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P11314 (SIGM2_REOVL) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Inner capsid protein sigma-2

Short name=Sigma2
Gene names
Name:S2
OrganismReovirus type 1 (strain Lang) (T1L) (Mammalian orthoreovirus 1) [Reference proteome]
Taxonomic identifier10884 [NCBI]
Taxonomic lineageVirusesdsRNA virusesReoviridaeSpinareovirinaeOrthoreovirus
Virus hostMammalia [TaxID: 40674]

Protein attributes

Sequence length418 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Inner capsid (core) component.

Subunit structure

Interacts with protein mu-NS; in viral inclusions. Ref.3

Subcellular location

Virion Potential. Note: Found in the inner capsid (150 copies).

Sequence similarities

Belongs to the orthoreovirus sigma-1 protein family.

Sequence caution

The sequence AAA47278.1 differs from that shown. Reason: Frameshift at position 323.

Ontologies

Keywords
   Cellular componentCapsid protein
Inner capsid protein
Virion
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentviral inner capsid

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 418418Inner capsid protein sigma-2
PRO_0000222751

Experimental info

Sequence conflict891I → V in AAA47278. Ref.2
Sequence conflict2051H → Y in AAA47278. Ref.2

Secondary structure

....................................................... 418
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P11314 [UniParc].

Last modified October 1, 1993. Version 2.
Checksum: 4B30CF9217BA1DDB

FASTA41847,110
        10         20         30         40         50         60 
MARAAFLFKT VGFGGLQNVP INDELSSHLL RAGNSPWQLT QFLDWISLGR GLATSALVPT 

        70         80         90        100        110        120 
AGSRYYQMSC LLSGTLQIPF RPNHRWGDIR FLRLVWSAPT LDGLVVAPPQ VLAQPALQAQ 

       130        140        150        160        170        180 
ADRVYDCDDY PFLARDPRFK HRVYQQLSAV TLLNLTGFGP ISYVRVDEDM WSGDVNQLLM 

       190        200        210        220        230        240 
NYFGHTFAEI AYTLCQASAN RPWEHDGTYA RMTQIILSLF WLSYVGVIHQ QNTYRTFYFQ 

       250        260        270        280        290        300 
CNRRGDAAEV WILSCSLNHS AQIRPGNRSL FVMPTSPDWN MDVNLILSST LTGCLCSGSQ 

       310        320        330        340        350        360 
LPLIDNNSVP AVSRNIHGWT GRAGNQLHGF QVRRMVTEFC DRLRRDGVMT QAQQNQIEAL 

       370        380        390        400        410 
ADQTQQFKRD KLEAWAREDD QYNQANPNST MFRTKPFTNA QWGRGNTGAT SAAIAALI 

« Hide

References

[1]"The S2 gene nucleotide sequences of prototype strains of the three reovirus serotypes: characterization of reovirus core protein sigma 2."
Dermody T.S., Schiff L.A., Nibert M.L., Coombs K.M., Fields B.N.
J. Virol. 65:5721-5731(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[2]"Biosynthesis of reovirus-specified polypeptides. Molecular cDNA cloning and nucleotide sequence of the reovirus serotype 1 Lang strain s2 mRNA which encodes the virion core polypeptide sigma 2."
George C.X., Crowe A., Munemitsu S.M., Atwater J.A., Samuel C.E.
Biochem. Biophys. Res. Commun. 147:1153-1161(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Reovirus nonstructural protein mu NS recruits viral core surface proteins and entering core particles to factory-like inclusions."
Broering T.J., Kim J., Miller C.L., Piggott C.D., Dinoso J.B., Nibert M.L., Parker J.S.L.
J. Virol. 78:1882-1892(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PROTEIN MU-NS.
[4]"Features of reovirus outer capsid protein mu1 revealed by electron cryomicroscopy and image reconstruction of the virion at 7.0 Angstrom resolution."
Zhang X., Ji Y., Zhang L., Harrison S.C., Marinescu D.C., Nibert M.L., Baker T.S.
Structure 13:1545-1557(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY ELECTRON MICROSCOPY (7.0 ANGSTROMS).
[5]"Structure of the reovirus core at 3.6 A resolution."
Reinisch K.M., Nibert M.L., Harrison S.C.
Nature 404:960-967(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.6 ANGSTROMS).
Strain: Reassortant F18.

Web resources

Virus Particle ExploreR db

Icosahedral capsid structure

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L19774 Genomic RNA. Translation: AAA47239.1.
M17598 mRNA. Translation: AAA47278.1. Frameshift.
PIRFOXRL2. A41306.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1EJ6X-ray3.60D/E1-418[»]
2CSEelectron microscopy7.00X/Y/Z1-418[»]
ProteinModelPortalP11314.
SMRP11314. Positions 2-418.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR004317. Sigma_1_2_reovir.
[Graphical view]
PfamPF03084. Sigma_1_2. 1 hit.
[Graphical view]
ProDomPD004419. Sigma_1_2_reovir. 1 hit.
[Graphical view] [Entries sharing at least one domain]
ProtoNetSearch...

Other

EvolutionaryTraceP11314.

Entry information

Entry nameSIGM2_REOVL
AccessionPrimary (citable) accession number: P11314
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: October 1, 1993
Last modified: October 16, 2013
This is version 74 of the entry and version 2 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references