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Protein

Non-structural protein NSs

Gene

NSS

Organism
Rift valley fever virus (strain ZH-548 M12) (RVFV)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Plays a role in the inhibiton of host innate immune response by promoting the degradation of host EIF2AK2/PKR. Cytoplasmic NSs interacts with host FBXW11 to degrade PKR whereas nuclear pool binds to host FBXO3 to target TFIIH subunit GTF2H1 for proteasomal degradation.4 Publications

GO - Biological processi

  • negative stranded viral RNA replication Source: CACAO
  • suppression by virus of host gene expression Source: CACAO
  • suppression by virus of host transcription Source: CACAO
  • suppression by virus of host transcription initiation from RNA polymerase II promoter Source: CACAO
  • suppression by virus of host type I interferon production Source: CACAO
Complete GO annotation...

Keywords - Biological processi

Eukaryotic host gene expression shutoff by virus, Eukaryotic host transcription shutoff by virus, Host gene expression shutoff by virus, Host-virus interaction, Inhibition of eukaryotic host transcription initiation by virus, Inhibition of host innate immune response by virus, Inhibition of host interferon signaling pathway by virus, Inhibition of host PKR by virus, Viral immunoevasion

Names & Taxonomyi

Protein namesi
Recommended name:
Non-structural protein NSs
Gene namesi
Name:NSS
OrganismiRift valley fever virus (strain ZH-548 M12) (RVFV)
Taxonomic identifieri11589 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA negative-strand virusesBunyaviridaePhlebovirus
Virus hostiAedes [TaxID: 7158]
Bos taurus (Bovine) [TaxID: 9913]
Bos taurus x Bison bison (beefalo) [TaxID: 297284]
Camelus bactrianus (Bactrian camel) [TaxID: 9837]
Capra hircus (Goat) [TaxID: 9925]
Homo sapiens (Human) [TaxID: 9606]
Ovis aries (Sheep) [TaxID: 9940]
Phlebotomus papatasi (Sandfly) [TaxID: 29031]
Proteomesi
  • UP000002477 Componenti: Genome

Subcellular locationi

Keywords - Cellular componenti

Host cytoplasm, Host nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 265265Non-structural protein NSsPRO_0000221979Add
BLAST

Interactioni

Subunit structurei

Interacts with host FBXW11; this interaction is important for PKR degradation (PubMed:21543505). Interacts with host FBXO3; this interaction is important for GT2H1 degradation (PubMed:26837067).2 Publications

Protein-protein interaction databases

IntActiP21698. 26 interactions.

Structurei

Secondary structure

1
265
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi253 – 2564Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2N0YNMR-B247-265[»]
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the phlebovirus NS-S protein family.Curated

Family and domain databases

InterProiIPR024376. RVFV_non-structural.
[Graphical view]
PfamiPF11073. NSs. 1 hit.
[Graphical view]
PIRSFiPIRSF003956. NS-S_PhleboV. 1 hit.

Sequencei

Sequence statusi: Complete.

P21698-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDYFPVISVD LQSGRRVVSV EYFRGDGPPR IPYSMVGPCC VFLMHHRPSH
60 70 80 90 100
EVRLRFSDFY NVGEFPYRVG LGDFASNVAP PPAKPFQRLI DLIGHMTLSD
110 120 130 140 150
FTRFPNLKEA ISWPLGEPSL AFFDLSSTRV HRNDDIRRDQ IATLAMRSCK
160 170 180 190 200
ITNDLEDSFA GLHRMIATEA ILRGIDLCLL PGFDLMYEVA HVQCVRLLQA
210 220 230 240 250
AKEDISNAVV PNSALIVLME ESLMLRSSLP SMMGRNNWIP VIPPIPDVEM
260
ESEEESDDDG FVEVD
Length:265
Mass (Da):29,903
Last modified:May 1, 1991 - v1
Checksum:iEF2608D29CEB6C84
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X53771 Genomic RNA. Translation: CAA37788.1.
PIRiC38552. MNVURV.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X53771 Genomic RNA. Translation: CAA37788.1.
PIRiC38552. MNVURV.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2N0YNMR-B247-265[»]
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP21698. 26 interactions.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

InterProiIPR024376. RVFV_non-structural.
[Graphical view]
PfamiPF11073. NSs. 1 hit.
[Graphical view]
PIRSFiPIRSF003956. NS-S_PhleboV. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Sequences and coding strategies of the S RNAs of Toscana and Rift Valley fever viruses compared to those of Punta Toro, Sicilian Sandfly fever, and Uukuniemi viruses."
    Giorgi C., Accardi L., Nicoletti L., Gro M.C., Takehara K., Hilditch C., Morikawa S., Bishop D.H.L.
    Virology 180:738-753(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  2. "NSs protein of rift valley fever virus induces the specific degradation of the double-stranded RNA-dependent protein kinase."
    Habjan M., Pichlmair A., Elliott R.M., Overby A.K., Glatter T., Gstaiger M., Superti-Furga G., Unger H., Weber F.
    J. Virol. 83:4365-4375(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  3. "Rift Valley fever virus NSs protein promotes post-transcriptional downregulation of protein kinase PKR and inhibits eIF2alpha phosphorylation."
    Ikegami T., Narayanan K., Won S., Kamitani W., Peters C.J., Makino S.
    PLoS Pathog. 5:E1000287-E1000287(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  4. "NSs protein of rift valley fever virus promotes posttranslational downregulation of the TFIIH subunit p62."
    Kalveram B., Lihoradova O., Ikegami T.
    J. Virol. 85:6234-6243(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH HOST FBXO3.
  5. "Protein Kinase R degradation is essential for Rift valley fever Virus infection and is regulated by SKP1-CUL1-F-box (SCF)FBXW11-NSs E3 ligase."
    Mudhasani R., Tran J.P., Retterer C., Kota K.P., Whitehouse C.A., Bavari S.
    PLoS Pathog. 12:E1005437-E1005437(2016) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH HOST FBXW11.
  6. "A OmegaXaV motif in the Rift Valley fever virus NSs protein is essential for degrading p62, forming nuclear filaments and virulence."
    Cyr N., de la Fuente C., Lecoq L., Guendel I., Chabot P.R., Kehn-Hall K., Omichinski J.G.
    Proc. Natl. Acad. Sci. U.S.A. 112:6021-6026(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 247-265, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiNSS_RVFVZ
AccessioniPrimary (citable) accession number: P21698
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: May 1, 1991
Last modified: April 13, 2016
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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.