REV_VILVK
ID REV_VILVK Reviewed; 167 AA.
AC P35957;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 23-FEB-2022, entry version 55.
DE RecName: Full=Protein Rev;
GN Name=rev;
OS Maedi visna virus (strain KV1772) (MVV) (Visna lentivirus).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX NCBI_TaxID=36374;
OH NCBI_TaxID=9940; Ovis aries (Sheep).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=8382414; DOI=10.1006/viro.1993.1106;
RA Andresson O.S., Elser J.E., Tobin G.J., Greenwood J.D., Gonda M.A.,
RA Georgsson G., Andresdottir V., Benediktsdottir E., Carlsdottir H.M.,
RA Maentylae E.O., Rafnar B., Palsson P.A., Casey J.W., Petursson G.;
RT "Nucleotide sequence and biological properties of a pathogenic proviral
RT molecular clone of neurovirulent visna virus.";
RL Virology 193:89-105(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 {ECO:0000250}. Host
CC cytoplasm {ECO:0000250}. Note=The presence of both nuclear import and
CC nuclear export signals leads to continuous shuttling between the
CC nucleus and cytoplasm. {ECO:0000250}.
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; L06906; AAA48357.1; ALT_SEQ; Genomic_RNA.
DR EMBL; S55323; AAB25464.1; -; Genomic_DNA.
DR SMR; P35957; -.
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 3: Inferred from homology;
KW Coiled coil; Host cytoplasm; Host nucleus; mRNA transport; RNA-binding;
KW Transport.
FT CHAIN 1..167
FT /note="Protein Rev"
FT /id="PRO_0000085482"
FT REGION 1..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 144..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 /evidence="ECO:0000250"
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"
SQ SEQUENCE 167 AA; 19164 MW; E7EA3A9429D9C9B5 CRC64;
MASKESKPSR TTRRGMEPPL RETWNQVLQE LVKRQQQEEE EQQGLVSGLQ ASKADQIYTG
NSGDRSTGGI GGKTKKKRGW YKWLRKLRAR EKNIPSQFYP DMESNMVGME NLTLETQLED
NALYNPATYI GDMAMDGREW MEWRESAQKE KRKGGLSGQR TNAYPGK
