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Q84940

- NSP1_ROTP5

UniProt

Q84940 - NSP1_ROTP5

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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

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. 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
Complete GO annotation...

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-KW
Complete GO annotation...

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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        10         20         30         40         50
MATFKDACYY YKRINKLNHA VLKLGVNDTW RPSPPTKYKG WCLDCCQHTD
60 70 80 90 100
LTYCRGCTMY HVCQWCSQYG RCFLDNEPHL LRMRTFKNEV TKDDLMNLVD
110 120 130 140 150
MYDTLFPMNQ KIVDKFINNT RQHKCRNECV NQWYNHLLMP ITLQSLSIEL
160 170 180 190 200
DGDVYYIFGY YDDMNNVNQT PFSFVNLVDI YDKLLLDDVN FTRMSFLPVT
210 220 230 240 250
LQQEYALRYF SKSRFISEQR KCVSDSHFSI NVLENLHNPS FKMQITRNCS
260 270 280 290 300
ELSSDWNGAC KLVKDTSAYF NILKTSHVEF YSISTRCRVF TQRKLKIASK
310 320 330 340 350
LIKPNYITSN HRTSATEVHN CKWCSINSSY TVWNDFRVKK IYDNIFNFLR
360 370 380 390 400
ALVKSNVNVG HCSSQEKIYE CVENILDVCD NEKWKTSVTK IFNYLEPVEL
410 420 430 440 450
NAVNYVLFNH EVNWDVINVL VQSIGKVPQI LTLNDVTTIM QSIIYEWFDT
460 470 480
KYMRNTPMTT FTVDKLRRLC TGSKTVDYDS GISDVE
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 29, 2014
This is version 52 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