ID Q6E3U7_9INFA Unreviewed; 228 AA. AC Q6E3U7; DT 16-AUG-2004, integrated into UniProtKB/TrEMBL. DT 16-AUG-2004, sequence version 1. DT 05-FEB-2008, entry version 18. DE Nonstructural protein 1 (Fragment). GN Name=NS1; OS Influenza A virus (A/duck/Fujian/01/2002(H5N1)). OC Viruses; ssRNA negative-strand viruses; Orthomyxoviridae; OC Influenzavirus A. OX NCBI_TaxID=274827; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=A/Duck/Fujian/01/2002; RX PubMed=15235128; DOI=10.1073/pnas.0403212101; RA Chen H., Deng G., Li Z., Tian G., Li Y., Jiao P., Zhang L., Liu Z., RA Webster R.G., Yu K.; RT "The evolution of H5N1 influenza viruses in ducks in southern China."; RL Proc. Natl. Acad. Sci. U.S.A. 101:10452-10457(2004). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=A/Duck/Fujian/01/2002; RA Chen H.L., Deng G.H., Li Z.J., Tian G.B., Li Y.B., Jiao P., Zhang L., RA Webster R.G., Yu K.; RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Inhibits post-transcriptional processing of cellular CC pre-mRNA, by binding and inhibiting two cellular proteins that are CC required for the 3'-end processing of cellular pre-mRNAs: the 30 CC kDa cleavage and polyadenylation specificity factor (CPSF4) and CC the poly(A)-binding protein 2 (PABPN1). This results in the CC accumulation of unprocessed 3' end pre-mRNAs which can't be CC exported from the nucleus. Cellular protein synthesis is thereby CC shut off very early after virus infection. This protein synthesis CC shut off is presumably necessary for the virus to escape CC interferon synthesis after activation of the IRF3 pathway, and CC therefore prevents establishment of cellular antiviral state. CC Viral protein synthesis is not affected by the inhibition of the CC cellular 3' end processing machinery because the poly(A) tails of CC viral mRNAs are produced by the viral polymerase, through a CC stuttering mechanism (By similarity). CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=In uninfected, CC transfected cells, NS1 is localized in the nucleus. Only in virus CC infected cells, the nuclear export signal is unveiled, presumably CC by a viral protein, and a fraction of NS1 is exported in the CC cytoplasm (By similarity). 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; AY585441; AAT12106.1; -; mRNA. DR SMR; Q6E3U7; 1-70. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR InterPro; IPR000256; Flu_NS1. DR InterPro; IPR009068; S15_NS1_RNA_bd. DR Gene3D; G3DSA:1.10.287.10; S15_NS1_RNA_bd; 1. DR Pfam; PF00600; Flu_NS1; 1. DR ProDom; PD000613; Flu_NS1; 1. PE 2: Evidence at transcript level; KW Host-virus interaction; Interferon antiviral system evasion; Nucleus; KW Suppressor of RNA silencing. FT NON_TER 228 228 SQ SEQUENCE 228 AA; 25969 MW; 073C0B09E174938A CRC64; MDSNTVSSFQ VDCFLWHVRK RFADQELGDA PFLDRLRRDQ KSLRGRGSTL GLDIETATRA GKQIVERILE EESDEALKMT IASLPAPRYL TEMTIEEMTR DWYMLMPRQK VTGSLWVRMD QAIMDKTIIF KANFSVIFDR LETLIPLRAF TEGGAIVGEI SPLPSVPGHT NEDVKNAIGV LIGGLEWNDN TVRVSETLQR FAWRSSDEDG RPPLPPKQKR KMARTIES //