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REV_EIAVC
ID   REV_EIAVC               Reviewed;         165 AA.
AC   P32543;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 2.
DT   02-JUN-2021, entry version 63.
DE   RecName: Full=Protein Rev;
DE   AltName: Full=3'-ORF protein;
GN   Name=rev;
OS   Equine infectious anemia virus (isolate CL22) (EIAV).
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX   NCBI_TaxID=31675;
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=1318398; DOI=10.1128/jvi.66.7.4085-4097.1992;
RA   Perry S.T., Flaherty M.T., Kelley M.J., Clabough D.L., Tronick S.R.,
RA   Coggins L., Whetter L., Lengel C.R., Fuller F.;
RT   "The surface envelope protein gene region of equine infectious anemia virus
RT   is not an important determinant of tropism in vitro.";
RL   J. Virol. 66:4085-4097(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=8394464; DOI=10.1128/jvi.67.9.5640-5646.1993;
RA   Rosin-Arbesfeld R., Rivlin M., Noiman S., Mashiah P., Yaniv A., Miki T.,
RA   Tronick S.R., Gazit A.;
RT   "Structural and functional characterization of rev-like transcripts of
RT   equine infectious anemia virus.";
RL   J. Virol. 67:5640-5646(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 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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA44782.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; M87581; AAA43006.1; ALT_SEQ; Genomic_RNA.
DR   EMBL; X63058; CAA44782.1; ALT_INIT; Genomic_RNA.
DR   SMR; P32543; -.
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   3: Inferred from homology;
KW   Coiled coil; Host cytoplasm; Host nucleus; mRNA transport; RNA-binding;
KW   Transport.
FT   CHAIN           1..165
FT                   /note="Protein Rev"
FT                   /id="PRO_0000085477"
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                   /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..33
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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
 
 
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