ID   REV_HV2UC               Reviewed;         150 AA.
AC   Q76631;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Protein Rev;
DE   AltName: Full=Regulator of expression of viral proteins;
GN   Name=rev;
OS   Human immunodeficiency virus type 2 subtype B (isolate UC1) (HIV-2).
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX   NCBI_TaxID=388822;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=2UC1;
RX   PubMed=8419635; DOI=10.1128/jvi.67.2.1006-1014.1993;
RA   Barnett S.W., Quiroga M., Werner A., Dina D., Levy J.A.;
RT   "Distinguishing features of an infectious molecular clone of the highly
RT   divergent and noncytopathic human immunodeficiency virus type 2 UC1
RT   strain.";
RL   J. Virol. 67:1006-1014(1993).
CC   -!- FUNCTION: Escorts unspliced or incompletely spliced viral pre-mRNAs
CC       (late transcripts) out of the nucleus of infected cells. These pre-
CC       mRNAs carry a recognition sequence called Rev responsive element (RRE)
CC       located in the env gene, that is not present in fully spliced viral
CC       mRNAs (early transcripts). This function is essential since most viral
CC       proteins are translated from unspliced or partially spliced pre-mRNAs
CC       which cannot exit the nucleus by the pathway used by fully processed
CC       cellular mRNAs (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homomultimer; when bound to the RRE. Multimeric assembly is
CC       essential for activity (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Host nucleus, host nucleolus. Host cytoplasm.
CC       Note=The presence of both nuclear import and nuclear export signals
CC       leads to continuous shuttling between the nucleus and cytoplasm.
CC       {ECO:0000250}.
CC   -!- DOMAIN: The RNA-binding motif binds to the RRE, a stem-and-loop
CC       structure present in incompletely spliced viral pre-mRNAs. This region
CC       also contains the NLS which mediates nuclear localization. These
CC       overlapping functions prevent Rev bound to RRE from undesirable return
CC       to the nucleus. When Rev binds the RRE, the NLS becomes masked while
CC       the NES remains accessible (By similarity). {ECO:0000250}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; L07625; AAA43939.1; -; Genomic_RNA.
DR   SMR; Q76631; -.
DR   Proteomes; UP000007428; Genome.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0044196; C:host cell nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR   InterPro; IPR000625; REV_protein.
DR   Pfam; PF00424; REV; 1.
PE   3: Inferred from homology;
KW   AIDS; Host cytoplasm; Host nucleus; mRNA transport; RNA-binding; Transport.
FT   CHAIN           1..150
FT                   /note="Protein Rev"
FT                   /id="PRO_0000245011"
FT   REGION          14..22
FT                   /note="Homomultimerization"
FT                   /evidence="ECO:0000250"
FT   REGION          20..41
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          103..150
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           33..47
FT                   /note="Nuclear localization signal and RNA-binding (RRE)"
FT                   /evidence="ECO:0000250"
FT   MOTIF           69..80
FT                   /note="Nuclear export signal and binding to XPO1"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        117..150
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   150 AA;  17186 MW;  2D2E4F7A9C8E392D CRC64;
     MTTREKDLQK GLRLLHLLHQ TNPYPQTPGT ASQRRNRRRR WKRRGLQILA LADRIRSLSD
     SPTEEPLDLA VQRLQELTVE DLPNPPTSTP TAQAFTCIPP VWDQLVPRSN PSSNEGCERD
     SCEHRKSPME SSQKDSGSNH RDPQEDQTRT