AVM

Protein name	Nuclear Export Protein
Uniprot protein ID	C3W610
Protein length	121 amino acids
Protein description	NEP can be divided into a protease-sensitive N-terminal domain (amino acids 1-53) and a protease-resistant C-terminal domain (amino acids 54-121), the crystal structure of which has been solved. NEP mediates the nuclear export of encapsidated genomic RNAs (ribonucleoproteins, RNPs). Acts as an adapter between viral RNPs complexes and the nuclear export machinery of the cell. Possesses no intrinsic RNA-binding activity, but includes a C-terminal M1-binding domain. This domain is believed to allow recognition of RNPs to which the M1 protein is bound. Because the M1 protein is not available in large quantities until the later stages of infection, such an indirect recognition mechanism probably ensures that genomic RNPs are not exported from the nucleus before sufficient quantities of viral mRNA and progeny genomic RNA have been synthesized. Furthermore, the RNPs enters the cytoplasm only when they have associated with the M1 protein that is necessary to guide them to the plasma membrane. May down-regulate viral RNA synthesis when overproduced.

Pubmed ID	26992820
Clinical information	No
Disease	-
Published year	2016
Journal	Influenza Other Respir Viruses
Title	Rapid spread of influenza A(H1N1)pdm09 viruses with a new set of specific mutations in the internal genes in the beginning of 2015/2017 epidemic season in Moscow and Saint Petersburg (Russian Federation)
Author	Andrey Komissarov,Artem Fadeev,Maria Sergeeva,Sergey Petrov,Kseniya Sintsova
Evidence	Whole-genome analysis revealed a composition of specific mutations in the internal genes (D2E and M83I in NEP, E125D in NS1, M105T in NP, Q208K in M1, and N204S in PA-X) that probably emerged before the beginning of 2015/2017 epidemic season.