NSP1_ROTH6
ID NSP1_ROTH6 Reviewed; 486 AA.
AC O40626; B3SRQ4; Q82042;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-APR-2009, sequence version 2.
DT 03-AUG-2022, entry version 66.
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/Indonesia/69M/1980/G8P4[10]) (RV-A).
OC Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC Reovirales; Reoviridae; Sedoreovirinae; Rotavirus; Rotavirus A.
OX NCBI_TaxID=10947;
OH NCBI_TaxID=9606; Homo sapiens (Human).
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA McCrae M.A.;
RL Submitted (APR-1994) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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; D38151; BAA20542.1; -; Genomic_RNA.
DR EMBL; Z32552; CAA83550.1; -; Genomic_RNA.
DR EMBL; EF672557; ABV53229.1; -; Genomic_DNA.
DR SMR; O40626; -.
DR PRIDE; O40626; -.
DR Proteomes; UP000001455; 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_0000369081"
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"
FT CONFLICT 3
FT /note="T -> S (in Ref. 2; CAA83550)"
FT CONFLICT 23..25
FT /note="KLG -> NLP (in Ref. 2; CAA83550)"
FT CONFLICT 42
FT /note="C -> Y (in Ref. 2; CAA83550)"
FT CONFLICT 188
FT /note="S -> T (in Ref. 1; BAA20542)"
FT CONFLICT 247
FT /note="R -> T (in Ref. 1; BAA20542)"
FT CONFLICT 361
FT /note="H -> D (in Ref. 1; BAA20542)"
FT CONFLICT 445
FT /note="Y -> D (in Ref. 2; CAA83550)"
FT CONFLICT 459
FT /note="T -> S (in Ref. 2; CAA83550)"
SQ SEQUENCE 486 AA; 57766 MW; AD2D967C72498467 CRC64;
MATFKDACYQ YKKLNKLNNA ILKLGANDVW RSSTLTKRKG WCLDCCQHTD LTYCQGCLIY
HVCEWCSQYS RCFLDDDPHL LRMRTFRNEV TKSDLENLIN MYDTLFPINQ KIVNKFTNII
KQHKCRNEYL TQWYNHFLMP ITLQSLSIEL DGDIYYIFGY YDDMHKINQT PFSFANLINK
YDVLLLDSIN FDRMAFLPLT LQQEYALRYF SKSRFITERR KYIETLHFSD NILNNLHNPN
FTLQVIRNCS NMSVEWNKAC NLIRNISDYF DILKSSHTES YNISPRCRMF TQYKLKIASK
LIKPNYVASN HNSLATEVHN CKWCSINNNS IVWTDFRIKN VYNDVFNFIR ALVKSNLYVG
HCSSEERIYE SIKDILNVCK ENEWNMLVTE IFNQLDPIKL NEDSYVLLNY EINWNVMNVL
INSIGKIPKI LTLNDVISIL RIIIYDWFDI RFMRNTPMTT FTVNKLKQLY EKDKTAEYDS
GISDVE
