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Reviewed, UniProtKB/Swiss-Prot P03528 (SIGM1_REOVD)

Last modified December 15, 2009. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Outer capsid protein sigma-1
      Short name=Sigma1
Alternative name(s):
    Hemagglutinin
    Cell attachment protein
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.

Ontologies

Keywords
   Biological processHost-virus interaction
   Cellular componentCapsid protein
Virion
   DomainCoiled coil
   Molecular functionHemagglutinin
   PTMGlycoprotein
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological processcell adhesion

Inferred from electronic annotation. Source: InterPro

cell recognition

Inferred from electronic annotation. Source: InterPro

interspecies interaction between organisms

Inferred from electronic annotation. Source: UniProtKB-KW

viral infectious cycle

Inferred from electronic annotation. Source: InterPro

   Cellular componentviral capsid

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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
P03528-1 [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: 6095208] [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: 3855545] [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: 4000269] [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: 2305549] [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: 18005692] [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: 11239401] [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: 11782420] [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: 17303562] [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[»]
ModBaseSearch...

Family and domain databases

InterProIPR002592. Vir_attach_sigma1_reovir.
IPR008982. Viral_att.
IPR009013. Viral_attachment_fibre_shaft.
[Graphical view]
PfamPF01664. Reo_sigma1. 1 hit.
[Graphical view]
ProtoNetSearch...

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: December 15, 2009
This is version 71 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectVirus (Virus annotation project)

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents