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P04506

- SIGM1_REOVL

UniProt

P04506 - SIGM1_REOVL

Protein

Outer capsid protein sigma-1

Gene

S1

Organism
Reovirus type 1 (strain Lang) (T1L) (Mammalian orthoreovirus 1)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 89 (01 Oct 2014)
      Sequence version 2 (01 Nov 1990)
      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 By similarity.By similarity

    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 1 (strain Lang) (T1L) (Mammalian orthoreovirus 1)
    Taxonomic identifieri10884 [NCBI]
    Taxonomic lineageiVirusesdsRNA virusesReoviridaeSpinareovirinaeOrthoreovirus
    Virus hostiMammalia [TaxID: 40674]
    ProteomesiUP000007253: Genome

    Subcellular locationi

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

    GO - Cellular componenti

    1. viral capsid Source: CACAO
    2. 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 – 470470Outer capsid protein sigma-1PRO_0000040667Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi21 – 211N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi121 – 1211N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi205 – 2051N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi353 – 3531N-linked (GlcNAc...); by hostSequence Analysis

    Post-translational modificationi

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

    Keywords - PTMi

    Glycoprotein

    Interactioni

    Subunit structurei

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

    Structurei

    Secondary structure

    1
    470
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi274 – 2785
    Beta strandi281 – 2855
    Turni290 – 2923
    Beta strandi293 – 2964
    Beta strandi299 – 3046
    Beta strandi315 – 3184
    Turni319 – 3224
    Beta strandi323 – 3264
    Helixi328 – 3314
    Beta strandi333 – 34513
    Beta strandi348 – 36114
    Beta strandi364 – 3696
    Beta strandi372 – 3754
    Beta strandi379 – 3868
    Helixi397 – 4004
    Beta strandi409 – 41911
    Beta strandi421 – 43717
    Beta strandi440 – 4478
    Beta strandi454 – 4585
    Beta strandi461 – 4666

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4GU3X-ray3.60A/B/C261-470[»]
    4GU4X-ray3.50A/B/C261-470[»]
    ProteinModelPortaliP04506.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 324324TailAdd
    BLAST
    Regioni325 – 470146HeadAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili26 – 4621Sequence 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.

    Sequencei

    Sequence statusi: Complete.

    P04506-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDASLITEIR KIVLQLSVSS NGSQSKEIEE IKKQVQVNVD DIRAANIKLD    50
    GLGRQIADIS NSISTIESRL GEMDNRLVGI SSQVTQLSNS VSQNTQSISS 100
    LGDRINAVEP RVDSLDTVTS NLTGRTSTLE ADVGSLRTEL AALTTRVTTE 150
    VTRLDGLINS GQNSIGELST RLSNVETSMV TTAGRGLQKN GNTLNVIVGN 200
    GMWFNSSNQL QLDLSGQSKG VGFVGTGMVV KIDTNYFAYN SNGEITLVSQ 250
    INELPSRVST LESAKIDSVL PPLTVREASG VRTLSFGYDT SDFTIINSVL 300
    SLRSRLTLPT YRYPLELDTA NNRVQVADRF GMRTGTWTGQ LQYQHPQLSW 350
    RANVTLNLMK VDDWLVLSFS QMTTNSIMAD GKFVINFVSG LSSGWQTGDT 400
    EPSSTIDPLS TTFAAVQFLN NGQRIDAFRI MGVSEWTDGE LEIKNYGGTY 450
    TGHTQVYWAP WTIMYPCNVR 470
    Length:470
    Mass (Da):51,404
    Last modified:November 1, 1990 - v2
    Checksum:iF4D18989AD54491C
    GO

    Sequence cautioni

    The sequence AAA47276.1 differs from that shown. Reason: Frameshift at position 410.
    The sequence AAA66877.1 differs from that shown. Reason: Frameshift at positions 410 and 434.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti91 – 911V → G in AAA66877. (PubMed:3855545)Curated
    Sequence conflicti91 – 911V → G in AAA47276. (PubMed:2430568)Curated
    Sequence conflicti169 – 1691S → F in AAA66877. (PubMed:3855545)Curated
    Sequence conflicti384 – 3841V → L in AAA47276. (PubMed:2430568)Curated
    Sequence conflicti409 – 4091L → W in AAA47242. (PubMed:2335823)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M10260 Genomic RNA. Translation: AAA66877.1. Frameshift.
    M14779 Genomic RNA. Translation: AAA47276.1. Frameshift.
    M32860 Genomic RNA. Translation: AAA47267.1.
    M35963 Genomic RNA. Translation: AAA47242.1.
    EF494445 Genomic RNA. Translation: ABP48923.1.
    AH002406 Genomic RNA. Translation: AAA47240.1.
    PIRiA04122. HMXRH1.
    A34829. HMXRL1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M10260 Genomic RNA. Translation: AAA66877.1 . Frameshift.
    M14779 Genomic RNA. Translation: AAA47276.1 . Frameshift.
    M32860 Genomic RNA. Translation: AAA47267.1 .
    M35963 Genomic RNA. Translation: AAA47242.1 .
    EF494445 Genomic RNA. Translation: ABP48923.1 .
    AH002406 Genomic RNA. Translation: AAA47240.1 .
    PIRi A04122. HMXRH1.
    A34829. HMXRL1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4GU3 X-ray 3.60 A/B/C 261-470 [» ]
    4GU4 X-ray 3.50 A/B/C 261-470 [» ]
    ProteinModelPortali P04506.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    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.
    ProtoNeti Search...

    Publicationsi

    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. "Biosynthesis of reovirus-specified polypeptides. Molecular cDNA cloning and nucleotide sequence of the reovirus serotype 1 Lang strain bicistronic s1 mRNA which encodes the minor capsid polypeptide sigma 1a and the nonstructural polypeptide sigma 1bNS."
      Munemitsu S.M., Atwater J.A., Samuel C.E.
      Biochem. Biophys. Res. Commun. 140:508-514(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    3. "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].
    4. "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].
    5. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
      Strain: Infectious clone.
    6. "Nature of the 3'-terminal sequences of the plus and minus strands of the S1 gene of reovirus serotypes 1, 2 and 3."
      Li J.K.-K., Keene J.D., Scheible P.P., Joklik W.K.
      Virology 105:41-51(1980) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-21.

    Entry informationi

    Entry nameiSIGM1_REOVL
    AccessioniPrimary (citable) accession number: P04506
    Secondary accession number(s): A4ZY30, P07937
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 13, 1987
    Last sequence update: November 1, 1990
    Last modified: October 1, 2014
    This is version 89 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programViral Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference 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