ID   A0A2Z5WNY7_9INFA        Unreviewed;       237 AA.
AC   A0A2Z5WNY7;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   22-FEB-2023, entry version 14.
DE   RecName: Full=Non-structural protein 1 {ECO:0000256|RuleBase:RU362113};
DE            Short=NS1 {ECO:0000256|RuleBase:RU362113};
GN   Name=NS1 {ECO:0000313|EMBL:BBC20469.1};
GN   Synonyms=NS {ECO:0000256|RuleBase:RU362113};
OS   Influenza A virus (A/duck/Mongolia/340/2011(H4N8)).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC   Insthoviricetes; Articulavirales; Orthomyxoviridae; Alphainfluenzavirus.
OX   NCBI_TaxID=1971561 {ECO:0000313|EMBL:BBC20469.1};
RN   [1] {ECO:0000313|EMBL:BBC20469.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=A/duck/Mongolia/340/2011 {ECO:0000313|EMBL:BBC20469.1};
RA   Suzuki M., Sakoda Y., Okamatsu M., Matsuno K.;
RT   "Characterization of avian influenza viruses isolated from ducks in Asia.";
RL   Submitted (DEC-2017) 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 RIGI ubiquitination, which normally triggers
CC       the antiviral transduction signal that leads to the activation of type
CC       I IFN genes by transcription factors IRF3 and IRF7. Prevents human
CC       EIF2AK2/PKR activation, either by binding double-strand RNA, or by
CC       interacting directly with EIF2AK2/PKR. This function may be important
CC       at the very beginning of the infection, when NS1 is mainly present in
CC       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 RIGI 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}.
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DR   EMBL; LC349395; BBC20469.1; -; Viral_cRNA.
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:0030291; F:protein serine/threonine kinase inhibitor activity; IEA:UniProtKB-KW.
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 signaling; IEA:UniProtKB-KW.
DR   GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; IEA:UniProtKB-KW.
DR   GO; GO:0039540; P:suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of host RIG-I activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.420.330; Influenza virus non-structural protein, effector domain; 1.
DR   Gene3D; 1.10.287.10; S15/NS1, RNA-binding; 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; Ns1 effector domain-like; 1.
DR   SUPFAM; SSF47060; S15/NS1 RNA-binding domain; 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..237
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        213..237
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   237 AA;  26955 MW;  4C8FA78AB3EA207F CRC64;
     MDSNTVSSFQ VDCFLWHVRK RFADQELGDA PFLDRLRRDQ KSLRGRGSTL GLDIETATRA
     GKQIVERILE EESDEALKMT IASVPASRYL TDMTLEEMSR DWFMLMPKQK VAGSLCIRMD
     QAIMDKNIIL KANFSVIFDR LETLILLRAF TEEGAIVGEI SPLPSLPGHT DEDVKNAIGV
     LIGGLEWNDN TVRVSETLQR FAWRSSNEDG RPPLPPKQKR KMARTIESEV RRNKMAD
//