VIF_HV1N5
ID VIF_HV1N5 Reviewed; 192 AA.
AC P12504;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 122.
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 NY5)
OS (HIV-1).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX NCBI_TaxID=11698;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Clone pNL4-3;
RA Buckler C.E., Buckler-White A.J., Willey R.L., McCoy J.;
RL Submitted (JUN-1988) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA Theodore T., Buckler-White A.J.;
RL Submitted (OCT-1992) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP INDUCTION.
RX PubMed=1830183; DOI=10.1016/0042-6822(91)90996-o;
RA Schwartz S., Felber B.K., Pavlakis G.N.;
RT "Expression of human immunodeficiency virus type 1 vif and vpr mRNAs is
RT Rev-dependent and regulated by splicing.";
RL Virology 183:677-686(1991).
RN [4]
RP ROLE IN VIRION MORPHOLOGY.
RX PubMed=8184544; DOI=10.1006/viro.1994.1300;
RA Hoglund S., Ohagen A., Lawrence K., Gabuzda D.;
RT "Role of vif during packing of the core of HIV-1.";
RL Virology 201:349-355(1994).
RN [5]
RP MUTAGENESIS OF 5-TRP-GLN-6; 12-GLN-VAL-13; 16-MET--ILE-18; 23-ARG-LEU-24;
RP 29-MET--ILE-31; 33-ARG-LYS-34; 38-TRP--TYR-40; 43-HIS-TYR-44;
RP 53-SER-GLU-54; 58-PRO-LEU-59; 69-TYR-TRP-70; 73-HIS-THR-74; 80-HIS-LEU-81;
RP 86-SER-ILE-87; 90-ARG--LYS-92; 97-GLN-VAL-98; 105-GLN--ILE-107;
RP 111-TYR-PHE-112; CYS-114; 121-ARG--THR-123; 127-ARG-ILE-128; CYS-133;
RP 135-TYR-GLN-136; 140-ASN-LYS-141; 144-SER--GLN-146; 147-TYR-LEU-148;
RP 156-PRO--GLN-158; LYS-157; 158-GLN--LYS-160; 161-PRO--LEU-164; SER-165;
RP VAL-166; 169-LEU-THR-170; 180-THR-LYS-181 AND 189-MET-ASN-190.
RX PubMed=10074113; DOI=10.1128/jvi.73.4.2675-2681.1999;
RA Simon J.H., Sheehy A.M., Carpenter E.A., Fouchier R.A., Malim M.H.;
RT "Mutational analysis of the human immunodeficiency virus type 1 Vif
RT protein.";
RL J. Virol. 73:2675-2681(1999).
RN [6]
RP MULTIMERIZATION.
RX PubMed=11071884; DOI=10.1074/jbc.m004895200;
RA Yang S., Sun Y., Zhang H.;
RT "The multimerization of human immunodeficiency virus type I Vif protein: a
RT requirement for Vif function in the viral life cycle.";
RL J. Biol. Chem. 276:4889-4893(2001).
RN [7]
RP INTERACTION WITH NUCLEOPROTEIN.
RX PubMed=11461998; DOI=10.1128/jvi.75.16.7252-7265.2001;
RA Khan M.A., Aberham C., Kao S., Akari H., Gorelick R., Bour S., Strebel K.;
RT "Human immunodeficiency virus type 1 Vif protein is packaged into the
RT nucleoprotein complex through an interaction with viral genomic RNA.";
RL J. Virol. 75:7252-7265(2001).
RN [8]
RP INTERACTION WITH HUMAN HCK.
RX PubMed=11278465; DOI=10.1074/jbc.m009076200;
RA Hassaine G., Courcoul M., Bessou G., Barthalay Y., Picard C., Olive D.,
RA Collette Y., Vigne R., Decroly E.;
RT "The tyrosine kinase Hck is an inhibitor of HIV-1 replication counteracted
RT by the viral vif protein.";
RL J. Biol. Chem. 276:16885-16893(2001).
RN [9]
RP PROTEIN SEQUENCE OF 2-9 AND 151-162, CLEAVAGE BY VIRAL PROTEASE, AND
RP MUTAGENESIS OF 149-ALA--ALA-151.
RX PubMed=12186895; DOI=10.1128/jvi.76.18.9112-9123.2002;
RA Khan M.A., Akari H., Kao S., Aberham C., Davis D., Buckler-White A.,
RA Strebel K.;
RT "Intravirion processing of the human immunodeficiency virus type 1 Vif
RT protein by the viral protease may be correlated with Vif function.";
RL J. Virol. 76:9112-9123(2002).
RN [10]
RP FUNCTION.
RX PubMed=14557625; DOI=10.1128/jvi.77.21.11398-11407.2003;
RA Kao S., Khan M.A., Miyagi E., Plishka R., Buckler-White A., Strebel K.;
RT "The human immunodeficiency virus type 1 Vif protein reduces intracellular
RT expression and inhibits packaging of APOBEC3G (CEM15), a cellular inhibitor
RT of virus infectivity.";
RL J. Virol. 77:11398-11407(2003).
RN [11]
RP INTERACTION WITH HUMAN SAT.
RX PubMed=12600646; DOI=10.1016/s1386-6532(02)00113-0;
RA Lake J.A., Carr J., Feng F., Mundy L., Burrell C., Li P.;
RT "The role of Vif during HIV-1 infection: interaction with novel host
RT cellular factors.";
RL J. Clin. Virol. 26:143-152(2003).
RN [12]
RP INTERACTION WITH HUMAN APOBEC3G.
RX PubMed=14528301; DOI=10.1038/nm946;
RA Marin M., Rose K.M., Kozak S.L., Kabat D.;
RT "HIV-1 Vif protein binds the editing enzyme APOBEC3G and induces its
RT degradation.";
RL Nat. Med. 9:1398-1403(2003).
RN [13]
RP INTERACTION WITH HUMAN CUL5 AND ELONGIN BC COMPLEX, AND MUTAGENESIS OF
RP SER-144; LEU-145; GLN-146; TYR-147; LEU-148; ALA-149 AND LEU-150.
RX PubMed=15574592; DOI=10.1101/gad.1249904;
RA Mehle A., Goncalves J., Santa-Marta M., McPike M., Gabuzda D.;
RT "Phosphorylation of a novel SOCS-box regulates assembly of the HIV-1 Vif-
RT Cul5 complex that promotes APOBEC3G degradation.";
RL Genes Dev. 18:2861-2866(2004).
RN [14]
RP INTERACTION WITH HUMAN APOBEC3G, AND MUTAGENESIS OF CYS-114 AND CYS-133.
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 [15]
RP INTERACTION WITH HUMAN UBCE7IP1.
RX PubMed=15367624; DOI=10.1128/jvi.78.19.10574-10581.2004;
RA Feng F., Davis A., Lake J.A., Carr J., Xia W., Burrell C., Li P.;
RT "Ring finger protein ZIN interacts with human immunodeficiency virus type 1
RT Vif.";
RL J. Virol. 78:10574-10581(2004).
RN [16]
RP INTERACTION WITH HUMAN CUL5, AND MUTAGENESIS OF HIS-108; CYS-114; CYS-133
RP AND HIS-139.
RX PubMed=16076960; DOI=10.1073/pnas.0502440102;
RA Luo K., Xiao Z., Ehrlich E., Yu Y., Liu B., Zheng S., Yu X.-F.;
RT "Primate lentiviral virion infectivity factors are substrate receptors that
RT assemble with cullin 5-E3 ligase through a HCCH motif to suppress
RT APOBEC3G.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:11444-11449(2005).
RN [17]
RP VARIANT 90-LYS--LYS-93.
RC STRAIN=Clinical Isolate;
RX PubMed=15989462; DOI=10.1089/aid.2005.21.565;
RA Farrow M.A., Somasundaran M., Zhang C., Gabuzda D., Sullivan J.L.,
RA Greenough T.C.;
RT "Nuclear localization of HIV type 1 Vif isolated from a long-term
RT asymptomatic individual and potential role in virus attenuation.";
RL AIDS Res. Hum. Retroviruses 21:565-574(2005).
RN [18]
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 ECO:0000269|PubMed:14557625}.
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 -!- INTERACTION:
CC P12504; Q9C0C7: AMBRA1; Xeno; NbExp=5; IntAct=EBI-779991, EBI-2512975;
CC P12504; Q13951: CBFB; Xeno; NbExp=10; IntAct=EBI-779991, EBI-718750;
CC P12504; Q13617: CUL2; Xeno; NbExp=6; IntAct=EBI-779991, EBI-456179;
CC P12504; Q93034: CUL5; Xeno; NbExp=11; IntAct=EBI-779991, EBI-1057139;
CC P12504; Q8TEB1: DCAF11; Xeno; NbExp=3; IntAct=EBI-779991, EBI-2213388;
CC P12504; Q99615: DNAJC7; Xeno; NbExp=3; IntAct=EBI-779991, EBI-357552;
CC P12504; Q15370: ELOB; Xeno; NbExp=5; IntAct=EBI-779991, EBI-301238;
CC P12504; Q15369: ELOC; Xeno; NbExp=5; IntAct=EBI-779991, EBI-301231;
CC P12504; Q13227: GPS2; Xeno; NbExp=2; IntAct=EBI-779991, EBI-713355;
CC P12504; P08631: HCK; Xeno; NbExp=3; IntAct=EBI-779991, EBI-346340;
CC P12504; O15379: HDAC3; Xeno; NbExp=2; IntAct=EBI-779991, EBI-607682;
CC P12504; Q16659: MAPK6; Xeno; NbExp=2; IntAct=EBI-779991, EBI-1384105;
CC P12504; P61289: PSME3; Xeno; NbExp=2; IntAct=EBI-779991, EBI-355546;
CC P12504; Q9NWF9-3: RNF216; Xeno; NbExp=4; IntAct=EBI-779991, EBI-723337;
CC P12504; Q9UBF6: RNF7; Xeno; NbExp=4; IntAct=EBI-779991, EBI-398632;
CC P12504; Q13501: SQSTM1; Xeno; NbExp=2; IntAct=EBI-779991, EBI-307104;
CC P12504; Q9UNE7: STUB1; Xeno; NbExp=2; IntAct=EBI-779991, EBI-357085;
CC P12504; P11441: UBL4A; Xeno; NbExp=2; IntAct=EBI-779991, EBI-356983;
CC P12504; Q8IWV8: UBR2; Xeno; NbExp=3; IntAct=EBI-779991, EBI-1237260;
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, ECO:0000269|PubMed:1830183}.
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. Thr-96 and
CC Ser-165 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-144
CC phosphorylation may inhibit elongin BC complex binding.
CC {ECO:0000269|PubMed:12186895}.
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: The infectious clone pNL4-3 is a chimeric provirus that
CC consists of DNA from HIV isolates NY5 (5' half) and BRU (3' half).
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}.
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DR EMBL; M19921; AAA44989.1; -; Genomic_RNA.
DR EMBL; M38431; AAB04038.1; -; Genomic_RNA.
DR PDB; 2MA9; NMR; -; A=139-174.
DR PDB; 3DCG; X-ray; 2.40 A; E/F=139-176.
DR PDB; 4N9F; X-ray; 3.30 A; 1/2/7/G/M/S/b/d/j/p/q/v=1-176.
DR PDB; 6NIL; EM; 3.90 A; C/F/I/L=1-113, C/F/I/L=158-176.
DR PDBsum; 2MA9; -.
DR PDBsum; 3DCG; -.
DR PDBsum; 4N9F; -.
DR PDBsum; 6NIL; -.
DR BMRB; P12504; -.
DR SMR; P12504; -.
DR DIP; DIP-36069N; -.
DR IntAct; P12504; 29.
DR BindingDB; P12504; -.
DR ChEMBL; CHEMBL4523940; -.
DR ABCD; P12504; 1 sequenced antibody.
DR EvolutionaryTrace; P12504; -.
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 1: Evidence at protein level;
KW 3D-structure; AIDS; Direct protein sequencing; Host cell membrane;
KW Host cytoplasm; Host membrane; Host-virus interaction; Membrane;
KW Phosphoprotein; 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_0000042762"
FT CHAIN 1..150
FT /note="p17"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04081"
FT /id="PRO_0000441079"
FT CHAIN 151..192
FT /note="p7"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04081"
FT /id="PRO_0000441080"
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 165..192
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"
FT MOD_RES 188
FT /note="Phosphothreonine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04081"
FT VARIANT 90..93
FT /note="RKKR -> KKRK (in strain: Clinical isolate; from an
FT asymptomatic patient; Vif is mislocalized to the nucleus
FT and non functional)"
FT MUTAGEN 5..6
FT /note="WQ->AA: 44% loss of viral infectivity."
FT /evidence="ECO:0000269|PubMed:10074113"
FT MUTAGEN 12..13
FT /note="QV->AA: No effect on viral infectivity."
FT /evidence="ECO:0000269|PubMed:10074113"
FT MUTAGEN 16..18
FT /note="MRI->AAA: 29% loss of viral infectivity."
FT /evidence="ECO:0000269|PubMed:10074113"
FT MUTAGEN 23..24
FT /note="RL->AA: 14% loss of viral infectivity."
FT /evidence="ECO:0000269|PubMed:10074113"
FT MUTAGEN 29..31
FT /note="MYI->AAV: 59% loss of viral infectivity."
FT /evidence="ECO:0000269|PubMed:10074113"
FT MUTAGEN 33..34
FT /note="RK->AA: 35% loss of viral infectivity."
FT /evidence="ECO:0000269|PubMed:10074113"
FT MUTAGEN 38..40
FT /note="WFY->AAA: 94% loss of viral infectivity."
FT /evidence="ECO:0000269|PubMed:10074113"
FT MUTAGEN 43..44
FT /note="HY->AA: 95% loss of viral infectivity."
FT /evidence="ECO:0000269|PubMed:10074113"
FT MUTAGEN 53..54
FT /note="SE->AA: 39% loss of viral infectivity."
FT /evidence="ECO:0000269|PubMed:10074113"
FT MUTAGEN 58..59
FT /note="PL->AA: 45% loss of viral infectivity."
FT /evidence="ECO:0000269|PubMed:10074113"
FT MUTAGEN 69..70
FT /note="YW->AA: 97% loss of viral infectivity."
FT /evidence="ECO:0000269|PubMed:10074113"
FT MUTAGEN 73..74
FT /note="HT->AA: No effect onviral infectivity."
FT /evidence="ECO:0000269|PubMed:10074113"
FT MUTAGEN 80..81
FT /note="HL->AA: 19% loss of viral infectivity."
FT /evidence="ECO:0000269|PubMed:10074113"
FT MUTAGEN 86..87
FT /note="SI->AA: 42% loss of viral infectivity."
FT /evidence="ECO:0000269|PubMed:10074113"
FT MUTAGEN 90..92
FT /note="RKK->AAA: No effect on viral infectivity."
FT /evidence="ECO:0000269|PubMed:10074113"
FT MUTAGEN 97..98
FT /note="QV->AA: 27% loss of viral infectivity."
FT /evidence="ECO:0000269|PubMed:10074113"
FT MUTAGEN 105..107
FT /note="QLI->AAV: 98% loss of viral infectivity."
FT /evidence="ECO:0000269|PubMed:10074113"
FT MUTAGEN 108
FT /note="H->L: Complete loss of interaction with CUL5."
FT /evidence="ECO:0000269|PubMed:16076960"
FT MUTAGEN 111..112
FT /note="YF->AA: 93% loss of viral infectivity."
FT /evidence="ECO:0000269|PubMed:10074113"
FT MUTAGEN 114
FT /note="C->S: 98% loss of viral infectivity. Complete loss
FT of interaction with CUL5."
FT /evidence="ECO:0000269|PubMed:10074113,
FT ECO:0000269|PubMed:14672928, ECO:0000269|PubMed:16076960"
FT MUTAGEN 121..123
FT /note="RNT->AAA: 35% increase of viral infectivity."
FT /evidence="ECO:0000269|PubMed:10074113"
FT MUTAGEN 127..128
FT /note="RI->AA: 10% loss of viral infectivity."
FT /evidence="ECO:0000269|PubMed:10074113"
FT MUTAGEN 133
FT /note="C->S: 95% loss of viral infectivity. Complete loss
FT of interaction with CUL5."
FT /evidence="ECO:0000269|PubMed:10074113,
FT ECO:0000269|PubMed:14672928, ECO:0000269|PubMed:16076960"
FT MUTAGEN 135..136
FT /note="YQ->AA: 73% loss of viral infectivity."
FT /evidence="ECO:0000269|PubMed:10074113"
FT MUTAGEN 139
FT /note="H->L: Complete loss of interaction with CUL5."
FT /evidence="ECO:0000269|PubMed:16076960"
FT MUTAGEN 140..141
FT /note="NK->AA: 68% loss of viral infectivity."
FT /evidence="ECO:0000269|PubMed:10074113"
FT MUTAGEN 144..146
FT /note="SLQ->AAA: 93% loss of viral infectivity."
FT /evidence="ECO:0000269|PubMed:10074113"
FT MUTAGEN 144
FT /note="S->A: 25% loss of interaction with CUL5y."
FT /evidence="ECO:0000269|PubMed:15574592"
FT MUTAGEN 145
FT /note="L->A: Complete loss of interaction with CUL5."
FT /evidence="ECO:0000269|PubMed:15574592"
FT MUTAGEN 146
FT /note="Q->A: 90% loss of interaction with CUL5."
FT /evidence="ECO:0000269|PubMed:15574592"
FT MUTAGEN 147..148
FT /note="YL->AA: 40% loss of viral infectivity."
FT /evidence="ECO:0000269|PubMed:10074113"
FT MUTAGEN 147
FT /note="Y->A: 40% loss of interaction with CUL5."
FT /evidence="ECO:0000269|PubMed:15574592"
FT MUTAGEN 148
FT /note="L->A: 35% loss of interaction with CUL5."
FT /evidence="ECO:0000269|PubMed:15574592"
FT MUTAGEN 149..151
FT /note="ALA->RKS: Complete loss of processing between p17
FT and p7. Complete loss of replication."
FT /evidence="ECO:0000269|PubMed:12186895"
FT MUTAGEN 149
FT /note="A->G: 75% loss of CUL5 binding activity."
FT /evidence="ECO:0000269|PubMed:15574592"
FT MUTAGEN 150
FT /note="L->A: 90% loss of CUL5 binding activity."
FT /evidence="ECO:0000269|PubMed:15574592"
FT MUTAGEN 151
FT /note="A->E: No effect on processing between p17 and p7."
FT MUTAGEN 151
FT /note="A->N: Slightly increased processing between p17 and
FT p7."
FT MUTAGEN 151
FT /note="A->P: Increased processing between p17 and p7."
FT MUTAGEN 151
FT /note="A->Y: Partial loss of processing between p17 and
FT p7."
FT MUTAGEN 156..158
FT /note="PKQ->AAA: No effect on viral infectivity."
FT /evidence="ECO:0000269|PubMed:10074113"
FT MUTAGEN 157
FT /note="K->A: No effect viral infectivity."
FT /evidence="ECO:0000269|PubMed:10074113"
FT MUTAGEN 158..160
FT /note="QIK->AAA: 9% loss of viral infectivity."
FT /evidence="ECO:0000269|PubMed:10074113"
FT MUTAGEN 160
FT /note="K->A: 33% loss of viral infectivity."
FT MUTAGEN 161..164
FT /note="PPLP->APLA: 88% loss of viral infectivity."
FT /evidence="ECO:0000269|PubMed:10074113"
FT MUTAGEN 161..163
FT /note="PPL->AAA: 97% loss of viral infectivity."
FT MUTAGEN 161
FT /note="P->A: 27% loss of viral infectivity."
FT MUTAGEN 162
FT /note="P->A: No effect viral infectivity."
FT MUTAGEN 163
FT /note="L->A: 26% loss of viral infectivity."
FT MUTAGEN 164
FT /note="P->A: 63% loss of viral infectivity."
FT MUTAGEN 165
FT /note="S->A: 67% loss of viral infectivity."
FT /evidence="ECO:0000269|PubMed:10074113"
FT MUTAGEN 166
FT /note="V->A: 20% loss of viral infectivity."
FT /evidence="ECO:0000269|PubMed:10074113"
FT MUTAGEN 169..170
FT /note="LT->AA: 42% loss of viral infectivity."
FT /evidence="ECO:0000269|PubMed:10074113"
FT MUTAGEN 180..181
FT /note="TK->AA: 5% loss of viral infectivity."
FT /evidence="ECO:0000269|PubMed:10074113"
FT MUTAGEN 189..190
FT /note="MN->AA: 4% loss of viral infectivity."
FT /evidence="ECO:0000269|PubMed:10074113"
FT STRAND 5..13
FT /evidence="ECO:0007829|PDB:4N9F"
FT HELIX 15..30
FT /evidence="ECO:0007829|PDB:4N9F"
FT TURN 34..37
FT /evidence="ECO:0007829|PDB:4N9F"
FT STRAND 39..41
FT /evidence="ECO:0007829|PDB:4N9F"
FT TURN 43..45
FT /evidence="ECO:0007829|PDB:4N9F"
FT STRAND 51..59
FT /evidence="ECO:0007829|PDB:4N9F"
FT STRAND 62..69
FT /evidence="ECO:0007829|PDB:4N9F"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:4N9F"
FT STRAND 83..91
FT /evidence="ECO:0007829|PDB:4N9F"
FT STRAND 94..97
FT /evidence="ECO:0007829|PDB:4N9F"
FT HELIX 100..109
FT /evidence="ECO:0007829|PDB:4N9F"
FT HELIX 119..125
FT /evidence="ECO:0007829|PDB:4N9F"
FT HELIX 136..138
FT /evidence="ECO:0007829|PDB:4N9F"
FT HELIX 145..154
FT /evidence="ECO:0007829|PDB:3DCG"
FT HELIX 166..169
FT /evidence="ECO:0007829|PDB:4N9F"
SQ SEQUENCE 192 AA; 22699 MW; 2830B3233E8ECD16 CRC64;
MENRWQVMIV WQVDRMRINT WKRLVKHHMY ISRKAKDWFY RHHYESTNPK ISSEVHIPLG
DAKLVITTYW GLHTGERDWH LGQGVSIEWR KKRYSTQVDP DLADQLIHLH YFDCFSESAI
RNTILGRIVS PRCEYQAGHN KVGSLQYLAL AALIKPKQIK PPLPSVRKLT EDRWNKPQKT
KGHRGSHTMN GH
