ID   NSP1_ROTHI              Reviewed;         486 AA.
AC   P30212;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   14-DEC-2022, entry version 64.
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/Human/Japan/IGV-80-3/XXXX/GXP[X]) (RV-A).
OC   Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC   Reovirales; Sedoreoviridae; Rotavirus; Rotavirus A.
OX   NCBI_TaxID=31574;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA   Kawagishi M., Matsuno S.;
RL   Submitted (MAY-1991) to the EMBL/GenBank/DDBJ databases.
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. Recognizes the host NF-kappa-B regulator BTRC through the
CC       presence of a DSGXS motif in the C-terminal substrate recognition
CC       domain. {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. Interacts
CC       with host BTRC. {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   -!- PTM: The C-terminal region is phosphorylated by host CKII/CSNK2A1.
CC       Phosphorylation of the DSGXS motif is essential for host NF-kappa-B
CC       inhibition. {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; X59297; CAA41986.1; -; Genomic_RNA.
DR   PIR; S15470; S15470.
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:0039644; P:suppression by virus of host NF-kappaB cascade; 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 NF-kappa-B by virus;
KW   Inhibition of host RLR pathway by virus;
KW   Interferon antiviral system evasion; Metal-binding; Phosphoprotein;
KW   RNA-binding; Viral immunoevasion.
FT   CHAIN           1..486
FT                   /note="Non-structural protein 1"
FT                   /id="PRO_0000149556"
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          317..486
FT                   /note="Interaction with host IRF3"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04088"
FT   MOTIF           479..483
FT                   /note="IKBKB-like degron (ILD) motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04088"
FT   MOTIF           480..483
FT                   /note="pLxIS motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04088"
SQ   SEQUENCE   486 AA;  57645 MW;  6A9E6033A3488D2B CRC64;
     MATFKDACYH YKRINKLNHT VLKLGVNDTW RPSPPTKYKG WCLDCCQHTD LTYCRGCTMY
     HVCQWCSQYG RCFLDNEPHL LRMRTFKNEV TKDDLKNLID MYETLFPMNQ RIVCRFINNT
     RQHKCRNECM TQWYNHLLLP ITLQSMSIEL DGDVYYVFGY YDNMNSINQT PFSFTNLVDI
     YDKLLLDDVN FTRMSFLPAS LQQEYALRYF SKSRFISEQR KCVNDSHFSI NVIENLHNPS
     FKVQITRNCS ELSFDWNKAC KLVKKISAYF DILKTSHIEF YSVSTRCRIF TQCKLKMASK
     LIKPNYITSN HKTLATEVHN CKWCSVNNSY TVWNDFRIKN IYDNIFNFLR ALVKSNVNIG
     HCSSQEKIYE YVEDVLNVCD DERWKTSIME IFNCLEPVEL DDVKYVLLNH EINWDVINVL
     VHSIGKVPQI LTLENVIAIM QSIIYEWFDI RYMRNTPMVT FTIDKLRRLH TGLKTVDYDS
     GISDIE
//