VIF_SIVTA
ID VIF_SIVTA Reviewed; 238 AA.
AC P89905;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 23-FEB-2022, entry version 87.
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.tantalus (SIV-agm.tan) (Simian
OS immunodeficiency virus African green monkey tantalus).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX NCBI_TaxID=349692;
OH NCBI_TaxID=60712; Chlorocebus tantalus (Tantalus monkey) (Cercopithecus tantalus).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=tantalus-1;
RX PubMed=9123848; DOI=10.1006/viro.1996.8387;
RA Soares M.A., Robertson D.L., Hui H., Allan J.S., Shaw G.M., Hahn B.H.;
RT "A full-length and replication-competent proviral clone of SIVAGM from
RT tantalus monkeys.";
RL Virology 228:394-399(1997).
RN [2]
RP INTERACTION WITH HUMAN CUL5, AND MUTAGENESIS OF HIS-111; CYS-117; CYS-135
RP AND HIS-141.
RX PubMed=16076960; DOI=10.1073/pnas.0502440102;
RA Luo K., Xiao Z., Ehrlich E., Yu Y., Liu B., Zheng S., Yu X.-F.;
RT "Primate lentiviral virion infectivity factors are substrate receptors that
RT assemble with cullin 5-E3 ligase through a HCCH motif to suppress
RT APOBEC3G.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:11444-11449(2005).
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; U58991; AAC57053.1; -; Genomic_DNA.
DR SMR; P89905; -.
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 1: Evidence at protein level;
KW Host cell membrane; Host cytoplasm; Host membrane; Host-virus interaction;
KW Membrane; Phosphoprotein; Ubl conjugation; Ubl conjugation pathway; Virion.
FT CHAIN 1..238
FT /note="Virion infectivity factor"
FT /id="PRO_0000085335"
FT REGION 159..175
FT /note="Multimerization"
FT /evidence="ECO:0000250"
FT REGION 188..214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 111..146
FT /note="HCCH motif"
FT /evidence="ECO:0000250"
FT MOTIF 152..161
FT /note="BC-box-like motif"
FT /evidence="ECO:0000250"
FT COMPBIAS 199..213
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 99
FT /note="Phosphothreonine; by host"
FT /evidence="ECO:0000250"
FT MOD_RES 152
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000250"
FT MUTAGEN 111
FT /note="H->L: Complete loss of interaction with CUL5."
FT /evidence="ECO:0000269|PubMed:16076960"
FT MUTAGEN 117
FT /note="C->S: Complete loss of interaction with CUL5."
FT /evidence="ECO:0000269|PubMed:16076960"
FT MUTAGEN 135
FT /note="C->S: Complete loss of interaction with CUL5."
FT /evidence="ECO:0000269|PubMed:16076960"
FT MUTAGEN 141
FT /note="H->L: Complete loss of interaction with CUL5."
FT /evidence="ECO:0000269|PubMed:16076960"
SQ SEQUENCE 238 AA; 28169 MW; 0E15A107E0627762 CRC64;
MEREKLWVTR LTWRVSGEHI DKWKGIVKYH MRNRLQDWTY LMHYQCGWAW YTCSRFLIPL
GGEGKIVVDC YWHLTPEQGW LSTYAVAISF ENWQNTYKTE VTPDVADHMI HCHYFPCFTD
RAIQQAIRGE SFLWCTYKEG HVAENHWGQV RSLQFLALTV YTDFLRNGRR KRFQGKKTRM
VRNLGSQQGA VGRMIKRHGS RTQSGSTTPF WERTPLPSME LLSGRRGKEW GTNDRKGL
