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Protein

Non-structural protein 1

Gene
N/A
Organism
Rotavirus A (strain RVA/Pig/United States/OSU/1977/G5P9[7]) (RV-A) (Rotavirus A (strain Ohio State University))
Status
Reviewed-Annotation score: 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 similarity1 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/Pig/United States/OSU/1977/G5P9[7]) (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

Complete GO annotation...

Keywords - Cellular componenti

Host cytoplasm, Host cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003678221 – 486Non-structural protein 1Add BLAST486

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 interactors.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 81RNA-bindingBy similarityAdd BLAST81
Regioni82 – 176Important for cytoskeleton localizationAdd BLAST95
Regioni313 – 486Interaction with IRF3Add BLAST174

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)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.

Q84940-1 [UniParc]FASTAAdd to basket

« Hide

        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)DescriptionActionsGraphical viewLength
Sequence conflicti102Y → F in CAA78092 (PubMed:7996134).Curated1
Sequence conflicti227H → R in CAA78092 (PubMed:7996134).Curated1
Sequence conflicti250S → N in CAA78092 (PubMed:7996134).Curated1
Sequence conflicti321C → S in CAA78092 (PubMed:7996134).Curated1
Sequence conflicti370E → Q in CAA78092 (PubMed:7996134).Curated1
Sequence conflicti449 – 450DT → TR in CAA78092 (PubMed:7996134).Curated2
Sequence conflicti478 – 479YD → CN in CAA78092 (PubMed:7996134).Curated2

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
U08432 Genomic RNA. Translation: AAA50495.1.
Z12107 Genomic RNA. Translation: CAA78092.1.
D38153 Genomic RNA. Translation: BAA20544.1.
PIRiS31805.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ84940. 19 interactors.

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_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: November 30, 2016
This is version 56 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

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.