ID   NSP1_ROTME              Reviewed;         493 AA.
AC   Q83444;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, 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/Mouse/Brazil/EHP/1981/G16P[20]) (RV-A).
OC   Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC   Reovirales; Reoviridae; Sedoreovirinae; Rotavirus; Rotavirus A.
OX   NCBI_TaxID=578840;
OH   NCBI_TaxID=39442; Mus musculus musculus (eastern European house mouse).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=8030275; DOI=10.1006/viro.1994.1471;
RA   Dunn S.J., Cross T.L., Greenberg H.B.;
RT   "Comparison of the rotavirus nonstructural protein NSP1 (NS53) from
RT   different species by sequence analysis and northern blot hybridization.";
RL   Virology 203:178-183(1994).
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; U08423; AAA50486.1; -; 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..493
FT                   /note="Non-structural protein 1"
FT                   /id="PRO_0000369078"
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          319..493
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   493 AA;  57597 MW;  DEE472048A58EBA7 CRC64;
     MAAFKDACFH YRRITKLNRE LLRIGANSSW TPAPPSNIRG WCLECCQLTN LTYCYGCSLH
     HVCQWCVQYG RCFLDDEPHL LRLRTVKSPI TTEKLASIVK MYQLLFPINH SIVKKFVKST
     KQHKCRNDFE LSWYNQLVLP ITLTAAAVHC DDCIYYIFGH YEGKANQSNL PYRFVNCVDE
     YDRLLLDDVN FDRMAFLPGR LQKYYAKRYF IASRIPSAQP AKLTYSDFSV KTLINSGAYA
     RRRIIYRSVT NFHWQSHEDP LNDLLLDKDK ILAALMTNER RPFLTHNLNF TSLLHELSEL
     VHHAKPCYLH SFHVQPASKV HCHSCSVAFD FHTVDWRIRR IYDDVMYFLR ACCRSNVSSG
     SCSSLDPMDA VVKAALLEMF TESFKHHAHL LFHCFDPVQI DDVSYILFNY PVNYDIYDFI
     IRTLATERLP FTLSYKQFTT ILFALVERWY DLSQIERLPL SIAPTNRLIE LQERGNLAEE
     FDLLLSSSDS EED