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NEP_I79A1
ID   NEP_I79A1               Reviewed;         121 AA.
AC   P13148;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1991, sequence version 2.
DT   03-AUG-2022, entry version 96.
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/Pintail/Alberta/119/1979 H4N6).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC   Insthoviricetes; Articulavirales; Orthomyxoviridae; Alphainfluenzavirus.
OX   NCBI_TaxID=384504;
OH   NCBI_TaxID=8782; Aves.
OH   NCBI_TaxID=9823; Sus scrofa (Pig).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=2525836; DOI=10.1016/0042-6822(89)90504-7;
RA   Treanor J.J., Snyder M.H., London W.T., Murphy B.R.;
RT   "The B allele of the NS gene of avian influenza viruses, but not the A
RT   allele, attenuates a human influenza A virus for squirrel monkeys.";
RL   Virology 171:1-9(1989).
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=P13148-1; Sequence=Displayed;
CC       Name=NS1;
CC         IsoId=P13140-1; 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.
CC       {ECO:0000255|HAMAP-Rule:MF_04067}.
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DR   EMBL; M25374; AAA43556.1; -; Genomic_RNA.
DR   PIR; H32662; MNIVB4.
DR   SMR; P13148; -.
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_0000079001"
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;  14347 MW;  ED8D049AE568AC6F CRC64;
     MDSNTVSSFQ DILMRMSKMQ LGSSSEDLNG MITQFESLKL YRDSLGEAVM RIGDLHSLQN
     RNGKWREQLS QKFEEIRWLI EEVRHRLKIT ENSFEQITFM QALQLLLEVE QEIRTFSFQL
     I
 
 
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