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P03528

- SIGM1_REOVD

UniProt

P03528 - SIGM1_REOVD

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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: 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: 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-1
PRO_0000040665Add
BLAST

Amino acid modifications

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

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

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortaliP03528.
SMRiP03528. Positions 250-455.

Miscellaneous databases

EvolutionaryTraceiP03528.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 307307Tail
Add
BLAST
Regioni308 – 455148Head
Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili116 – 14833 Reviewed prediction
Add
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

MDPRLREEVV RLIIALTSDN GASLSKGLES RVSALEKTSQ IHSDTILRIT    50
QGLDDANKRI IALEQSRDDL VASVSDAQLA ISRLESSIGA LQTVVNGLDS 100
SVTQLGARVG QLETGLAELR VDHDNLVARV DTAERNIGSL TTELSTLTLR 150
VTSIQADFES RISTLERTAV TSAGAPLSIR NNRMTMGLND GLTLSGNNLA 200
IRLPGNTGLN IQNGGLQFRF NTDQFQIVNN NLTLKTTVFD SINSRIGATE 250
QSYVASAVTP LRLNSSTKVL DMLIDSSTLE INSSGQLTVR STSPNLRYPI 300
ADVSGGIGMS PNYRFRQSMW IGIVSYSGSG LNWRVQVNSD IFIVDDYIHI 350
CLPAFDGFSI ADGGDLSLNF VTGLLPPLLT GDTEPAFHND VVTYGAQTVA 400
IGLSSGGAPQ YMSKNLWVEQ WQDGVLRLRV EGGGSITHSN SKWPAMTVSY 450
PRSFT 455
Length:455
Mass (Da):49,095
Last modified:July 22, 2008 - v3
Checksum:iF376721B9F936A34
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti22 – 221A → V in ABP48919. 1 Publication
Sequence conflicti118 – 1192EL → DV in CAA25605. 1 Publication
Sequence conflicti118 – 1192EL → DV in AAA47274. 1 Publication
Sequence conflicti163 – 1631S → T in AAA47275. 1 Publication
Sequence conflicti408 – 4081A → T in ABP48919. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
PIRi S25234.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1KKE X-ray 2.60 A/B/C 246-455 [» ]
2OJ5 X-ray 1.75 A/B/C/D/E/F 293-455 [» ]
2OJ6 X-ray 1.85 A/B/C/D/E/F 293-455 [» ]
3EOY X-ray 3.40 A/B/C/D/E/F 293-455 [» ]
3S6X X-ray 2.25 A/B/C 170-455 [» ]
3S6Y X-ray 2.79 A/B/C 170-455 [» ]
3S6Z X-ray 2.28 A/B/C 170-455 [» ]
ProteinModelPortali P03528.
SMRi P03528. Positions 250-455.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P03528.

Family and domain databases

Gene3Di 2.10.25.20. 1 hit.
2.60.90.20. 1 hit.
InterProi IPR008982. Adenovirus_pIV-rel_att.
IPR009013. Attachment_protein_shaft_dom.
IPR027314. Sigma1_globular_dom.
IPR002592. Vir_attach_sigma1_reovir.
[Graphical view ]
Pfami PF01664. Reo_sigma1. 1 hit.
[Graphical view ]
SUPFAMi SSF49835. SSF49835. 1 hit.
SSF51225. SSF51225. 1 hit.
ProtoNeti Search...

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(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. 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(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.

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: July 9, 2014
This is version 90 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

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