Database: UniProt
Entry: C7TQ88_9HIV1
LinkDB: C7TQ88_9HIV1
Original site: C7TQ88_9HIV1 
ID   C7TQ88_9HIV1            Unreviewed;       192 AA.
AC   C7TQ88;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   10-FEB-2021, entry version 52.
DE   RecName: Full=Virion infectivity factor {ECO:0000256|HAMAP-Rule:MF_04081};
DE            Short=Vif {ECO:0000256|HAMAP-Rule:MF_04081};
DE   AltName: Full=SOR protein {ECO:0000256|HAMAP-Rule:MF_04081};
DE   Contains:
DE     RecName: Full=p17 {ECO:0000256|HAMAP-Rule:MF_04081};
DE   Contains:
DE     RecName: Full=p7 {ECO:0000256|HAMAP-Rule:MF_04081};
GN   Name=vif {ECO:0000256|HAMAP-Rule:MF_04081,
GN   ECO:0000313|EMBL:CAT00601.1};
OS   HIV-1 M_02CD.LBTB084.
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX   NCBI_TaxID=576901 {ECO:0000313|EMBL:CAT00601.1, ECO:0000313|Proteomes:UP000120202};
RN   [1] {ECO:0000313|Proteomes:UP000120202}
RX   PubMed=19678767; DOI=10.1089/aid.2008.0283;
RA   Vidal N., Bazepeo S.E., Mulanga C., Delaporte E., Peeters M.;
RT   "Genetic characterization of eight full-length HIV type 1 genomes from the
RT   Democratic Republic of Congo (DRC) reveal a new subsubtype, A5, in the A
RT   radiation that predominates in the recombinant structure of CRF26_A5U.";
RL   AIDS Res. Hum. Retroviruses 25:823-832(2009).
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:0000256|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:0000256|HAMAP-Rule:MF_04081}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004413};
CC       Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004413};
CC       Cytoplasmic side {ECO:0000256|ARBA:ARBA00004413}. Host cell membrane
CC       {ECO:0000256|ARBA:ARBA00004501, ECO:0000256|HAMAP-Rule:MF_04081};
CC       Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004501,
CC       ECO:0000256|HAMAP-Rule:MF_04081}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004501, ECO:0000256|HAMAP-Rule:MF_04081}. Host
CC       cytoplasm {ECO:0000256|HAMAP-Rule:MF_04081}. Virion {ECO:0000256|HAMAP-
CC       Rule:MF_04081}. Membrane {ECO:0000256|ARBA:ARBA00004287}; Peripheral
CC       membrane protein {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004287}. Note=In the cytoplasm, 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. Incorporated in virions at
CC       a ratio of approximately 7 to 20 molecules per virion.
CC       {ECO:0000256|HAMAP-Rule:MF_04081}.
CC   -!- INDUCTION: Expressed late during infection in a Rev-dependent manner.
CC       {ECO:0000256|HAMAP-Rule:MF_04081}.
CC   -!- DOMAIN: The BC-like-box motif mediates the interaction with elongin BC
CC       complex. {ECO:0000256|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:0000256|HAMAP-Rule:MF_04081}.
CC   -!- PTM: Highly phosphorylated on serine and threonine residues.
CC       {ECO:0000256|HAMAP-Rule:MF_04081}.
CC   -!- PTM: Polyubiquitinated and degraded by the proteasome in the presence
CC       of APOBEC3G. {ECO:0000256|HAMAP-Rule:MF_04081}.
CC   -!- PTM: Processed in virion by the viral protease. {ECO:0000256|HAMAP-
CC       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:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_04081}.
CC   -!- SIMILARITY: Belongs to the primate lentivirus group Vif protein family.
CC       {ECO:0000256|ARBA:ARBA00006372, ECO:0000256|HAMAP-Rule:MF_04081,
CC       ECO:0000256|RuleBase:RU003341}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_04081}.
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DR   EMBL; FM877781; CAT00601.1; -; Genomic_DNA.
DR   Proteomes; UP000120202; 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:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0019012; C:virion; IEA:UniProtKB-SubCell.
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.
PE   2: Evidence at transcript level;
KW   Host cell membrane {ECO:0000256|HAMAP-Rule:MF_04081};
KW   Host cytoplasm {ECO:0000256|ARBA:ARBA00023200, ECO:0000256|HAMAP-
KW   Rule:MF_04081}; Host membrane {ECO:0000256|HAMAP-Rule:MF_04081};
KW   Host-virus interaction {ECO:0000256|HAMAP-Rule:MF_04081};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_04081};
KW   Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_04081};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_04081};
KW   Ubl conjugation {ECO:0000256|ARBA:ARBA00022843, ECO:0000256|HAMAP-
KW   Rule:MF_04081};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786, ECO:0000256|HAMAP-
KW   Rule:MF_04081}; Virion {ECO:0000256|HAMAP-Rule:MF_04081}.
FT   CHAIN           1..192
FT                   /note="Virion infectivity factor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04081"
FT                   /id="PRO_5023231263"
FT   CHAIN           1..150
FT                   /note="p17"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04081"
FT                   /id="PRO_5023231264"
FT   CHAIN           151..192
FT                   /note="p7"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04081"
FT                   /id="PRO_5023231265"
FT   REGION          14..17
FT                   /note="Interaction with host APOBEC3F; F1-box"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04081"
FT   REGION          40..44
FT                   /note="Interaction with host APOBEC3G; G-box"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04081"
FT   REGION          54..72
FT                   /note="Interaction with host APOBEC3F and APOBEC3G; FG-box"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04081"
FT   REGION          74..79
FT                   /note="Interaction with host APOBEC3F; F2-box"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04081"
FT   REGION          75..114
FT                   /note="RNA-binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04081"
FT   REGION          151..164
FT                   /note="Multimerization"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04081"
FT   REGION          163..192
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          171..172
FT                   /note="Membrane association"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04081"
FT   MOTIF           108..139
FT                   /note="HCCH motif"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04081"
FT   MOTIF           144..153
FT                   /note="BC-box-like motif"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04081"
FT   COMPBIAS        163..186
FT                   /note="Polyampholyte"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            150..151
FT                   /note="Cleavage in virion (by viral protease)"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04081"
FT   MOD_RES         96
FT                   /note="Phosphothreonine; by host MAP4K1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04081"
FT   MOD_RES         144
FT                   /note="Phosphoserine; by host"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04081"
FT   MOD_RES         165
FT                   /note="Phosphoserine; by host MAP4K1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04081"
SQ   SEQUENCE   192 AA;  22937 MW;  BB8C6B5917D585E5 CRC64;
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