ID   NEP_INBLE               Reviewed;         122 AA.
AC   P03511;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   03-AUG-2022, entry version 94.
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 B virus (strain B/Lee/1940).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC   Insthoviricetes; Articulavirales; Orthomyxoviridae; Betainfluenzavirus.
OX   NCBI_TaxID=518987;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=6283137; DOI=10.1128/jvi.42.1.186-193.1982;
RA   Briedis D.J., Lamb R.A.;
RT   "Influenza B virus genome: sequences and structural organization of RNA
RT   segment 8 and the mRNAs coding for the NS1 and NS2 proteins.";
RL   J. Virol. 42:186-193(1982).
RN   [2]
RP   INTERACTION WITH HUMAN XPO1.
RX   PubMed=11462009; DOI=10.1128/jvi.75.16.7375-7383.2001;
RA   Paragas J., Talon J., O'Neill R.E., Anderson D.K., Garcia-Sastre A.,
RA   Palese P.;
RT   "Influenza B and C virus NEP (NS2) proteins possess nuclear export
RT   activities.";
RL   J. Virol. 75:7375-7383(2001).
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=P03511-1; Sequence=Displayed;
CC       Name=NS1;
CC         IsoId=P03502-1; Sequence=External;
CC   -!- SIMILARITY: Belongs to the influenza viruses NEP family.
CC       {ECO:0000255|HAMAP-Rule:MF_04067}.
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; J02096; AAA43755.1; -; Genomic_RNA.
DR   PIR; A04099; MNIVB.
DR   RefSeq; NP_056665.1; NC_002211.1. [P03511-1]
DR   PRIDE; P03511; -.
DR   GeneID; 26824007; -.
DR   KEGG; vg:26824007; -.
DR   Proteomes; UP000008158; Genome.
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   1: Evidence at protein level;
KW   Alternative splicing; Host nucleus; Host-virus interaction;
KW   Reference proteome; Transport; Virion.
FT   CHAIN           1..122
FT                   /note="Nuclear export protein"
FT                   /id="PRO_0000079015"
FT   MOTIF           10..19
FT                   /note="Nuclear export signal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04067"
FT   MOTIF           86..95
FT                   /note="Nuclear export signal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04067"
SQ   SEQUENCE   122 AA;  14238 MW;  8DFBB44B4B210E23 CRC64;
     MADNMTTTQI EWRMKKMAIG SSTHSSSVLM KDIQSQFEQL KLRWESYPNL VKSTDYHQKR
     ETIRLATEEL YLLSKRIDDS ILFHKTVIAN SSIIADMIVS LSLLETLYEM KDVVEVYSRQ
     CL