ID   NSP1_ROTEL              Reviewed;         492 AA.
AC   O39822;
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/L338/1988/G13P12[18])
OS   (RV-A).
OC   Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC   Reovirales; Reoviridae; Sedoreovirinae; Rotavirus; Rotavirus A.
OX   NCBI_TaxID=36441;
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; D38158; BAA20549.1; -; Genomic_RNA.
DR   PRIDE; O39822; -.
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..492
FT                   /note="Non-structural protein 1"
FT                   /id="PRO_0000369072"
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..492
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   492 AA;  58174 MW;  5DF0703BA4754C82 CRC64;
     MATFKDACFH YRKITKINRE LLKIGANSIW TPVRSDKIKG WCIECCQLTE LVFCSGCSLA
     HVCQWCVRNK RCFLDSQPHL LKLRTFEAPI TKEKLQCVIS MYNMLFPINE NIINRFKKNV
     KQKKCRNEFN ATWYNQLLLP ITLNAAVFKF QSRIVYVFGF YEGTTACGYL PYRMVNCIDI
     YDRLLLDSVN FDRMSALPSD LQALYAQKYF KISRLPSMKL RQVYYSDFTK QNLITKYRTK
     TRITHRNVSK INWDTDIELH NDLMHNKHRI LTALTTAEEK QFEVHDVNLG RIKADMFELG
     HHCKPNYISS NHWQPASRVS LCRWCNIKYA FRNMDWRMES MYNELMSFIQ SCYKSNANVD
     HCSSIESVYP MVRNVFWHST TKYIDETLEK LFNMMNPVNI DNQKVISFHW QIDLSLYLHI
     KMILKTEALP FMLKVHEFQS IVKGIINQWC DFSKVSELPI CVESTDTLLR MYEQGELSEE
     YELLISDSDG DE