ID A0A0U2SS25_9INFA Unreviewed; 230 AA. AC A0A0U2SS25; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 02-JUN-2021, entry version 26. DE RecName: Full=Non-structural protein 1 {ECO:0000256|RuleBase:RU362113}; DE Short=NS1 {ECO:0000256|RuleBase:RU362113}; GN Name=NS1 {ECO:0000313|EMBL:ALR82593.1}; GN Synonyms=NS {ECO:0000256|RuleBase:RU362113}; OS Influenza A virus (A/wild bird/Wuhan/WHHN58/2014(H1N1)). OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina; OC Insthoviricetes; Articulavirales; Orthomyxoviridae; Alphainfluenzavirus. OX NCBI_TaxID=1756090 {ECO:0000313|EMBL:ALR82593.1, ECO:0000313|Proteomes:UP000119134}; RN [1] {ECO:0000313|EMBL:ALR82593.1, ECO:0000313|Proteomes:UP000119134} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=A/wild bird/Wuhan/WHHN58/2014 {ECO:0000313|EMBL:ALR82593.1}; RA Chen L.-J., Lin X.-D., Guo W.-P., Tian J.-H., Zhang Y.-Z.; RT "Diversity and evolution of avian influenza viruses in live poultry RT markets, free range poultry and wetland regions in China."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Inhibits post-transcriptional processing of cellular pre- CC mRNA, by binding and inhibiting two cellular proteins that are required CC for the 3'-end processing of cellular pre-mRNAs: the 30 kDa cleavage CC and polyadenylation specificity factor/CPSF4 and the poly(A)-binding CC protein 2/PABPN1. In turn, unprocessed 3' end pre-mRNAs accumulate in CC the host nucleus and are no longer exported to the cytoplasm. Cellular CC protein synthesis is thereby shut off very early after virus infection. CC Viral protein synthesis is not affected by the inhibition of the CC cellular 3' end processing machinery because the poly(A) tails of viral CC mRNAs are produced by the viral polymerase through a stuttering CC mechanism. {ECO:0000256|RuleBase:RU362113}. CC -!- FUNCTION: Prevents the establishment of the cellular antiviral state by CC inhibiting TRIM25-mediated DDX58 ubiquitination, which normally CC triggers the antiviral transduction signal that leads to the activation CC of type I IFN genes by transcription factors IRF3 and IRF7. Prevents CC human EIF2AK2/PKR activation, either by binding double-strand RNA, or CC by interacting directly with EIF2AK2/PKR. This function may be CC important at the very beginning of the infection, when NS1 is mainly CC present in the cytoplasm. Also binds poly(A) and U6 snRNA. CC {ECO:0000256|RuleBase:RU362113}. CC -!- SUBUNIT: Homodimer. Interacts with host TRIM25 (via coiled coil); this CC interaction specifically inhibits TRIM25 multimerization and TRIM25- CC mediated DDX58 CARD ubiquitination. Interacts with human EIF2AK2/PKR, CC CPSF4, IVNS1ABP and PABPN1. {ECO:0000256|RuleBase:RU362113}. CC -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000256|RuleBase:RU362113}. CC Host cytoplasm {ECO:0000256|RuleBase:RU362113}. CC -!- DOMAIN: The dsRNA-binding region is required for suppression of RNA CC silencing. {ECO:0000256|RuleBase:RU362113}. CC -!- SIMILARITY: Belongs to the influenza A viruses NS1 family. CC {ECO:0000256|RuleBase:RU362113}. 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; KU143424; ALR82593.1; -; Viral_cRNA. DR Proteomes; UP000119134; Genome. DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW. DR GO; GO:0039524; P:suppression by virus of host mRNA processing; IEA:UniProtKB-UniRule. DR GO; GO:0039580; P:suppression by virus of host PKR activity; IEA:UniProtKB-KW. DR GO; GO:0039540; P:suppression by virus of host RIG-I activity; IEA:UniProtKB-KW. DR GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; IEA:UniProtKB-KW. DR Gene3D; 3.30.420.330; -; 1. DR HAMAP; MF_04066; INFV_NS1; 1. DR InterPro; IPR004208; NS1. DR InterPro; IPR000256; NS1A. DR InterPro; IPR038064; NS1A_effect_dom-like_sf. DR InterPro; IPR009068; S15_NS1_RNA-bd. DR Pfam; PF00600; Flu_NS1; 1. DR SUPFAM; SSF143021; SSF143021; 1. DR SUPFAM; SSF47060; SSF47060; 1. PE 3: Inferred from homology; KW Eukaryotic host gene expression shutoff by virus KW {ECO:0000256|ARBA:ARBA00023247, ECO:0000256|RuleBase:RU362113}; KW Host cytoplasm {ECO:0000256|ARBA:ARBA00023200, KW ECO:0000256|RuleBase:RU362113}; KW Host gene expression shutoff by virus {ECO:0000256|ARBA:ARBA00022995, KW ECO:0000256|RuleBase:RU362113}; KW Host mRNA suppression by virus {ECO:0000256|ARBA:ARBA00022557, KW ECO:0000256|RuleBase:RU362113}; KW Host nucleus {ECO:0000256|ARBA:ARBA00022562, KW ECO:0000256|RuleBase:RU362113}; KW Host-virus interaction {ECO:0000256|ARBA:ARBA00022581, KW ECO:0000256|RuleBase:RU362113}; KW Inhibition of host innate immune response by virus KW {ECO:0000256|ARBA:ARBA00022632}; KW Inhibition of host interferon signaling pathway by virus KW {ECO:0000256|ARBA:ARBA00022830}; KW Inhibition of host PKR by virus {ECO:0000256|ARBA:ARBA00023041}; KW Inhibition of host pre-mRNA processing by virus KW {ECO:0000256|ARBA:ARBA00022834, ECO:0000256|RuleBase:RU362113}; KW Inhibition of host RIG-I by virus {ECO:0000256|ARBA:ARBA00023090}; KW Inhibition of host RLR pathway by virus {ECO:0000256|ARBA:ARBA00022482}; KW Interferon antiviral system evasion {ECO:0000256|ARBA:ARBA00023258, KW ECO:0000256|RuleBase:RU362113}; KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|RuleBase:RU362113}; KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}; KW Viral immunoevasion {ECO:0000256|ARBA:ARBA00023280}. FT REGION 205..230 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 213..230 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 230 AA; 26071 MW; 4514E86F929B5EC3 CRC64; MDSNTVSSFQ VDCFLWHVRK RFADQELGDA PFLDRLRRDQ KSLRGRGSTL GLDIETATRA GKQIVERILE EESDEALKMT IASVPASRYL TDMTLEEMSR DWFMLMPKQK VAGSLCIRMD QAIMDKNITL KANFSVIFDR LETLILLRAF TEEGAIVGEI SPLPSLPGHT DEDVKNAIGV LIGGLEWNDN TVRVSETLQR FAWRSSNEDG RPPLPPKQKR KMARTIESEV //