P11314 (SIGM2_REOVL) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Inner capsid protein sigma-2
Short name=Sigma2

Gene names

Name:

S2

Organism

Reovirus type 1 (strain Lang) (T1L) (Mammalian orthoreovirus 1) [Reference proteome]

Taxonomic identifier

10884 [NCBI]

Taxonomic lineage

Viruses › dsRNA viruses › Reoviridae › Spinareovirinae › Orthoreovirus › Mammalian orthoreovirus › Mammalian orthoreovirus 1

Virus host

Mammalia [TaxID: 40674]

Protein attributes

Sequence length	418 AA.
Sequence status	Complete.
Protein existence	Evidence 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 component	Virion
Molecular function	Capsid protein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Cellular_component	viral capsid Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 418

418

Inner capsid protein sigma-2

PRO_0000222751

Experimental info

Sequence conflict

89

1

I → V in AAA47278. Ref.2

Sequence conflict

205

1

H → Y in AAA47278. Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

418

Helix Strand Turn

Details...

Beta strand

7 – 9

3

Helix

23 – 29

7

Helix

39 – 45

7

Helix

64 – 72

9

Turn

76 – 80

5

Helix

109 – 112

4

Beta strand

124 – 126

3

Helix

127 – 129

3

Helix

131 – 134

4

Helix

137 – 154

18

Beta strand

162 – 166

5

Helix

168 – 170

3

Helix

175 – 179

5

Helix

180 – 182

3

Helix

187 – 200

14

Helix

209 – 224

16

Beta strand

232 – 234

3

Beta strand

237 – 241

5

Beta strand

251 – 255

5

Beta strand

268 – 272

5

Helix

277 – 281

5

Helix

283 – 291

9

Helix

306 – 308

3

Helix

311 – 313

3

Helix

332 – 345

14

Helix

351 – 385

35

Helix

399 – 401

3

Helix

410 – 415

6

Sequences

	Sequence		Length	Mass (Da)
	P11314 [UniParc]. Last modified October 1, 1993. Version 2. Checksum: 4B30CF9217BA1DDB	FASTA	418	47,110
	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

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.

PIR

FOXRL2. A41306.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1EJ6	X-ray	3.60	D/E	1-418	[»]
2CSE	electron microscopy	7.00	X/Y/Z	1-418	[»]

ProteinModelPortal

P11314.

SMR

P11314. Positions 2-418.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

InterPro

IPR004317. Sigma_1_2_reovir.
[Graphical view]

Pfam

PF03084. Sigma_1_2. 1 hit.
[Graphical view]

ProDom

PD004419. Sigma_1_2_reovir. 1 hit.
[Graphical view] [Entries sharing at least one domain]

ProtoNet

Search...

Other

EvolutionaryTrace

P11314.

Entry information

Entry name

SIGM2_REOVL

Accession

Primary (citable) accession number: P11314

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	October 1, 1993
Last modified:	April 3, 2013
This is version 72 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program