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P03528

- SIGM1_REOVD

UniProt

P03528 - SIGM1_REOVD

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
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    • History
      Entry version 91 (01 Oct 2014)
      Sequence version 3 (22 Jul 2008)
      Previous versions | rss
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    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

    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

    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 – 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.
    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

    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

    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:
    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: October 1, 2014
    This is version 91 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