REV_EIAVY
ID REV_EIAVY Reviewed; 165 AA.
AC P20919;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 02-JUN-2021, entry version 71.
DE RecName: Full=Protein Rev;
DE AltName: Full=3'-ORF protein;
GN Name=rev;
OS Equine infectious anemia virus (strain Wyoming) (EIAV).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX NCBI_TaxID=11672;
OH NCBI_TaxID=9793; Equus asinus (Donkey) (Equus africanus asinus).
OH NCBI_TaxID=9796; Equus caballus (Horse).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2158694; DOI=10.1016/0042-6822(90)90254-o;
RA Noiman S., Gazit A., Tori O., Sherman L., Miki T., Tronick S.R., Yaniv A.;
RT "Identification of sequences encoding the equine infectious anemia virus
RT tat gene.";
RL Virology 176:280-288(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2164593; DOI=10.1128/jvi.64.8.3716-3725.1990;
RA Stephens R.M., Derse D., Rice N.R.;
RT "Cloning and characterization of cDNAs encoding equine infectious anemia
RT virus tat and putative Rev proteins.";
RL J. Virol. 64:3716-3725(1990).
RN [3]
RP NUCLEAR EXPORT SIGNAL.
RX PubMed=8230455; DOI=10.1128/jvi.67.12.7317-7323.1993;
RA Fridell R.A., Partin K.M., Carpenter S., Cullen B.R.;
RT "Identification of the activation domain of equine infectious anemia virus
RT rev.";
RL J. Virol. 67:7317-7323(1993).
RN [4]
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).
RN [5]
RP CHARACTERIZATION, RNA-BINDING, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP LYS-159; ARG-160; ARG-161; ARG-162 AND LYS-163.
RX PubMed=16571801; DOI=10.1128/jvi.80.8.3844-3852.2006;
RA Lee J.-H., Murphy S.C., Belshan M., Sparks W.O., Wannemuehler Y., Liu S.,
RA Hope T.J., Dobbs D., Carpenter S.;
RT "Characterization of functional domains of equine infectious anemia virus
RT Rev suggests a bipartite RNA-binding domain.";
RL J. Virol. 80:3844-3852(2006).
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 two recognition sequences that function as Rev responsive
CC element (RRE), that are not present in fully spliced viral mRNAs (early
CC transcripts). This function is essential since most viral proteins are
CC translated from unspliced or partially spliced pre-mRNAs which cannot
CC exit the nucleus by the pathway used by fully processed cellular mRNAs
CC (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:16571801}. Host cytoplasm
CC {ECO:0000269|PubMed:16571801}. 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 bipartite RNA-binding motif binds to the RREs present in
CC incompletely spliced viral pre-mRNAs. It consists of a central region,
CC and a C-terminal region that also contains the NLS which mediates
CC nuclear localization. These overlapping functions prevent Rev bound to
CC RRE from undesirable return to the nucleus. When Rev binds the RRE, the
CC NLS becomes masked while the NES remains accessible.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA43027.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M36592; AAB02404.1; -; Genomic_RNA.
DR EMBL; M54797; AAA43027.1; ALT_INIT; Genomic_RNA.
DR PIR; B46357; ASLJ22.
DR SMR; P20919; -.
DR ELM; P20919; -.
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:0019031; C:viral envelope; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR InterPro; IPR021311; EIAV_Rev.
DR InterPro; IPR001361; Gp90_EIAV.
DR Pfam; PF00971; EIAV_GP90; 1.
DR Pfam; PF11129; EIAV_Rev; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Host cytoplasm; Host nucleus; mRNA transport; RNA-binding;
KW Transport.
FT CHAIN 1..165
FT /note="Protein Rev"
FT /id="PRO_0000085478"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 56..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 57..130
FT /note="RNA-binding (RRE)"
FT REGION 144..165
FT /note="RNA-binding (RRE)"
FT REGION 146..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1..26
FT /evidence="ECO:0000255"
FT MOTIF 32..55
FT /note="Nuclear export signal"
FT /evidence="ECO:0000305"
FT MOTIF 159..163
FT /note="Nuclear localization signal"
FT COMPBIAS 1..33
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 159
FT /note="K->A: Complete loss of nuclear import; when
FT associated with A-160."
FT /evidence="ECO:0000269|PubMed:16571801"
FT MUTAGEN 160
FT /note="R->A: Complete loss of nuclear import; when
FT associated with A-159 or A-161."
FT /evidence="ECO:0000269|PubMed:16571801"
FT MUTAGEN 161
FT /note="R->A: Complete loss of nuclear import; when
FT associated with A-160 or A-162."
FT /evidence="ECO:0000269|PubMed:16571801"
FT MUTAGEN 162
FT /note="R->A: Complete loss of nuclear import; when
FT associated with A-161 or A-163."
FT /evidence="ECO:0000269|PubMed:16571801"
FT MUTAGEN 163
FT /note="K->A: Complete loss of nuclear import; when
FT associated with A-162."
FT /evidence="ECO:0000269|PubMed:16571801"
FT CONFLICT 30
FT /note="K -> I (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 59
FT /note="C -> Y (in Ref. 2; AAA43027)"
FT /evidence="ECO:0000305"
FT CONFLICT 88
FT /note="T -> A (in Ref. 2; AAA43027)"
FT /evidence="ECO:0000305"
FT CONFLICT 114
FT /note="R -> Q (in Ref. 2; AAA43027)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 165 AA; 19810 MW; 04FDEB0830888F36 CRC64;
MAESKEARDQ EMNLKEESKE EKRRNDWWKK DPQGPLESDQ WCRVLRQSLP EEKIPSQTCI
ARRHLGPGPT QHTPSRRDRW IRGQILQTEV LQERLEWRIR GVQQAAKELG EVNRGIWREL
YFREDQRGDF SAWGGYQRAQ ERLWGEQSSP RVLRPGDSKR RRKHL
