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Protein Vpr (R ORF protein) (Viral protein R)

 VPR_HV1BR               Reviewed;          96 AA.
P05928;
01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
01-NOV-1988, sequence version 1.
30-AUG-2017, entry version 119.
RecName: Full=Protein Vpr {ECO:0000255|HAMAP-Rule:MF_04080};
AltName: Full=R ORF protein {ECO:0000255|HAMAP-Rule:MF_04080};
AltName: Full=Viral protein R {ECO:0000255|HAMAP-Rule:MF_04080};
Name=vpr {ECO:0000255|HAMAP-Rule:MF_04080};
Human immunodeficiency virus type 1 group M subtype B (isolate
BRU/LAI) (HIV-1).
Viruses; Retro-transcribing viruses; Retroviridae; Orthoretrovirinae;
Lentivirus; Primate lentivirus group.
NCBI_TaxID=11686;
NCBI_TaxID=9606; Homo sapiens (Human).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=2981635; DOI=10.1016/0092-8674(85)90303-4;
Wain-Hobson S., Sonigo P., Danos O., Cole S., Alizon M.;
"Nucleotide sequence of the AIDS virus, LAV.";
Cell 40:9-17(1985).
[2]
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.
[3]
FUNCTION.
PubMed=2136707;
Cohen E.A., Terwilliger E.F., Jalinoos Y., Proulx J., Sodroski J.G.,
Haseltine W.A.;
"Identification of HIV-1 vpr product and function.";
J. Acquir. Immune Defic. Syndr. 3:11-18(1990).
[4]
FUNCTION.
PubMed=2139896;
Cohen E.A., Dehni G., Sodroski J.G., Haseltine W.A.;
"Human immunodeficiency virus vpr product is a virion-associated
regulatory protein.";
J. Virol. 64:3097-3099(1990).
[5]
SUBCELLULAR LOCATION.
PubMed=8411357;
Lu Y.L., Spearman P., Ratner L.;
"Human immunodeficiency virus type 1 viral protein R localization in
infected cells and virions.";
J. Virol. 67:6542-6550(1993).
[6]
MUTAGENESIS OF ARG-32; ARG-62 AND CYS-76.
PubMed=8230445;
Paxton W., Connor R.I., Landau N.R.;
"Incorporation of Vpr into human immunodeficiency virus type 1
virions: requirement for the p6 region of gag and mutational
analysis.";
J. Virol. 67:7229-7237(1993).
[7]
FUNCTION.
PubMed=8041786; DOI=10.1073/pnas.91.15.7311;
Heinzinger N.K., Bukinsky M.I., Haggerty S.A., Ragland A.M.,
Kewalramani V., Lee M.A., Gendelman H.E., Ratner L., Stevenson M.,
Emerman M.;
"The Vpr protein of human immunodeficiency virus type 1 influences
nuclear localization of viral nucleic acids in nondividing host
cells.";
Proc. Natl. Acad. Sci. U.S.A. 91:7311-7315(1994).
[8]
INTERACTION WITH HUMAN SP1.
PubMed=7592727; DOI=10.1074/jbc.270.43.25564;
Wang L., Mukherjee S., Jia F., Narayan O., Zhao L.J.;
"Interaction of virion protein Vpr of human immunodeficiency virus
type 1 with cellular transcription factor Sp1 and trans-activation of
viral long terminal repeat.";
J. Biol. Chem. 270:25564-25569(1995).
[9]
FUNCTION.
PubMed=7724608; DOI=10.1073/pnas.92.8.3621;
Refaeli Y., Levy D.N., Weiner D.B.;
"The glucocorticoid receptor type II complex is a target of the HIV-1
vpr gene product.";
Proc. Natl. Acad. Sci. U.S.A. 92:3621-3625(1995).
[10]
INTERACTION WITH P6-GAG.
PubMed=7474102;
Lu Y.L., Bennett R.P., Wills J.W., Gorelick R., Ratner L.;
"A leucine triplet repeat sequence (LXX)4 in p6gag is important for
Vpr incorporation into human immunodeficiency virus type 1
particles.";
J. Virol. 69:6873-6879(1995).
[11]
FUNCTION.
PubMed=7474100;
Re F., Braaten D., Franke E.K., Luban J.;
"Human immunodeficiency virus type 1 Vpr arrests the cell cycle in G2
by inhibiting the activation of p34cdc2-cyclin B.";
J. Virol. 69:6859-6864(1995).
[12]
FUNCTION.
PubMed=7666531;
Jowett J.B., Planelles V., Poon B., Shah N.P., Chen M.L., Chen I.S.;
"The human immunodeficiency virus type 1 vpr gene arrests infected T
cells in the G2 + M phase of the cell cycle.";
J. Virol. 69:6304-6313(1995).
[13]
INTERACTION WITH HUMAN UNG.
PubMed=8551605;
Bouhamdan M., Benichou S., Rey F., Navarro J.-M., Agostini I.,
Spire B., Camonis J., Slupphaug G., Vigne R., Benarous R., Sire J.;
"Human immunodeficiency virus type 1 Vpr protein binds to the uracil
DNA glycosylase DNA repair enzyme.";
J. Virol. 70:697-704(1996).
[14]
INTERACTION WITH HUMAN TFIIB.
PubMed=8800208; DOI=10.1006/jmbi.1996.0485;
Agostini I., Navarro J.-M., Rey F., Bouhamdan M., Spire B., Vigne R.,
Sire J.;
"The human immunodeficiency virus type 1 Vpr transactivator:
cooperation with promoter-bound activator domains and binding to
TFIIB.";
J. Mol. Biol. 261:599-606(1996).
[15]
MUTAGENESIS OF 80-ARG--ARG-90.
PubMed=9514978; DOI=10.1006/viro.1998.9028;
Zhou Y., Lu Y., Ratner L.;
"Arginine residues in the C-terminus of HIV-1 Vpr are important for
nuclear localization and cell cycle arrest.";
Virology 242:414-424(1998).
[16]
FUNCTION.
PubMed=9657723; DOI=10.1126/science.281.5374.266;
Poon B., Grovit-Ferbas K., Stewart S.A., Chen I.S.;
"Cell cycle arrest by Vpr in HIV-1 virions and insensitivity to
antiretroviral agents.";
Science 281:266-269(1998).
[17]
SUBCELLULAR LOCATION.
PubMed=9817747; DOI=10.1083/jcb.143.4.875;
Jenkins Y., McEntee M., Weis K., Greene W.C.;
"Characterization of HIV-1 vpr nuclear import: analysis of signals and
pathways.";
J. Cell Biol. 143:875-885(1998).
[18]
INTERACTION WITH HUMAN RAD23A.
PubMed=9371639;
Withers-Ward E.S., Jowett J.B., Stewart S.A., Xie Y.M., Garfinkel A.,
Shibagaki Y., Chow S.A., Shah N., Hanaoka F., Sawitz D.G.,
Armstrong R.W., Souza L.M., Chen I.S.;
"Human immunodeficiency virus type 1 Vpr interacts with HHR23A, a
cellular protein implicated in nucleotide excision DNA repair.";
J. Virol. 71:9732-9742(1997).
[19]
INTERACTION WITH HUMAN COPS6, AND MUTAGENESIS OF ALA-30;
20-LEU--LEU-26; ALA-59; LEU-67; HIS-71; GLY-75 AND CYS-76.
PubMed=9520381; DOI=10.1073/pnas.95.7.3419;
Mahalingam S., Ayyavoo V., Patel M., Kieber-Emmons T., Kao G.D.,
Muschel R.J., Weiner D.B.;
"HIV-1 Vpr interacts with a human 34-kDa mov34 homologue, a cellular
factor linked to the G2/M phase transition of the mammalian cell
cycle.";
Proc. Natl. Acad. Sci. U.S.A. 95:3419-3424(1998).
[20]
INTERACTION WITH HUMAN KPNA1 AND KPNA2.
PubMed=9463369; DOI=10.1093/emboj/17.4.909;
Popov S., Rexach M., Zybarth G., Reiling N., Lee M.A., Ratner L.,
Lane C.M., Moore M.S., Blobel G., Bukrinsky M.;
"Viral protein R regulates nuclear import of the HIV-1 pre-integration
complex.";
EMBO J. 17:909-917(1998).
[21]
INTERACTION WITH HUMAN SP1.
PubMed=9685344; DOI=10.1074/jbc.273.32.20052;
Sawaya B.E., Khalili K., Mercer W.E., Denisova L., Amini S.;
"Cooperative actions of HIV-1 Vpr and p53 modulate viral gene
transcription.";
J. Biol. Chem. 273:20052-20057(1998).
[22]
MUTAGENESIS OF LEU-23; GLU-25; ALA-30; VAL-57; ARG-62; ILE-63;
68-LEU--ILE-70 AND ARG-80.
PubMed=9837715; DOI=10.1006/jmbi.1998.2206;
Forget J., Yao X.J., Mercier J., Cohen E.A.;
"Human immunodeficiency virus type 1 vpr protein transactivation
function: mechanism and identification of domains involved.";
J. Mol. Biol. 284:915-923(1998).
[23]
FUNCTION.
PubMed=9539783; DOI=10.1073/pnas.95.8.4595;
Piller S.C., Jans P., Gage P.W., Jans D.A.;
"Extracellular HIV-1 virus protein R causes a large inward current and
cell death in cultured hippocampal neurons: implications for AIDS
pathology.";
Proc. Natl. Acad. Sci. U.S.A. 95:4595-4600(1998).
[24]
FUNCTION.
PubMed=9525900; DOI=10.1074/jbc.273.14.8009;
Bouhamdan M., Xue Y., Baudat Y., Hu B., Sire J., Pomerantz R.J.,
Duan L.X.;
"Diversity of HIV-1 Vpr interactions involves usage of the WXXF motif
of host cell proteins.";
J. Biol. Chem. 273:8009-8016(1998).
[25]
INTERACTION WITH HUMAN TFIIB.
PubMed=9874563; DOI=10.1084/jem.189.1.51;
Kino T., Gragerov A., Kopp J.B., Stauber R.H., Pavlakis G.N.,
Chrousos G.P.;
"The HIV-1 virion-associated protein vpr is a coactivator of the human
glucocorticoid receptor.";
J. Exp. Med. 189:51-62(1999).
[26]
MUTAGENESIS OF GLU-17; TRP-18; GLU-24; GLU-25; HIS-33; PHE-34; TRP-54;
HIS-71; HIS-78; SER-79; ARG-88; ALA-89 AND ARG-90.
PubMed=10074177;
Chen M., Elder R.T., Yu M., O'Gorman M.G., Selig L., Benarous R.,
Yamamoto A., Zhao Y.;
"Mutational analysis of Vpr-induced G2 arrest, nuclear localization,
and cell death in fission yeast.";
J. Virol. 73:3236-3245(1999).
[27]
MUTAGENESIS OF GLU-25; ALA-30; VAL-57 AND ARG-80.
PubMed=10359081; DOI=10.1016/S0014-5793(99)00501-3;
Agostini I., Navarro J.M., Bouhamdan M., Willetts K., Rey F.,
Spire B., Vigne R., Pomerantz R., Sire J.;
"The HIV-1 Vpr co-activator induces a conformational change in
TFIIB.";
FEBS Lett. 450:235-239(1999).
[28]
FUNCTION.
PubMed=10518572; DOI=10.1073/pnas.96.21.12039;
Stewart S.A., Poon B., Jowett J.B., Xie Y., Chen I.S.;
"Lentiviral delivery of HIV-1 Vpr protein induces apoptosis in
transformed cells.";
Proc. Natl. Acad. Sci. U.S.A. 96:12039-12043(1999).
[29]
MUTAGENESIS OF GLU-21; GLU-24; GLU-58 AND ARG-95.
PubMed=10196319;
Piller S.C., Ewart G.D., Jans D.A., Gage P.W., Cox G.B.;
"The amino-terminal region of Vpr from human immunodeficiency virus
type 1 forms ion channels and kills neurons.";
J. Virol. 73:4230-4238(1999).
[30]
MUTAGENESIS OF ARG-73.
PubMed=10775627; DOI=10.1128/JVI.74.10.4877-4881.2000;
Sawaya B.E., Khalili K., Gordon J., Srinivasan A., Richardson M.,
Rappaport J., Amini S.;
"Transdominant activity of human immunodeficiency virus type 1 Vpr
with a mutation at residue R73.";
J. Virol. 74:4877-4881(2000).
[31]
FUNCTION.
PubMed=10620603; DOI=10.1084/jem.191.1.33;
Jacotot E., Ravagnan L., Loeffler M., Ferri K.F., Vieira H.L.A.,
Zamzami N., Costantini P., Druillennec S., Hoebeke J., Briand J.-P.,
Irinopoulou T., Daugas E., Susin S.A., Cointe D., Xie Z.H., Reed J.C.,
Roques B.P., Kroemer G.;
"The HIV-1 viral protein R induces apoptosis via a direct effect on
the mitochondrial permeability transition pore.";
J. Exp. Med. 191:33-46(2000).
[32]
PHOSPHORYLATION AT SER-79; SER-94 AND SER-96, AND MUTAGENESIS OF
SER-79; SER-94 AND SER-96.
STRAIN=Clone pNL4-3;
PubMed=10864665; DOI=10.1128/JVI.74.14.6520-6527.2000;
Zhou Y., Ratner L.;
"Phosphorylation of human immunodeficiency virus type 1 Vpr regulates
cell cycle arrest.";
J. Virol. 74:6520-6527(2000).
[33]
FUNCTION.
PubMed=10708425; DOI=10.1128/JVI.74.7.3105-3111.2000;
Stewart S.A., Poon B., Song J.Y., Chen I.S.;
"Human immunodeficiency virus type 1 vpr induces apoptosis through
caspase activation.";
J. Virol. 74:3105-3111(2000).
[34]
PHOSPHORYLATION AT SER-79.
PubMed=11860675; DOI=10.1089/088922202753472856;
Agostini I., Popov S., Hao T., Li J.H., Dubrovsky L., Chaika O.,
Chaika N., Lewis R., Bukrinsky M.;
"Phosphorylation of Vpr regulates HIV type 1 nuclear import and
macrophage infection.";
AIDS Res. Hum. Retroviruses 18:283-288(2002).
[35]
FUNCTION.
PubMed=12573582; DOI=10.1006/viro.2002.1777;
Chowdhury I.H., Wang X.F., Landau N.R., Robb M.L., Polonis V.R.,
Birx D.L., Kim J.H.;
"HIV-1 Vpr activates cell cycle inhibitor p21/Waf1/Cip1: a potential
mechanism of G2/M cell cycle arrest.";
Virology 305:371-377(2003).
[36]
FUNCTION.
PubMed=12634356; DOI=10.1128/JVI.77.7.3962-3972.2003;
Poon B., Chen I.S.;
"Human immunodeficiency virus type 1 (HIV-1) Vpr enhances expression
from unintegrated HIV-1 DNA.";
J. Virol. 77:3962-3972(2003).
[37]
INTERACTION WITH HUMAN CDC25C.
PubMed=14972559; DOI=10.1016/j.virol.2003.10.007;
Goh W.C., Manel N., Emerman M.;
"The human immunodeficiency virus Vpr protein binds Cdc25C:
implications for G2 arrest.";
Virology 318:337-349(2004).
[38]
INTERACTION WITH HUMAN SLC25A4; SLC25A5 AND SLC25A6.
PubMed=16120388; DOI=10.1016/j.mito.2004.06.012;
Deniaud A., Brenner C., Kroemer G.;
"Mitochondrial membrane permeabilization by HIV-1 Vpr.";
Mitochondrion 4:223-233(2004).
[39]
INTERACTION WITH ANKHD1.
PubMed=16098192; DOI=10.1111/j.1742-4658.2005.04821.x;
Miles M.C., Janket M.L., Wheeler E.D., Chattopadhyay A., Majumder B.,
Dericco J., Schafer E.A., Ayyavoo V.;
"Molecular and functional characterization of a novel splice variant
of ANKHD1 that lacks the KH domain and its role in cell survival and
apoptosis.";
FEBS J. 272:4091-4102(2005).
[40]
REVIEW.
PubMed=16511342;
Moon H.S., Yang J.S.;
"Role of HIV Vpr as a regulator of apoptosis and an effector on
bystander cells.";
Mol. Cells 21:7-20(2006).
[41]
INTERACTION WITH HUMAN SF3B2.
PubMed=16923959; DOI=10.1128/MCB.01170-06;
Terada Y., Yasuda Y.;
"Human immunodeficiency virus type 1 Vpr induces G2 checkpoint
activation by interacting with the splicing factor SAP145.";
Mol. Cell. Biol. 26:8149-8158(2006).
[42]
FUNCTION.
PubMed=17314515;
Le Rouzic E., Belaiedouni N., Estrabaud E., Morel M., Rain J.-C.,
Transy C., Margottin-Goguet F.;
"HIV1 Vpr arrests the cell cycle by recruiting DCAF1/VprBP, a receptor
of the Cul4-DDB1 ubiquitin ligase.";
Cell Cycle 6:182-188(2007).
[43]
FUNCTION.
PubMed=17630831; DOI=10.1371/journal.ppat.0030085;
Belzile J.P., Duisit G., Rougeau N., Mercier J., Finzi A., Cohen E.A.;
"HIV-1 Vpr-mediated G2 arrest involves the DDB1-CUL4A[VPRBP] E3
ubiquitin ligase.";
PLoS Pathog. 3:E85-E85(2007).
[44]
INTERACTION WITH HOST DCAF1.
PubMed=23612978; DOI=10.1074/jbc.M112.416735;
Wang X., Singh S., Jung H.Y., Yang G., Jun S., Sastry K.J., Park J.I.;
"HIV-1 Vpr protein inhibits telomerase activity via the EDD-DDB1-VPRBP
E3 ligase complex.";
J. Biol. Chem. 288:15474-15480(2013).
[45]
INTERACTION WITH HOST DCAF1.
PubMed=24116224; DOI=10.1371/journal.pone.0077320;
Maudet C., Sourisce A., Dragin L., Lahouassa H., Rain J.C.,
Bouaziz S., Ramirez B.C., Margottin-Goguet F.;
"HIV-1 Vpr Induces the Degradation of ZIP and sZIP, Adaptors of the
NuRD Chromatin Remodeling Complex, by Hijacking DCAF1/VprBP.";
PLoS ONE 8:E77320-E77320(2013).
-!- FUNCTION: During virus entry, plays a role in the transport of the
viral pre-integration (PIC) complex to the host nucleus. This
function is crucial for viral infection of non-dividing
macrophages. May act directly at the nuclear pore complex, by
binding nucleoporins phenylalanine-glycine (FG)-repeat regions.
{ECO:0000255|HAMAP-Rule:MF_04080, ECO:0000269|PubMed:10518572,
ECO:0000269|PubMed:10620603, ECO:0000269|PubMed:10708425,
ECO:0000269|PubMed:12573582, ECO:0000269|PubMed:12634356,
ECO:0000269|PubMed:17314515, ECO:0000269|PubMed:17630831,
ECO:0000269|PubMed:2136707, ECO:0000269|PubMed:2139896,
ECO:0000269|PubMed:7474100, ECO:0000269|PubMed:7666531,
ECO:0000269|PubMed:7724608, ECO:0000269|PubMed:8041786,
ECO:0000269|PubMed:9525900, ECO:0000269|PubMed:9539783,
ECO:0000269|PubMed:9657723}.
-!- FUNCTION: During virus replication, may deplete host UNG protein,
and incude G2-M cell cycle arrest. Acts by targeting specific host
proteins for degradation by the 26S proteasome, through
association with the cellular CUL4A-DDB1 E3 ligase complex by
direct interaction with host VPRPB/DCAF-1. Cell cycle arrest
reportedly occurs within hours of infection and is not blocked by
antiviral agents, suggesting that it is initiated by the VPR
carried into the virion. Additionally, VPR induces apoptosis in a
cell cycle dependent manner suggesting that these two effects are
mechanistically linked. Detected in the serum and cerebrospinal
fluid of AIDS patient, VPR may also induce cell death to bystander
cells. {ECO:0000255|HAMAP-Rule:MF_04080}.
-!- SUBUNIT: Homooligomer, may form homodimer. Interacts with p6-gag
region of the Pr55 Gag precursor protein through a (Leu-X-X)4
motif near the C-terminus of the P6gag protein. Interacts with
host UNG. May interact with host RAD23A/HHR23A. Interacts with
host VPRBP/DCAF1, leading to hijack the CUL4A-RBX1-DDB1-
DCAF1/VPRBP complex, mediating ubiquitination of host proteins
such as TERT and ZGPAT and arrest of the cell cycle in G2 phase.
{ECO:0000255|HAMAP-Rule:MF_04080, ECO:0000269|PubMed:14972559,
ECO:0000269|PubMed:16098192, ECO:0000269|PubMed:16120388,
ECO:0000269|PubMed:16923959, ECO:0000269|PubMed:23612978,
ECO:0000269|PubMed:24116224, ECO:0000269|PubMed:7474102,
ECO:0000269|PubMed:7592727, ECO:0000269|PubMed:8551605,
ECO:0000269|PubMed:8800208, ECO:0000269|PubMed:9371639,
ECO:0000269|PubMed:9463369, ECO:0000269|PubMed:9520381,
ECO:0000269|PubMed:9685344, ECO:0000269|PubMed:9874563}.
-!- INTERACTION:
Q9Y4B6-3:DCAF1 (xeno); NbExp=2; IntAct=EBI-9210238, EBI-9915372;
-!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04080}.
Host nucleus {ECO:0000255|HAMAP-Rule:MF_04080}. Host extracellular
space {ECO:0000255|HAMAP-Rule:MF_04080}. Note=Incorporation into
virion is dependent on p6 GAG sequences. Lacks a canonical nuclear
localization signal, thus import into nucleus may function
independently of the human importin pathway. Detected in high
quantity in the serum and cerebrospinal fluid of AIDS patient.
{ECO:0000255|HAMAP-Rule:MF_04080}.
-!- PTM: Phosphorylated on several residues by host. These
phosphorylations regulate VPR activity for the nuclear import of
the HIV-1 pre-integration complex. {ECO:0000255|HAMAP-
Rule:MF_04080, ECO:0000269|PubMed:10864665,
ECO:0000269|PubMed:11860675}.
-!- 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: 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_04080}.
-!- SIMILARITY: Belongs to the HIV-1 VPR protein family.
{ECO:0000255|HAMAP-Rule:MF_04080}.
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EMBL; K02013; AAB59749.1; -; Genomic_RNA.
ProteinModelPortal; P05928; -.
SMR; P05928; -.
IntAct; P05928; 13.
iPTMnet; P05928; -.
OrthoDB; VOG090001DK; -.
Proteomes; UP000007692; Genome.
GO; GO:0043655; C:extracellular space of host; IEA:UniProtKB-SubCell.
GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
GO; GO:0019012; C:virion; IEA:UniProtKB-SubCell.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0039592; P:suppression by virus of G2/M transition of host mitotic cell cycle; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
GO; GO:0075732; P:viral penetration into host nucleus; IEA:UniProtKB-KW.
HAMAP; MF_04080; HIV_VPR; 1.
InterPro; IPR000012; RetroV_VpR/X.
Pfam; PF00522; VPR; 1.
PRINTS; PR00444; HIVVPRVPX.
1: Evidence at protein level;
Activator; AIDS; Apoptosis; Cell cycle; Complete proteome;
Host G2/M cell cycle arrest by virus; Host nucleus;
Host-virus interaction; Ion channel; Ion transport;
Modulation of host cell cycle by virus; Phosphoprotein;
Reference proteome; Transcription; Transcription regulation;
Transport; Viral penetration into host nucleus; Virion;
Virus entry into host cell.
CHAIN 1 96 Protein Vpr.
/FTId=PRO_0000085439.
REGION 1 42 Homooligomerization. {ECO:0000255|HAMAP-
Rule:MF_04080}.
MOD_RES 79 79 Phosphoserine; by host.
{ECO:0000255|HAMAP-Rule:MF_04080,
ECO:0000269|PubMed:10864665,
ECO:0000269|PubMed:11860675}.
MOD_RES 94 94 Phosphoserine; by host.
{ECO:0000255|HAMAP-Rule:MF_04080,
ECO:0000269|PubMed:10864665}.
MOD_RES 96 96 Phosphoserine; by host.
{ECO:0000255|HAMAP-Rule:MF_04080,
ECO:0000269|PubMed:10864665}.
VARIANT 15 15 H -> Y (in strain: Clone pNL4-3).
VARIANT 28 28 N -> S (in strain: Clone pNL4-3).
VARIANT 41 41 G -> N (in strain: Clone pNL4-3).
VARIANT 85 85 Q -> R (in strain: Clone pNL4-3).
MUTAGEN 17 17 E->D: No effect.
{ECO:0000269|PubMed:10074177}.
MUTAGEN 18 18 W->R: Partial loss of cell killing.
{ECO:0000269|PubMed:10074177}.
MUTAGEN 20 26 LELLEEL->AEAAEEA: Partial loss of nuclear
localization.
{ECO:0000269|PubMed:9520381}.
MUTAGEN 21 21 E->Q: Partial loss of Na(+) permeability
for ion channel function.
{ECO:0000269|PubMed:10196319}.
MUTAGEN 23 23 L->F: 80% loss incorporation into virion.
10% loss of LTR transactivation.
{ECO:0000269|PubMed:9837715}.
MUTAGEN 24 24 E->G: Partial loss of cell killing.
{ECO:0000269|PubMed:10074177,
ECO:0000269|PubMed:10196319}.
MUTAGEN 24 24 E->Q: Partial loss of Na(+) permeability
for ion channel function.
{ECO:0000269|PubMed:10074177,
ECO:0000269|PubMed:10196319}.
MUTAGEN 25 25 E->K: 75% loss incorporation into virion.
Perinuclear localization. Partial loss of
cell killing. No effect on human TFIIB
binding. {ECO:0000269|PubMed:10074177,
ECO:0000269|PubMed:10359081,
ECO:0000269|PubMed:9837715}.
MUTAGEN 30 30 A->F: 80% loss incorporation into virion.
Perinuclear localization. 56% loss of LTR
transactivation. No effect on human TFIIB
binding. {ECO:0000269|PubMed:10359081,
ECO:0000269|PubMed:9520381,
ECO:0000269|PubMed:9837715}.
MUTAGEN 30 30 A->L: Complete loss of G2/M cell cycle
arrest. {ECO:0000269|PubMed:10359081,
ECO:0000269|PubMed:9520381,
ECO:0000269|PubMed:9837715}.
MUTAGEN 32 32 R->A: No effect on incorporation in
virion. {ECO:0000269|PubMed:8230445}.
MUTAGEN 33 33 H->R: Partial loss of nuclear
localization, cell killing and G2/M cell
cycle arrest.
{ECO:0000269|PubMed:10074177}.
MUTAGEN 34 34 F->I: Partial loss of cell killing and
nuclear localization.
{ECO:0000269|PubMed:10074177}.
MUTAGEN 54 54 W->R: Partial loss of cell killing.
{ECO:0000269|PubMed:10074177}.
MUTAGEN 57 57 V->L: 25% loss incorporation into virion.
Perinuclear localization. No effect on
human TFIIB binding.
{ECO:0000269|PubMed:10359081,
ECO:0000269|PubMed:9837715}.
MUTAGEN 58 58 E->Q: No effect on ion channel activity.
{ECO:0000269|PubMed:10196319}.
MUTAGEN 59 59 A->P: Complete loss of G2/M cell cycle
arrest. {ECO:0000269|PubMed:9520381}.
MUTAGEN 62 62 R->A: No effect on incorporation in
virion. {ECO:0000269|PubMed:8230445,
ECO:0000269|PubMed:9837715}.
MUTAGEN 62 62 R->P: 30% loss incorporation into virion.
Perinuclear localization. 8% loss of LTR
transactivation.
{ECO:0000269|PubMed:8230445,
ECO:0000269|PubMed:9837715}.
MUTAGEN 63 63 I->F: 10% loss incorporation into virion.
Perinuclear localization. 31% loss of LTR
transactivation.
{ECO:0000269|PubMed:9837715}.
MUTAGEN 63 63 I->K: 35% loss incorporation into virion.
Perinuclear localization. 22% loss of LTR
transactivation.
{ECO:0000269|PubMed:9837715}.
MUTAGEN 67 67 L->S: Partial loss of nuclear
localization. Complete loss of G2/M cell
cycle arrest.
{ECO:0000269|PubMed:9520381}.
MUTAGEN 68 70 LFI->KFR: Complete loss of G2/M cell
cycle arrest. Perinuclear localization.
66% loss of LTR transactivation.
{ECO:0000269|PubMed:9837715}.
MUTAGEN 71 71 H->C: Complete loss of G2/M cell cycle
arrest. {ECO:0000269|PubMed:10074177,
ECO:0000269|PubMed:9520381}.
MUTAGEN 71 71 H->R: Partial loss of nuclear
localization, cell killing and G2/M cell
cycle arrest.
{ECO:0000269|PubMed:10074177,
ECO:0000269|PubMed:9520381}.
MUTAGEN 73 73 R->A,S: Complete loss of LTR
transactivation and of G2/M cell cycle
arrest. Transdominant mutation.
{ECO:0000269|PubMed:10775627}.
MUTAGEN 75 75 G->A: Complete loss of G2/M cell cycle
arrest. {ECO:0000269|PubMed:9520381}.
MUTAGEN 76 76 C->A: Complete loss of incorporation in
virion. {ECO:0000269|PubMed:8230445,
ECO:0000269|PubMed:9520381}.
MUTAGEN 76 76 C->S: Complete loss of G2/M cell cycle
arrest. {ECO:0000269|PubMed:8230445,
ECO:0000269|PubMed:9520381}.
MUTAGEN 78 78 H->R: Partial loss of G2/M cell cycle
arrest. {ECO:0000269|PubMed:10074177}.
MUTAGEN 79 79 S->A: Complete loss of cell cycle arrest.
{ECO:0000269|PubMed:10074177,
ECO:0000269|PubMed:10864665}.
MUTAGEN 80 90 RIGVTQQRRAR->NIGVTNQNNAN: Partial loss of
nuclear localization.
{ECO:0000269|PubMed:9514978}.
MUTAGEN 80 80 R->A: Complete loss of G2/M cell cycle
arrest. 66% loss of LTR transactivation.
Complete loss of human TFIIB binding.
{ECO:0000269|PubMed:10359081,
ECO:0000269|PubMed:9837715}.
MUTAGEN 88 88 R->K: Partial loss of G2/M cell cycle
arrest. {ECO:0000269|PubMed:10074177}.
MUTAGEN 89 89 A->T: No effect.
{ECO:0000269|PubMed:10074177}.
MUTAGEN 90 90 R->K: Partial loss of cell killing and
G2/M cell cycle arrest.
{ECO:0000269|PubMed:10074177}.
MUTAGEN 94 94 S->G: Partial loss of cell cycle arrest.
{ECO:0000269|PubMed:10864665}.
MUTAGEN 95 95 R->Q: No effect on ion channel activity.
{ECO:0000269|PubMed:10196319}.
MUTAGEN 96 96 S->P: No effect on cell cycle arrest.
{ECO:0000269|PubMed:10864665}.
SEQUENCE 96 AA; 11295 MW; 42892A4186E83D3E CRC64;
MEQAPEDQGP QREPHNEWTL ELLEELKNEA VRHFPRIWLH GLGQHIYETY GDTWAGVEAI
IRILQQLLFI HFRIGCRHSR IGVTQQRRAR NGASRS


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