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NEP_I91A0
ID   NEP_I91A0               Reviewed;         121 AA.
AC   Q77ZM4;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=Nuclear export protein {ECO:0000255|HAMAP-Rule:MF_04067};
DE            Short=NEP {ECO:0000255|HAMAP-Rule:MF_04067};
DE   AltName: Full=Non-structural protein 2 {ECO:0000255|HAMAP-Rule:MF_04067};
DE            Short=NS2 {ECO:0000255|HAMAP-Rule:MF_04067};
GN   Name=NS {ECO:0000255|HAMAP-Rule:MF_04067};
OS   Influenza A virus (strain A/Equine/Alaska/1/1991 H3N8).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC   Insthoviricetes; Articulavirales; Orthomyxoviridae; Alphainfluenzavirus.
OX   NCBI_TaxID=387213;
OH   NCBI_TaxID=8782; Aves.
OH   NCBI_TaxID=9796; Equus caballus (Horse).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=9739336; DOI=10.1007/s007050050400;
RA   Lindstrom S., Endo A., Sugita S., Pecoraro M., Hiromoto Y., Kamada M.,
RA   Takahashi T., Nerome K.;
RT   "Phylogenetic analyses of the matrix and non-structural genes of equine
RT   influenza viruses.";
RL   Arch. Virol. 143:1585-1598(1998).
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 bound to
CC       the protein M1. Since protein M1 is not available in large quantities
CC       before late stages of infection, such an indirect recognition mechanism
CC       probably ensures that genomic RNPs are not exported from the host
CC       nucleus until sufficient quantities of viral mRNA and progeny genomic
CC       RNA have been synthesized. Furthermore, the RNPs enter the host
CC       cytoplasm only when associated with the M1 protein that is necessary to
CC       guide them to the plasma membrane. May down-regulate viral RNA
CC       synthesis when overproduced. {ECO:0000255|HAMAP-Rule:MF_04067}.
CC   -!- SUBUNIT: Interacts with protein M1. May interact with host nucleoporin
CC       RAB/HRB and exportin XPO1/CRM1. {ECO:0000255|HAMAP-Rule:MF_04067}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04067}. Host
CC       nucleus {ECO:0000255|HAMAP-Rule:MF_04067}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=NEP; Synonyms=NS2;
CC         IsoId=Q77ZM4-1; Sequence=Displayed;
CC       Name=NS1;
CC         IsoId=Q77ZM3-1; Sequence=External;
CC   -!- SIMILARITY: Belongs to the influenza viruses NEP family.
CC       {ECO:0000255|HAMAP-Rule:MF_04067}.
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DR   EMBL; AF001667; AAC31259.1; -; Genomic_RNA.
DR   SMR; Q77ZM4; -.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0044423; C:virion component; IEA:UniProtKB-UniRule.
DR   GO; GO:0039675; P:exit of virus from host cell nucleus through nuclear pore; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_04067; INFV_NEP; 1.
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..121
FT                   /note="Nuclear export protein"
FT                   /id="PRO_0000324233"
FT   MOTIF           12..21
FT                   /note="Nuclear export signal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04067"
FT   MOTIF           85..94
FT                   /note="Nuclear export signal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04067"
SQ   SEQUENCE   121 AA;  14418 MW;  B8422160815EB5CD CRC64;
     MDSNTVSSFQ DILMRMSKMQ LGSSSEDLNG MIIRLESLKL YRDSLGEAVM RMGDLHSLQS
     RNEKWREQLS QKFEEIRWLI EEVRHRLKNT ENSFEQITFM QALQLLLEVE QEIRTFSFQL
     I
 
 
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