NSP1_ROTHP
ID NSP1_ROTHP Reviewed; 486 AA.
AC B3SRV2;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 23-FEB-2022, entry version 39.
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 (strain RVA/Human/United States/P/1974/G3P1A[8]) (RV-A).
OC Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC Reovirales; Reoviridae; Sedoreovirinae; Rotavirus; Rotavirus A.
OX NCBI_TaxID=10957;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=18786998; DOI=10.1128/jvi.01402-08;
RA Heiman E.M., McDonald S.M., Barro M., Taraporewala Z.F., Bar-Magen T.,
RA Patton J.T.;
RT "Group A human rotavirus genomics: evidence that gene constellations are
RT influenced by viral protein interactions.";
RL J. Virol. 82:11106-11116(2008).
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; EF672599; ABV53277.1; -; Genomic_RNA.
DR PRIDE; B3SRV2; -.
DR Proteomes; UP000007047; Genome.
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_0000369088"
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; 57672 MW; C3DA6ECA736AE858 CRC64;
MATFKDACYH YKRINKLNHT VLKLGVNDTW RSSPPTKYKG WCLDCCQHTD LTYCRGCTMY
HVCQWCSQYG RCFLDNEPHL LRMRTFKNEV TKDDLKNLID MYEILFPMNQ KIVCRFINNT
RQHKCRNECM TQWYNHLLLP ITLQSMSIEL DGDVYYVFGY YDNMNSINQT PFSFTNLVDI
YDKLLLDDVN FARMSFLPAS LQQEYALRYF SKSRFISEQR KCVNDSHFSI NVLENLHNPS
FKVQITRNCS ELSFDWNEAC KLVKNVSAYF DMLKTSHIEF YSVSTRCRIF TQCKLKMASK
LIKPNYITSN HKTLATEVHN CKWCSVNNSY TVWNDFRIKK IYDNIFNFLR ALVKSNVNIG
HCSSQEKIYE YVEDVLNVCD DERWKTSIME IFNCLEPVEL DDVKYVLFNH EINWDVINVL
VHSIGKVPQI LTLENVITIM QSIIYEWFDI RYMRNTPMVT FTIDKLRRLH TGLKTVEYDS
GISDIE
