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Q99FX5 (NSP1_ROTS4) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 46. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Non-structural protein 1

Short name=NSP1
Alternative name(s):
NCVP2
Non-structural RNA-binding protein 53
Short name=NS53
OrganismRotavirus A (strain SA11-4F G3-P6[1]-Ix-Rx-Cx-Mx-Ax-Nx-Tx-Ex-Hx) (RV-A) (Simian Agent 11 (strain 4F))
Taxonomic identifier36436 [NCBI]
Taxonomic lineageVirusesdsRNA virusesReoviridaeSedoreovirinaeRotavirusRotavirus A
Virus hostMacaca mulatta (Rhesus macaque) [TaxID: 9544]

Protein attributes

Sequence length496 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.3 Ref.4 Ref.5

Subunit structure

Interacts (via C-terminus) with host IRF3; this interaction leads to IRF3 degradation. Interacts with host IRF7; this interaction leads to IRF7 degradation. Ref.3 Ref.5

Subcellular location

Host cytoplasmhost cytoskeleton Ref.2.

Domain

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.

Sequence similarities

Belongs to the rotavirus A NSP1 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 496496Non-structural protein 1
PRO_0000367820

Regions

Zinc finger42 – 7938 Potential
Region1 – 8181RNA-binding
Region82 – 17796Important for cytoskeleton localization
Region317 – 496180Interaction with IRF3

Natural variations

Natural variant4791T → I in strain: Isolate 5S.
Natural variant480 – 49617Missing in strain: Isolate 5S.

Sequences

Sequence LengthMass (Da)Tools
Q99FX5 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 5877EA0A0C078CAD

FASTA49658,565
        10         20         30         40         50         60 
MATFKDACFH YRRLTALNRR LCNIGANSIC MPVPDAKIKG WCLECCQIAD LTHCYGCSLP 

        70         80         90        100        110        120 
HVCKWCVQNR RCFLDNEPHL LKLRTVKHPI TKDKLQCIID LYNIIFPIND KVIRKFERMI 

       130        140        150        160        170        180 
KQRKCRNQYK IEWYNHLLLP ITLNAAAFKF DENNLYYVFG LYEKSVSDIY APYRIVNFIN 

       190        200        210        220        230        240 
EFDKLLLDDI NFTRMSNLPI ELRNHYAKKY FQLSRLPSSK LKQIYFSDFT KETVIFNTYT 

       250        260        270        280        290        300 
KTPGRSIYRN VTEFNWRDEL ELYSDLKNDK NKLIAAMMTS KYTRFYAHDN NFGRLKMTIF 

       310        320        330        340        350        360 
ELGHHCQPNY VASNHPGNAS DIQYCKWCNI KYFLSKIDWR IRDMYNLLME FIKDCYKSNV 

       370        380        390        400        410        420 
NVGHCSSVEN IYPLIKRLIW SLFTNHMDQT IEEVFNHMSP VSVEGTNVIM LILGLNISLY 

       430        440        450        460        470        480 
NEIKRTLNVD SIPMVLNLNE FSSIVKSISS KWYNVDELDK LPMSIKSTEE LIEMKNSGTL 

       490 
TEEFELLISN SEDDNE 

« Hide

References

[1]"Effect of intragenic rearrangement and changes in the 3' consensus sequence on NSP1 expression and rotavirus replication."
Patton J.T., Taraporewala Z.F., Chen D., Chizhikov V., Jones M.T., Elhelu A., Collins M., Kearney K., Wagner M., Hoshino Y., Gouvea V.
J. Virol. 75:2076-2086(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[2]"Deletion mapping of the rotavirus metalloprotein NS53 (NSP1): the conserved cysteine-rich region is essential for virus-specific RNA binding."
Hua J.J., Chen X., Patton J.T.
J. Virol. 68:3990-4000(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: RNA-BINDING, SUBCELLULAR LOCATION.
[3]"Rotavirus nonstructural protein 1 subverts innate immune response by inducing degradation of IFN regulatory factor 3."
Barro M., Patton J.T.
Proc. Natl. Acad. Sci. U.S.A. 102:4114-4119(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH HUMAN IRF3.
[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: FUNCTION.
[5]"Rotavirus NSP1 inhibits expression of type I interferon by antagonizing the function of interferon regulatory factors IRF3, IRF5, and IRF7."
Barro M., Patton J.T.
J. Virol. 81:4473-4481(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH HUMAN IRF7.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF290883 Genomic RNA. Translation: AAK14071.1.
AF290884 Genomic RNA. Translation: AAK14072.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR002148. Rotavirus_NSP1.
[Graphical view]
PfamPF00981. Rota_NS53. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameNSP1_ROTS4
AccessionPrimary (citable) accession number: Q99FX5
Secondary accession number(s): Q99FX4
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: June 1, 2001
Last modified: June 11, 2014
This is version 46 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families