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Protein

Non-structural protein 3

Gene
N/A
Organism
Rotavirus A (strain SA11-Both G3-P5B[2]-I2-R2-C5-M5-A5-N2-T5-E2-H5) (RV-A) (Simian Agent 11 (strain Both))
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Involved in translation of viral mRNAs and shutoff of host protein synthesis. It is unclear whether it is required for the translation of viral mRNAs as well. Functions similarly to, and competes with the cellular poly(A)-binding protein PABPC1. Binds the conserved sequence 'GACC' at the 3' end of viral mRNAs and allows circularization of viral mRNAs in translation. Interacts with ZC3H7B/RoXaN and with the eukaryotic translation initiation factor eIF4G, using the same region employed by PABP-C1. NSP3 thus displaces PABPC1 from eIF4G, inhibiting the translation of cellular poly(A) mRNAs. Also responsible for the nuclear relocalization of PABPC1 upon rotavirus infection (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Eukaryotic host gene expression shutoff by virus, Eukaryotic host translation shutoff by virus, Host gene expression shutoff by virus, Host-virus interaction, Translation regulation

Keywords - Ligandi

RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Non-structural protein 3
Short name:
NSP3
Alternative name(s):
NCVP4
Non-structural RNA-binding protein 34
Short name:
NS34
OrganismiRotavirus A (strain SA11-Both G3-P5B[2]-I2-R2-C5-M5-A5-N2-T5-E2-H5) (RV-A) (Simian Agent 11 (strain Both))
Taxonomic identifieri37137 [NCBI]
Taxonomic lineageiVirusesdsRNA virusesReoviridaeSedoreovirinaeRotavirusRotavirus A
Virus hostiMacaca mulatta (Rhesus macaque) [TaxID: 9544]
ProteomesiUP000007180 Componenti: Genome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 315315Non-structural protein 3PRO_0000149541Add
BLAST

Interactioni

Subunit structurei

Homodimer. Interacts (via the coiled-coil region) with host ZC3H7B (via LD motif). Interacts with host EIF4G1 (By similarity).By similarity

Protein-protein interaction databases

IntActiP03536. 1 interaction.

Structurei

Secondary structure

1
315
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi8 – 3225Combined sources
Helixi39 – 5618Combined sources
Helixi61 – 7414Combined sources
Helixi79 – 8911Combined sources
Helixi93 – 10715Combined sources
Helixi114 – 12310Combined sources
Beta strandi125 – 1273Combined sources
Beta strandi136 – 1383Combined sources
Helixi141 – 1477Combined sources
Beta strandi152 – 1554Combined sources
Helixi156 – 1616Combined sources
Helixi209 – 2113Combined sources
Helixi212 – 25039Combined sources
Helixi256 – 26611Combined sources
Helixi274 – 30330Combined sources
Turni304 – 3074Combined sources
Beta strandi309 – 3113Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KNZX-ray2.45A/B/C/D/I/J/M/N4-164[»]
1LJ2X-ray2.38A/B206-315[»]
ProteinModelPortaliP03536.
SMRiP03536. Positions 7-163, 206-315.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP03536.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni4 – 149146RNA-bindingAdd
BLAST
Regioni150 – 20657DimerizationAdd
BLAST
Regioni170 – 23465Interaction with ZC3H7BBy similarityAdd
BLAST
Regioni208 – 315108Interaction with EIF4G1Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili166 – 23772Sequence AnalysisAdd
BLAST

Sequence similaritiesi

Belongs to the rotavirus A NSP3 family.Curated

Keywords - Domaini

Coiled coil

Family and domain databases

InterProiIPR002873. Rotavirus_NSP3.
[Graphical view]
PfamiPF01665. Rota_NSP3. 1 hit.
[Graphical view]
SUPFAMiSSF69903. SSF69903. 1 hit.

Sequencei

Sequence statusi: Complete.

P03536-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLKMESTQQM AVSIINSSFE AAVVAATSAL ENMGIEYDYQ DIYSRVKNKF
60 70 80 90 100
DFVMDDSGVK NNPIGKAITI DQALNNKFGS AIRNRNWLAD TSRPAKLDED
110 120 130 140 150
VNKLRMMLSS KGIDQKMRVL NACFSVKRIP GKSSSIIKCT KLMRDKLERG
160 170 180 190 200
EVEVDDSFVD EKMEVDTIDW KSRYEQLEQR FESLKSRVNE KYNNWVLKAR
210 220 230 240 250
KMNENMHSLQ NVIPQQQAHI AELQVYNNKL ERDLQNKIGS LTSSIEWYLR
260 270 280 290 300
SMELDPEIKA DIEQQINSID AINPLHAFDD LESVIRNLIS DYDKLFLMFK
310
GLIQRCNYQY SFGCE
Length:315
Mass (Da):36,445
Last modified:July 21, 1986 - v1
Checksum:i06BE050DDE9218E9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X00355 Genomic RNA. Translation: CAA25102.1.
PIRiA04142. MNXR4S.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X00355 Genomic RNA. Translation: CAA25102.1.
PIRiA04142. MNXR4S.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KNZX-ray2.45A/B/C/D/I/J/M/N4-164[»]
1LJ2X-ray2.38A/B206-315[»]
ProteinModelPortaliP03536.
SMRiP03536. Positions 7-163, 206-315.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP03536. 1 interaction.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP03536.

Family and domain databases

InterProiIPR002873. Rotavirus_NSP3.
[Graphical view]
PfamiPF01665. Rota_NSP3. 1 hit.
[Graphical view]
SUPFAMiSSF69903. SSF69903. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Nucleotide sequence of the dsRNA genomic segment 7 of Simian 11 rotavirus."
    Both G.W., Bellamy A.R., Siegman L.J.
    Nucleic Acids Res. 12:1621-1626(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  2. "Recognition of the rotavirus mRNA 3' consensus by an asymmetric NSP3 homodimer."
    Deo R.C., Groft C.M., Rajashankar K.R., Burley S.K.
    Cell 108:71-81(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 4-164, RNA-BINDING.
  3. "Recognition of eIF4G by rotavirus NSP3 reveals a basis for mRNA circularization."
    Groft C.M., Burley S.K.
    Mol. Cell 9:1273-1283(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.38 ANGSTROMS) OF 206-315.

Entry informationi

Entry nameiNSP3_ROTS1
AccessioniPrimary (citable) accession number: P03536
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: January 7, 2015
This is version 81 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

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.