NEP_I33A0
ID NEP_I33A0 Reviewed; 121 AA.
AC Q89733;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 86.
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/Wilson-Smith/1933 H1N1) (Influenza A virus
OS (strain A/WS/1933 H1N1)).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Insthoviricetes; Articulavirales; Orthomyxoviridae; Alphainfluenzavirus.
OX NCBI_TaxID=381518;
OH NCBI_TaxID=8782; Aves.
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA Husak P.J.;
RL Thesis (1994), Robert Wood Johnson Medical School, United States.
RN [2]
RP INTERACTION WITH HUMAN XPO1.
RX PubMed=11118210; DOI=10.1093/emboj/19.24.6751;
RA Neumann G., Hughes M.T., Kawaoka Y.;
RT "Influenza A virus NS2 protein mediates vRNP nuclear export through NES-
RT independent interaction with hCRM1.";
RL EMBO J. 19:6751-6758(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=Q89733-1; Sequence=Displayed;
CC Name=NS1;
CC IsoId=Q82506-1; 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; U13682; AAA21581.1; -; mRNA.
DR EMBL; U13683; AAA21583.1; -; Genomic_RNA.
DR SMR; Q89733; -.
DR Proteomes; UP000000834; 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..121
FT /note="Nuclear export protein"
FT /id="PRO_0000079014"
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; 14327 MW; B15C14C594F55922 CRC64;
MDPNTVSSFQ DILMRMSKMQ LGSSSEDLNG IITQFESLKL YRDSLGEAVM RMGDLHSLQN
RNGKWREQLG QKFEEIRWLI EEVRHRLKIT ENSFEQITFM QALQLLLEVE QEIRTFSFQL
I