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Q66811

- VSGP_EBOIC

UniProt

Q66811 - VSGP_EBOIC

Protein

Pre-small/secreted glycoprotein

Gene

GP

Organism
Ivory Coast ebolavirus (strain Cote d'Ivoire-94) (CIEBOV) (Cote d'Ivoire Ebola virus)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 57 (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
    Sitei324 – 3252Cleavage; 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
    OrganismiIvory Coast ebolavirus (strain Cote d'Ivoire-94) (CIEBOV) (Cote d'Ivoire Ebola virus)
    Taxonomic identifieri128999 [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]

    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 – 3232Sequence AnalysisAdd
    BLAST
    Chaini33 – 365333Pre-small/secreted glycoproteinBy similarityPRO_0000037494Add
    BLAST
    Chaini33 – 324292Small/secreted glycoproteinBy similarityPRO_0000037495Add
    BLAST
    Chaini325 – 36541Delta-peptideBy similarityPRO_0000037496Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi40 – 401N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi53 – 53InterchainBy similarity
    Disulfide bondi108 ↔ 135By similarity
    Disulfide bondi121 ↔ 147By similarity
    Glycosylationi204 – 2041N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi228 – 2281N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi257 – 2571N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi268 – 2681N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi306 – 306InterchainBy 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

    ProteinModelPortaliQ66811.
    SMRiQ66811. Positions 32-278.
    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.

    Q66811-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGASGILQLP RERFRKTSFF VWVIILFHKV FSIPLGVVHN NTLQVSDIDK    50
    FVCRDKLSST SQLKSVGLNL EGNGVATDVP TATKRWGFRA GVPPKVVNYE 100
    AGEWAENCYN LAIKKVDGSE CLPEAPEGVR DFPRCRYVHK VSGTGPCPGG 150
    LAFHKEGAFF LYDRLASTII YRGTTFAEGV IAFLILPKAR KDFFQSPPLH 200
    EPANMTTDPS SYYHTTTINY VVDNFGTNTT EFLFQVDHLT YVQLEARFTP 250
    QFLVLLNETI YSDNRRSNTT GKLIWKINPT VDTSMGEWAF WENKKTSQKP 300
    FQVKSCLSYL YQKPRTRSLT RQRRSLLPSP PTTTQAKTTK NWFQRIPLQW 350
    FRCKTSRERT QCQPQ 365
    Length:365
    Mass (Da):41,690
    Last modified:November 1, 1996 - v1
    Checksum:iD2D39579392F9C28
    GO

    RNA editingi

    Partially edited. RNA editing at this position consists of an insertion of one adenine nucleotide. The sequence displayed here is the small secreted glycoprotein, derived from the unedited RNA. The edited RNA gives rise to the full-length transmembrane glycoprotein (AC Q66810).

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U28006 Genomic RNA. Translation: AAB37092.1.

    Keywords - Coding sequence diversityi

    RNA editing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U28006 Genomic RNA. Translation: AAB37092.1 .

    3D structure databases

    ProteinModelPortali Q66811.
    SMRi Q66811. Positions 32-278.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    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.

    Entry informationi

    Entry nameiVSGP_EBOIC
    AccessioniPrimary (citable) accession number: Q66811
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 57 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programViral Protein Annotation Program

    Miscellaneousi

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3