ID   H8XZV9_9INFA            Unreviewed;       230 AA.
AC   H8XZV9;
DT   16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT   16-MAY-2012, sequence version 1.
DT   09-DEC-2015, entry version 21.
DE   RecName: Full=Non-structural protein 1 {ECO:0000256|RuleBase:RU362113, ECO:0000256|SAAS:SAAS00412050};
DE            Short=NS1 {ECO:0000256|RuleBase:RU362113};
GN   Name=NS1 {ECO:0000313|EMBL:ADV39809.1};
GN   Synonyms=NS {ECO:0000256|RuleBase:RU362113};
OS   Influenza A virus (A/Kolkata/985/2007(H1N1)).
OC   Viruses; ssRNA viruses; ssRNA negative-strand viruses;
OC   Orthomyxoviridae; Influenzavirus A.
OX   NCBI_TaxID=701039 {ECO:0000313|EMBL:ADV39809.1};
RN   [1] {ECO:0000313|EMBL:ADV39809.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=A/KOL/985/2007 {ECO:0000313|EMBL:ADV39809.1};
RA   Sarkar-Dutta M., Chawla-Sarkar M.;
RL   Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADV39809.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=A/KOL/985/2007 {ECO:0000313|EMBL:ADV39809.1};
RX   PubMed=22217077;
RA   Sarkar M., Chanda S., Chakrabarti S., Mazumdar J., Ganguly A.,
RA   Chadha M.S., Mishra A.C., Chawla-Sarkar M.;
RT   "Surveillance in eastern India (2007-2009) revealed reassortment event
RT   involving ns and PB1-F2 gene segments among co-circulating influenza a
RT   subtypes.";
RL   Virol. J. 9:3-3(2012).
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. Viral protein synthesis
CC       is not affected by the inhibition of the cellular 3' end
CC       processing machinery because the poly(A) tails of viral mRNAs are
CC       produced by the viral polymerase through a stuttering mechanism
CC       (By similarity). {ECO:0000256|SAAS:SAAS00412348}.
CC   -!- FUNCTION: Prevents the establishment of the cellular antiviral
CC       state by inhibiting TRIM25-mediated DDX58 ubiquitination, which
CC       normally triggers the antiviral transduction signal that leads to
CC       the activation of type I IFN genes by transcription factors like
CC       IRF3 and IRF7. Prevents human EIF2AK2/PKR activation, either by
CC       binding double-strand RNA, or by interacting directly with
CC       EIF2AK2/PKR. This function may be important at the very beginning
CC       of the infection, when NS1 is mainly present in the cytoplasm.
CC       Also binds poly(A) and U6 snRNA. Suppresses the RNA silencing-
CC       based antiviral response in Drosophila cells (By similarity).
CC       {ECO:0000256|SAAS:SAAS00412141}.
CC   -!- SUBUNIT: Homodimer. Interacts with host TRIM25 (via coiled coil);
CC       this interaction specifically inhibits TRIM25 multimerization and
CC       TRIM25-mediated DDX58 CARD ubiquitination. Interacts with human
CC       EIF2AK2/PKR, CPSF4, IVNS1ABP and PABPN1 (By similarity).
CC       {ECO:0000256|SAAS:SAAS00412452}.
CC   -!- SUBCELLULAR LOCATION: Host nucleus
CC       {ECO:0000256|RuleBase:RU362113}. Host cytoplasm
CC       {ECO:0000256|RuleBase:RU362113}.
CC   -!- DOMAIN: The dsRNA-binding region is required for suppression of
CC       RNA 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; HQ853514; ADV39809.1; -; Viral_cRNA.
DR   ProteinModelPortal; H8XZV9; -.
DR   SMR; H8XZV9; 1-73, 79-205.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0042025; C:host cell nucleus; 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-KW.
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; 1.10.287.10; -; 1.
DR   InterPro; IPR000256; Flu_NS1.
DR   InterPro; IPR009068; S15_NS1_RNA-bd.
DR   Pfam; PF00600; Flu_NS1; 1.
DR   SUPFAM; SSF47060; SSF47060; 1.
PE   3: Inferred from homology;
KW   Eukaryotic host gene expression shutoff by virus
KW   {ECO:0000256|RuleBase:RU362113, ECO:0000256|SAAS:SAAS00141176};
KW   Host cytoplasm {ECO:0000256|RuleBase:RU362113,
KW   ECO:0000256|SAAS:SAAS00141091};
KW   Host gene expression shutoff by virus {ECO:0000256|RuleBase:RU362113,
KW   ECO:0000256|SAAS:SAAS00141187};
KW   Host mRNA suppression by virus {ECO:0000256|RuleBase:RU362113,
KW   ECO:0000256|SAAS:SAAS00141209};
KW   Host nucleus {ECO:0000256|RuleBase:RU362113,
KW   ECO:0000256|SAAS:SAAS00141173};
KW   Host-virus interaction {ECO:0000256|RuleBase:RU362113,
KW   ECO:0000256|SAAS:SAAS00141310};
KW   Inhibition of host innate immune response by virus
KW   {ECO:0000256|SAAS:SAAS00141196};
KW   Inhibition of host interferon signaling pathway by virus
KW   {ECO:0000256|SAAS:SAAS00141275};
KW   Inhibition of host PKR by virus {ECO:0000256|SAAS:SAAS00141437};
KW   Inhibition of host pre-mRNA processing by virus
KW   {ECO:0000256|RuleBase:RU362113, ECO:0000256|SAAS:SAAS00141362};
KW   Inhibition of host RIG-I by virus {ECO:0000256|SAAS:SAAS00141190};
KW   Inhibition of host RLR pathway by virus
KW   {ECO:0000256|SAAS:SAAS00141185};
KW   Interferon antiviral system evasion {ECO:0000256|RuleBase:RU362113,
KW   ECO:0000256|SAAS:SAAS00141166};
KW   RNA-binding {ECO:0000256|RuleBase:RU362113,
KW   ECO:0000256|SAAS:SAAS00141244};
KW   Viral immunoevasion {ECO:0000256|SAAS:SAAS00141437}.
SQ   SEQUENCE   230 AA;  25801 MW;  F99B53149B12F196 CRC64;
     MDSHTVSSFQ VDCFLWHVRK QVADQDLGDA PFLDRLRRDQ KSLKGRGSTL GLNIETATCV
     GKQIVERILK EESDEALKMT MASALASRYL TDMTVEEMSR DWFMLMPKQK VAGPLCVRMD
     QAIMDKNIIL KANFSVIFDR LENLTLLRAF TEEGAIVGEI SPLPSFPGHT NEDVKNAIGV
     LIGGLEWNDN TVRVSETLQR FAWRSSNETG GPPFTTTQKR KMAGTTRSEV
//