ID   NSP1_ROTEH              Reviewed;         491 AA.
AC   O39821;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   23-FEB-2022, entry version 58.
DE   RecName: Full=Non-structural protein 1 {ECO:0000255|HAMAP-Rule:MF_04088};
DE            Short=NSP1 {ECO:0000255|HAMAP-Rule:MF_04088};
DE   AltName: Full=NCVP2 {ECO:0000255|HAMAP-Rule:MF_04088};
DE   AltName: Full=Non-structural RNA-binding protein 53 {ECO:0000255|HAMAP-Rule:MF_04088};
DE            Short=NS53 {ECO:0000255|HAMAP-Rule:MF_04088};
OS   Rotavirus A (isolate RVA/Equine/United Kingdom/H2/1976/G3P4[12]) (RV-A)
OS   (Rotavirus A (isolate H-2)).
OC   Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC   Reovirales; Reoviridae; Sedoreovirinae; Rotavirus; unclassified Rotavirus.
OX   NCBI_TaxID=10939;
OH   NCBI_TaxID=9796; Equus caballus (Horse).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=8629937; DOI=10.1007/bf01718584;
RA   Kojima K., Taniguchi K., Kobayashi N.;
RT   "Species-specific and interspecies relatedness of NSP1 sequences in human,
RT   porcine, bovine, feline, and equine rotavirus strains.";
RL   Arch. Virol. 141:1-12(1996).
CC   -!- FUNCTION: Plays a role in the inhibition of host innate immunity by
CC       inducing the degradation of key host factors required to activate
CC       interferon production such as IRF3, IRF5 or IRF7. Associates with
CC       components of cullin RING ligases (CRLs) including CUL1 or CUL3, which
CC       are essential multisubunit ubiquitination complexes, to modulate their
CC       activities. {ECO:0000255|HAMAP-Rule:MF_04088}.
CC   -!- SUBUNIT: Interacts (via C-terminus) with host IRF3; this interaction
CC       leads to IRF3 degradation. Interacts with host IRF7; this interaction
CC       leads to IRF7 degradation. Interacts with host CUL1 and CUL3.
CC       {ECO:0000255|HAMAP-Rule:MF_04088}.
CC   -!- SUBCELLULAR LOCATION: Host cytoplasm, host cytoskeleton
CC       {ECO:0000255|HAMAP-Rule:MF_04088}.
CC   -!- DOMAIN: The integrity of the zinc-binding domain in NSP1 is important
CC       for degradation of host IRF3. {ECO:0000255|HAMAP-Rule:MF_04088}.
CC   -!- DOMAIN: The pLxIS motif targets host IRF3 for degradation; however
CC       phosphorylation of NSP1 pLxIS motif is not required for its activity.
CC       {ECO:0000255|HAMAP-Rule:MF_04088}.
CC   -!- SIMILARITY: Belongs to the rotavirus NSP1 family. {ECO:0000255|HAMAP-
CC       Rule:MF_04088}.
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DR   EMBL; D38157; BAA20548.1; -; Genomic_RNA.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-UniRule.
DR   GO; GO:0044163; C:host cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0039548; P:suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of IRF3 activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0039557; P:suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of IRF7 activity; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_04088; ROTA_NSP1; 1.
DR   InterPro; IPR002148; Rotavirus_NSP1.
DR   Pfam; PF00981; Rota_NS53; 1.
PE   3: Inferred from homology;
KW   Host cytoplasm; Host cytoskeleton; Host-virus interaction;
KW   Inhibition of host innate immune response by virus;
KW   Inhibition of host IRF3 by virus; Inhibition of host IRF7 by virus;
KW   Inhibition of host RLR pathway by virus;
KW   Interferon antiviral system evasion; Metal-binding; RNA-binding;
KW   Viral immunoevasion.
FT   CHAIN           1..491
FT                   /note="Non-structural protein 1"
FT                   /id="PRO_0000369071"
FT   REGION          1..81
FT                   /note="RNA-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04088"
FT   REGION          42..79
FT                   /note="Zinc-binding domain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04088"
FT   REGION          82..176
FT                   /note="Important for cytoskeleton localization"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04088"
FT   REGION          318..491
FT                   /note="Interaction with host IRF3"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04088"
FT   MOTIF           483..486
FT                   /note="pLxIS motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04088"
SQ   SEQUENCE   491 AA;  57783 MW;  2C1933A5DCE09042 CRC64;
     MATFKDACFH YRKITKLNRE LLRIGANSVW TSVQSNKIKG WCVECCQLTE LTYCSGCSLA
     HVCQLCITNK RCFLDSQPHL LKLRTFESPI TKEKLQCVIN LYDKLFPINN TIINKFKKST
     RQRKCRNGLN ETWYNQLLLP ITLNAAVFKF KTRTVYVFGF YEGSVSVENL PYRIINCIDI
     YDRLLLDQIN FERMNSLPVS LQSIYAQKYF RVSRIPSMKL RQIYYSDFTK QNLITKYRTK
     SRIVHRNISK INWNTEIELH NTLTHNKNKI LEILSTSIER QFLVHDINLG RVKADMFELG
     HQCKPNYVSS NHWQPASKIS VCKWCNIKYA FKDMDWRMES MYNELMSFIQ ACYKSNTNVD
     HCSSIESIYP IIRNVYWHST TNYIDETLNK LFSMMNPVCI DSQSVINFHC QIDLSLYLHI
     KMILEMEVLP FILNVNQFKD IIKGIMNQWC NFSKLSELPL CIESTTTLLE LEKQGKLSEE
     YDLLISDSDD D