ID   VIF_SIVV1               Reviewed;         232 AA.
AC   P27974;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   23-FEB-2022, entry version 81.
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 agm.vervet (isolate AGM155) (SIV-agm.ver)
OS   (Simian immunodeficiency virus African green monkey vervet).
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX   NCBI_TaxID=11727;
OH   NCBI_TaxID=9527; Cercopithecidae (Old World monkeys).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=2304139; DOI=10.1128/jvi.64.3.1086-1092.1990;
RA   Johnson P.R., Fomsgaard A., Allan J.S., Gravell M., London W.T.,
RA   Olmstead R.A., Hirsch V.M.;
RT   "Simian immunodeficiency viruses from African green monkeys display unusual
RT   genetic diversity.";
RL   J. Virol. 64:1086-1092(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   -!- MISCELLANEOUS: The 155 isolate is from a monkey imported from Kenya.
CC   -!- SIMILARITY: Belongs to the primate lentivirus group Vif protein family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M29975; AAA91907.1; -; Genomic_RNA.
DR   SMR; P27974; -.
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..232
FT                   /note="Virion infectivity factor"
FT                   /id="PRO_0000085326"
FT   REGION          157..172
FT                   /note="Multimerization"
FT                   /evidence="ECO:0000250"
FT   REGION          164..232
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           112..142
FT                   /note="HCCH motif"
FT                   /evidence="ECO:0000250"
FT   MOTIF           150..159
FT                   /note="BC-box-like motif"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        193..207
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         100
FT                   /note="Phosphothreonine; by host"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         150
FT                   /note="Phosphoserine; by host"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   232 AA;  27193 MW;  35BC2D8E68D3FCED CRC64;
     MSQEKHWVMR LTWKVQEEVI TKWQGIVRYW MNKRNLKWEY KMHYQITWAW YTMSRYVIPL
     PGSGEIHVDI YWHLAPKQGW LSTYAVGIQY VSLVNDKYRT ELDPNTADSM IHCHYFTCFT
     DRAIQQALRG NRFIFCQFPG GHKLTGQVPS LQYLALLAHQ NGLRKRSQRG ETRRTRNLGS
     QQGAVGRMAQ RYGRRNQQRS QTAFWPRTPI PSMELLSGGR GETGKTHSGK GI