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P04507 (SIGM1_REOVJ) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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 2 (strain D5/Jones) (T2J) (Mammalian orthoreovirus 2) [Complete proteome]
Taxonomic identifier10885 [NCBI]
Taxonomic lineageVirusesdsRNA virusesReoviridaeSpinareovirinaeOrthoreovirus
Virus hostMammalia [TaxID: 40674]

Protein attributes

Sequence length462 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 By similarity.

Subunit structure

Homotrimer. Interacts (via the head region) with human F11R By similarity.

Subcellular location

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

Post-translational modification

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

Sequence similarities

Belongs to the orthoreovirus sigma-1 protein family.

Sequence caution

The sequence AAA66879.1 differs from that shown. Reason: Frameshift at positions 370 and 415.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 462462Outer capsid protein sigma-1
PRO_0000040666

Regions

Region1 – 317317Tail
Region318 – 462145Head
Coiled coil18 – 4932 Potential

Amino acid modifications

Glycosylation2371N-linked (GlcNAc...); by host Potential
Glycosylation2431N-linked (GlcNAc...); by host Potential
Glycosylation2971N-linked (GlcNAc...); by host Potential
Glycosylation4131N-linked (GlcNAc...); by host Potential

Experimental info

Sequence conflict1471V → L in AAA47268. Ref.2
Sequence conflict2071L → V in AAA47251. Ref.3
Sequence conflict4391H → Y in AAA47251. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P04507 [UniParc].

Last modified July 22, 2008. Version 3.
Checksum: 87383752835EEA8F

FASTA46250,466
        10         20         30         40         50         60 
MSDLVQLIRR EILLLTGNGE SANSKHEIEE IKKQIKDISA DVNRISNIVD SIQGQLGGLS 

        70         80         90        100        110        120 
VRVSAIESGV SENGNRIDRL ERDVSGISAS VSGIDSRLSE LGDRVNVAEQ RIGQLDTVTD 

       130        140        150        160        170        180 
NLLERASRLE TEVSAITNDL GSLNTRVTTE LNDVRQTIAA IDTRLTTLET DAVTSVGQGL 

       190        200        210        220        230        240 
QKTGNSIKVI VGTGMWFDRN NVLQLFLSNQ QKGLGFIDNG MVVKIDTQYF SFDSNGNITL 

       250        260        270        280        290        300 
NNNISGLPAR TGSLEASRID VVAPPLVIQS TGSTRLLRLM YEAVDFVVTN NVLTLRNRSV 

       310        320        330        340        350        360 
TPTFKFPLEL NSADNSVSIH RNYRIRLGQW SGQLEYHTPS LRWNAPVTVN LMRVDDWLIL 

       370        380        390        400        410        420 
SFTRFSTSGI LASGKFVLNF VTGLSPGWAT GSTEPSTTTN PLSTTFAAIQ FINGSSRVDA 

       430        440        450        460 
FRILGVAEWN AGELEITNHG GTYTAHTNVD WAPMTIMYPC LG 

« Hide

References

[1]"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 RNA].
[2]"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 [GENOMIC RNA].
[3]"Structure of the reovirus cell-attachment protein: a model for the domain organization of sigma 1."
Nibert M.L., Dermody T.S., Fields B.N.
J. Virol. 64:2976-2989(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M10261 Genomic RNA. Translation: AAA66879.1. Frameshift.
M32861 Genomic RNA. Translation: AAA47268.1.
M35964 Genomic RNA. Translation: AAA47251.1.
PIRHMXRH2. A04123.
C34829.

3D structure databases

ProteinModelPortalP04507.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D2.60.90.20. 1 hit.
InterProIPR008982. Adenovirus_pIV-rel_att.
IPR027314. Sigma1_globular_dom.
IPR002592. Vir_attach_sigma1_reovir.
[Graphical view]
PfamPF01664. Reo_sigma1. 1 hit.
[Graphical view]
SUPFAMSSF49835. SSF49835. 1 hit.
ProtoNetSearch...

Entry information

Entry nameSIGM1_REOVJ
AccessionPrimary (citable) accession number: P04507
Secondary accession number(s): Q85663
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: July 22, 2008
Last modified: February 19, 2014
This is version 84 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