ID   NSP1_ROTF6              Reviewed;         492 AA.
AC   O56831;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   23-FEB-2022, entry version 56.
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/Cat/Japan/FRV64/1989/G3P5B[3]) (RV-A).
OC   Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC   Reovirales; Reoviridae; Sedoreovirinae; Rotavirus; unclassified Rotavirus.
OX   NCBI_TaxID=39010;
OH   NCBI_TaxID=9685; Felis catus (Cat) (Felis silvestris catus).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9316942; DOI=10.1128/jcm.35.10.2703-2705.1997;
RA   Fujiwara Y., Nakagomi O.;
RT   "Interspecies sharing of two distinct nonstructural protein 1 alleles among
RT   human and animal rotaviruses as revealed by dot blot hybridization.";
RL   J. Clin. Microbiol. 35:2703-2705(1997).
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; D78362; BAA24411.1; -; mRNA.
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   2: Evidence at transcript level;
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_0000369066"
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;  57754 MW;  81F3760E3BC6F573 CRC64;
     MATFKDACFH YRKITKLNRE LLRIGANSVW IPVSSNKIKG WCIECCQLTE LTFCHGCSLA
     HVCQWCIQNK RCFLDNEPHL LKLRSFESPI TKEKLQCIID LYNLLFPINP GIINRFKKIV
     NQRKCRNEFE QSWYNQLLFP ITLNAAVFKF HSREVYVFGL YEGSSSCIDL PYRIVNCIDL
     YDRLLLDQIN FERMSSLPAS LQSVYANKYF KLSRLPSMKL KQIYYSDFSK QNLINKCKIK
     SRIVLRNLTE FTWDSQVSLH NDVINNKEKI LTALSTSSLK RFETHDLNLG RVKADIFELG
     HHCKPNYISS NHWQPASKVS QCRWCNVKYV FRNMDWKMES MYNELLSFIQ ACYKSNVNVG
     NCSSIESAYP LVKDMLWHSI TKYIDQTIEK LFNVMNPVKV DGQQVISFHW QIDVALYIHI
     KMILKTETLP FAFTLNQFRS IIKGIVNQWY DVTELDYLPL CTEQTDKLVK LEEEGKISEE
     HELLISDSED DD