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P04507

- SIGM1_REOVJ

UniProt

P04507 - SIGM1_REOVJ

Protein

Outer capsid protein sigma-1

Gene

S1

Organism
Reovirus type 2 (strain D5/Jones) (T2J) (Mammalian orthoreovirus 2)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 85 (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 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 2 (strain D5/Jones) (T2J) (Mammalian orthoreovirus 2)
    Taxonomic identifieri10885 [NCBI]
    Taxonomic lineageiVirusesdsRNA virusesReoviridaeSpinareovirinaeOrthoreovirus
    Virus hostiMammalia [TaxID: 40674]
    ProteomesiUP000006370: Genome

    Subcellular locationi

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

    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 – 462462Outer capsid protein sigma-1PRO_0000040666Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi237 – 2371N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi243 – 2431N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi297 – 2971N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi413 – 4131N-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

    3D structure databases

    ProteinModelPortaliP04507.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 317317TailAdd
    BLAST
    Regioni318 – 462145HeadAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili18 – 4932Sequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Keywords - Domaini

    Coiled coil

    Family and domain databases

    Gene3Di2.60.90.20. 1 hit.
    InterProiIPR008982. Adenovirus_pIV-rel_att.
    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.

    P04507-1 [UniParc]FASTAAdd to Basket

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    MSDLVQLIRR EILLLTGNGE SANSKHEIEE IKKQIKDISA DVNRISNIVD    50
    SIQGQLGGLS VRVSAIESGV SENGNRIDRL ERDVSGISAS VSGIDSRLSE 100
    LGDRVNVAEQ RIGQLDTVTD NLLERASRLE TEVSAITNDL GSLNTRVTTE 150
    LNDVRQTIAA IDTRLTTLET DAVTSVGQGL QKTGNSIKVI VGTGMWFDRN 200
    NVLQLFLSNQ QKGLGFIDNG MVVKIDTQYF SFDSNGNITL NNNISGLPAR 250
    TGSLEASRID VVAPPLVIQS TGSTRLLRLM YEAVDFVVTN NVLTLRNRSV 300
    TPTFKFPLEL NSADNSVSIH RNYRIRLGQW SGQLEYHTPS LRWNAPVTVN 350
    LMRVDDWLIL SFTRFSTSGI LASGKFVLNF VTGLSPGWAT GSTEPSTTTN 400
    PLSTTFAAIQ FINGSSRVDA FRILGVAEWN AGELEITNHG GTYTAHTNVD 450
    WAPMTIMYPC LG 462
    Length:462
    Mass (Da):50,466
    Last modified:July 22, 2008 - v3
    Checksum:i87383752835EEA8F
    GO

    Sequence cautioni

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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti147 – 1471V → L in AAA47268. (PubMed:2305549)Curated
    Sequence conflicti207 – 2071L → V in AAA47251. (PubMed:2335823)Curated
    Sequence conflicti439 – 4391H → Y in AAA47251. (PubMed:2335823)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M10261 Genomic RNA. Translation: AAA66879.1. Frameshift.
    M32861 Genomic RNA. Translation: AAA47268.1.
    M35964 Genomic RNA. Translation: AAA47251.1.
    PIRiA04123. HMXRH2.
    C34829.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M10261 Genomic RNA. Translation: AAA66879.1 . Frameshift.
    M32861 Genomic RNA. Translation: AAA47268.1 .
    M35964 Genomic RNA. Translation: AAA47251.1 .
    PIRi A04123. HMXRH2.
    C34829.

    3D structure databases

    ProteinModelPortali P04507.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    Gene3Di 2.60.90.20. 1 hit.
    InterProi IPR008982. Adenovirus_pIV-rel_att.
    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. "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].

    Entry informationi

    Entry nameiSIGM1_REOVJ
    AccessioniPrimary (citable) accession number: P04507
    Secondary accession number(s): Q85663
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 13, 1987
    Last sequence update: July 22, 2008
    Last modified: October 1, 2014
    This is version 85 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

    Complete proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3