NS1_INBYA
ID NS1_INBYA Reviewed; 281 AA.
AC P08013;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 23-FEB-2022, entry version 82.
DE RecName: Full=Non-structural protein 1 {ECO:0000255|HAMAP-Rule:MF_04066};
DE Short=NS1 {ECO:0000255|HAMAP-Rule:MF_04066};
DE AltName: Full=NS1A {ECO:0000255|HAMAP-Rule:MF_04066};
GN Name=NS {ECO:0000255|HAMAP-Rule:MF_04066};
OS Influenza B virus (strain B/Yamagata/1/1973).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Insthoviricetes; Articulavirales; Orthomyxoviridae; Betainfluenzavirus.
OX NCBI_TaxID=11550;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=3811235; DOI=10.1016/0042-6822(87)90399-0;
RA Norton G.P., Tanaka T., Tobita K., Nakada S., Buonagurio D.A.,
RA Greenspan D., Krystal M., Palese P.;
RT "Infectious influenza A and B virus variants with long carboxyl terminal
RT deletions in the NS1 polypeptides.";
RL Virology 156:204-213(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Mutant AWBY-234;
RX PubMed=2136779; DOI=10.1016/0042-6822(90)90082-3;
RA Tobita K., Tanaka T., Odagiri T., Tashiro M., Feng S.Y.;
RT "Nucleotide sequence and some biological properties of the NS gene of a
RT newly isolated influenza B virus mutant which has a long carboxyl terminal
RT deletion in the NS1 protein.";
RL Virology 174:314-319(1990).
RN [3]
RP FUNCTION AS A SUPPRESSOR OF RNA SILENCING.
RX PubMed=14745017; DOI=10.1073/pnas.0308308100;
RA Li W.-X., Li H., Lu R., Li F., Dus M., Atkinson P., Brydon E.W.A.,
RA Johnson K.L., Garcia-Sastre A., Ball L.A., Palese P., Ding S.-W.;
RT "Interferon antagonist proteins of influenza and vaccinia viruses are
RT suppressors of RNA silencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:1350-1355(2004).
RN [4]
RP REVIEW.
RX PubMed=12758165; DOI=10.1016/s0042-6822(03)00119-3;
RA Krug R.M., Yuan W., Noah D.L., Latham A.G.;
RT "Intracellular warfare between human influenza viruses and human cells: the
RT roles of the viral NS1 protein.";
RL Virology 309:181-189(2003).
CC -!- FUNCTION: Binds and inhibits the conjugation of the ubiquitin-like
CC G1P2/ISG15 protein to its target proteins. Since G1P2/ISG15 is an early
CC antiviral protein, NS1 may inhibit the host antiviral response.
CC Prevents EIF2AK2/PKR activation, either by binding double strand RNA or
CC by interacting directly with EIF2AK2/PKR. Also binds poly(A) and U6
CC snRNA. {ECO:0000255|HAMAP-Rule:MF_04066, ECO:0000269|PubMed:14745017}.
CC -!- SUBUNIT: Homodimer. Interacts with and inhibits human G1P2 conjugation
CC by UBE1L. {ECO:0000255|HAMAP-Rule:MF_04066}.
CC -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04066}.
CC Host nucleus {ECO:0000255|HAMAP-Rule:MF_04066}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=NS1;
CC IsoId=P08013-1; Sequence=Displayed;
CC Name=NEP; Synonyms=NS2;
CC IsoId=P08014-1; Sequence=External;
CC -!- DOMAIN: Both N-terminus and C-terminus can inhibit IFN-beta promoter
CC activation and IRF-3 nuclear translocation.
CC -!- SIMILARITY: Belongs to the influenza B viruses NS1 family.
CC {ECO:0000255|HAMAP-Rule:MF_04066}.
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DR EMBL; M16633; AAA43761.1; -; Genomic_RNA.
DR EMBL; M32749; AAA43757.1; -; Genomic_RNA.
DR PIR; A33778; MNIVAW.
DR PIR; C27529; MNIV73.
DR SMR; P08013; -.
DR PRIDE; P08013; -.
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:0039579; P:suppression by virus of host ISG15-protein conjugation; IEA:UniProtKB-KW.
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 HAMAP; MF_04066; INFV_NS1; 1.
DR InterPro; IPR004208; NS1.
DR InterPro; IPR009068; S15_NS1_RNA-bd.
DR Pfam; PF02942; Flu_B_NS1; 1.
DR PIRSF; PIRSF003938; Flu_B_NS1; 1.
DR SUPFAM; SSF47060; SSF47060; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Host cytoplasm; Host nucleus; Host-virus interaction;
KW Inhibition of host innate immune response by virus;
KW Inhibition of host interferon signaling pathway by virus;
KW Inhibition of host ISG15 by virus; Inhibition of host PKR by virus;
KW Interferon antiviral system evasion; RNA-binding; Viral immunoevasion.
FT CHAIN 1..281
FT /note="Non-structural protein 1"
FT /id="PRO_0000078972"
FT REGION 1..103
FT /note="G1P2-binding"
FT REGION 1..93
FT /note="RNA-binding and homodimerization"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04066"
FT MOTIF 50..55
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04066"
FT VARIANT 66
FT /note="E -> V (in strain: Mutant AWBY-234)"
FT VARIANT 90
FT /note="F -> L (in strain: Mutant AWBY-234)"
FT VARIANT 91..281
FT /note="Missing (in strain: Mutant AWBY-234)"
SQ SEQUENCE 281 AA; 31943 MW; B5551E6D64ABC5D8 CRC64;
MADNMTTTQI EVGPGATNAT INFEAGILEC YERLSWQRAL DYPGQDRLNR LKRKLESRIK
THNKSEPESK RMSLEERKAI GVKMMKVLLF MNPSAGIEGF EPYCMKNSSN SNCPNCNWTD
YPPTSGKCLD DIEEEPENVD DPTEIVLRDM NNKDARQKIK EEVNTQKEGK FRLTIKRDIR
NVLSLRVLVN GTFLKHPNGY KSLSTLHRLN AYDQSGRLVA KLVATDDLTV EDEEDGHRIL
NSLFERFNEG HSKPIRAAET AVGVLSQFGQ EHRLSPEEGD N