ID   NEP_INCHY               Reviewed;         182 AA.
AC   Q9ENX7;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 46.
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 C virus (strain C/Hyogo/1/1983).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC   Insthoviricetes; Articulavirales; Orthomyxoviridae; Gammainfluenzavirus.
OX   NCBI_TaxID=203225;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=9823; Sus scrofa (Pig).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=10900030; DOI=10.1099/0022-1317-81-8-1933;
RA   Alamgir A.S.M., Matsuzaki Y., Hongo S., Tsuchiya E., Sugawara K.,
RA   Muraki Y., Nakamura K.;
RT   "Phylogenetic analysis of influenza C virus nonstructural (NS) protein
RT   genes and identification of the NS2 protein.";
RL   J. Gen. Virol. 81:1933-1940(2000).
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=Q9ENX7-1; Sequence=Displayed;
CC       Name=NS1;
CC         IsoId=Q9ENX6-1; Sequence=External;
CC   -!- SIMILARITY: Belongs to the influenza viruses NEP family.
CC       {ECO:0000255|HAMAP-Rule:MF_04067}.
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DR   EMBL; AB034167; BAB12072.1; -; Genomic_RNA.
DR   SMR; Q9ENX7; -.
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; IPR005188; Flu_C_NS2.
DR   InterPro; IPR000968; Flu_NS2.
DR   Pfam; PF03555; Flu_C_NS2; 1.
PE   3: Inferred from homology;
KW   Alternative splicing; Host nucleus; Host-virus interaction; Transport;
KW   Virion.
FT   CHAIN           1..182
FT                   /note="Nuclear export protein"
FT                   /id="PRO_0000269460"
FT   MOTIF           96..105
FT                   /note="Nuclear export signal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04067"
FT   MOTIF           122..132
FT                   /note="Nuclear export signal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04067"
SQ   SEQUENCE   182 AA;  20838 MW;  ADA4E962A30E8094 CRC64;
     MSDKTVKSTN LMAFIATKML ERQEDLDTCT EMQVEKMKTS TKARLRTESS FAPRTWEDAI
     KDEILRRSVD TSSLDKWPEL KQELENVSDA LKADSLWLPM KSLSLYSKVS NQEPNSIPIG
     EMKHQILTRL KLICSRLEKL DLNLSKAVLG IQNSEDLILI IYNRDICKTT ILMIKSLCNS
     LI