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Protein

Outer capsid protein sigma-1

Gene

S1

Organism
Reovirus type 3 (strain Dearing) (T3D) (Mammalian orthoreovirus 3)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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.

GO - Biological processi

  1. cell adhesion Source: InterPro
  2. viral entry into host cell Source: UniProtKB-KW
  3. virion attachment to host cell Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hemagglutinin

Keywords - Biological processi

Host-virus interaction, Viral attachment to host cell, Virus entry into host cell

Names & Taxonomyi

Protein namesi
Recommended name:
Outer capsid protein sigma-1
Short name:
Sigma1
Alternative name(s):
Cell attachment protein
Hemagglutinin
Gene namesi
Name:S1
OrganismiReovirus type 3 (strain Dearing) (T3D) (Mammalian orthoreovirus 3)
Taxonomic identifieri10886 [NCBI]
Taxonomic lineageiVirusesdsRNA virusesReoviridaeSpinareovirinaeOrthoreovirus
Virus hostiMammalia [TaxID: 40674]
ProteomesiUP000006373 Componenti: Genome

Subcellular locationi

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

GO - Cellular componenti

  1. viral outer capsid Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Capsid protein, Outer capsid protein, Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 455455Outer capsid protein sigma-1PRO_0000040665Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi231 – 2311N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi264 – 2641N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi282 – 2821N-linked (GlcNAc...); by hostSequence Analysis

Post-translational modificationi

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

Keywords - PTMi

Glycoprotein

Interactioni

Subunit structurei

Homotrimer. Interacts (via the head region) with human F11R.1 Publication

Structurei

Secondary structure

1
455
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi177 – 1804Combined sources
Beta strandi183 – 1864Combined sources
Beta strandi192 – 1954Combined sources
Beta strandi198 – 2014Combined sources
Beta strandi207 – 2126Combined sources
Beta strandi215 – 2184Combined sources
Turni222 – 2243Combined sources
Beta strandi225 – 2284Combined sources
Beta strandi231 – 2344Combined sources
Helixi236 – 2394Combined sources
Helixi240 – 25011Combined sources
Beta strandi261 – 2644Combined sources
Turni265 – 2684Combined sources
Beta strandi269 – 2724Combined sources
Turni276 – 2783Combined sources
Beta strandi279 – 2813Combined sources
Beta strandi287 – 2893Combined sources
Beta strandi300 – 3034Combined sources
Beta strandi306 – 3094Combined sources
Helixi311 – 3144Combined sources
Beta strandi316 – 32813Combined sources
Beta strandi331 – 34414Combined sources
Beta strandi347 – 3526Combined sources
Beta strandi355 – 3584Combined sources
Beta strandi362 – 3698Combined sources
Beta strandi372 – 3743Combined sources
Helixi380 – 3834Combined sources
Turni386 – 3894Combined sources
Beta strandi394 – 40815Combined sources
Beta strandi410 – 42213Combined sources
Beta strandi425 – 4317Combined sources
Beta strandi439 – 4435Combined sources
Beta strandi446 – 4527Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
SMRiP03528. Positions 250-455.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP03528.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 307307TailAdd
BLAST
Regioni308 – 455148HeadAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili116 – 14833Sequence AnalysisAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Coiled coil

Family and domain databases

Gene3Di2.10.25.20. 1 hit.
2.60.90.20. 1 hit.
InterProiIPR008982. Adenovirus_pIV-rel_att.
IPR009013. Attachment_protein_shaft_dom.
IPR027314. Sigma1_globular_dom.
IPR002592. Vir_attach_sigma1_reovir.
[Graphical view]
PfamiPF01664. Reo_sigma1. 1 hit.
[Graphical view]
SUPFAMiSSF49835. SSF49835. 1 hit.
SSF51225. SSF51225. 1 hit.

Sequencei

Sequence statusi: Complete.

P03528-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDPRLREEVV RLIIALTSDN GASLSKGLES RVSALEKTSQ IHSDTILRIT
60 70 80 90 100
QGLDDANKRI IALEQSRDDL VASVSDAQLA ISRLESSIGA LQTVVNGLDS
110 120 130 140 150
SVTQLGARVG QLETGLAELR VDHDNLVARV DTAERNIGSL TTELSTLTLR
160 170 180 190 200
VTSIQADFES RISTLERTAV TSAGAPLSIR NNRMTMGLND GLTLSGNNLA
210 220 230 240 250
IRLPGNTGLN IQNGGLQFRF NTDQFQIVNN NLTLKTTVFD SINSRIGATE
260 270 280 290 300
QSYVASAVTP LRLNSSTKVL DMLIDSSTLE INSSGQLTVR STSPNLRYPI
310 320 330 340 350
ADVSGGIGMS PNYRFRQSMW IGIVSYSGSG LNWRVQVNSD IFIVDDYIHI
360 370 380 390 400
CLPAFDGFSI ADGGDLSLNF VTGLLPPLLT GDTEPAFHND VVTYGAQTVA
410 420 430 440 450
IGLSSGGAPQ YMSKNLWVEQ WQDGVLRLRV EGGGSITHSN SKWPAMTVSY

PRSFT
Length:455
Mass (Da):49,095
Last modified:July 22, 2008 - v3
Checksum:iF376721B9F936A34
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti22 – 221A → V in ABP48919 (PubMed:18005692).Curated
Sequence conflicti118 – 1192EL → DV in CAA25605 (PubMed:4000269).Curated
Sequence conflicti118 – 1192EL → DV in AAA47274 (PubMed:2305549).Curated
Sequence conflicti163 – 1631S → T in AAA47275 (PubMed:3855545).Curated
Sequence conflicti408 – 4081A → T in ABP48919 (PubMed:18005692).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M10262 Genomic DNA. Translation: AAA47275.1.
X01161 Genomic RNA. Translation: CAA25605.1.
M32862 mRNA. Translation: AAA47274.1.
EF494441 Genomic RNA. Translation: ABP48919.1.
PIRiS25234.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M10262 Genomic DNA. Translation: AAA47275.1.
X01161 Genomic RNA. Translation: CAA25605.1.
M32862 mRNA. Translation: AAA47274.1.
EF494441 Genomic RNA. Translation: ABP48919.1.
PIRiS25234.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
SMRiP03528. Positions 250-455.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP03528.

Family and domain databases

Gene3Di2.10.25.20. 1 hit.
2.60.90.20. 1 hit.
InterProiIPR008982. Adenovirus_pIV-rel_att.
IPR009013. Attachment_protein_shaft_dom.
IPR027314. Sigma1_globular_dom.
IPR002592. Vir_attach_sigma1_reovir.
[Graphical view]
PfamiPF01664. Reo_sigma1. 1 hit.
[Graphical view]
SUPFAMiSSF49835. SSF49835. 1 hit.
SSF51225. SSF51225. 1 hit.
ProtoNetiSearch...

Publicationsi

  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(1983) [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(1984) [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(1984) [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(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    Strain: Infectious clone.
  6. 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(2001) [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(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 292-455.

Entry informationi

Entry nameiSIGM1_REOVD
AccessioniPrimary (citable) accession number: P03528
Secondary accession number(s): A4ZY26, Q85668
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 22, 2008
Last modified: April 1, 2015
This is version 94 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.