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Q84940

- NSP1_ROTP5

UniProt

Q84940 - NSP1_ROTP5

Protein

Non-structural protein 1

Gene
N/A
Organism
Rotavirus A (strain Pig/United States/OSU/1977 G5-P9[7]-I5-R1-C1-M1-A1-N1-T1-E1-H1) (RV-A) (Rotavirus A (strain Ohio State University))
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 51 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    Seems to induce the proteasome-dependent degradation of IRF3, IRF5 and IRF7, thereby antagonizing the cellular interferon response and establishment of the antiviral state. Binds and targets IRF3 early post-infection and suppresses IRF3 nuclear translocation By similarity.By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri42 – 7938Sequence AnalysisAdd
    BLAST

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. protein binding Source: UniProtKB
    3. RNA binding Source: UniProtKB-KW

    GO - Biological processi

    1. suppression by virus of host IRF3 activity Source: UniProtKB-KW
    2. suppression by virus of host IRF7 activity Source: UniProtKB-KW
    3. suppression by virus of host NF-kappaB transcription factor activity Source: UniProtKB-KW

    Keywords - Biological processi

    Host-virus interaction, Inhibition of host innate immune response by virus, Inhibition of host IRF3 by virus, Inhibition of host IRF7 by virus, Inhibition of host NF-kappa-B by virus, Inhibition of host RLR pathway by virus, Interferon antiviral system evasion, Viral immunoevasion

    Keywords - Ligandi

    Metal-binding, RNA-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Non-structural protein 1
    Short name:
    NSP1
    Alternative name(s):
    NCVP2
    Non-structural RNA-binding protein 53
    Short name:
    NS53
    OrganismiRotavirus A (strain Pig/United States/OSU/1977 G5-P9[7]-I5-R1-C1-M1-A1-N1-T1-E1-H1) (RV-A) (Rotavirus A (strain Ohio State University))
    Taxonomic identifieri10915 [NCBI]
    Taxonomic lineageiVirusesdsRNA virusesReoviridaeSedoreovirinaeRotavirus
    Virus hostiSus scrofa (Pig) [TaxID: 9823]

    Subcellular locationi

    GO - Cellular componenti

    1. host cell cytoplasm Source: UniProtKB-KW
    2. host cytoskeleton Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Host cytoplasm, Host cytoskeleton

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 486486Non-structural protein 1PRO_0000367822Add
    BLAST

    Interactioni

    Subunit structurei

    Interacts (via C-terminus) with host IRF3; this interaction leads to IRF3 degradation. Interacts with host IRF7; this interaction leads to IRF7 degradation By similarity.By similarity

    Protein-protein interaction databases

    IntActiQ84940. 19 interactions.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 8181RNA-bindingBy similarityAdd
    BLAST
    Regioni82 – 17695Important for cytoskeleton localizationAdd
    BLAST
    Regioni313 – 486174Interaction with IRF3Add
    BLAST

    Domaini

    The zinc-finger domain is important, but not sufficient for binding and degrading IRF3. It is sometimes described as a RING zinc-finger, but it is atypical and it is unclear whether it is related with ubiquitin ligase activity By similarity.By similarity

    Sequence similaritiesi

    Belongs to the rotavirus A NSP1 family.Curated

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri42 – 7938Sequence AnalysisAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Family and domain databases

    InterProiIPR002148. Rotavirus_NSP1.
    [Graphical view]
    PfamiPF00981. Rota_NS53. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q84940-1 [UniParc]FASTAAdd to Basket

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    MATFKDACYY YKRINKLNHA VLKLGVNDTW RPSPPTKYKG WCLDCCQHTD    50
    LTYCRGCTMY HVCQWCSQYG RCFLDNEPHL LRMRTFKNEV TKDDLMNLVD 100
    MYDTLFPMNQ KIVDKFINNT RQHKCRNECV NQWYNHLLMP ITLQSLSIEL 150
    DGDVYYIFGY YDDMNNVNQT PFSFVNLVDI YDKLLLDDVN FTRMSFLPVT 200
    LQQEYALRYF SKSRFISEQR KCVSDSHFSI NVLENLHNPS FKMQITRNCS 250
    ELSSDWNGAC KLVKDTSAYF NILKTSHVEF YSISTRCRVF TQRKLKIASK 300
    LIKPNYITSN HRTSATEVHN CKWCSINSSY TVWNDFRVKK IYDNIFNFLR 350
    ALVKSNVNVG HCSSQEKIYE CVENILDVCD NEKWKTSVTK IFNYLEPVEL 400
    NAVNYVLFNH EVNWDVINVL VQSIGKVPQI LTLNDVTTIM QSIIYEWFDT 450
    KYMRNTPMTT FTVDKLRRLC TGSKTVDYDS GISDVE 486
    Length:486
    Mass (Da):57,235
    Last modified:November 1, 1996 - v1
    Checksum:iE42BAC8CDF5BF666
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti102 – 1021Y → F in CAA78092. (PubMed:7996134)Curated
    Sequence conflicti227 – 2271H → R in CAA78092. (PubMed:7996134)Curated
    Sequence conflicti250 – 2501S → N in CAA78092. (PubMed:7996134)Curated
    Sequence conflicti321 – 3211C → S in CAA78092. (PubMed:7996134)Curated
    Sequence conflicti370 – 3701E → Q in CAA78092. (PubMed:7996134)Curated
    Sequence conflicti449 – 4502DT → TR in CAA78092. (PubMed:7996134)Curated
    Sequence conflicti478 – 4792YD → CN in CAA78092. (PubMed:7996134)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U08432 Genomic RNA. Translation: AAA50495.1.
    Z12107 Genomic RNA. Translation: CAA78092.1.
    D38153 Genomic RNA. Translation: BAA20544.1.
    PIRiS31805.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U08432 Genomic RNA. Translation: AAA50495.1 .
    Z12107 Genomic RNA. Translation: CAA78092.1 .
    D38153 Genomic RNA. Translation: BAA20544.1 .
    PIRi S31805.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q84940. 19 interactions.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    InterProi IPR002148. Rotavirus_NSP1.
    [Graphical view ]
    Pfami PF00981. Rota_NS53. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Comparison of the rotavirus nonstructural protein NSP1 (NS53) from different species by sequence analysis and northern blot hybridization."
      Dunn S.J., Cross T.L., Greenberg H.B.
      Virology 203:178-183(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    2. "Molecular biology of rotaviruses. IX. Conservation and divergence in genome segment 5."
      Xu L.I., Tian Y., Tarlow O., Harbour D.A., McCrae M.A.
      J. Gen. Virol. 75:3413-3421(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    3. "Species-specific and interspecies relatedness of NSP1 sequences in human, porcine, bovine, feline, and equine rotavirus strains."
      Kojima K., Taniguchi K., Kobayashi N.
      Arch. Virol. 141:1-12(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    4. "Zinc-binding domain of rotavirus NSP1 is required for proteasome-dependent degradation of IRF3 and autoregulatory NSP1 stability."
      Graff J.W., Ewen J., Ettayebi K., Hardy M.E.
      J. Gen. Virol. 88:613-620(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA], FUNCTION.

    Entry informationi

    Entry nameiNSP1_ROTP5
    AccessioniPrimary (citable) accession number: Q84940
    Secondary accession number(s): Q85037
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 24, 2009
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 51 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programViral Protein Annotation Program

    Miscellaneousi

    Caution

    NSP1 has been shown (PubMed:17251580) to be almost unable to bind and degrade IRF3 in cell culture. However, this does not implies that it is the case in vivo, since the down-regulation of host antiviral state is not essential for the virus in cell culture and the used cells were not of porcine origin.1 Publication

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3