ID   H8XZV3_9INFA            Unreviewed;       230 AA.
AC   H8XZV3;
DT   16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT   16-MAY-2012, sequence version 1.
DT   05-JUN-2019, entry version 39.
DE   RecName: Full=Non-structural protein 1 {ECO:0000256|RuleBase:RU362113, ECO:0000256|SAAS:SAAS00965123};
DE            Short=NS1 {ECO:0000256|RuleBase:RU362113};
GN   Name=NS1 {ECO:0000313|EMBL:ADV39803.1};
GN   Synonyms=NS {ECO:0000256|RuleBase:RU362113};
OS   Influenza A virus (A/KOL/964/2007(H1N1)).
OC   Viruses; Riboviria; Negarnaviricota; Polyploviricotina;
OC   Insthoviricetes; Articulavirales; Orthomyxoviridae;
OC   Alphainfluenzavirus.
OX   NCBI_TaxID=943998 {ECO:0000313|EMBL:ADV39803.1};
RN   [1] {ECO:0000313|EMBL:ADV39803.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=A/KOL/964/2007 {ECO:0000313|EMBL:ADV39803.1};
RA   Sarkar-Dutta M., Chawla-Sarkar M.;
RL   Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADV39803.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=A/KOL/964/2007 {ECO:0000313|EMBL:ADV39803.1};
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 the
CC       poly(A)-binding protein 2/PABPN1. In turn, unprocessed 3' end pre-
CC       mRNAs accumulate in the host nucleus and are no longer exported to
CC       the cytoplasm. Cellular protein synthesis is thereby shut off very
CC       early after virus infection. Viral protein synthesis is not
CC       affected by the inhibition of the cellular 3' end processing
CC       machinery because the poly(A) tails of viral mRNAs are produced by
CC       the viral polymerase through a stuttering mechanism.
CC       {ECO:0000256|RuleBase:RU362113, ECO:0000256|SAAS:SAAS01036581}.
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 IRF3
CC       and IRF7. Prevents human EIF2AK2/PKR activation, either by binding
CC       double-strand RNA, or by interacting directly with EIF2AK2/PKR.
CC       This function may be important at the very beginning of the
CC       infection, when NS1 is mainly present in the cytoplasm. Also binds
CC       poly(A) and U6 snRNA. {ECO:0000256|RuleBase:RU362113,
CC       ECO:0000256|SAAS:SAAS01036591}.
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.
CC       {ECO:0000256|RuleBase:RU362113, ECO:0000256|SAAS:SAAS01036600}.
CC   -!- SUBCELLULAR LOCATION: Host cytoplasm
CC       {ECO:0000256|RuleBase:RU362113, ECO:0000256|SAAS:SAAS00965118}.
CC       Host nucleus {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, ECO:0000256|SAAS:SAAS01036574}.
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DR   EMBL; HQ853511; ADV39803.1; -; 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: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|RuleBase:RU362113, ECO:0000256|SAAS:SAAS01036575};
KW   Host cytoplasm {ECO:0000256|RuleBase:RU362113,
KW   ECO:0000256|SAAS:SAAS00965142};
KW   Host gene expression shutoff by virus {ECO:0000256|RuleBase:RU362113,
KW   ECO:0000256|SAAS:SAAS01036577};
KW   Host mRNA suppression by virus {ECO:0000256|RuleBase:RU362113,
KW   ECO:0000256|SAAS:SAAS01036583};
KW   Host nucleus {ECO:0000256|RuleBase:RU362113,
KW   ECO:0000256|SAAS:SAAS00965098};
KW   Host-virus interaction {ECO:0000256|RuleBase:RU362113,
KW   ECO:0000256|SAAS:SAAS00965144};
KW   Inhibition of host innate immune response by virus
KW   {ECO:0000256|SAAS:SAAS00965111};
KW   Inhibition of host interferon signaling pathway by virus
KW   {ECO:0000256|SAAS:SAAS00965146};
KW   Inhibition of host PKR by virus {ECO:0000256|SAAS:SAAS00965157};
KW   Inhibition of host pre-mRNA processing by virus
KW   {ECO:0000256|RuleBase:RU362113, ECO:0000256|SAAS:SAAS01036585};
KW   Inhibition of host RIG-I by virus {ECO:0000256|SAAS:SAAS01036586};
KW   Inhibition of host RLR pathway by virus
KW   {ECO:0000256|SAAS:SAAS01036584};
KW   Interferon antiviral system evasion {ECO:0000256|RuleBase:RU362113,
KW   ECO:0000256|SAAS:SAAS00965145};
KW   RNA-binding {ECO:0000256|RuleBase:RU362113,
KW   ECO:0000256|SAAS:SAAS00965112};
KW   Viral immunoevasion {ECO:0000256|SAAS:SAAS00965157}.
FT   REGION      205    230       Disordered. {ECO:0000256|MobiDB-lite:
FT                                H8XZV3}.
SQ   SEQUENCE   230 AA;  25786 MW;  F99B5310CA12F196 CRC64;
     MDSHTVSSFQ VDCFLWHVRK QVADQDLGDA PFLDRLRRDQ KSLKGRGSTL GLNIETATCV
     GKQIVERILK EESDEALKMT MASALASRYL TDMTVEEMSR DWFMLMPKQK VAGPLCVRMD
     QAIMDKNIIL KANFSVIFDR LENLTLLRAF TEEGAIVGEI SPLPSFPGHT NEDVKNAIGV
     LIGGLEWNDN TVRVSETLQR FAWRSSNETG GPPFTTTQNR KMAGTTRSEV
//