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Non-structural protein 1 (NS1) (NS1A)

 NS1_I34A1               Reviewed;         230 AA.
P03496; Q20N32; Q67267; Q71QT3;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
25-OCT-2017, entry version 122.
RecName: Full=Non-structural protein 1 {ECO:0000255|HAMAP-Rule:MF_04066};
Short=NS1 {ECO:0000255|HAMAP-Rule:MF_04066};
AltName: Full=NS1A {ECO:0000255|HAMAP-Rule:MF_04066};
Name=NS {ECO:0000255|HAMAP-Rule:MF_04066};
Influenza A virus (strain A/Puerto Rico/8/1934 H1N1).
Viruses; ssRNA viruses; ssRNA negative-strand viruses;
Orthomyxoviridae; Influenzavirus A.
NCBI_TaxID=211044;
NCBI_TaxID=8782; Aves.
NCBI_TaxID=9606; Homo sapiens (Human).
NCBI_TaxID=9823; Sus scrofa (Pig).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=7465426; DOI=10.1093/nar/8.23.5845;
Baez M., Taussig R., Zazra J.J., Young J.F., Palese P., Reisfeld A.,
Skalka A.M.;
"Complete nucleotide sequence of the influenza A/PR/8/34 virus NS gene
and comparison with the NS genes of the A/Udorn/72 and
A/FPV/Rostock/34 strains.";
Nucleic Acids Res. 8:5845-5858(1980).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=11779399; DOI=10.1098/rstb.2001.0979;
Schickli J.H., Flandorfer A., Nakaya T., Martinez-Sobrido L.,
Garcia-Sastre A., Palese P.;
"Plasmid-only rescue of influenza A virus vaccine candidates.";
Philos. Trans. R. Soc. Lond., B, Biol. Sci. 356:1965-1973(2001).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC RNA], AND REVERSE GENETICS.
PubMed=15163504; DOI=10.1016/j.virusres.2004.02.028;
de Wit E., Spronken M.I.J., Bestebroer T.M., Rimmelzwaan G.F.,
Osterhaus A.D.M.E., Fouchier R.A.M.;
"Efficient generation and growth of influenza virus A/PR/8/34 from
eight cDNA fragments.";
Virus Res. 103:155-161(2004).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
Ghedin E., Spiro D., Miller N., Zaborsky J., Feldblyum T., Subbu V.,
Shumway M., Sparenborg J., Groveman L., Halpin R., Sitz J., Koo H.,
Salzberg S.L., Webster R.G., Hoffmann E., Krauss S., Naeve C., Bao Y.,
Bolotov P., Dernovoy D., Kiryutin B., Lipman D.J., Tatusova T.;
"The NIAID influenza genome sequencing project.";
Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
[5]
REVIEW.
PubMed=12758165; DOI=10.1016/S0042-6822(03)00119-3;
Krug R.M., Yuan W., Noah D.L., Latham A.G.;
"Intracellular warfare between human influenza viruses and human
cells: the roles of the viral NS1 protein.";
Virology 309:181-189(2003).
[6]
INTERACTION WITH HUMAN TRIM25, AND MUTAGENESIS OF ARG-38; LYS-41;
GLU-96 AND GLU-97.
PubMed=19454348; DOI=10.1016/j.chom.2009.04.006;
Gack M.U., Albrecht R.A., Urano T., Inn K.-S., Huang I.-C.,
Carnero E., Farzan M., Inoue S., Jung J.U., Garcia-Sastre A.;
"Influenza A virus NS1 targets the ubiquitin ligase TRIM25 to evade
recognition by the host viral RNA sensor RIG-I.";
Cell Host Microbe 5:439-449(2009).
[7]
ISGYLATION AT LYS-20; LYS-41; LYS-108; LYS-110; LYS-126; LYS-217 AND
LYS-219, AND MUTAGENESIS OF LYS-20; LYS-41; LYS-108; LYS-110; LYS-126;
LYS-217 AND LYS-219.
PubMed=20385878; DOI=10.4049/jimmunol.0903588;
Tang Y., Zhong G., Zhu L., Liu X., Shan Y., Feng H., Bu Z., Chen H.,
Wang C.;
"Herc5 attenuates influenza A virus by catalyzing ISGylation of viral
NS1 protein.";
J. Immunol. 184:5777-5790(2010).
-!- FUNCTION: Prevents the establishment of the cellular antiviral
state by inhibiting TRIM25-mediated DDX58 ubiquitination, which
normally triggers the antiviral transduction signal that leads to
the activation of type I IFN genes by transcription factors IRF3
and IRF7. Prevents human EIF2AK2/PKR activation, either by binding
double-strand RNA, or by interacting directly with EIF2AK2/PKR.
This function may be important at the very beginning of the
infection, when NS1 is mainly present in the cytoplasm. Also binds
poly(A) and U6 snRNA. {ECO:0000255|HAMAP-Rule:MF_04066}.
-!- FUNCTION: Inhibits post-transcriptional processing of cellular
pre-mRNA, by binding and inhibiting two cellular proteins that are
required for the 3'-end processing of cellular pre-mRNAs: the 30
kDa cleavage and polyadenylation specificity factor/CPSF4 and the
poly(A)-binding protein 2/PABPN1. In turn, unprocessed 3' end pre-
mRNAs accumulate in the host nucleus and are no longer exported to
the cytoplasm. Cellular protein synthesis is thereby shut off very
early after virus infection. Viral protein synthesis is not
affected by the inhibition of the cellular 3' end processing
machinery because the poly(A) tails of viral mRNAs are produced by
the viral polymerase through a stuttering mechanism.
{ECO:0000255|HAMAP-Rule:MF_04066}.
-!- SUBUNIT: Homodimer. Interacts with host TRIM25 (via coiled coil);
this interaction specifically inhibits TRIM25 multimerization and
TRIM25-mediated DDX58 CARD ubiquitination. Interacts with human
EIF2AK2/PKR, CPSF4, IVNS1ABP and PABPN1. {ECO:0000255|HAMAP-
Rule:MF_04066}.
-!- INTERACTION:
Self; NbExp=4; IntAct=EBI-2547442, EBI-2547442;
P55265:ADAR (xeno); NbExp=8; IntAct=EBI-2547442, EBI-2462104;
Q12906:ILF3 (xeno); NbExp=3; IntAct=EBI-2547442, EBI-78756;
P27986:PIK3R1 (xeno); NbExp=6; IntAct=EBI-2547442, EBI-79464;
O00459:PIK3R2 (xeno); NbExp=13; IntAct=EBI-2547442, EBI-346930;
O75569:PRKRA (xeno); NbExp=3; IntAct=EBI-2547442, EBI-713955;
O95793:STAU1 (xeno); NbExp=6; IntAct=EBI-2547442, EBI-358174;
Q14258:TRIM25 (xeno); NbExp=3; IntAct=EBI-2547442, EBI-2341129;
-!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000255|HAMAP-
Rule:MF_04066}. Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04066}.
Note=In uninfected, transfected cells, NS1 is localized in the
nucleus. Only in virus infected cells, the nuclear export signal
is unveiled, presumably by a viral protein, and a fraction of NS1
is exported in the cytoplasm. {ECO:0000255|HAMAP-Rule:MF_04066}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=NS1;
IsoId=P03496-1; Sequence=Displayed;
Name=NEP; Synonyms=NS2;
IsoId=P03508-1; Sequence=External;
-!- DOMAIN: The dsRNA-binding region is required for suppression of
RNA silencing. {ECO:0000255|HAMAP-Rule:MF_04066}.
-!- PTM: Upon interferon induction, ISGylated via host HERC5; this
results in the impairment of NS1 interaction with RNA targets due
to its inability to form homodimers and to interact with host
EIF2AK2/PKR. There are two ISGylated forms: one form is ISGylated
at Lys-20, Lys-41, Lys-217, and Lys-219, and another one at Lys-
108, Lys-110, and Lys-126, they represent band I and II
respectively. Lys-126 and Lys-217 are critical for host antiviral
response in vivo. {ECO:0000255|HAMAP-Rule:MF_04066,
ECO:0000269|PubMed:20385878}.
-!- SIMILARITY: Belongs to the influenza A viruses NS1 family.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; V01104; CAA24292.1; ALT_SEQ; Genomic_RNA.
EMBL; J02150; AAA43536.1; -; Genomic_RNA.
EMBL; AF389122; AAM75163.1; -; Genomic_RNA.
EMBL; EF467817; ABO21703.1; -; Genomic_RNA.
EMBL; CY009448; ABD77680.1; -; Genomic_RNA.
RefSeq; NP_040984.1; NC_002020.1.
PDB; 2GX9; X-ray; 2.10 A; A/B=79-207.
PDB; 2ZKO; X-ray; 1.70 A; A/B=1-70.
PDB; 3L4Q; X-ray; 2.30 A; A/B=73-230.
PDB; 3O9Q; X-ray; 2.50 A; A/B=79-230.
PDB; 3O9R; X-ray; 2.00 A; A/B=79-230.
PDB; 3O9S; X-ray; 2.48 A; A/B=79-230.
PDB; 3O9T; X-ray; 2.20 A; A/B=79-230.
PDB; 3O9U; X-ray; 3.20 A; A/B/C/D/E/F/G/H=79-230.
PDB; 3RVC; X-ray; 1.80 A; A=79-230.
PDBsum; 2GX9; -.
PDBsum; 2ZKO; -.
PDBsum; 3L4Q; -.
PDBsum; 3O9Q; -.
PDBsum; 3O9R; -.
PDBsum; 3O9S; -.
PDBsum; 3O9T; -.
PDBsum; 3O9U; -.
PDBsum; 3RVC; -.
ProteinModelPortal; P03496; -.
SMR; P03496; -.
DIP; DIP-29081N; -.
IntAct; P03496; 222.
MINT; MINT-3381930; -.
GeneID; 956533; -.
KEGG; vg:956533; -.
KO; K19396; -.
OrthoDB; VOG090000NT; -.
Reactome; R-HSA-1169408; ISG15 antiviral mechanism.
Reactome; R-HSA-168276; NS1 Mediated Effects on Host Pathways.
Reactome; R-HSA-168315; Inhibition of Host mRNA Processing and RNA Silencing.
Reactome; R-HSA-168888; Inhibition of IFN-beta.
Reactome; R-HSA-169131; Inhibition of PKR.
Reactome; R-HSA-192823; Viral mRNA Translation.
EvolutionaryTrace; P03496; -.
Proteomes; UP000009255; Genome.
Proteomes; UP000109386; Genome.
Proteomes; UP000116373; Genome.
Proteomes; UP000170967; Genome.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
GO; GO:0030683; P:evasion or tolerance by virus of host immune response; TAS:Reactome.
GO; GO:0075733; P:intracellular transport of virus; TAS:Reactome.
GO; GO:0046778; P:modification by virus of host mRNA processing; TAS:Reactome.
GO; GO:0019054; P:modulation by virus of host process; TAS:Reactome.
GO; GO:0039524; P:suppression by virus of host mRNA processing; IEA:UniProtKB-KW.
GO; GO:0039580; P:suppression by virus of host PKR activity; IEA:UniProtKB-KW.
GO; GO:0039540; P:suppression by virus of host RIG-I activity; IEA:UniProtKB-KW.
GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; IEA:UniProtKB-KW.
GO; GO:0019083; P:viral transcription; TAS:Reactome.
Gene3D; 1.10.287.10; -; 1.
HAMAP; MF_04066; INFV_NS1; 1.
InterPro; IPR000256; Flu_NS1.
InterPro; IPR009068; S15_NS1_RNA-bd.
Pfam; PF00600; Flu_NS1; 1.
SUPFAM; SSF47060; SSF47060; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome;
Eukaryotic host gene expression shutoff by virus; Host cytoplasm;
Host gene expression shutoff by virus; Host mRNA suppression by virus;
Host nucleus; Host-virus interaction;
Inhibition of host innate immune response by virus;
Inhibition of host interferon signaling pathway by virus;
Inhibition of host PKR by virus;
Inhibition of host pre-mRNA processing by virus;
Inhibition of host RIG-I by virus;
Inhibition of host RLR pathway by virus;
Interferon antiviral system evasion; Isopeptide bond;
Reference proteome; RNA-binding; Ubl conjugation; Viral immunoevasion.
CHAIN 1 230 Non-structural protein 1.
/FTId=PRO_0000078945.
REGION 1 73 RNA-binding and homodimerization.
{ECO:0000255|HAMAP-Rule:MF_04066}.
REGION 180 215 CPSF4-binding. {ECO:0000255|HAMAP-
Rule:MF_04066}.
REGION 223 230 PABPN1-binding. {ECO:0000255|HAMAP-
Rule:MF_04066}.
MOTIF 34 38 Nuclear localization signal.
{ECO:0000255|HAMAP-Rule:MF_04066}.
MOTIF 137 146 Nuclear export signal.
{ECO:0000255|HAMAP-Rule:MF_04066}.
CROSSLNK 20 20 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ISG15); in
band I form; by host.
{ECO:0000269|PubMed:20385878}.
CROSSLNK 41 41 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ISG15); in
band I form; by host.
{ECO:0000269|PubMed:20385878}.
CROSSLNK 108 108 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ISG15); in
band II form; by host.
{ECO:0000269|PubMed:20385878}.
CROSSLNK 110 110 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ISG15); in
band II form; by host.
{ECO:0000269|PubMed:20385878}.
CROSSLNK 126 126 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ISG15); in
band II form; by host.
{ECO:0000269|PubMed:20385878}.
CROSSLNK 217 217 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ISG15); in
band I form; by host.
{ECO:0000269|PubMed:20385878}.
CROSSLNK 219 219 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ISG15); in
band I form; by host.
{ECO:0000269|PubMed:20385878}.
MUTAGEN 20 20 K->A: No of ISGylation of band I form;
when associated with K-41; K-217 and K-
219. {ECO:0000269|PubMed:20385878}.
MUTAGEN 38 38 R->A: Complete loss of inhibition of
DDX58 CARD ubiquitination; when
associated with A-41.
{ECO:0000269|PubMed:19454348}.
MUTAGEN 41 41 K->A: Complete loss of inhibition of
DDX58 CARD ubiquitination; when
associated with A-38.
{ECO:0000269|PubMed:19454348,
ECO:0000269|PubMed:20385878}.
MUTAGEN 41 41 K->A: No of ISGylation of band I form;
when associated with K-20; K-217 and K-
219. {ECO:0000269|PubMed:19454348,
ECO:0000269|PubMed:20385878}.
MUTAGEN 96 96 E->A: Complete loss of inhibition of
DDX58 CARD ubiquitination; when
associated with A-97.
{ECO:0000269|PubMed:19454348}.
MUTAGEN 97 97 E->A: Complete loss of inhibition of
DDX58 CARD ubiquitination; when
associated with A-96.
{ECO:0000269|PubMed:19454348}.
MUTAGEN 108 108 K->A: No of ISGylation of band II form;
when associated with K-110 and K-126.
{ECO:0000269|PubMed:20385878}.
MUTAGEN 110 110 K->A: No of ISGylation of band II form;
when associated with K-108 and K-126.
{ECO:0000269|PubMed:20385878}.
MUTAGEN 126 126 K->A: No of ISGylation of band II form;
when associated with K-108 and K-110.
{ECO:0000269|PubMed:20385878}.
MUTAGEN 217 217 K->A: No of ISGylation of band I form;
when associated with K-20; K-41 and K-
219. {ECO:0000269|PubMed:20385878}.
MUTAGEN 219 219 K->A: No of ISGylation of band I form;
when associated with K-20; K-41 and K-
217. {ECO:0000269|PubMed:20385878}.
CONFLICT 55 55 E -> K (in Ref. 4; ABD77680).
CONFLICT 101 101 D -> E (in Ref. 2; AAA43536).
HELIX 3 24 {ECO:0000244|PDB:2ZKO}.
HELIX 30 50 {ECO:0000244|PDB:2ZKO}.
HELIX 54 69 {ECO:0000244|PDB:2ZKO}.
STRAND 88 93 {ECO:0000244|PDB:3RVC}.
HELIX 95 99 {ECO:0000244|PDB:3RVC}.
STRAND 105 112 {ECO:0000244|PDB:3RVC}.
STRAND 115 120 {ECO:0000244|PDB:3RVC}.
STRAND 127 137 {ECO:0000244|PDB:3RVC}.
STRAND 140 151 {ECO:0000244|PDB:3RVC}.
STRAND 156 162 {ECO:0000244|PDB:3RVC}.
HELIX 171 187 {ECO:0000244|PDB:3RVC}.
STRAND 191 194 {ECO:0000244|PDB:3RVC}.
HELIX 196 201 {ECO:0000244|PDB:3RVC}.
SEQUENCE 230 AA; 25868 MW; 2F7EC18E3EE7A4BE CRC64;
MDPNTVSSFQ VDCFLWHVRK RVADQELGDA PFLDRLRRDQ KSLRGRGSTL GLDIETATRA
GKQIVERILK EESDEALKMT MASVPASRYL TDMTLEEMSR DWSMLIPKQK VAGPLCIRMD
QAIMDKNIIL KANFSVIFDR LETLILLRAF TEEGAIVGEI SPLPSLPGHT AEDVKNAVGV
LIGGLEWNDN TVRVSETLQR FAWRSSNENG RPPLTPKQKR EMAGTIRSEV


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