位置:首页 > 蛋白库 > NEP_I24A0
NEP_I24A0
ID   NEP_I24A0               Reviewed;         118 AA.
AC   P08275;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1988, sequence version 1.
DT   29-SEP-2021, entry version 89.
DE   RecName: Full=Nuclear export protein;
DE            Short=NEP;
DE   AltName: Full=Non-structural protein 2;
DE            Short=NS2;
DE   Flags: Fragment;
GN   Name=NS;
OS   Influenza A virus (strain A/Chicken/Japan/1924 H7N7).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC   Insthoviricetes; Articulavirales; Orthomyxoviridae; Alphainfluenzavirus.
OX   NCBI_TaxID=11340;
OH   NCBI_TaxID=8782; Aves.
OH   NCBI_TaxID=9796; Equus caballus (Horse).
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=9709; Phocidae (true seals).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=2954302; DOI=10.1016/0042-6822(87)90223-6;
RA   Nakajima K., Nobusawa E., Ogawa T., Nakajima S.;
RT   "Genetic divergence of the NS genes of avian influenza viruses.";
RL   Virology 158:465-468(1987).
CC   -!- FUNCTION: Mediates the nuclear export of encapsidated genomic RNAs
CC       (ribonucleoproteins, RNPs). Acts as an adapter between viral RNPs
CC       complexes and the nuclear export machinery of the cell. Possesses no
CC       intrinsic RNA-binding activity, but includes a C-terminal M1-binding
CC       domain. This domain is believed to allow recognition of RNPs to which
CC       the M1 protein is bound. Because the M1 protein is not available in
CC       large quantities until the later stages of infection, such an indirect
CC       recognition mechanism probably ensures that genomic RNPs are not
CC       exported from the nucleus before sufficient quantities of viral mRNA
CC       and progeny genomic RNA have been synthesized. Furthermore, the RNPs
CC       enters the cytoplasm only when they have associated with the M1 protein
CC       that is necessary to guide them to the plasma membrane. May down-
CC       regulate viral RNA synthesis when overproduced (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Binds M1 protein. May interact with human nucleoporin RAB/HRB
CC       and exportin XPO1/CRM1 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000305}. Host nucleus {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=NEP; Synonyms=NS2;
CC         IsoId=P08275-1; Sequence=Displayed;
CC       Name=NS1;
CC         IsoId=P08274-1; Sequence=External;
CC   -!- MISCELLANEOUS: Average number present in a viral particle is estimated
CC       to be 130-200 molecules.
CC   -!- SIMILARITY: Belongs to the influenza viruses NEP family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M16561; AAA43505.1; -; Genomic_RNA.
DR   SMR; P08275; -.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0039675; P:exit of virus from host cell nucleus through nuclear pore; IEA:InterPro.
DR   InterPro; IPR000968; Flu_NS2.
DR   Pfam; PF00601; Flu_NS2; 1.
PE   3: Inferred from homology;
KW   Alternative splicing; Host nucleus; Host-virus interaction; Transport;
KW   Virion.
FT   CHAIN           <1..118
FT                   /note="Nuclear export protein"
FT                   /id="PRO_0000078980"
FT   MOTIF           9..18
FT                   /note="Nuclear export signal"
FT                   /evidence="ECO:0000250"
FT   MOTIF           82..91
FT                   /note="Nuclear export signal"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
SQ   SEQUENCE   118 AA;  13925 MW;  D6A8B4D34A163A46 CRC64;
     NTVSSFQDIL MRMSKMQLGT SSEDLNGMIT QLESLKLYRD SLGEAVMRVG DLHSLQSRNG
     KWREQLSQKF EEIRWLIEEV RHKLKITENS FEQITFMQAL QLLLEVEQEI RTFSFQLI
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024