ID   REV_EIAV9               Reviewed;         165 AA.
AC   P11305;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 2.
DT   02-JUN-2021, entry version 67.
DE   RecName: Full=Protein Rev;
DE   AltName: Full=3'-ORF protein;
GN   Name=rev;
OS   Equine infectious anemia virus (isolate 1369) (EIAV).
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX   NCBI_TaxID=11670;
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=3035786; DOI=10.1016/0042-6822(87)90202-9;
RA   Kawakami T., Sherman L., Dahlberg J., Gazit A., Yaniv A., Tronick S.R.,
RA   Aaronson S.A.;
RT   "Nucleotide sequence analysis of equine infectious anemia virus proviral
RT   DNA.";
RL   Virology 158:300-312(1987).
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 {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 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 (By similarity).
CC       {ECO:0000250}.
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DR   EMBL; M16575; AAB59864.1; ALT_SEQ; Genomic_RNA.
DR   PIR; D27842; ASLJEW.
DR   PDB; 4ZUS; X-ray; 2.60 A; C=87-97.
DR   PDBsum; 4ZUS; -.
DR   SMR; P11305; -.
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   3D-structure; Coiled coil; Host cytoplasm; Host nucleus; mRNA transport;
KW   RNA-binding; Transport.
FT   CHAIN           1..165
FT                   /note="Protein Rev"
FT                   /id="PRO_0000085479"
FT   REGION          1..35
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          57..130
FT                   /note="RNA-binding (RRE)"
FT                   /evidence="ECO:0000250"
FT   REGION          144..165
FT                   /note="RNA-binding (RRE)"
FT                   /evidence="ECO:0000250"
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:0000250"
FT   MOTIF           159..163
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        1..30
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   165 AA;  19765 MW;  9305D0B8309A1436 CRC64;
     MAESKEARDQ EMNLKEESKE EKRRNDWWKI DPQGPLESDQ WCRVLRQSLP EEKIPSQTCI
     ARRHLGPGPT QHTPSRRDRW IRGQILQAEV LQERLEWRIR GVQQAAKELG EVNRGIWREL
     YFREDQRGDF SAWGGYQRAQ ERLWGEQSSP RVLRPGDSKR RRKHL