VIF_HV1Z6
ID VIF_HV1Z6 Reviewed; 188 AA.
AC P04596;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Virion infectivity factor {ECO:0000255|HAMAP-Rule:MF_04081};
DE Short=Vif {ECO:0000255|HAMAP-Rule:MF_04081};
DE AltName: Full=SOR protein {ECO:0000255|HAMAP-Rule:MF_04081};
DE Contains:
DE RecName: Full=p17 {ECO:0000255|HAMAP-Rule:MF_04081};
DE Contains:
DE RecName: Full=p7 {ECO:0000255|HAMAP-Rule:MF_04081};
GN Name=vif {ECO:0000255|HAMAP-Rule:MF_04081};
OS Human immunodeficiency virus type 1 group M subtype D (isolate Z6) (HIV-1).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX NCBI_TaxID=11708;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=3036660; DOI=10.1016/0378-1119(87)90396-9;
RA Srinivasan A., Anand R., York D., Ranganathan P., Feorino P.,
RA Schochetman G., Curran J., Kalyanaraman V.S., Luciw P.A.,
RA Sanchez-Pescador R.;
RT "Molecular characterization of human immunodeficiency virus from Zaire:
RT nucleotide sequence analysis identifies conserved and variable domains in
RT the envelope gene.";
RL Gene 52:71-82(1987).
RN [2]
RP REVIEW.
RX PubMed=15177194; DOI=10.1016/j.molmed.2004.04.008;
RA Rose K.M., Marin M., Kozak S.L., Kabat D.;
RT "The viral infectivity factor (Vif) of HIV-1 unveiled.";
RL Trends Mol. Med. 10:291-297(2004).
CC -!- FUNCTION: Counteracts the innate antiviral activity of host APOBEC3F
CC and APOBEC3G. Forms a complex with host APOBEC3F and APOBEC3G thus
CC preventing the entry of these lethally hypermutating enzymes into
CC progeny virions. Recruits an active E3 ubiquitin ligase complex
CC composed of elongin BC, CUL5, and RBX2 to induce polyubiquitination of
CC APOBEC3G and APOBEC3F. In turn, they are directed to the 26S proteasome
CC for degradation. Vif interaction with APOBEC3G also blocks its cytidine
CC deaminase activity in a proteasome-independent manner, suggesting a
CC dual inhibitory mechanism. May interact directly with APOBEC3G mRNA in
CC order to inhibit its translation. Seems to play a role in viral
CC morphology by affecting the stability of the viral nucleoprotein core.
CC Finally, Vif also contributes to the G2 cell cycle arrest observed in
CC HIV infected cells. {ECO:0000255|HAMAP-Rule:MF_04081}.
CC -!- SUBUNIT: Homomultimer; in vitro and presumably in vivo. Interacts with
CC viral RNA and Pr55Gag precursor; these interactions mediate Vif
CC incorporation into the virion. Interacts with the viral reverse
CC transcriptase. Interacts with human APOBEC3F and APOBEC3G. Interacts
CC with host UBCE7IP1 isoform 3/ZIN and possibly with SAT. Interacts with
CC host tyrosine kinases HCK and FYN; these interactions may decrease
CC level of phosphorylated APOBEC3G incorporation into virions. Interacts
CC with host ABCE1; this interaction may play a role in protecting viral
CC RNA from damage during viral assembly. Forms an E3 ligase complex by
CC interacting with host CUL5 and elongin BC complex (ELOB and ELOC).
CC Interacts with host MDM2; this interaction targets Vif for degradation
CC by the proteasome. {ECO:0000255|HAMAP-Rule:MF_04081}.
CC -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04081}.
CC Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04081}; Peripheral
CC membrane protein {ECO:0000255|HAMAP-Rule:MF_04081}; Cytoplasmic side
CC {ECO:0000255|HAMAP-Rule:MF_04081}. Virion {ECO:0000255|HAMAP-
CC Rule:MF_04081}. Note=In the cytoplasm, 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. Incorporated in virions at a ratio of
CC approximately 7 to 20 molecules per virion. {ECO:0000255|HAMAP-
CC Rule:MF_04081}.
CC -!- INDUCTION: Expressed late during infection in a Rev-dependent manner.
CC {ECO:0000255|HAMAP-Rule:MF_04081}.
CC -!- DOMAIN: The BC-like-box motif mediates the interaction with elongin BC
CC complex. {ECO:0000255|HAMAP-Rule:MF_04081}.
CC -!- DOMAIN: The HCCH motif (H-x(5)-C-x(18)-C-x(5)-H) mediates the
CC interaction with CUL5. {ECO:0000255|HAMAP-Rule:MF_04081}.
CC -!- PTM: Processed in virion by the viral protease. {ECO:0000255|HAMAP-
CC Rule:MF_04081}.
CC -!- PTM: Highly phosphorylated on serine and threonine residues.
CC {ECO:0000255|HAMAP-Rule:MF_04081}.
CC -!- PTM: Polyubiquitinated and degraded by the proteasome in the presence
CC of APOBEC3G. {ECO:0000255|HAMAP-Rule:MF_04081}.
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 {ECO:0000255|HAMAP-Rule:MF_04081}.
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 {ECO:0000255|HAMAP-Rule:MF_04081}.
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. {ECO:0000255|HAMAP-Rule:MF_04081}.
CC -!- SIMILARITY: Belongs to the primate lentivirus group Vif protein family.
CC {ECO:0000255|HAMAP-Rule:MF_04081}.
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DR EMBL; K03458; AAA45379.1; -; Genomic_RNA.
DR PIR; B26192; ASLJZR.
DR SMR; P04596; -.
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-UniRule.
DR GO; GO:0044423; C:virion component; IEA:UniProtKB-UniRule.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0019058; P:viral life cycle; IEA:InterPro.
DR HAMAP; MF_04081; HIV_VIF; 1.
DR InterPro; IPR000475; Vif.
DR Pfam; PF00559; Vif; 1.
DR PRINTS; PR00349; VIRIONINFFCT.
PE 3: Inferred from homology;
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..188
FT /note="Virion infectivity factor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04081"
FT /id="PRO_0000043068"
FT CHAIN 1..150
FT /note="p17"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04081"
FT /id="PRO_0000043069"
FT CHAIN 151..188
FT /note="p7"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04081"
FT /id="PRO_0000043070"
FT REGION 14..17
FT /note="Interaction with host APOBEC3F; F1-box"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04081"
FT REGION 40..44
FT /note="Interaction with host APOBEC3G; G-box"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04081"
FT REGION 54..72
FT /note="Interaction with host APOBEC3F and APOBEC3G; FG-box"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04081"
FT REGION 74..79
FT /note="Interaction with host APOBEC3F; F2-box"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04081"
FT REGION 75..114
FT /note="RNA-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04081"
FT REGION 151..164
FT /note="Multimerization"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04081"
FT REGION 166..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 171..172
FT /note="Membrane association"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04081"
FT MOTIF 108..139
FT /note="HCCH motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04081"
FT MOTIF 144..153
FT /note="BC-box-like motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04081"
FT SITE 150..151
FT /note="Cleavage in virion (by viral protease)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04081"
FT MOD_RES 96
FT /note="Phosphothreonine; by host MAP4K1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04081"
FT MOD_RES 144
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04081"
FT MOD_RES 165
FT /note="Phosphoserine; by host MAP4K1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04081"
SQ SEQUENCE 188 AA; 22159 MW; E3B67D89E0ACDB4F CRC64;
MENRWQVMIV WQVDRMRIRT WKSLVKHHMY VSKKASRWFY RHHYDSPHPK ISSEVHIPLG
EARLVVKTYW GLHTGERDWH LGQGVSIEWR KRRYSTQVDP GLADQLIHMY YFDCFSEAAI
RKAILGHIVS HRCEYQAGHS KVGSLQYLAL TALIAPKKIK PPLPSVRKLT EDRWNKPQKT
KGHKGAIQ
