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Protein Rev (ART/TRS) (Anti-repression transactivator) (Regulator of expression of viral proteins)

 REV_HV1BR               Reviewed;         116 AA.
P04620;
13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
13-AUG-1987, sequence version 1.
05-DEC-2018, entry version 108.
RecName: Full=Protein Rev {ECO:0000255|HAMAP-Rule:MF_04077};
AltName: Full=ART/TRS {ECO:0000255|HAMAP-Rule:MF_04077};
AltName: Full=Anti-repression transactivator {ECO:0000255|HAMAP-Rule:MF_04077};
AltName: Full=Regulator of expression of viral proteins {ECO:0000255|HAMAP-Rule:MF_04077};
Name=rev {ECO:0000255|HAMAP-Rule:MF_04077};
Human immunodeficiency virus type 1 group M subtype B (isolate
BRU/LAI) (HIV-1).
Viruses; Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
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]
INTERACTION WITH HUMAN KPNB1, AND MUTAGENESIS OF ARG-38; ARG-39;
LEU-78 AND LEU-81.
PubMed=9405152; DOI=10.1006/jmbi.1997.1420;
Henderson B.R., Percipalle P.;
"Interactions between HIV Rev and nuclear import and export factors:
the Rev nuclear localisation signal mediates specific binding to human
importin-beta.";
J. Mol. Biol. 274:693-707(1997).
[4]
REVIEW.
PubMed=10328811; DOI=10.1006/abbi.1999.1207;
Hope T.J.;
"The ins and outs of HIV Rev.";
Arch. Biochem. Biophys. 365:186-191(1999).
-!- FUNCTION: Escorts unspliced or incompletely spliced viral pre-
mRNAs (late transcripts) out of the nucleus of infected cells.
These pre-mRNAs carry a recognition sequence called Rev responsive
element (RRE) located in the env gene, that is not present in
fully spliced viral mRNAs (early transcripts). This function is
essential since most viral proteins are translated from unspliced
or partially spliced pre-mRNAs which cannot exit the nucleus by
the pathway used by fully processed cellular mRNAs. Rev itself is
translated from a fully spliced mRNA that readily exits the
nucleus. Rev's nuclear localization signal (NLS) binds directly to
KPNB1/Importin beta-1 without previous binding to KPNA1/Importin
alpha-1. KPNB1 binds to the GDP bound form of RAN (Ran-GDP) and
targets Rev to the nucleus. In the nucleus, the conversion from
Ran-GDP to Ran-GTP dissociates Rev from KPNB1 and allows Rev's
binding to the RRE in viral pre-mRNAs. Rev multimerization on the
RRE via cooperative assembly exposes its nuclear export signal
(NES) to the surface. Rev can then form a complex with XPO1/CRM1
and Ran-GTP, leading to nuclear export of the complex. Conversion
from Ran-GTP to Ran-GDP mediates dissociation of the
Rev/RRE/XPO1/RAN complex, so that Rev can return to the nucleus
for a subsequent round of export. Beside KPNB1, also seems to
interact with TNPO1/Transportin-1, RANBP5/IPO5 and IPO7/RANBP7 for
nuclear import. The nucleoporin-like HRB/RIP is an essential
cofactor that probably indirectly interacts with Rev to release
HIV RNAs from the perinuclear region to the cytoplasm.
{ECO:0000255|HAMAP-Rule:MF_04077}.
-!- SUBUNIT: Homomultimer; when bound to the RRE. Multimeric assembly
is essential for activity and may involve XPO1. Binds to human
KPNB1, XPO1, TNPO1, RANBP5 and IPO7. Interacts with the viral
Integrase. Interacts with human KHDRBS1. Interacts with human
NAP1; this interaction decreases Rev multimerization and
stimulates its activity. Interacts with human DEAD-box helicases
DDX3 and DDX24; these interactions may serve for viral RNA export
to the cytoplasm and packaging, respectively. Interacts with human
PSIP1; this interaction may inhibit HIV-1 DNA integration by
promoting dissociation of the Integrase-LEDGF/p75 complex.
{ECO:0000255|HAMAP-Rule:MF_04077}.
-!- INTERACTION:
P52292:KPNA2 (xeno); NbExp=2; IntAct=EBI-10687101, EBI-349938;
Q14974:KPNB1 (xeno); NbExp=3; IntAct=EBI-10687101, EBI-286758;
-!- SUBCELLULAR LOCATION: Host nucleus, host nucleolus
{ECO:0000255|HAMAP-Rule:MF_04077}. Host cytoplasm
{ECO:0000255|HAMAP-Rule:MF_04077}. Note=The presence of both
nuclear import and nuclear export signals leads to continuous
shuttling between the nucleus and cytoplasm. {ECO:0000255|HAMAP-
Rule:MF_04077}.
-!- DOMAIN: The RNA-binding motif binds to the RRE, a 240 bp stem-and-
loop structure present in incompletely spliced viral pre-mRNAs.
This region also contains the NLS which mediates nuclear
localization via KPNB1 binding and, when the N-terminal sequence
is present, nucleolar targeting. These overlapping functions
prevent Rev bound to RRE from undesirable return to the nucleus.
When Rev binds the RRE, the NLS becomes masked while the NES
remains accessible. The leucine-rich NES mediates binding to human
XPO1. {ECO:0000255|HAMAP-Rule:MF_04077}.
-!- PTM: Asymmetrically arginine dimethylated at one site by host
PRMT6. Methylation impairs the RNA-binding activity and export of
viral RNA from the nucleus to the cytoplasm. {ECO:0000255|HAMAP-
Rule:MF_04077}.
-!- PTM: Phosphorylated by protein kinase CK2. Presence of, and maybe
binding to the N-terminus of the regulatory beta subunit of CK2 is
necessary for CK2-mediated Rev's phosphorylation.
{ECO:0000255|HAMAP-Rule:MF_04077}.
-!- 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_04077}.
-!- SIMILARITY: Belongs to the HIV-1 REV protein family.
{ECO:0000255|HAMAP-Rule:MF_04077}.
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EMBL; K02013; AAB59746.1; -; Genomic_RNA.
EMBL; M19921; AAA44986.1; -; Genomic_RNA.
SMR; P04620; -.
IntAct; P04620; 2.
OrthoDB; VOG090001FN; -.
Proteomes; UP000007692; Genome.
GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0044196; C:host cell nucleolus; IEA:UniProtKB-SubCell.
GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:UniProtKB-UniRule.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-UniRule.
GO; GO:0016032; P:viral process; IEA:UniProtKB-UniRule.
HAMAP; MF_04077; REV_HIV1; 1.
InterPro; IPR000625; REV_protein.
Pfam; PF00424; REV; 1.
1: Evidence at protein level;
AIDS; Complete proteome; Host cytoplasm; Host nucleus;
Host-virus interaction; Methylation; mRNA transport; Phosphoprotein;
RNA-binding; Transport.
CHAIN 1 116 Protein Rev.
/FTId=PRO_0000085260.
REGION 18 26 Homomultimerization. {ECO:0000255|HAMAP-
Rule:MF_04077}.
MOTIF 34 50 Nuclear localization signal and RNA-
binding (RRE). {ECO:0000255|HAMAP-
Rule:MF_04077}.
MOTIF 73 84 Nuclear export signal and binding to
XPO1. {ECO:0000255|HAMAP-Rule:MF_04077}.
COMPBIAS 38 50 Poly-Arg.
MOD_RES 5 5 Phosphoserine; by host CK2.
{ECO:0000255|HAMAP-Rule:MF_04077}.
MOD_RES 8 8 Phosphoserine; by host CK2.
{ECO:0000255|HAMAP-Rule:MF_04077}.
MOD_RES 92 92 Phosphoserine; by host.
{ECO:0000255|HAMAP-Rule:MF_04077}.
MOD_RES 99 99 Phosphoserine; by host.
{ECO:0000255|HAMAP-Rule:MF_04077}.
VARIANT 11 15 DLLKA -> ELIRT (in strain: Clone pNL4-3).
VARIANT 21 21 F -> L (in strain: Clone pNL4-3).
MUTAGEN 38 38 R->D: No effect on KPNB1 binding; when
associated with L-39.
{ECO:0000269|PubMed:9405152}.
MUTAGEN 39 39 R->L: No effect on KPNB1 binding; when
associated with D-38.
{ECO:0000269|PubMed:9405152}.
MUTAGEN 78 78 L->A: Complete loss of Rev export.
{ECO:0000269|PubMed:9405152}.
MUTAGEN 81 81 L->A: Complete loss of Rev export.
{ECO:0000269|PubMed:9405152}.
SEQUENCE 116 AA; 13067 MW; 30DA320AF302FBCD CRC64;
MAGRSGDSDE DLLKAVRLIK FLYQSNPPPN PEGTRQARRN RRRRWRERQR QIHSISERIL
STYLGRSAEP VPLQLPPLER LTLDCNEDCG TSGTQGVGSP QILVESPTVL ESGTKE


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