ID   NEP_I67A0               Reviewed;         121 AA.
AC   Q6XTD9;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 66.
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/Tokyo/3/1967 H2N2).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC   Insthoviricetes; Articulavirales; Orthomyxoviridae; Alphainfluenzavirus.
OX   NCBI_TaxID=380960;
OH   NCBI_TaxID=8782; Aves.
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=15380362; DOI=10.1016/j.virol.2004.06.009;
RA   Lindstrom S.E., Cox N.J., Klimov A.;
RT   "Genetic analysis of human H2N2 and early H3N2 influenza viruses, 1957-
RT   1972: evidence for genetic divergence and multiple reassortment events.";
RL   Virology 328:101-119(2004).
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=Q6XTD9-1; Sequence=Displayed;
CC       Name=NS1;
CC         IsoId=Q6XTD8-1; Sequence=External;
CC   -!- SIMILARITY: Belongs to the influenza viruses NEP family.
CC       {ECO:0000255|HAMAP-Rule:MF_04067}.
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DR   EMBL; AY210183; AAO46632.1; -; Genomic_RNA.
DR   SMR; Q6XTD9; -.
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_0000324201"
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;  14409 MW;  66E423638CB0D92A CRC64;
     MDSNTVSSFQ DILLRMSKMR LGSSSEDLNG MITQFESLKL YRDSLGEAVM RMGDIHSLQN
     RNSKWREQLG QKFEEIRWLI EEVRHRLKIT ENSFEQITFM QALQLLFEVE QEIRTFSFQL
     I