ID   VIF_SIVCZ               Reviewed;         193 AA.
AC   P17284;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   23-FEB-2022, entry version 91.
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 CPZ GAB1) (SIV-cpz) (Chimpanzee
OS   immunodeficiency virus).
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX   NCBI_TaxID=402771;
OH   NCBI_TaxID=9596; Pan (chimpanzees).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=2188136; DOI=10.1038/345356a0;
RA   Huet T., Cheynier R., Meyerhans A., Roelants G., Wain-Hobson S.;
RT   "Genetic organization of a chimpanzee lentivirus related to HIV-1.";
RL   Nature 345:356-359(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 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   -!- SIMILARITY: Belongs to the primate lentivirus group Vif protein family.
CC       {ECO:0000305}.
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DR   EMBL; X52154; CAA36402.1; -; Genomic_RNA.
DR   PIR; S09985; ASLJSI.
DR   SMR; P17284; -.
DR   Proteomes; UP000009153; 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: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; Reference proteome; Ubl conjugation;
KW   Ubl conjugation pathway; Virion.
FT   CHAIN           1..193
FT                   /note="Virion infectivity factor"
FT                   /id="PRO_0000085336"
FT   REGION          75..114
FT                   /note="RNA-binding"
FT                   /evidence="ECO:0000250"
FT   REGION          152..165
FT                   /note="Multimerization"
FT                   /evidence="ECO:0000250"
FT   REGION          171..172
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"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         145
FT                   /note="Phosphoserine; by host"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         166
FT                   /note="Phosphoserine; by host"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         189
FT                   /note="Phosphothreonine; by host"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   193 AA;  23048 MW;  F241C31C0B2A241F CRC64;
     MENRWQVMIV WQVDRMRIKT WNSLVKYHIY RSKKARGWFY RHHYDHPNPK VASEIHIPFR
     DYSKLIVTTY WALSPGERAW HLGHGVSIQW RLGSYVTQVD PFTADRLIHS QYFDCFAETA
     IRRAILGQLV APRCEYKEGH RQVGSLQFLA LKALISERRH RPPLPSVAKL TEDRWNKHQR
     TKVHQENLTR NGH