REV_VILV
ID REV_VILV Reviewed; 167 AA.
AC P21280;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1991, sequence version 1.
DT 23-FEB-2022, entry version 59.
DE RecName: Full=Protein Rev;
GN Name=rev; Synonyms=vep;
OS Maedi visna virus (strain 1514) (MVV) (Visna lentivirus).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX NCBI_TaxID=11742;
OH NCBI_TaxID=9940; Ovis aries (Sheep).
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2545028; DOI=10.1016/0042-6822(89)90524-2;
RA Gourdou I., Mazarin V., Querat G., Sauze N., Vigne R.;
RT "The open reading frame S of visna virus genome is a trans-activating
RT gene.";
RL Virology 171:170-178(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2536163; DOI=10.1073/pnas.86.2.414;
RA Davis J.L., Clements J.E.;
RT "Characterization of a cDNA clone encoding the visna virus transactivating
RT protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:414-418(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2846892; DOI=10.1128/jvi.62.12.4813-4818.1988;
RA Mazarin V., Gourdou I., Querat G., Sauze N., Vigne R.;
RT "Genetic structure and function of an early transcript of visna virus.";
RL J. Virol. 62:4813-4818(1988).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=8009861; DOI=10.1006/viro.1994.1367;
RA Schoborg R.V., Clements J.E.;
RT "The Rev protein of visna virus is localized to the nucleus of infected
RT cells.";
RL Virology 202:485-490(1994).
RN [5]
RP NUCLEAR EXPORT SIGNAL.
RX PubMed=8642662; DOI=10.1128/jvi.70.4.2350-2359.1996;
RA Meyer B.E., Meinkoth J.L., Malim M.H.;
RT "Nuclear transport of human immunodeficiency virus type 1, visna virus, and
RT equine infectious anemia virus Rev proteins: identification of a family of
RT transferable nuclear export signals.";
RL J. Virol. 70:2350-2359(1996).
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
CC {ECO:0000269|PubMed:8009861}. Host cytoplasm
CC {ECO:0000269|PubMed:8009861}. Note=The presence of both nuclear import
CC and nuclear export signals leads to continuous shuttling between the
CC nucleus and cytoplasm. {ECO:0000305}.
CC -!- DOMAIN: The RNA-binding motif binds to the RRE present in incompletely
CC spliced viral pre-mRNAs. This region also contains the NLS which
CC mediates nuclear localization. These overlapping functions prevent Rev
CC bound to RRE from undesirable return to the nucleus. When Rev binds the
CC RRE, the NLS becomes masked while the NES remains accessible (By
CC similarity). {ECO:0000250}.
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DR EMBL; J04359; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; M23048; AAA48363.1; -; mRNA.
DR EMBL; M25409; AAA50348.1; -; Genomic_RNA.
DR PIR; B32184; VKLJVS.
DR SMR; P21280; -.
DR PRIDE; P21280; -.
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:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR InterPro; IPR016400; Rev_lentivir.
DR PIRSF; PIRSF003867; Rev_lenti-OC; 1.
PE 2: Evidence at transcript level;
KW Coiled coil; Host cytoplasm; Host nucleus; mRNA transport; RNA-binding;
KW Transport.
FT CHAIN 1..167
FT /note="Protein Rev"
FT /id="PRO_0000085481"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 33..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 142..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 21..45
FT /evidence="ECO:0000255"
FT MOTIF 75..92
FT /note="Nuclear localization signal and RNA-binding (RRE)"
FT /evidence="ECO:0000250"
FT MOTIF 106..115
FT /note="Nuclear export signal"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..68
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..156
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 13
FT /note="W -> R (in Ref. 2; AAA48363)"
FT /evidence="ECO:0000305"
FT CONFLICT 38
FT /note="E -> D (in Ref. 1; AAA50348)"
FT /evidence="ECO:0000305"
FT CONFLICT 66
FT /note="S -> T (in Ref. 2; AAA48363)"
FT /evidence="ECO:0000305"
FT CONFLICT 101
FT /note="D -> N (in Ref. 2; AAA48363)"
FT /evidence="ECO:0000305"
FT CONFLICT 150
FT /note="E -> K (in Ref. 1; AAA50348)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 167 AA; 19226 MW; 3AB557533AF9849F CRC64;
MASKESKPSR TTWRDMEPPL RETWNQVLQE LVKRQQQEEE EQQGLVSGLQ ASKADQIYTG
NSGDRSTGGI GGKTKKKRGW YKWLRKLRAR EKNIPSQFYP DMESNMVGME NLTLETQLED
NALYNPATHI GDMAMDGREW MEWRESAQKE KRKGGLSGQR TNAYPGK
