VIF_SIVTN
ID VIF_SIVTN Reviewed; 198 AA.
AC Q8AII0;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 23-FEB-2022, entry version 67.
DE RecName: Full=Virion infectivity factor;
DE Short=Vif;
OS Simian immunodeficiency virus (isolate TAN1) (SIV-cpz) (Chimpanzee
OS immunodeficiency virus).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX NCBI_TaxID=388910;
OH NCBI_TaxID=9598; Pan troglodytes (Chimpanzee).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=12525658; DOI=10.1128/jvi.77.3.2233-2242.2003;
RA Santiago M.L., Bibollet-Ruche F., Bailes E., Kamenya S., Muller M.N.,
RA Lukasik M., Pusey A.E., Collins D.A., Wrangham R.W., Goodall J., Shaw G.M.,
RA Sharp P.M., Hahn B.H.;
RT "Amplification of a complete simian immunodeficiency virus genome from
RT fecal RNA of a wild chimpanzee.";
RL J. Virol. 77:2233-2242(2003).
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.
CC Interacts with host ABCE1, which seems to be involved in lentiviruses
CC capsid formation and displays RNase L inhibitor activity. This
CC interaction may play a role in protecting viral RNA from damage during
CC viral assembly. May interact with host SAT, which is a regulator of
CC polyamine cell level. This interaction may be relevant since polyamines
CC affect viral RNA properties (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homomultimer; in vitro and presumably in vivo. Interacts with
CC viral Pr55Gag precursor, host APOBEC3G, UBCE7IP1 isoform 3/ZIN, ABCE1
CC and possibly with SAT. Forms an E3 ligase complex by interacting with
CC host CUL5 and elongin BC complex (ELOB and ELOC) (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Host cytoplasm. Host cell membrane; Peripheral
CC membrane protein; Cytoplasmic side. Virion {ECO:0000250}. Note=Seems to
CC colocalize with intermediate filament vimentin. A fraction is
CC associated with the cytoplasmic side of cellular membranes, presumably
CC via the interaction with Pr55Gag precursor.
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: Highly phosphorylated on serine and threonine residues. Thr-97 and
CC Ser-171 are phosphorylated by the mitogen activated kinase MAP4K1 (By
CC similarity). {ECO:0000250}.
CC -!- PTM: Polyubiquitinated and degraded by the proteasome in the presence
CC of APOBEC3G. {ECO:0000250}.
CC -!- MISCELLANEOUS: Required for replication in 'nonpermissive' cells,
CC including primary T-cells, macrophages and certain T-cell lines, but is
CC dispensable for replication in 'permissive' cell lines, such as 293T
CC cells. In nonpermissive cells, Vif-defective viruses can produce
CC virions, but they fail to complete reverse transcription and cannot
CC successfully infect new cells (By similarity). {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 (By similarity). {ECO:0000250}.
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; AF447763; AAO13961.1; -; Genomic_RNA.
DR SMR; Q8AII0; -.
DR Proteomes; UP000007222; 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:0003723; F:RNA binding; 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; RNA-binding; Ubl conjugation;
KW Ubl conjugation pathway; Virion.
FT CHAIN 1..198
FT /note="Virion infectivity factor"
FT /evidence="ECO:0000250"
FT /id="PRO_0000248293"
FT REGION 76..115
FT /note="RNA-binding"
FT /evidence="ECO:0000255"
FT REGION 152..170
FT /note="Multimerization"
FT /evidence="ECO:0000250"
FT REGION 159..198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 177..178
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 COMPBIAS 172..190
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 97
FT /note="Phosphothreonine; by host MAP4K1"
FT /evidence="ECO:0000250"
FT MOD_RES 145
FT /note="Phosphothreonine; by host"
FT /evidence="ECO:0000250"
FT MOD_RES 171
FT /note="Phosphoserine; by host MAP4K1"
FT /evidence="ECO:0000250"
SQ SEQUENCE 198 AA; 23383 MW; 65B2A1E82CC5040E CRC64;
MENRWQVQVV WMIDRMRLRT WTSLVKHHIF TTKCCKDWKY RHHYETDTPK RAGEIHIPLT
ERSKLVVLHY WGLACGERPW HLGHGIGLEW RQGKYSTQID PETADQLIHT RYFTCFAAGA
VRQAILGERI LTFCHFQSGH RQVGTLQFLA FRKVVESQDK QPKGPRRPLP SVTKLTEDRW
NKHRTTTGRR ENHTLSGC
