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Protein

Non-structural protein 1

Gene
N/A
Organism
Rotavirus A (strain RVA/Cow/United States/B641/XXXX/G6P7[5]) (RV-A)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

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.1 Publication

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri42 – 79Sequence analysisAdd BLAST38

GO - Molecular functioni

GO - Biological processi

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 RVA/Cow/United States/B641/XXXX/G6P7[5]) (RV-A)
Taxonomic identifieri10928 [NCBI]
Taxonomic lineageiVirusesdsRNA virusesReoviridaeSedoreovirinaeRotavirusRotavirus A
Virus hostiBos taurus (Bovine) [TaxID: 9913]

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Host cytoplasm, Host cytoskeleton

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi54C → A: 90% loss of IRF3 binding. Complete loss of IRF3 degradation. 1 Publication1
Mutagenesisi79H → L: 95% loss of IRF3 binding. Complete loss of IRF3 degradation. 1 Publication1
Mutagenesisi136H → L: 70% loss of IRF3 binding. No effect on IRF3 degradation. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003678191 – 491Non-structural protein 1Add BLAST491

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

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 81RNA-bindingBy similarityAdd BLAST81
Regioni82 – 176Important for cytoskeleton localizationAdd BLAST95
Regioni316 – 491Interaction with IRF3Add BLAST176

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.

Sequence similaritiesi

Belongs to the rotavirus A NSP1 family.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri42 – 79Sequence analysisAdd BLAST38

Keywords - Domaini

Zinc-finger

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

Q8JZ13-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATFKDACYH YKKLNKLNSL VLKLGANDEW RPAPVTKYKG WCLDCCQYTN
60 70 80 90 100
LTYCRGCALY HVCQWCSQYN RCFLDEEPHL LRMRTFKDVV TKEDIEGLLT
110 120 130 140 150
MYETLFPINE KLVNKFINSV KQRKCRNEYL LEWYNHLLMP ITLQALTINL
160 170 180 190 200
EDNVYYMFGY YDCMEHENQT PFQFVNLLEK YDKLLLDDRN FHRMSHLPVI
210 220 230 240 250
LQQEYALRYF SKSRFLSKGK KRLSRSDFSD NLMEDRHSPT SLMQVVRNCI
260 270 280 290 300
SIHIDDCEWN KACTLIVDAR NYISIMNSSY TEHYSVSQRC KLFTKYKFGI
310 320 330 340 350
VSKLVKPNYI FSSHESCALN VHNCKWCQIN NHYKVWEDFR LRKIYNNVMD
360 370 380 390 400
FIRALVKSNV NVGHCSSQES VYKYVPDLFL ICKTEKWSEA VEMLFNYLEP
410 420 430 440 450
VNVNGTEYVL LDYEVNWEVR GLVMQNMDGK VPRILNMNDT KKILSAMIFD
460 470 480 490
WFDTRYMRET PMTTSTTNQL RTLNKRNELI DEYDLELSDV E
Length:491
Mass (Da):58,600
Last modified:October 1, 2002 - v1
Checksum:iB91058CEC1D07E54
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF458087 mRNA. Translation: AAM21601.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF458087 mRNA. Translation: AAM21601.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

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

Entry informationi

Entry nameiNSP1_ROTB4
AccessioniPrimary (citable) accession number: Q8JZ13
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: October 1, 2002
Last modified: November 30, 2016
This is version 54 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.