ID   VIF_SIVGB               Reviewed;         172 AA.
AC   P22383;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1991, sequence version 1.
DT   23-FEB-2022, entry version 84.
DE   RecName: Full=Virion infectivity factor;
DE            Short=Vif;
DE   AltName: Full=Q protein;
DE   AltName: Full=SOR protein;
GN   Name=vif;
OS   Simian immunodeficiency virus (isolate GB1) (SIV-mnd) (Simian
OS   immunodeficiency virus mandrill).
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX   NCBI_TaxID=11732;
OH   NCBI_TaxID=9527; Cercopithecidae (Old World monkeys).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=2797181; DOI=10.1038/341539a0;
RA   Tsujimoto H., Hasegawa A., Maki N., Fukasawa M., Miura T., Speidel S.,
RA   Cooper R.W., Moriyama E.N., Gojobori T., Hayami M.;
RT   "Sequence of a novel simian immunodeficiency virus from a wild-caught
RT   African mandrill.";
RL   Nature 341:539-541(1989).
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 host APOBEC3G. The interaction between Vif
CC       and APOBEC3G is species-specific, which may play a role in restricting
CC       the replication of SIV to their host. Forms an E3 ligase complex by
CC       interacting with host 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=Seems to colocalize with
CC       intermediate filament vimentin. A fraction is associated with the
CC       cytoplasmic side of cellular membranes, presumably via the interaction
CC       with Pr55Gag precursor (By similarity). {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: 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 is an African mandrill isolate.
CC   -!- SIMILARITY: Belongs to the primate lentivirus group Vif protein family.
CC       {ECO:0000305}.
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DR   EMBL; M27470; AAB49570.1; -; Genomic_RNA.
DR   SMR; P22383; -.
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   Host cell membrane; Host cytoplasm; Host membrane; Host-virus interaction;
KW   Membrane; Phosphoprotein; Ubl conjugation; Ubl conjugation pathway; Virion.
FT   CHAIN           1..172
FT                   /note="Virion infectivity factor"
FT                   /id="PRO_0000085330"
FT   MOTIF           119..150
FT                   /note="HCCH motif"
FT                   /evidence="ECO:0000250"
FT   MOTIF           157..166
FT                   /note="BC-box-like motif"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         107
FT                   /note="Phosphothreonine; by host"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         157
FT                   /note="Phosphoserine; by host"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   172 AA;  20499 MW;  205E7BDDE6265FCB CRC64;
     MERVERIVRL TWKVSSQRIE KWHWLVRRQM AWATANNEEG CWWLYPHFMA YNEWYTCSKV
     VIIINRDIRL IVRSYWHLQI EVGCLSTYAV SIEAVVRPPP FEKEWCTEIT PEVADHLIHL
     HFYDCFMDSA VMKAIRGEEV LKVCRFPAGH KAQGVLSLQF LCLRVIYGPE ER