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Q66800

- VSGP_EBORR

UniProt

Q66800 - VSGP_EBORR

Protein

Pre-small/secreted glycoprotein

Gene

GP

Organism
Reston ebolavirus (strain Reston-89) (REBOV) (Reston Ebola virus)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 62 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    sGP seems to possess an anti-inflammatory activity as it can reverse the barrier-decreasing effects of TNF alpha. Might therefore contribute to the lack of inflammatory reaction seen during infection in spite the of extensive necrosis and massive virus production. Does not seem to be involved in activation of primary macrophages. Does not seem to interact specifically with neutrophils By similarity.By similarity
    Delta-peptide does not seem to be involved in activation of primary macrophages.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei325 – 3262Cleavage; by host furinBy similarity

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Pre-small/secreted glycoprotein
    Short name:
    pre-sGP
    Cleaved into the following 2 chains:
    Gene namesi
    Name:GP
    OrganismiReston ebolavirus (strain Reston-89) (REBOV) (Reston Ebola virus)
    Taxonomic identifieri386032 [NCBI]
    Taxonomic lineageiVirusesssRNA negative-strand virusesMononegaviralesFiloviridaeEbolavirus
    Virus hostiEpomops franqueti (Franquet's epauleted fruit bat) [TaxID: 77231]
    Homo sapiens (Human) [TaxID: 9606]
    Myonycteris torquata (Little collared fruit bat) [TaxID: 77243]
    Sus scrofa (Pig) [TaxID: 9823]
    ProteomesiUP000007207: Genome

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3333Sequence AnalysisAdd
    BLAST
    Chaini34 – 367334Pre-small/secreted glycoproteinBy similarityPRO_0000037497Add
    BLAST
    Chaini34 – 325292Small/secreted glycoproteinBy similarityPRO_0000037498Add
    BLAST
    Chaini326 – 36742Delta-peptideBy similarityPRO_0000037499Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi41 – 411N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi54 – 54InterchainBy similarity
    Disulfide bondi109 ↔ 136By similarity
    Disulfide bondi122 ↔ 148By similarity
    Glycosylationi205 – 2051N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi229 – 2291N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi239 – 2391N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi258 – 2581N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi269 – 2691N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi307 – 307InterchainBy similarity

    Post-translational modificationi

    Pre-sGP is N-glycosylated. This precursor is processed into mature sGP and delta-peptide by host furin or furin-like proteases. The cleavage site corresponds to the furin optimal cleavage sequence [KR]-X-[KR]-R. Both cleavage fragments contain sialic acid, but only the delta-peptide is O-glycosylated By similarity.By similarity

    Keywords - PTMi

    Cleavage on pair of basic residues, Disulfide bond, Glycoprotein

    Interactioni

    Subunit structurei

    sGP is a homodimer; disulfide-linked. The homodimers are linked by two disulfide bonds in a parallel orientation. Delta-peptide is a monomer By similarity.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliQ66800.
    SMRiQ66800. Positions 33-285.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the filoviruses glycoprotein family.Curated

    Keywords - Domaini

    Signal

    Family and domain databases

    InterProiIPR014625. GPC_FiloV.
    IPR002561. GPC_filovir-type_extra_dom.
    [Graphical view]
    PfamiPF01611. Filo_glycop. 1 hit.
    [Graphical view]
    PIRSFiPIRSF036874. GPC_FiloV. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q66800-1 [UniParc]FASTAAdd to Basket

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    MGSGYQLLQL PRERFRKTSF LVWVIILFQR AISMPLGIVT NSTLKATEID    50
    QLVCRDKLSS TSQLKSVGLN LEGNGIATDV PSATKRWGFR SGVPPKVVSY 100
    EAGEWAENCY NLEIKKSDGS ECLPLPPDGV RGFPRCRYVH KVQGTGPCPG 150
    DLAFHKNGAF FLYDRLASTV IYRGTTFAEG VVAFLILSEP KKHFWKATPA 200
    HEPVNTTDDS TSYYMTLTLS YEMSNFGGNE SNTLFKVDNH TYVQLDRPHT 250
    PQFLVQLNET LRRNNRLSNS TGRLTWTLDP KIEPDVGEWA FWETKKTFPN 300
    NFMEKTCISK FYQPTPTTPQ IRARRELSKE KLATTHPPTT PSWFQRIPLQ 350
    WFQCSLQDGQ RKCRPKV 367
    Length:367
    Mass (Da):41,771
    Last modified:November 1, 1996 - v1
    Checksum:iF3953243F5420C40
    GO

    RNA editingi

    Partially edited. RNA editing at this position consists of an insertion of one or two adenine nucleotides. The sequence displayed here is the full-length transmembrane glycoprotein GP, derived from the +1A edited RNA. The unedited RNA gives rise to the small secreted glycoprotein sGP (AC Q66799), the +2A edited RNA gives rise to the super small secreted glycoprotein ssGP (AC P0C771).

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti312 – 3121Y → H.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U23152 Genomic RNA. Translation: AAC54884.1.
    AF034645 Genomic RNA. Translation: AAC24345.1.
    AF522874 Genomic RNA. Translation: AAN04451.1.
    AY769362 Genomic RNA. Translation: AAV48578.1.
    RefSeqiNP_690584.1. NC_004161.1.

    Genome annotation databases

    GeneIDi955190.

    Keywords - Coding sequence diversityi

    RNA editing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U23152 Genomic RNA. Translation: AAC54884.1 .
    AF034645 Genomic RNA. Translation: AAC24345.1 .
    AF522874 Genomic RNA. Translation: AAN04451.1 .
    AY769362 Genomic RNA. Translation: AAV48578.1 .
    RefSeqi NP_690584.1. NC_004161.1.

    3D structure databases

    ProteinModelPortali Q66800.
    SMRi Q66800. Positions 33-285.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 955190.

    Family and domain databases

    InterProi IPR014625. GPC_FiloV.
    IPR002561. GPC_filovir-type_extra_dom.
    [Graphical view ]
    Pfami PF01611. Filo_glycop. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF036874. GPC_FiloV. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "The virion glycoproteins of Ebola viruses are encoded in two reading frames and are expressed through transcriptional editing."
      Sanchez A., Trappier S.G., Mahy B.W.J., Peters C.J., Nichol S.T.
      Proc. Natl. Acad. Sci. U.S.A. 93:3602-3607(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA], RNA EDITING.
    2. Volchkov V.E.
      Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    3. "Molecular characterization of an isolate from the 1989/90 epizootic of Ebola virus Reston among macaques imported into the United States."
      Groseth A., Stroeher U., Theriault S., Feldmann H.
      Virus Res. 87:155-163(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    4. "A reconstituted replication and transcription system for Ebola virus Reston and comparison with Ebola virus Zaire."
      Boehmann Y., Enterlein S., Randolf A., Muehlberger E.I.
      Virology 332:406-417(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
      Strain: Isolate Pennsylvania-89.

    Entry informationi

    Entry nameiVSGP_EBORR
    AccessioniPrimary (citable) accession number: Q66800
    Secondary accession number(s): Q5UAK7, Q8JPX7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 62 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

    Complete proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3