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Database: UniProt
Entry: VIF_HV1H2
LinkDB: VIF_HV1H2
Original site: VIF_HV1H2 
ID   VIF_HV1H2               Reviewed;         192 AA.
AC   P69723; P03401;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   13-AUG-1987, sequence version 1.
DT   02-DEC-2020, entry version 106.
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 B (isolate HXB2)
OS   (HIV-1).
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX   NCBI_TaxID=11706;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=3040055; DOI=10.1089/aid.1987.3.57;
RA   Ratner L., Fisher A., Jagodzinski L.L., Mitsuya H., Liou R.-S., Gallo R.C.,
RA   Wong-Staal F.;
RT   "Complete nucleotide sequences of functional clones of the AIDS virus.";
RL   AIDS Res. Hum. Retroviruses 3:57-69(1987).
RN   [2]
RP   SUBCELLULAR LOCATION.
RX   PubMed=8289374; DOI=10.1128/jvi.68.2.704-712.1994;
RA   Goncalves J., Jallepalli P., Gabuzda D.H.;
RT   "Subcellular localization of the Vif protein of human immunodeficiency
RT   virus type 1.";
RL   J. Virol. 68:704-712(1994).
RN   [3]
RP   MUTAGENESIS OF 157-LYS--LYS-160 AND 173-ARG--ARG-184.
RX   PubMed=7474141; DOI=10.1128/jvi.69.11.7196-7204.1995;
RA   Goncalves J., Shi B., Yang X., Gabuzda D.;
RT   "Biological activity of human immunodeficiency virus type 1 Vif requires
RT   membrane targeting by C-terminal basic domains.";
RL   J. Virol. 69:7196-7204(1995).
RN   [4]
RP   SUBCELLULAR LOCATION.
RX   PubMed=8523563; DOI=10.1128/jvi.70.1.494-507.1996;
RA   Karczewski M.K., Strebel K.;
RT   "Cytoskeleton association and virion incorporation of the human
RT   immunodeficiency virus type 1 Vif protein.";
RL   J. Virol. 70:494-507(1996).
RN   [5]
RP   PHOSPHORYLATION AT SER-144; THR-155 AND THR-188, AND MUTAGENESIS OF
RP   SER-144.
RX   PubMed=8626571; DOI=10.1074/jbc.271.17.10121;
RA   Yang X., Goncalves J., Gabuzda D.;
RT   "Phosphorylation of Vif and its role in HIV-1 replication.";
RL   J. Biol. Chem. 271:10121-10129(1996).
RN   [6]
RP   FUNCTION.
RX   PubMed=8970997; DOI=10.1128/jvi.70.12.8701-8709.1996;
RA   Goncalves J., Korin Y., Zack J., Gabuzda D.;
RT   "Role of Vif in human immunodeficiency virus type 1 reverse
RT   transcription.";
RL   J. Virol. 70:8701-8709(1996).
RN   [7]
RP   INCORPORATION IN THE VIRION.
RX   PubMed=8709234; DOI=10.1128/jvi.70.9.6106-6111.1996;
RA   Camaur D., Trono D.;
RT   "Characterization of human immunodeficiency virus type 1 Vif particle
RT   incorporation.";
RL   J. Virol. 70:6106-6111(1996).
RN   [8]
RP   INTERACTION WITH PR55GAG.
RX   PubMed=9371595; DOI=10.1128/jvi.71.12.9358-9365.1997;
RA   Bouyac M., Courcoul M., Bertoia G., Baudat Y., Gabuzda D., Blanc D.,
RA   Chazal N., Boulanger P., Sire J., Vigne R., Spire B.;
RT   "Human immunodeficiency virus type 1 Vif protein binds to the Pr55Gag
RT   precursor.";
RL   J. Virol. 71:9358-9365(1997).
RN   [9]
RP   PHOSPHORYLATION AT THR-96 AND SER-165 BY MAP4K1, PROTEIN SEQUENCE OF
RP   159-164 AND 94-98, AND MUTAGENESIS OF THR-96.
RX   PubMed=9792705; DOI=10.1074/jbc.273.45.29879;
RA   Yang X., Gabuzda D.;
RT   "Mitogen-activated protein kinase phosphorylates and regulates the HIV-1
RT   Vif protein.";
RL   J. Biol. Chem. 273:29879-29887(1998).
RN   [10]
RP   FUNCTION.
RX   PubMed=14564014; DOI=10.1126/science.1089591;
RA   Yu X., Yu Y., Liu B., Luo K., Kong W., Mao P., Yu X.F.;
RT   "Induction of APOBEC3G ubiquitination and degradation by an HIV-1 Vif-Cul5-
RT   SCF complex.";
RL   Science 302:1056-1060(2003).
RN   [11]
RP   FUNCTION, AND MUTAGENESIS OF CYS-114; CYS-133 AND THR-188.
RX   PubMed=14672928; DOI=10.1074/jbc.m313093200;
RA   Mehle A., Strack B., Ancuta P., Zhang C., McPike M., Gabuzda D.;
RT   "Vif overcomes the innate antiviral activity of APOBEC3G by promoting its
RT   degradation in the ubiquitin-proteasome pathway.";
RL   J. Biol. Chem. 279:7792-7798(2004).
RN   [12]
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).
RN   [13]
RP   INTERACTION WITH HOST HCK AND FYN.
RX   PubMed=15752743; DOI=10.1016/j.bbrc.2005.02.057;
RA   Douaisi M., Dussart S., Courcoul M., Bessou G., Lerner E.C., Decroly E.,
RA   Vigne R.;
RT   "The tyrosine kinases Fyn and Hck favor the recruitment of tyrosine-
RT   phosphorylated APOBEC3G into vif-defective HIV-1 particles.";
RL   Biochem. Biophys. Res. Commun. 329:917-924(2005).
RN   [14]
RP   INTERACTION WITH HOST APOBEC3F AND APOBEC3G.
RX   PubMed=17522216; DOI=10.1128/jvi.00395-07;
RA   Russell R.A., Pathak V.K.;
RT   "Identification of two distinct human immunodeficiency virus type 1 Vif
RT   determinants critical for interactions with human APOBEC3G and APOBEC3F.";
RL   J. Virol. 81:8201-8210(2007).
RN   [15]
RP   FUNCTION IN CELL CYCLE ARREST.
RX   PubMed=17056089; DOI=10.1016/j.virol.2006.09.026;
RA   Wang J., Shackelford J.M., Casella C.R., Shivers D.K., Rapaport E.L.,
RA   Liu B., Yu X.F., Finkel T.H.;
RT   "The Vif accessory protein alters the cell cycle of human immunodeficiency
RT   virus type 1 infected cells.";
RL   Virology 359:243-252(2007).
RN   [16]
RP   INTERACTION WITH HOST APOBEC3F AND APOBEC3G.
RX   PubMed=18619467; DOI=10.1016/j.jmb.2008.06.061;
RA   He Z., Zhang W., Chen G., Xu R., Yu X.F.;
RT   "Characterization of conserved motifs in HIV-1 Vif required for APOBEC3G
RT   and APOBEC3F interaction.";
RL   J. Mol. Biol. 381:1000-1011(2008).
RN   [17]
RP   INTERACTION WITH HOST MDM2.
RX   PubMed=19128510; DOI=10.1186/1742-4690-6-1;
RA   Izumi T., Takaori-Kondo A., Shirakawa K., Higashitsuji H., Itoh K., Io K.,
RA   Matsui M., Iwai K., Kondoh H., Sato T., Tomonaga M., Ikeda S., Akari H.,
RA   Koyanagi Y., Fujita J., Uchiyama T.;
RT   "MDM2 is a novel E3 ligase for HIV-1 Vif.";
RL   Retrovirology 6:1-1(2009).
RN   [18]
RP   INTERACTION WITH THE REVERSE TRANSCRIPTASE.
RX   PubMed=19369217; DOI=10.1093/nar/gkp226;
RA   Kataropoulou A., Bovolenta C., Belfiore A., Trabatti S., Garbelli A.,
RA   Porcellini S., Lupo R., Maga G.;
RT   "Mutational analysis of the HIV-1 auxiliary protein Vif identifies
RT   independent domains important for the physical and functional interaction
RT   with HIV-1 reverse transcriptase.";
RL   Nucleic Acids Res. 37:3660-3669(2009).
RN   [19]
RP   FUNCTION.
RX   PubMed=19910370; DOI=10.1093/nar/gkp1009;
RA   Mercenne G., Bernacchi S., Richer D., Bec G., Henriet S., Paillart J.C.,
RA   Marquet R.;
RT   "HIV-1 Vif binds to APOBEC3G mRNA and inhibits its translation.";
RL   Nucleic Acids Res. 38:633-646(2010).
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       ECO:0000269|PubMed:14564014, ECO:0000269|PubMed:14672928,
CC       ECO:0000269|PubMed:17056089, ECO:0000269|PubMed:19910370,
CC       ECO:0000269|PubMed:8970997}.
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       ECO:0000269|PubMed:15752743, ECO:0000269|PubMed:17522216,
CC       ECO:0000269|PubMed:18619467, ECO:0000269|PubMed:19128510,
CC       ECO:0000269|PubMed:19369217, ECO:0000269|PubMed:9371595}.
CC   -!- INTERACTION:
CC       P69723; P69723: vif; NbExp=4; IntAct=EBI-15528966, EBI-15528966;
CC       P69723; Q9HC16: APOBEC3G; Xeno; NbExp=3; IntAct=EBI-15528966, EBI-717839;
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: Highly phosphorylated on serine and threonine residues (By
CC       similarity). Thr-96 and Ser-165 are phosphorylated by the mitogen
CC       activated kinase MAP4K1. As the HIV-1 replication can be activated by
CC       stress and mitogens, these phosphorylations could be involved in this
CC       process. Ser-144 phosphorylation may inhibit elongin BC complex
CC       binding. {ECO:0000255|HAMAP-Rule:MF_04081, ECO:0000269|PubMed:8626571,
CC       ECO:0000269|PubMed:9792705}.
CC   -!- PTM: Processed in virion by the viral protease. {ECO:0000255|HAMAP-
CC       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, ECO:0000305}.
CC   -!- WEB RESOURCE: Name=BioAfrica HIV proteomics resource; Note=Vif entry;
CC       URL="http://www.bioafrica.net/proteomics/VIFprot.html";
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DR   EMBL; K03455; AAB50260.1; -; Genomic_RNA.
DR   RefSeq; NP_057851.1; NC_001802.1.
DR   SMR; P69723; -.
DR   BioGRID; 1205539; 63.
DR   DIP; DIP-61318N; -.
DR   IntAct; P69723; 5.
DR   iPTMnet; P69723; -.
DR   PRIDE; P69723; -.
DR   GeneID; 155459; -.
DR   KEGG; vg:155459; -.
DR   Reactome; R-HSA-162585; Uncoating of the HIV Virion.
DR   Reactome; R-HSA-162588; Budding and maturation of HIV virion.
DR   Reactome; R-HSA-162592; Integration of provirus.
DR   Reactome; R-HSA-162594; Early Phase of HIV Life Cycle.
DR   Reactome; R-HSA-164516; Minus-strand DNA synthesis.
DR   Reactome; R-HSA-164525; Plus-strand DNA synthesis.
DR   Reactome; R-HSA-164843; 2-LTR circle formation.
DR   Reactome; R-HSA-173107; Binding and entry of HIV virion.
DR   Reactome; R-HSA-175474; Assembly Of The HIV Virion.
DR   Reactome; R-HSA-175567; Integration of viral DNA into host genomic DNA.
DR   Reactome; R-HSA-177539; Autointegration results in viral DNA circles.
DR   Reactome; R-HSA-180585; Vif-mediated degradation of APOBEC3G.
DR   Reactome; R-HSA-180689; APOBEC3G mediated resistance to HIV-1 infection.
DR   Reactome; R-HSA-180910; Vpr-mediated nuclear import of PICs.
DR   PRO; PR:P69723; -.
DR   Proteomes; UP000002241; 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-UniRule.
DR   GO; GO:0019012; C:virion; IEA:UniProtKB-SubCell.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0075713; P:establishment of integrated proviral latency; TAS:Reactome.
DR   GO; GO:0019064; P:fusion of virus membrane with host plasma membrane; TAS:Reactome.
DR   GO; GO:0051169; P:nuclear transport; TAS:Reactome.
DR   GO; GO:0006278; P:RNA-dependent DNA biosynthetic process; TAS:Reactome.
DR   GO; GO:0019061; P:uncoating of virus; TAS:Reactome.
DR   GO; GO:0019058; P:viral life cycle; TAS:Reactome.
DR   GO; GO:0019068; P:virion assembly; TAS:Reactome.
DR   DisProt; DP00875; -.
DR   HAMAP; MF_04081; HIV_VIF; 1.
DR   InterPro; IPR000475; Vif.
DR   Pfam; PF00559; Vif; 1.
DR   PRINTS; PR00349; VIRIONINFFCT.
PE   1: Evidence at protein level;
KW   AIDS; Direct protein sequencing; Host cell membrane; Host cytoplasm;
KW   Host membrane; Host-virus interaction; Membrane; Phosphoprotein;
KW   Reference proteome; RNA-binding; Ubl conjugation; Ubl conjugation pathway;
KW   Virion.
FT   CHAIN           1..192
FT                   /note="Virion infectivity factor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04081"
FT                   /id="PRO_0000042759"
FT   CHAIN           1..150
FT                   /note="p17"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04081"
FT                   /id="PRO_0000042760"
FT   CHAIN           151..192
FT                   /note="p7"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04081"
FT                   /id="PRO_0000042761"
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          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                   ECO:0000269|PubMed:9792705"
FT   MOD_RES         144
FT                   /note="Phosphoserine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04081,
FT                   ECO:0000269|PubMed:8626571"
FT   MOD_RES         155
FT                   /note="Phosphothreonine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04081,
FT                   ECO:0000269|PubMed:8626571"
FT   MOD_RES         165
FT                   /note="Phosphoserine; by host MAP4K1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04081,
FT                   ECO:0000269|PubMed:9792705"
FT   MOD_RES         188
FT                   /note="Phosphothreonine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04081,
FT                   ECO:0000269|PubMed:8626571"
FT   MUTAGEN         96
FT                   /note="T->A: 90% loss of reverse transcriptase activity in
FT                   virions; no effect on the ability to decrease APOBEC3G
FT                   level."
FT                   /evidence="ECO:0000269|PubMed:9792705"
FT   MUTAGEN         96
FT                   /note="T->E: Complete loss of viral infectivity in non
FT                   permissive cells; no effect on the ability to decrease
FT                   APOBEC3G level."
FT                   /evidence="ECO:0000269|PubMed:9792705"
FT   MUTAGEN         114
FT                   /note="C->S: Reduces the ability to decrease APOBEC3G
FT                   level; when associated with S-133."
FT                   /evidence="ECO:0000269|PubMed:14672928"
FT   MUTAGEN         133
FT                   /note="C->S: Reduces the ability to decrease APOBEC3G
FT                   level; when associated with S-114."
FT                   /evidence="ECO:0000269|PubMed:14672928"
FT   MUTAGEN         144
FT                   /note="S->A: 90% loss of viral infectivity in non
FT                   permissive cells; no effect on the ability to decrease
FT                   APOBEC3G level."
FT                   /evidence="ECO:0000269|PubMed:8626571"
FT   MUTAGEN         157..160
FT                   /note="KKIK->AAIA: 75% loss of membrane binding; decrease
FT                   Pr55Gag binding."
FT                   /evidence="ECO:0000269|PubMed:7474141"
FT   MUTAGEN         173..179
FT                   /note="RWNKPQK->AWNAPQA: 40% loss of membrane binding;
FT                   decrease Pr55Gag binding."
FT   MUTAGEN         179..184
FT                   /note="KTKGHR->ATAGHA: 25% loss of membrane binding;
FT                   decrease Pr55Gag binding."
FT   MUTAGEN         188
FT                   /note="T->A: No effect on the ability to decrease APOBEC3G
FT                   level."
FT                   /evidence="ECO:0000269|PubMed:14672928"
SQ   SEQUENCE   192 AA;  22513 MW;  D22589F3955CBE40 CRC64;
     MENRWQVMIV WQVDRMRIRT WKSLVKHHMY VSGKARGWFY RHHYESPHPR ISSEVHIPLG
     DARLVITTYW GLHTGERDWH LGQGVSIEWR KKRYSTQVDP ELADQLIHLY YFDCFSDSAI
     RKALLGHIVS PRCEYQAGHN KVGSLQYLAL AALITPKKIK PPLPSVTKLT EDRWNKPQKT
     KGHRGSHTMN GH
//
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