VIF_HV1SC
ID VIF_HV1SC Reviewed; 109 AA.
AC P05899;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1988, sequence version 1.
DT 29-SEP-2021, entry version 86.
DE RecName: Full=Virion infectivity factor;
DE Short=Vif;
DE AltName: Full=SOR protein;
DE Contains:
DE RecName: Full=p17;
DE Contains:
DE RecName: Full=p7;
DE Flags: Fragment;
GN Name=vif;
OS Human immunodeficiency virus type 1 group M subtype B (isolate SC) (HIV-1).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX NCBI_TaxID=11702;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=3369091; DOI=10.1016/0042-6822(88)90568-5;
RA Gurgo C., Guo H.-G., Franchini G., Aldovini A., Collalti E., Farrell K.,
RA Wong-Staal F., Gallo R.C., Reitz M.S. Jr.;
RT "Envelope sequences of two new United States HIV-1 isolates.";
RL Virology 164:531-536(1988).
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, human APOBEC3G, UBCE7IP1 isoform 3/ZIN, ABCE1
CC and possibly with SAT. Binds human HCK in vitro, but since this protein
CC does not seem to be expressed in CD4+ cells, the significance of this
CC interaction remains unclear. The interaction between Vif and APOBEC3G
CC is species-specific, which may play a role in restricting the
CC replication of HIV to humans. Forms an E3 ligase complex by interacting
CC with human CUL5 and elongin BC complex (ELOB and ELOC) (By similarity).
CC {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=In the cytoplasm, seems
CC to 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. Incorporated in virions at
CC a ratio of approximately 7 to 20 molecules per virion (By similarity).
CC {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. Thr-13 and
CC Ser-82 are phosphorylated by the mitogen activated kinase MAP4K1. As
CC the HIV-1 replication can be activated by stress and mitogens, these
CC phosphorylations could be involved in this process. Ser-61
CC phosphorylation may inhibit elongin BC complex binding (By similarity).
CC {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 -!- MISCELLANEOUS: HIV-1 lineages are divided in three main groups, M (for
CC Major), O (for Outlier), and N (for New, or Non-M, Non-O). The vast
CC majority of strains found worldwide belong to the group M. Group O
CC seems to be endemic to and largely confined to Cameroon and neighboring
CC countries in West Central Africa, where these viruses represent a small
CC minority of HIV-1 strains. The group N is represented by a limited
CC number of isolates from Cameroonian persons. The group M is further
CC subdivided in 9 clades or subtypes (A to D, F to H, J and K).
CC -!- MISCELLANEOUS: The SC isolate was taken from an ARC patient in 1984 in
CC Southern California.
CC -!- SIMILARITY: Belongs to the primate lentivirus group Vif protein family.
CC {ECO:0000305}.
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DR EMBL; M17450; AAA45059.1; -; Genomic_RNA.
DR SMR; P05899; -.
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 AIDS; Host cell membrane; Host cytoplasm; Host membrane;
KW Host-virus interaction; Membrane; Phosphoprotein; RNA-binding;
KW Ubl conjugation; Ubl conjugation pathway; Virion.
FT CHAIN <1..109
FT /note="Virion infectivity factor"
FT /id="PRO_0000085315"
FT CHAIN <1..67
FT /note="p17"
FT /evidence="ECO:0000250"
FT /id="PRO_0000297502"
FT CHAIN 68..109
FT /note="p7"
FT /evidence="ECO:0000250"
FT /id="PRO_0000297503"
FT REGION <1..31
FT /note="RNA-binding"
FT /evidence="ECO:0000255"
FT REGION 68..81
FT /note="Multimerization"
FT /evidence="ECO:0000250"
FT REGION 75..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 88..89
FT /note="Membrane association"
FT /evidence="ECO:0000250"
FT MOTIF 25..56
FT /note="HCCH motif"
FT /evidence="ECO:0000250"
FT MOTIF 61..70
FT /note="BC-box-like motif"
FT /evidence="ECO:0000250"
FT COMPBIAS 81..96
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 67..68
FT /note="Cleavage in virion (by viral protease)"
FT /evidence="ECO:0000250"
FT MOD_RES 13
FT /note="Phosphothreonine; by host MAP4K1"
FT /evidence="ECO:0000250"
FT MOD_RES 61
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000250"
FT MOD_RES 82
FT /note="Phosphoserine; by host MAP4K1"
FT /evidence="ECO:0000250"
FT MOD_RES 105
FT /note="Phosphothreonine; by host"
FT /evidence="ECO:0000250"
FT NON_TER 1
SQ SEQUENCE 109 AA; 12308 MW; 3D1BB3599F78B727 CRC64;
GVSIEWTKKR YSTQVDPDLA DRLIHLYYFD CFSESAIRNA ILGALVSGRC EYQAGHNKVG
SLQYLALTAL ITPKKTKPPL PSVRKLTEDR WNKPQKTKGH RGSHTMNGH
