NSP1_ROTHD
ID NSP1_ROTHD Reviewed; 486 AA.
AC P35423; B3SRS8;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 23-FEB-2022, entry version 76.
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/DS-1/1976/G2P1B[4]) (RV-A)
OS (Rotavirus A (strain DS1)).
OC Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC Reovirales; Reoviridae; Sedoreovirinae; Rotavirus; Rotavirus A.
OX NCBI_TaxID=10950;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=8395125; DOI=10.1006/viro.1993.1492;
RA Hua J.J., Mansell E.E., Patton J.T.;
RT "Comparative analysis of the rotavirus NS53 gene: conservation of basic and
RT cysteine-rich regions in the protein and possible stem-loop structures in
RT the RNA.";
RL Virology 196:372-378(1993).
RN [2]
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. {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; L18945; AAA47332.1; -; Genomic_RNA.
DR EMBL; EF672578; ABV53253.1; -; Genomic_RNA.
DR Proteomes; UP000001457; 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: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..486
FT /note="Non-structural protein 1"
FT /id="PRO_0000149555"
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 480..483
FT /note="pLxIS motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04088"
FT CONFLICT 130
FT /note="S -> L (in Ref. 2; ABV53253)"
FT CONFLICT 331
FT /note="I -> T (in Ref. 2; ABV53253)"
FT CONFLICT 374
FT /note="E -> D (in Ref. 2; ABV53253)"
FT CONFLICT 481
FT /note="R -> G (in Ref. 2; ABV53253)"
SQ SEQUENCE 486 AA; 57991 MW; C802AF023F629CB5 CRC64;
MATFKDACYQ YKKLNKLNNA VLKLGANDVW RPSTLTKRKG WCLDCCQHTD LTYCQGCLIY
HVCEWCSQYN RCFLDDDPHL LRMRTFRNEI TKSDLENLIN MYNTLFPINK KIVHKFANTI
KQHKCRNEYS TQWYNHFLMP ITLQSLSIEL DGDIYYIFGY YDDMHKINQT PFSFTNLISK
YDMLLLDSIN FDRMAFLPLT LQQEYALRYF SKSRFITERR KCIEILHFSD NILDNLHNPN
FTLQVIRNCS NMSVEWNKAC NIIRNISDYF DILKSSHTEF YNISPRCRMF TQYKLKIASK
LIKPNYVASN HNSLATEVHN CKWCSINNNS IVWNDFRIKN VYNDIFNFIR ALVKSNLYVG
HCSSEEKIYE SIKEVLNVCK ENEWNMLVTE MFNQLEPIKL NENNYILLNY EINWNVMNVL
INSIGKIPKI LTLSDVILIL RIIIYDWFDI RFMRNTPMTT FTVNKLKQLY EKDRTAEHDS
RISDIE
