VIF_HV2NZ
ID VIF_HV2NZ Reviewed; 215 AA.
AC P05901;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1988, sequence version 1.
DT 29-SEP-2021, entry version 83.
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 NIH-Z) (HIV-2).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX NCBI_TaxID=11719;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3261862; DOI=10.1073/pnas.85.16.5941;
RA Zagury J.F., Franchini G., Reitz M.S. Jr., Collalti E., Starcich B.R.,
RA Hall L., Fargnoli K.A., Jagodzinski L.L., Guo H.-G., Laure F., Arya S.K.,
RA Josephs S.F., Zagury D., Wong-Staal F., Gallo R.C.;
RT "Genetic variability between isolates of human immunodeficiency virus (HIV)
RT type 2 is comparable to the variability among HIV type 1.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:5941-5945(1988).
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 -!- SIMILARITY: Belongs to the primate lentivirus group Vif protein family.
CC {ECO:0000305}.
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DR EMBL; J03654; AAB00756.1; -; Genomic_DNA.
DR SMR; P05901; -.
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: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; Ubl conjugation;
KW Ubl conjugation pathway; Virion.
FT CHAIN 1..215
FT /note="Virion infectivity factor"
FT /id="PRO_0000085323"
FT REGION 154..167
FT /note="Multimerization"
FT /evidence="ECO:0000250"
FT REGION 162..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 COMPBIAS 166..191
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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; 25321 MW; 9B4A1F36A9690BFC CRC64;
MEEGKRWIVV PIWRVPGRME RWHSLVKYLK YRTKDLEKVC YVPHHKVGWA WWTCSRVIFP
LKENSHLEIQ AYWNLTPEKG WLSSHSVRIT WYTEKFWTDV TPDCADTLIH STYFSCFTAG
EVRRAIRGEK LLSCCKYPRA HRSQVPSLQF LALVVVQQND RSQGNSATRK QRRGDYRRGL
RMARQDSRGY KQRGSESPPT RAHFPGLAEV LEILA
