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Virion infectivity factor (Vif) (SOR protein) [Cleaved into: p17; p7]

 VIF_HV1N5               Reviewed;         192 AA.
P12504;
01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
01-OCT-1989, sequence version 1.
25-OCT-2017, entry version 106.
RecName: Full=Virion infectivity factor {ECO:0000255|HAMAP-Rule:MF_04081};
Short=Vif {ECO:0000255|HAMAP-Rule:MF_04081};
AltName: Full=SOR protein {ECO:0000255|HAMAP-Rule:MF_04081};
Contains:
RecName: Full=p17 {ECO:0000255|HAMAP-Rule:MF_04081};
Contains:
RecName: Full=p7 {ECO:0000255|HAMAP-Rule:MF_04081};
Name=vif {ECO:0000255|HAMAP-Rule:MF_04081};
Human immunodeficiency virus type 1 group M subtype B (isolate NY5)
(HIV-1).
Viruses; Retro-transcribing viruses; Retroviridae; Orthoretrovirinae;
Lentivirus; Primate lentivirus group.
NCBI_TaxID=11698;
NCBI_TaxID=9606; Homo sapiens (Human).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Clone pNL4-3;
Buckler C.E., Buckler-White A.J., Willey R.L., McCoy J.;
Submitted (JUN-1988) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
Theodore T., Buckler-White A.J.;
Submitted (OCT-1992) to the EMBL/GenBank/DDBJ databases.
[3]
INDUCTION.
PubMed=1830183; DOI=10.1016/0042-6822(91)90996-O;
Schwartz S., Felber B.K., Pavlakis G.N.;
"Expression of human immunodeficiency virus type 1 vif and vpr mRNAs
is Rev-dependent and regulated by splicing.";
Virology 183:677-686(1991).
[4]
ROLE IN VIRION MORPHOLOGY.
PubMed=8184544; DOI=10.1006/viro.1994.1300;
Hoglund S., Ohagen A., Lawrence K., Gabuzda D.;
"Role of vif during packing of the core of HIV-1.";
Virology 201:349-355(1994).
[5]
MUTAGENESIS OF 5-TRP-GLN-6; 12-GLN-VAL-13; 16-MET--ILE-18;
23-ARG-LEU-24; 29-MET--ILE-31; 33-ARG-LYS-34; 38-TRP--TYR-40;
43-HIS-TYR-44; 53-SER-GLU-54; 58-PRO-LEU-59; 69-TYR-TRP-70;
73-HIS-THR-74; 80-HIS-LEU-81; 86-SER-ILE-87; 90-ARG--LYS-92;
97-GLN-VAL-98; 105-GLN--ILE-107; 111-TYR-PHE-112; CYS-114;
121-ARG--THR-123; 127-ARG-ILE-128; CYS-133; 135-TYR-GLN-136;
140-ASN-LYS-141; 144-SER--GLN-146; 147-TYR-LEU-148; 156-PRO--GLN-158;
LYS-157; 158-GLN--LYS-160; 161-PRO--LEU-164; SER-165; VAL-166;
169-LEU-THR-170; 180-THR-LYS-181 AND 189-MET-ASN-190.
PubMed=10074113;
Simon J.H., Sheehy A.M., Carpenter E.A., Fouchier R.A., Malim M.H.;
"Mutational analysis of the human immunodeficiency virus type 1 Vif
protein.";
J. Virol. 73:2675-2681(1999).
[6]
MULTIMERIZATION.
PubMed=11071884; DOI=10.1074/jbc.M004895200;
Yang S., Sun Y., Zhang H.;
"The multimerization of human immunodeficiency virus type I Vif
protein: a requirement for Vif function in the viral life cycle.";
J. Biol. Chem. 276:4889-4893(2001).
[7]
INTERACTION WITH NUCLEOPROTEIN.
PubMed=11461998; DOI=10.1128/JVI.75.16.7252-7265.2001;
Khan M.A., Aberham C., Kao S., Akari H., Gorelick R., Bour S.,
Strebel K.;
"Human immunodeficiency virus type 1 Vif protein is packaged into the
nucleoprotein complex through an interaction with viral genomic RNA.";
J. Virol. 75:7252-7265(2001).
[8]
INTERACTION WITH HUMAN HCK.
PubMed=11278465; DOI=10.1074/jbc.M009076200;
Hassaine G., Courcoul M., Bessou G., Barthalay Y., Picard C.,
Olive D., Collette Y., Vigne R., Decroly E.;
"The tyrosine kinase Hck is an inhibitor of HIV-1 replication
counteracted by the viral vif protein.";
J. Biol. Chem. 276:16885-16893(2001).
[9]
PROTEIN SEQUENCE OF 2-9 AND 151-162, CLEAVAGE BY VIRAL PROTEASE, AND
MUTAGENESIS OF 149-ALA--ALA-151.
PubMed=12186895; DOI=10.1128/JVI.76.18.9112-9123.2002;
Khan M.A., Akari H., Kao S., Aberham C., Davis D., Buckler-White A.,
Strebel K.;
"Intravirion processing of the human immunodeficiency virus type 1 Vif
protein by the viral protease may be correlated with Vif function.";
J. Virol. 76:9112-9123(2002).
[10]
FUNCTION.
PubMed=14557625; DOI=10.1128/JVI.77.21.11398-11407.2003;
Kao S., Khan M.A., Miyagi E., Plishka R., Buckler-White A.,
Strebel K.;
"The human immunodeficiency virus type 1 Vif protein reduces
intracellular expression and inhibits packaging of APOBEC3G (CEM15), a
cellular inhibitor of virus infectivity.";
J. Virol. 77:11398-11407(2003).
[11]
INTERACTION WITH HUMAN SAT.
PubMed=12600646; DOI=10.1016/S1386-6532(02)00113-0;
Lake J.A., Carr J., Feng F., Mundy L., Burrell C., Li P.;
"The role of Vif during HIV-1 infection: interaction with novel host
cellular factors.";
J. Clin. Virol. 26:143-152(2003).
[12]
INTERACTION WITH HUMAN APOBEC3G.
PubMed=14528301; DOI=10.1038/nm946;
Marin M., Rose K.M., Kozak S.L., Kabat D.;
"HIV-1 Vif protein binds the editing enzyme APOBEC3G and induces its
degradation.";
Nat. Med. 9:1398-1403(2003).
[13]
INTERACTION WITH HUMAN CUL5 AND ELONGIN BC COMPLEX, AND MUTAGENESIS OF
SER-144; LEU-145; GLN-146; TYR-147; LEU-148; ALA-149 AND LEU-150.
PubMed=15574592; DOI=10.1101/gad.1249904;
Mehle A., Goncalves J., Santa-Marta M., McPike M., Gabuzda D.;
"Phosphorylation of a novel SOCS-box regulates assembly of the HIV-1
Vif-Cul5 complex that promotes APOBEC3G degradation.";
Genes Dev. 18:2861-2866(2004).
[14]
INTERACTION WITH HUMAN APOBEC3G, AND MUTAGENESIS OF CYS-114 AND
CYS-133.
PubMed=14672928; DOI=10.1074/jbc.M313093200;
Mehle A., Strack B., Ancuta P., Zhang C., McPike M., Gabuzda D.;
"Vif overcomes the innate antiviral activity of APOBEC3G by promoting
its degradation in the ubiquitin-proteasome pathway.";
J. Biol. Chem. 279:7792-7798(2004).
[15]
INTERACTION WITH HUMAN UBCE7IP1.
PubMed=15367624; DOI=10.1128/JVI.78.19.10574-10581.2004;
Feng F., Davis A., Lake J.A., Carr J., Xia W., Burrell C., Li P.;
"Ring finger protein ZIN interacts with human immunodeficiency virus
type 1 Vif.";
J. Virol. 78:10574-10581(2004).
[16]
INTERACTION WITH HUMAN CUL5, AND MUTAGENESIS OF HIS-108; CYS-114;
CYS-133 AND HIS-139.
PubMed=16076960; DOI=10.1073/pnas.0502440102;
Luo K., Xiao Z., Ehrlich E., Yu Y., Liu B., Zheng S., Yu X.-F.;
"Primate lentiviral virion infectivity factors are substrate receptors
that assemble with cullin 5-E3 ligase through a HCCH motif to suppress
APOBEC3G.";
Proc. Natl. Acad. Sci. U.S.A. 102:11444-11449(2005).
[17]
VARIANT 90-LYS--LYS-93.
STRAIN=Clinical Isolate;
PubMed=15989462; DOI=10.1089/aid.2005.21.565;
Farrow M.A., Somasundaran M., Zhang C., Gabuzda D., Sullivan J.L.,
Greenough T.C.;
"Nuclear localization of HIV type 1 Vif isolated from a long-term
asymptomatic individual and potential role in virus attenuation.";
AIDS Res. Hum. Retroviruses 21:565-574(2005).
[18]
REVIEW.
PubMed=15177194; DOI=10.1016/j.molmed.2004.04.008;
Rose K.M., Marin M., Kozak S.L., Kabat D.;
"The viral infectivity factor (Vif) of HIV-1 unveiled.";
Trends Mol. Med. 10:291-297(2004).
-!- FUNCTION: Counteracts the innate antiviral activity of host
APOBEC3F and APOBEC3G. Forms a complex with host APOBEC3F and
APOBEC3G thus preventing the entry of these lethally hypermutating
enzymes into progeny virions. Recruits an active E3 ubiquitin
ligase complex composed of elongin BC, CUL5, and RBX2 to induce
polyubiquitination of APOBEC3G and APOBEC3F. In turn, they are
directed to the 26S proteasome for degradation. Vif interaction
with APOBEC3G also blocks its cytidine deaminase activity in a
proteasome-independent manner, suggesting a dual inhibitory
mechanism. May interact directly with APOBEC3G mRNA in order to
inhibit its translation. Seems to play a role in viral morphology
by affecting the stability of the viral nucleoprotein core.
Finally, Vif also contributes to the G2 cell cycle arrest observed
in HIV infected cells. {ECO:0000255|HAMAP-Rule:MF_04081,
ECO:0000269|PubMed:14557625}.
-!- SUBUNIT: Homomultimer; in vitro and presumably in vivo. Interacts
with viral RNA and Pr55Gag precursor; these interactions mediate
Vif incorporation into the virion. Interacts with the viral
reverse transcriptase. Interacts with human APOBEC3F and APOBEC3G.
Interacts with host UBCE7IP1 isoform 3/ZIN and possibly with SAT.
Interacts with host tyrosine kinases HCK and FYN; these
interactions may decrease level of phosphorylated APOBEC3G
incorporation into virions. Interacts with host ABCE1; this
interaction may play a role in protecting viral RNA from damage
during viral assembly. Forms an E3 ligase complex by interacting
with host CUL5 and elongin BC complex (ELOB and ELOC). Interacts
with host MDM2; this interaction targets Vif for degradation by
the proteasome. {ECO:0000255|HAMAP-Rule:MF_04081}.
-!- INTERACTION:
Q9C0C7:AMBRA1 (xeno); NbExp=5; IntAct=EBI-779991, EBI-2512975;
Q13951:CBFB (xeno); NbExp=10; IntAct=EBI-779991, EBI-718750;
Q13617:CUL2 (xeno); NbExp=6; IntAct=EBI-779991, EBI-456179;
Q93034:CUL5 (xeno); NbExp=11; IntAct=EBI-779991, EBI-1057139;
Q8TEB1:DCAF11 (xeno); NbExp=3; IntAct=EBI-779991, EBI-2213388;
Q99615:DNAJC7 (xeno); NbExp=3; IntAct=EBI-779991, EBI-357552;
Q15370:ELOB (xeno); NbExp=5; IntAct=EBI-779991, EBI-301238;
Q15369:ELOC (xeno); NbExp=5; IntAct=EBI-779991, EBI-301231;
Q13227:GPS2 (xeno); NbExp=2; IntAct=EBI-779991, EBI-713355;
P08631:HCK (xeno); NbExp=3; IntAct=EBI-779991, EBI-346340;
O15379:HDAC3 (xeno); NbExp=2; IntAct=EBI-779991, EBI-607682;
Q16659:MAPK6 (xeno); NbExp=2; IntAct=EBI-779991, EBI-1384105;
P61289:PSME3 (xeno); NbExp=2; IntAct=EBI-779991, EBI-355546;
Q9NWF9-3:RNF216 (xeno); NbExp=4; IntAct=EBI-779991, EBI-723337;
Q9UBF6:RNF7 (xeno); NbExp=4; IntAct=EBI-779991, EBI-398632;
Q13501:SQSTM1 (xeno); NbExp=2; IntAct=EBI-779991, EBI-307104;
Q9UNE7:STUB1 (xeno); NbExp=2; IntAct=EBI-779991, EBI-357085;
P11441:UBL4A (xeno); NbExp=2; IntAct=EBI-779991, EBI-356983;
Q8IWV8:UBR2 (xeno); NbExp=3; IntAct=EBI-779991, EBI-1237260;
-!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000255|HAMAP-
Rule:MF_04081}. Host cell membrane {ECO:0000255|HAMAP-
Rule:MF_04081}; Peripheral membrane protein {ECO:0000255|HAMAP-
Rule:MF_04081}; Cytoplasmic side {ECO:0000255|HAMAP-
Rule:MF_04081}. Virion {ECO:0000255|HAMAP-Rule:MF_04081}. Note=In
the cytoplasm, seems to colocalize with intermediate filament
vimentin. A fraction is associated with the cytoplasmic side of
cellular membranes, presumably via the interaction with Pr55Gag
precursor. Incorporated in virions at a ratio of approximately 7
to 20 molecules per virion. {ECO:0000255|HAMAP-Rule:MF_04081}.
-!- INDUCTION: Expressed late during infection in a Rev-dependent
manner. {ECO:0000255|HAMAP-Rule:MF_04081,
ECO:0000269|PubMed:1830183}.
-!- DOMAIN: The BC-like-box motif mediates the interaction with
elongin BC complex. {ECO:0000255|HAMAP-Rule:MF_04081}.
-!- DOMAIN: The HCCH motif (H-x(5)-C-x(18)-C-x(5)-H) mediates the
interaction with CUL5. {ECO:0000255|HAMAP-Rule:MF_04081}.
-!- PTM: Highly phosphorylated on serine and threonine residues. Thr-
96 and Ser-165 are phosphorylated by the mitogen activated kinase
MAP4K1. As the HIV-1 replication can be activated by stress and
mitogens, these phosphorylations could be involved in this
process. Ser-144 phosphorylation may inhibit elongin BC complex
binding. {ECO:0000269|PubMed:12186895}.
-!- PTM: Processed in virion by the viral protease.
{ECO:0000255|HAMAP-Rule:MF_04081}.
-!- PTM: Highly phosphorylated on serine and threonine residues.
{ECO:0000255|HAMAP-Rule:MF_04081}.
-!- PTM: Polyubiquitinated and degraded by the proteasome in the
presence of APOBEC3G. {ECO:0000255|HAMAP-Rule:MF_04081}.
-!- MISCELLANEOUS: The infectious clone pNL4-3 is a chimeric provirus
that consists of DNA from HIV isolates NY5 (5' half) and BRU (3'
half).
-!- MISCELLANEOUS: Vif-defective viruses show catastrophic failure in
reverse transcription due to APOBEC-induced mutations that
initiate a DNA base repair pathway and compromise the structural
integrity of the ssDNA. In the absence of Vif, the virion is
morphologically abnormal. {ECO:0000255|HAMAP-Rule:MF_04081}.
-!- MISCELLANEOUS: HIV-1 lineages are divided in three main groups, M
(for Major), O (for Outlier), and N (for New, or Non-M, Non-O).
The vast majority of strains found worldwide belong to the group
M. Group O seems to be endemic to and largely confined to Cameroon
and neighboring countries in West Central Africa, where these
viruses represent a small minority of HIV-1 strains. The group N
is represented by a limited number of isolates from Cameroonian
persons. The group M is further subdivided in 9 clades or subtypes
(A to D, F to H, J and K). {ECO:0000255|HAMAP-Rule:MF_04081}.
-!- MISCELLANEOUS: Required for replication in 'nonpermissive' cells,
including primary T-cells, macrophages and certain T-cell lines,
but is dispensable for replication in 'permissive' cell lines,
such as 293T cells. In nonpermissive cells, Vif-defective viruses
can produce virions, but they fail to complete reverse
transcription and cannot successfully infect new cells.
{ECO:0000255|HAMAP-Rule:MF_04081}.
-!- SIMILARITY: Belongs to the primate lentivirus group Vif protein
family. {ECO:0000255|HAMAP-Rule:MF_04081, ECO:0000305}.
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EMBL; M19921; AAA44989.1; -; Genomic_RNA.
EMBL; M38431; AAB04038.1; -; Genomic_RNA.
PDB; 2MA9; NMR; -; A=139-174.
PDB; 3DCG; X-ray; 2.40 A; E/F=139-176.
PDB; 4N9F; X-ray; 3.30 A; 1/2/7/G/M/S/b/d/j/p/q/v=1-176.
PDBsum; 2MA9; -.
PDBsum; 3DCG; -.
PDBsum; 4N9F; -.
ProteinModelPortal; P12504; -.
SMR; P12504; -.
DIP; DIP-36069N; -.
IntAct; P12504; 29.
EvolutionaryTrace; P12504; -.
GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
GO; GO:0019012; C:virion; IEA:UniProtKB-SubCell.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
GO; GO:0019058; P:viral life cycle; IEA:InterPro.
HAMAP; MF_04081; HIV_VIF; 1.
InterPro; IPR000475; Viral_infect.
Pfam; PF00559; Vif; 1.
PRINTS; PR00349; VIRIONINFFCT.
1: Evidence at protein level;
3D-structure; AIDS; Direct protein sequencing; Host cell membrane;
Host cytoplasm; Host membrane; Host-virus interaction; Membrane;
Phosphoprotein; RNA-binding; Ubl conjugation; Ubl conjugation pathway;
Virion.
CHAIN 1 192 Virion infectivity factor.
{ECO:0000255|HAMAP-Rule:MF_04081}.
/FTId=PRO_0000042762.
CHAIN 1 150 p17. {ECO:0000255|HAMAP-Rule:MF_04081}.
/FTId=PRO_0000441079.
CHAIN 151 192 p7. {ECO:0000255|HAMAP-Rule:MF_04081}.
/FTId=PRO_0000441080.
REGION 14 17 Interaction with host APOBEC3F; F1-box.
{ECO:0000255|HAMAP-Rule:MF_04081}.
REGION 40 44 Interaction with host APOBEC3G; G-box.
{ECO:0000255|HAMAP-Rule:MF_04081}.
REGION 54 72 Interaction with host APOBEC3F and
APOBEC3G; FG-box. {ECO:0000255|HAMAP-
Rule:MF_04081}.
REGION 74 79 Interaction with host APOBEC3F; F2-box.
{ECO:0000255|HAMAP-Rule:MF_04081}.
REGION 75 114 RNA-binding. {ECO:0000255|HAMAP-
Rule:MF_04081}.
REGION 151 164 Multimerization. {ECO:0000255|HAMAP-
Rule:MF_04081}.
REGION 171 172 Membrane association. {ECO:0000255|HAMAP-
Rule:MF_04081}.
MOTIF 108 139 HCCH motif. {ECO:0000255|HAMAP-
Rule:MF_04081}.
MOTIF 144 153 BC-box-like motif. {ECO:0000255|HAMAP-
Rule:MF_04081}.
SITE 150 151 Cleavage in virion (by viral protease).
{ECO:0000255|HAMAP-Rule:MF_04081}.
MOD_RES 96 96 Phosphothreonine; by host MAP4K1.
{ECO:0000255|HAMAP-Rule:MF_04081}.
MOD_RES 144 144 Phosphoserine; by host.
{ECO:0000255|HAMAP-Rule:MF_04081}.
MOD_RES 165 165 Phosphoserine; by host MAP4K1.
{ECO:0000255|HAMAP-Rule:MF_04081}.
MOD_RES 188 188 Phosphothreonine; by host.
{ECO:0000255|HAMAP-Rule:MF_04081}.
VARIANT 90 93 RKKR -> KKRK (in strain: Clinical
isolate; from an asymptomatic patient;
Vif is mislocalized to the nucleus and
non functional).
MUTAGEN 5 6 WQ->AA: 44% loss of viral infectivity.
{ECO:0000269|PubMed:10074113}.
MUTAGEN 12 13 QV->AA: No effect on viral infectivity.
{ECO:0000269|PubMed:10074113}.
MUTAGEN 16 18 MRI->AAA: 29% loss of viral infectivity.
{ECO:0000269|PubMed:10074113}.
MUTAGEN 23 24 RL->AA: 14% loss of viral infectivity.
{ECO:0000269|PubMed:10074113}.
MUTAGEN 29 31 MYI->AAV: 59% loss of viral infectivity.
{ECO:0000269|PubMed:10074113}.
MUTAGEN 33 34 RK->AA: 35% loss of viral infectivity.
{ECO:0000269|PubMed:10074113}.
MUTAGEN 38 40 WFY->AAA: 94% loss of viral infectivity.
{ECO:0000269|PubMed:10074113}.
MUTAGEN 43 44 HY->AA: 95% loss of viral infectivity.
{ECO:0000269|PubMed:10074113}.
MUTAGEN 53 54 SE->AA: 39% loss of viral infectivity.
{ECO:0000269|PubMed:10074113}.
MUTAGEN 58 59 PL->AA: 45% loss of viral infectivity.
{ECO:0000269|PubMed:10074113}.
MUTAGEN 69 70 YW->AA: 97% loss of viral infectivity.
{ECO:0000269|PubMed:10074113}.
MUTAGEN 73 74 HT->AA: No effect onviral infectivity.
{ECO:0000269|PubMed:10074113}.
MUTAGEN 80 81 HL->AA: 19% loss of viral infectivity.
{ECO:0000269|PubMed:10074113}.
MUTAGEN 86 87 SI->AA: 42% loss of viral infectivity.
{ECO:0000269|PubMed:10074113}.
MUTAGEN 90 92 RKK->AAA: No effect on viral infectivity.
{ECO:0000269|PubMed:10074113}.
MUTAGEN 97 98 QV->AA: 27% loss of viral infectivity.
{ECO:0000269|PubMed:10074113}.
MUTAGEN 105 107 QLI->AAV: 98% loss of viral infectivity.
{ECO:0000269|PubMed:10074113}.
MUTAGEN 108 108 H->L: Complete loss of interaction with
CUL5. {ECO:0000269|PubMed:16076960}.
MUTAGEN 111 112 YF->AA: 93% loss of viral infectivity.
{ECO:0000269|PubMed:10074113}.
MUTAGEN 114 114 C->S: 98% loss of viral infectivity.
Complete loss of interaction with CUL5.
{ECO:0000269|PubMed:10074113,
ECO:0000269|PubMed:14672928,
ECO:0000269|PubMed:16076960}.
MUTAGEN 121 123 RNT->AAA: 35% increase of viral
infectivity.
{ECO:0000269|PubMed:10074113}.
MUTAGEN 127 128 RI->AA: 10% loss of viral infectivity.
{ECO:0000269|PubMed:10074113}.
MUTAGEN 133 133 C->S: 95% loss of viral infectivity.
Complete loss of interaction with CUL5.
{ECO:0000269|PubMed:10074113,
ECO:0000269|PubMed:14672928,
ECO:0000269|PubMed:16076960}.
MUTAGEN 135 136 YQ->AA: 73% loss of viral infectivity.
{ECO:0000269|PubMed:10074113}.
MUTAGEN 139 139 H->L: Complete loss of interaction with
CUL5. {ECO:0000269|PubMed:16076960}.
MUTAGEN 140 141 NK->AA: 68% loss of viral infectivity.
{ECO:0000269|PubMed:10074113}.
MUTAGEN 144 146 SLQ->AAA: 93% loss of viral infectivity.
{ECO:0000269|PubMed:10074113}.
MUTAGEN 144 144 S->A: 25% loss of interaction with CUL5y.
{ECO:0000269|PubMed:15574592}.
MUTAGEN 145 145 L->A: Complete loss of interaction with
CUL5. {ECO:0000269|PubMed:15574592}.
MUTAGEN 146 146 Q->A: 90% loss of interaction with CUL5.
{ECO:0000269|PubMed:15574592}.
MUTAGEN 147 148 YL->AA: 40% loss of viral infectivity.
{ECO:0000269|PubMed:10074113}.
MUTAGEN 147 147 Y->A: 40% loss of interaction with CUL5.
{ECO:0000269|PubMed:15574592}.
MUTAGEN 148 148 L->A: 35% loss of interaction with CUL5.
{ECO:0000269|PubMed:15574592}.
MUTAGEN 149 151 ALA->RKS: Complete loss of processing
between p17 and p7. Complete loss of
replication.
{ECO:0000269|PubMed:12186895}.
MUTAGEN 149 149 A->G: 75% loss of CUL5 binding activity.
{ECO:0000269|PubMed:15574592}.
MUTAGEN 150 150 L->A: 90% loss of CUL5 binding activity.
{ECO:0000269|PubMed:15574592}.
MUTAGEN 151 151 A->E: No effect on processing between p17
and p7.
MUTAGEN 151 151 A->N: Slightly increased processing
between p17 and p7.
MUTAGEN 151 151 A->P: Increased processing between p17
and p7.
MUTAGEN 151 151 A->Y: Partial loss of processing between
p17 and p7.
MUTAGEN 156 158 PKQ->AAA: No effect on viral infectivity.
{ECO:0000269|PubMed:10074113}.
MUTAGEN 157 157 K->A: No effect viral infectivity.
{ECO:0000269|PubMed:10074113}.
MUTAGEN 158 160 QIK->AAA: 9% loss of viral infectivity.
{ECO:0000269|PubMed:10074113}.
MUTAGEN 160 160 K->A: 33% loss of viral infectivity.
MUTAGEN 161 164 PPLP->APLA: 88% loss of viral
infectivity.
{ECO:0000269|PubMed:10074113}.
MUTAGEN 161 163 PPL->AAA: 97% loss of viral infectivity.
MUTAGEN 161 161 P->A: 27% loss of viral infectivity.
MUTAGEN 162 162 P->A: No effect viral infectivity.
MUTAGEN 163 163 L->A: 26% loss of viral infectivity.
MUTAGEN 164 164 P->A: 63% loss of viral infectivity.
MUTAGEN 165 165 S->A: 67% loss of viral infectivity.
{ECO:0000269|PubMed:10074113}.
MUTAGEN 166 166 V->A: 20% loss of viral infectivity.
{ECO:0000269|PubMed:10074113}.
MUTAGEN 169 170 LT->AA: 42% loss of viral infectivity.
{ECO:0000269|PubMed:10074113}.
MUTAGEN 180 181 TK->AA: 5% loss of viral infectivity.
{ECO:0000269|PubMed:10074113}.
MUTAGEN 189 190 MN->AA: 4% loss of viral infectivity.
{ECO:0000269|PubMed:10074113}.
STRAND 5 13 {ECO:0000244|PDB:4N9F}.
HELIX 15 30 {ECO:0000244|PDB:4N9F}.
TURN 34 37 {ECO:0000244|PDB:4N9F}.
STRAND 39 41 {ECO:0000244|PDB:4N9F}.
TURN 43 45 {ECO:0000244|PDB:4N9F}.
STRAND 51 59 {ECO:0000244|PDB:4N9F}.
STRAND 62 69 {ECO:0000244|PDB:4N9F}.
STRAND 73 75 {ECO:0000244|PDB:4N9F}.
STRAND 83 91 {ECO:0000244|PDB:4N9F}.
STRAND 94 97 {ECO:0000244|PDB:4N9F}.
HELIX 100 109 {ECO:0000244|PDB:4N9F}.
HELIX 119 125 {ECO:0000244|PDB:4N9F}.
HELIX 136 138 {ECO:0000244|PDB:4N9F}.
HELIX 145 154 {ECO:0000244|PDB:3DCG}.
HELIX 166 169 {ECO:0000244|PDB:4N9F}.
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


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