VIF_SIVM1
ID VIF_SIVM1 Reviewed; 214 AA.
AC P05903;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1988, sequence version 1.
DT 29-SEP-2021, entry version 93.
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 Mm142-83) (SIV-mac) (Simian
OS immunodeficiency virus rhesus monkey).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX NCBI_TaxID=11733;
OH NCBI_TaxID=9527; Cercopithecidae (Old World monkeys).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3649576; DOI=10.1038/328543a0;
RA Chakrabarti L., Guyader M., Alizon M., Daniel M.D., Desrosiers R.C.,
RA Tiollais P., Sonigo P.;
RT "Sequence of simian immunodeficiency virus from macaque and its
RT relationship to other human and simian retroviruses.";
RL Nature 328:543-547(1987).
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 a macaque isolate.
CC -!- SIMILARITY: Belongs to the primate lentivirus group Vif protein family.
CC {ECO:0000305}.
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DR EMBL; Y00277; CAA68381.1; -; Genomic_DNA.
DR SMR; P05903; -.
DR Proteomes; UP000007220; 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; Ubl conjugation; Ubl conjugation pathway; Virion.
FT CHAIN 1..214
FT /note="Virion infectivity factor"
FT /id="PRO_0000085331"
FT REGION 154..166
FT /note="Multimerization"
FT /evidence="ECO:0000250"
FT REGION 180..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 110..141
FT /note="HCCH motif"
FT /evidence="ECO:0000250"
FT MOTIF 147..156
FT /note="BC-box-like motif"
FT /evidence="ECO:0000250"
FT COMPBIAS 180..194
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 98
FT /note="Phosphothreonine; by host"
FT /evidence="ECO:0000250"
FT MOD_RES 147
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000250"
SQ SEQUENCE 214 AA; 25329 MW; E2DA71A380D595C8 CRC64;
MEEEKRWIVV PTWRIPERLE RWHSLIKYLK YKTKDLQKAC YVPHHKVGWA WWTCSRVIFP
LQEGSHLEVQ GYWNLTPERG WLSTYAVRIT WYSKDFWTDV TPEYADILLH STYFPCFTAG
EVRRAIRGER LLSCCRFPRA HKHQVPSLQY LALRVVSHVR SQGENPTWKQ WRRDNRRSLR
VAKQNSRGDK QRGGKPPTEG ANFPGLAKVL GILA