
DR   Pfam; PF00559; Vif; 1.
DR   PRINTS; PR00349; VIRIONINFFCT.
PE   2: Evidence at transcript level;
KW   AIDS; Host cell membrane; Host cytoplasm; Host membrane;
KW   Host-virus interaction; Membrane; Phosphoprotein; Reference proteome;
KW   Ubl conjugation; Ubl conjugation pathway; Virion.
FT   CHAIN           1..215
FT                   /note="Virion infectivity factor"
FT                   /id="PRO_0000085317"
FT   REGION          154..167
FT                   /note="Multimerization"
FT                   /evidence="ECO:0000250"
FT   MOTIF           110..141
FT                   /note="HCCH motif"
FT                   /evidence="ECO:0000250"
FT   MOTIF           147..156
FT                   /note="BC-box-like motif"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         98
FT                   /note="Phosphothreonine; by host MAP4K1"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         147
FT                   /note="Phosphoserine; by host"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   215 AA;  25312 MW;  89C68E82703CDF28 CRC64;
     MEEDRNWIVV PTWRVPGRME KWHALVKYLK YRTKDLEEVR YVPHHKVGWA WWTCSRVIFP
     LQGKSHLEIQ AYWNLTPEKG WLSSHAVRLT WYTEKFWTDV TPDCADILIH STYFSCFTAG
     EVRRAIRGEK LLSCCNYPQA HKAQVPSLQY LALVVVQQND RPQRKGTARK QWRRDHWRGL
     RVAREDHRSL KQGGSEPSAP RAHFPGVAKV LEILA
//
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