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P03528 (SIGM1_REOVD) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 90. 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·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Outer capsid protein sigma-1

Short name=Sigma1
Alternative name(s):
Cell attachment protein
Hemagglutinin
Gene names
Name:S1
OrganismReovirus type 3 (strain Dearing) (T3D) (Mammalian orthoreovirus 3) [Complete proteome]
Taxonomic identifier10886 [NCBI]
Taxonomic lineageVirusesdsRNA virusesReoviridaeSpinareovirinaeOrthoreovirus
Virus hostMammalia [TaxID: 40674]

Protein attributes

Sequence length455 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Fiber-like molecule that attaches the virion to the host cell membrane by binding to the primary receptor F11R/JAM-A and to sialic acid containing proteins (coreceptor). The interaction of sigma-1 with F11R is required for NF-kB activation and apoptosis. Binding to both sialic acid and F11R is required to induce maximal levels of apoptosis.

Subunit structure

Homotrimer. Interacts (via the head region) with human F11R. Ref.6

Subcellular location

Virion. Note: Found in the outer capsid (36 copies).

Post-translational modification

Undergoes dramatic conformational rearrangements during viral disassembly in the endocytic pathway.

Sequence similarities

Belongs to the orthoreovirus sigma-1 protein family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 455455Outer capsid protein sigma-1
PRO_0000040665

Regions

Region1 – 307307Tail
Region308 – 455148Head
Coiled coil116 – 14833 Potential

Amino acid modifications

Glycosylation2311N-linked (GlcNAc...); by host Potential
Glycosylation2641N-linked (GlcNAc...); by host Potential
Glycosylation2821N-linked (GlcNAc...); by host Potential

Experimental info

Sequence conflict221A → V in ABP48919. Ref.5
Sequence conflict118 – 1192EL → DV in CAA25605. Ref.3
Sequence conflict118 – 1192EL → DV in AAA47274. Ref.4
Sequence conflict1631S → T in AAA47275. Ref.2
Sequence conflict4081A → T in ABP48919. Ref.5

Secondary structure

.............................................................. 455
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P03528 [UniParc].

Last modified July 22, 2008. Version 3.
Checksum: F376721B9F936A34

FASTA45549,095
        10         20         30         40         50         60 
MDPRLREEVV RLIIALTSDN GASLSKGLES RVSALEKTSQ IHSDTILRIT QGLDDANKRI 

        70         80         90        100        110        120 
IALEQSRDDL VASVSDAQLA ISRLESSIGA LQTVVNGLDS SVTQLGARVG QLETGLAELR 

       130        140        150        160        170        180 
VDHDNLVARV DTAERNIGSL TTELSTLTLR VTSIQADFES RISTLERTAV TSAGAPLSIR 

       190        200        210        220        230        240 
NNRMTMGLND GLTLSGNNLA IRLPGNTGLN IQNGGLQFRF NTDQFQIVNN NLTLKTTVFD 

       250        260        270        280        290        300 
SINSRIGATE QSYVASAVTP LRLNSSTKVL DMLIDSSTLE INSSGQLTVR STSPNLRYPI 

       310        320        330        340        350        360 
ADVSGGIGMS PNYRFRQSMW IGIVSYSGSG LNWRVQVNSD IFIVDDYIHI CLPAFDGFSI 

       370        380        390        400        410        420 
ADGGDLSLNF VTGLLPPLLT GDTEPAFHND VVTYGAQTVA IGLSSGGAPQ YMSKNLWVEQ 

       430        440        450 
WQDGVLRLRV EGGGSITHSN SKWPAMTVSY PRSFT 

« Hide

References

[1]"Molecular cloning and sequencing of the reovirus (serotype 3) S1 gene which encodes the viral cell attachment protein sigma 1."
Nagata L., Masri S.A., Mah D.C.W., Lee P.W.K.
Nucleic Acids Res. 12:8699-8710(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[2]"Sequences of the S1 genes of the three serotypes of reovirus."
Cashdollar L.W., Chmelo R.A., Wiener J.R., Joklik W.K.
Proc. Natl. Acad. Sci. U.S.A. 82:24-28(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Sequence of reovirus haemagglutinin predicts a coiled-coil structure."
Bassel-Duby R., Jayasuriya A.K., Chatterjee D., Sonenberg N., Maizel J.V. Jr., Fields B.N.
Nature 315:421-423(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[4]"Identification of conserved domains in the cell attachment proteins of the three serotypes of reovirus."
Duncan R., Horne D., Cashdollar L.W., Joklik W.K., Lee P.W.K.
Virology 174:399-409(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[5]"A plasmid-based reverse genetics system for animal double-stranded RNA viruses."
Kobayashi T., Antar A.A., Boehme K.W., Danthi P., Eby E.A., Guglielmi K.M., Holm G.H., Johnson E.M., Maginnis M.S., Naik S., Skelton W.B., Wetzel J.D., Wilson G.J., Chappell J.D., Dermody T.S.
Cell Host Microbe 1:147-157(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
Strain: Infectious clone.
[6]"Junction adhesion molecule is a receptor for reovirus."
Barton E.S., Forrest J.C., Connolly J.L., Chappell J.D., Liu Y., Schnell F.J., Nusrat A., Parkos C.A., Dermody T.S.
Cell 104:441-451(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HUMAN F11R.
[7]"Crystal structure of reovirus attachment protein sigma1 reveals evolutionary relationship to adenovirus fiber."
Chappell J.D., Prota A.E., Dermody T.S., Stehle T.
EMBO J. 21:1-11(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 246-455.
[8]"The reovirus sigma1 aspartic acid sandwich: a trimerization motif poised for conformational change."
Schelling P., Guglielmi K.M., Kirchner E., Paetzold B., Dermody T.S., Stehle T.
J. Biol. Chem. 282:11582-11589(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 292-455.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M10262 Genomic DNA. Translation: AAA47275.1.
X01161 Genomic RNA. Translation: CAA25605.1.
M32862 mRNA. Translation: AAA47274.1.
EF494441 Genomic RNA. Translation: ABP48919.1.
PIRS25234.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1KKEX-ray2.60A/B/C246-455[»]
2OJ5X-ray1.75A/B/C/D/E/F293-455[»]
2OJ6X-ray1.85A/B/C/D/E/F293-455[»]
3EOYX-ray3.40A/B/C/D/E/F293-455[»]
3S6XX-ray2.25A/B/C170-455[»]
3S6YX-ray2.79A/B/C170-455[»]
3S6ZX-ray2.28A/B/C170-455[»]
ProteinModelPortalP03528.
SMRP03528. Positions 250-455.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D2.10.25.20. 1 hit.
2.60.90.20. 1 hit.
InterProIPR008982. Adenovirus_pIV-rel_att.
IPR009013. Attachment_protein_shaft_dom.
IPR027314. Sigma1_globular_dom.
IPR002592. Vir_attach_sigma1_reovir.
[Graphical view]
PfamPF01664. Reo_sigma1. 1 hit.
[Graphical view]
SUPFAMSSF49835. SSF49835. 1 hit.
SSF51225. SSF51225. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP03528.

Entry information

Entry nameSIGM1_REOVD
AccessionPrimary (citable) accession number: P03528
Secondary accession number(s): A4ZY26, Q85668
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 22, 2008
Last modified: July 9, 2014
This is version 90 of the entry and version 3 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