Database: UniProt
Original site: VIF_SIVTN 
ID   VIF_SIVTN               Reviewed;         198 AA.
AC   Q8AII0;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   02-DEC-2020, entry version 64.
DE   RecName: Full=Virion infectivity factor;
DE            Short=Vif;
OS   Simian immunodeficiency virus (isolate TAN1) (SIV-cpz) (Chimpanzee
OS   immunodeficiency virus).
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX   NCBI_TaxID=388910;
OH   NCBI_TaxID=9598; Pan troglodytes (Chimpanzee).
RN   [1]
RX   PubMed=12525658; DOI=10.1128/jvi.77.3.2233-2242.2003;
RA   Santiago M.L., Bibollet-Ruche F., Bailes E., Kamenya S., Muller M.N.,
RA   Lukasik M., Pusey A.E., Collins D.A., Wrangham R.W., Goodall J., Shaw G.M.,
RA   Sharp P.M., Hahn B.H.;
RT   "Amplification of a complete simian immunodeficiency virus genome from
RT   fecal RNA of a wild chimpanzee.";
RL   J. Virol. 77:2233-2242(2003).
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.
CC       Interacts with host ABCE1, which seems to be involved in lentiviruses
CC       capsid formation and displays RNase L inhibitor activity. This
CC       interaction may play a role in protecting viral RNA from damage during
CC       viral assembly. May interact with host SAT, which is a regulator of
CC       polyamine cell level. This interaction may be relevant since polyamines
CC       affect viral RNA properties (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homomultimer; in vitro and presumably in vivo. Interacts with
CC       viral Pr55Gag precursor, host APOBEC3G, UBCE7IP1 isoform 3/ZIN, ABCE1
CC       and possibly with SAT. Forms an E3 ligase complex by interacting with
CC       host CUL5 and elongin BC complex (ELOB and ELOC) (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Host cytoplasm. Host cell membrane; Peripheral
CC       membrane protein; Cytoplasmic side. Virion {ECO:0000250}. Note=Seems to
CC       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.
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: Highly phosphorylated on serine and threonine residues. Thr-97 and
CC       Ser-171 are phosphorylated by the mitogen activated kinase MAP4K1 (By
CC       similarity). {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 (By similarity). {ECO:0000250}.
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       (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the primate lentivirus group Vif protein family.
CC       {ECO:0000305}.
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DR   EMBL; AF447763; AAO13961.1; -; Genomic_RNA.
DR   SMR; Q8AII0; -.
DR   Proteomes; UP000007222; 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:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0019058; P:viral life cycle; IEA:InterPro.
DR   InterPro; IPR000475; Vif.
DR   Pfam; PF00559; Vif; 1.
PE   2: Evidence at transcript level;
KW   Host cell membrane; Host cytoplasm; Host membrane; Host-virus interaction;
KW   Membrane; Phosphoprotein; Reference proteome; RNA-binding; Ubl conjugation;
KW   Ubl conjugation pathway; Virion.
FT   CHAIN           1..198
FT                   /note="Virion infectivity factor"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000248293"
FT   REGION          76..115
FT                   /note="RNA-binding"
FT                   /evidence="ECO:0000255"
FT   REGION          152..170
FT                   /note="Multimerization"
FT                   /evidence="ECO:0000250"
FT   REGION          177..178
FT                   /note="Membrane association"
FT                   /evidence="ECO:0000250"
FT   MOTIF           109..140
FT                   /note="HCCH motif"
FT                   /evidence="ECO:0000250"
FT   MOTIF           145..154
FT                   /note="BC-box-like motif"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         97
FT                   /note="Phosphothreonine; by host MAP4K1"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         145
FT                   /note="Phosphothreonine; by host"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         171
FT                   /note="Phosphoserine; by host MAP4K1"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   198 AA;  23383 MW;  65B2A1E82CC5040E CRC64;
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