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P07939

- SIGM3_REOVL

UniProt

P07939 - SIGM3_REOVL

Protein

Outer capsid protein sigma-3

Gene

S4

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 86 (01 Oct 2014)
      Sequence version 1 (01 Aug 1988)
      Previous versions | rss
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    Functioni

    Stimulates translation by blocking the activation of the dsRNA-dependent protein kinase EIF2AK2/PKR, thereby inhibiting the host interferon response. Sigma3 prevents the activation of EIF2AK2 by competing with the kinase for dsRNA-binding By similarity.By similarity
    The viral outer shell polypeptides, of which sigma-3 is one, impose structural constraints that prevent elongation of nascent transcripts by the RNA-dependent RNA polymerase lambda-3.1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri51 – 7323CCHC-typeBy similarityAdd
    BLAST

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. RNA binding Source: UniProtKB-KW
    3. structural molecule activity Source: InterPro

    GO - Biological processi

    1. regulation of transcription, DNA-templated Source: UniProtKB-KW
    2. regulation of translation Source: UniProtKB-KW
    3. suppression by virus of host PKR activity Source: UniProtKB-KW
    4. suppression by virus of host type I interferon-mediated signaling pathway Source: UniProtKB-KW
    5. transcription, DNA-templated Source: UniProtKB-KW
    6. viral life cycle Source: InterPro

    Keywords - Biological processi

    Host-virus interaction, Inhibition of host innate immune response by virus, Inhibition of host interferon signaling pathway by virus, Inhibition of host PKR by virus, Interferon antiviral system evasion, Transcription, Transcription regulation, Translation regulation, Viral immunoevasion

    Keywords - Ligandi

    Metal-binding, RNA-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Outer capsid protein sigma-3
    Short name:
    Sigma3
    Gene namesi
    Name:S4
    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. Each subunit is positioned with the small lobe anchoring it to the protein mu1 on the surface of the virion, and the large lobe, the site of initial cleavages during entry-related proteolytic disassembly, protruding outwards By similarity.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 – 365365Outer capsid protein sigma-3PRO_0000222754Add
    BLAST

    Post-translational modificationi

    Cleaved during virus the endosomal proteolytic disassembly of the outer capsid.By similarity

    Interactioni

    Subunit structurei

    Heterohexamer of three sigma-3 and three Mu-1 proteins. The RNA-binding form is probably a homodimer By similarity.By similarity

    Protein-protein interaction databases

    IntActiP07939. 10 interactions.

    Structurei

    Secondary structure

    1
    365
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi8 – 1811
    Turni19 – 213
    Beta strandi25 – 273
    Turni28 – 303
    Beta strandi41 – 455
    Beta strandi48 – 514
    Turni52 – 543
    Beta strandi57 – 637
    Helixi79 – 813
    Helixi83 – 11028
    Helixi115 – 1239
    Beta strandi126 – 1305
    Helixi133 – 1353
    Turni141 – 1433
    Helixi159 – 17618
    Beta strandi180 – 1867
    Helixi189 – 1924
    Helixi199 – 2035
    Beta strandi221 – 2233
    Helixi226 – 2305
    Helixi232 – 2343
    Helixi236 – 2427
    Helixi246 – 2494
    Helixi252 – 2543
    Beta strandi259 – 2613
    Beta strandi270 – 2723
    Helixi275 – 2773
    Beta strandi282 – 2843
    Helixi288 – 2925
    Helixi293 – 2953
    Helixi296 – 30510
    Helixi308 – 3158
    Helixi319 – 33416
    Helixi338 – 3414
    Beta strandi351 – 3544
    Beta strandi356 – 3583
    Beta strandi362 – 3654

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1JMUX-ray2.80G/H/I1-365[»]
    2CSEelectron microscopy7.00D/E/F/G/H/I/M/N/O/S1-365[»]
    ProteinModelPortaliP07939.
    SMRiP07939. Positions 1-365.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP07939.

    Family & Domainsi

    Sequence similaritiesi

    Contains 1 CCHC-type zinc finger.Curated

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri51 – 7323CCHC-typeBy similarityAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Family and domain databases

    InterProiIPR000153. Reo_capsid_sigma3.
    IPR023634. Reovirus_capsid_sigma-3_dom.
    [Graphical view]
    PfamiPF00979. Reovirus_cap. 1 hit.
    [Graphical view]
    SUPFAMiSSF64465. SSF64465. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P07939-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEVCLPNGHQ IVDLINNAFE GRVSIYSAQE GWDKTISAQP DMMVCGGAVV    50
    CMHCLGVVGS LQRKLKHLPH HRCNQQIRHQ DYVDVQFADR VTAHWKRGML 100
    SFVAQMHAMM NDVSPEDLDR VRTEGGSLVE LNWLQVDPNS MFRSIHSSWT 150
    DPLQVVDDLD TKLDQYWTAL NLMIDSSDLV PNFMMRDPSH AFNGVRLEGD 200
    ARQTQFSRTF DSRSSLEWGV MVYDYSELEH DPSKGRAYRK ELVTPARDFG 250
    HFGLSHYSRA TTPILGKMPA VFSGMLTGNC KMYPFIKGTA KLKTVRKLVD 300
    SVNHAWGVEK IRYALGPGGM TGWYDRTMQQ APIVLTPAAL TMFSDTTKFG 350
    DLDYPVMIGD PMILG 365
    Length:365
    Mass (Da):41,156
    Last modified:August 1, 1988 - v1
    Checksum:i859808F2BF92B141
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti325 – 3251D → N in CAA43783. (PubMed:1736524)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M13139 Genomic RNA. Translation: AAA47272.1.
    X61586 Genomic RNA. Translation: CAA43783.1.
    PIRiA24245. MNXRS4.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M13139 Genomic RNA. Translation: AAA47272.1 .
    X61586 Genomic RNA. Translation: CAA43783.1 .
    PIRi A24245. MNXRS4.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1JMU X-ray 2.80 G/H/I 1-365 [» ]
    2CSE electron microscopy 7.00 D/E/F/G/H/I/M/N/O/S 1-365 [» ]
    ProteinModelPortali P07939.
    SMRi P07939. Positions 1-365.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P07939. 10 interactions.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P07939.

    Family and domain databases

    InterProi IPR000153. Reo_capsid_sigma3.
    IPR023634. Reovirus_capsid_sigma-3_dom.
    [Graphical view ]
    Pfami PF00979. Reovirus_cap. 1 hit.
    [Graphical view ]
    SUPFAMi SSF64465. SSF64465. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Biosynthesis of reovirus-specified polypeptides. Molecular cDNA cloning and nucleotide sequence of the reovirus serotype 1 Lang strain s4 mRNA which encodes the major capsid surface polypeptide sigma 3."
      Atwater J.A., Manemitsu S.M., Samuel C.E.
      Biochem. Biophys. Res. Commun. 136:183-192(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    2. "Translational effects and sequence comparisons of the three serotypes of the reovirus S4 gene."
      Seliger L.S., Giantini M., Shatkin A.J.
      Virology 187:202-210(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    3. "Transcriptional activities of reovirus RNA polymerase in recoated cores. Initiation and elongation are regulated by separate mechanisms."
      Farsetta D.L., Chandran K., Nibert M.L.
      J. Biol. Chem. 275:39693-39701(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    4. "Structure of the reovirus membrane-penetration protein, Mu1, in a complex with is protector protein, Sigma3."
      Liemann S., Chandran K., Baker T.S., Nibert M.L., Harrison S.C.
      Cell 108:283-295(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH MU-1.
    5. "Features of reovirus outer capsid protein mu1 revealed by electron cryomicroscopy and image reconstruction of the virion at 7.0 Angstrom resolution."
      Zhang X., Ji Y., Zhang L., Harrison S.C., Marinescu D.C., Nibert M.L., Baker T.S.
      Structure 13:1545-1557(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY ELECTRON MICROSCOPY (7.0 ANGSTROMS).

    Entry informationi

    Entry nameiSIGM3_REOVL
    AccessioniPrimary (citable) accession number: P07939
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: August 1, 1988
    Last modified: October 1, 2014
    This is version 86 of the entry and version 1 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