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P69358

- FUS_MEASZ

UniProt

P69358 - FUS_MEASZ

Protein

Fusion glycoprotein F0

Gene

F

Organism
Measles virus (strain Edmonston-Zagreb vaccine) (MeV) (Subacute sclerose panencephalitis virus)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 53 (01 Oct 2014)
      Sequence version 1 (01 Aug 1988)
      Previous versions | rss
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    Functioni

    Class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and plasma cell membrane fusion, the heptad repeat (HR) regions assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and plasma cell membranes. Directs fusion of viral and cellular membranes leading to delivery of the nucleocapsid into the cytoplasm. This fusion is pH independent and occurs directly at the outer cell membrane. The trimer of F1-F2 (F protein) probably interacts with H at the virion surface. Upon HN binding to its cellular receptor, the hydrophobic fusion peptide is unmasked and interacts with the cellular membrane, inducing the fusion between cell and virion membranes. Later in infection, F proteins expressed at the plasma membrane of infected cells could mediate fusion with adjacent cells to form syncytia, a cytopathic effect that could lead to tissue necrosis By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei112 – 1132Cleavage; by hostBy similarity

    GO - Biological processi

    1. fusion of virus membrane with host plasma membrane Source: UniProtKB-KW
    2. induction by virus of host cell-cell fusion Source: InterPro

    Keywords - Biological processi

    Fusion of virus membrane with host cell membrane, Fusion of virus membrane with host membrane, Viral penetration into host cytoplasm, Virus entry into host cell

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Fusion glycoprotein F0
    Cleaved into the following 2 chains:
    Gene namesi
    Name:F
    OrganismiMeasles virus (strain Edmonston-Zagreb vaccine) (MeV) (Subacute sclerose panencephalitis virus)
    Taxonomic identifieri70149 [NCBI]
    Taxonomic lineageiVirusesssRNA negative-strand virusesMononegaviralesParamyxoviridaeParamyxovirinaeMorbillivirus
    Virus hostiHomo sapiens (Human) [TaxID: 9606]

    Subcellular locationi

    GO - Cellular componenti

    1. host cell plasma membrane Source: UniProtKB-SubCell
    2. integral component of membrane Source: UniProtKB-KW
    3. viral envelope Source: UniProtKB-KW
    4. virion membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Host cell membrane, Host membrane, Membrane, Viral envelope protein, Virion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2323Sequence AnalysisAdd
    BLAST
    Chaini24 – 550527Fusion glycoprotein F0PRO_0000039276Add
    BLAST
    Chaini24 – 11289Fusion glycoprotein F2PRO_0000039277Add
    BLAST
    Chaini113 – 550438Fusion glycoprotein F1PRO_0000039278Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi29 – 291N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi61 – 611N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi67 – 671N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi68 ↔ 195Interchain (between F2 and F1 chains)By similarity
    Disulfide bondi334 ↔ 343By similarity
    Disulfide bondi358 ↔ 366By similarity
    Disulfide bondi390 ↔ 395By similarity
    Disulfide bondi397 ↔ 420By similarity

    Post-translational modificationi

    The inactive precursor F0 is glycosylated and proteolytically cleaved into F1 and F2 to be functionally active. The cleavage is mediated by cellular proteases during the transport and maturation of the polypeptide By similarity.By similarity

    Keywords - PTMi

    Cleavage on pair of basic residues, Disulfide bond, Glycoprotein

    Interactioni

    Subunit structurei

    Homotrimer of disulfide-linked F1-F2.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliP69358.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini24 – 494471ExtracellularBy similarityAdd
    BLAST
    Topological domaini516 – 55035CytoplasmicBy similarityAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei495 – 51521HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni113 – 13725Fusion peptideBy similarityAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili138 – 16629Sequence AnalysisAdd
    BLAST
    Coiled coili462 – 48726Sequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Keywords - Domaini

    Coiled coil, Signal, Transmembrane, Transmembrane helix

    Family and domain databases

    InterProiIPR000776. Fusion_F0_Paramyxovir.
    [Graphical view]
    PfamiPF00523. Fusion_gly. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P69358-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGLKVNVSAI FMAVLLTLQT PTGQIHWGNL SKIGVVGIGS ASYKVMTRSS    50
    HQSLVIKLMP NITLLNNCTR VEIAEYRRLL RTVLEPIRDA LNAMTQNIRP 100
    VQSVASSRRH KRFAGVVLAG AALGVATAAQ ITAGIALHQS MLNSQAIDNL 150
    RASLETTNQA IEAIRQAGQE MILAVQGVQD YINNELIPSM NQLSCDLIGQ 200
    KLGLKLLRYY TEILSLFGPS LRDPISAEIS IQALSYALGG DINKVLEKLG 250
    YSGGDLLGIL ESRGIKARIT HVDTESYFIV LSIAYPTLSE IKGVIVHRLE 300
    GVSYNIGSQE WYTTVPKYVA TQGYLISNFD ESSCTFMPEG TVCSQNALYP 350
    MSPLLQECLR GSTKSCARTL VSGSFGNRFI LSQGNLIANC ASILCKCYTT 400
    GTIINQDPDK ILTYIAADHC PVVEVNGVTI QVGSRRYPDA VYLHRIDLGP 450
    PISLERLDVG TNLGNAIAKL EDAKELLESS DQILRSMKGL SSTSIVYILI 500
    AVCLGGLIGI PALICCCRGR CNKKGEQVGM SRPGLKPDLT GTSKSYVRSL 550
    Length:550
    Mass (Da):59,532
    Last modified:August 1, 1988 - v1
    Checksum:i7AA4F1CA82169093
    GO

    Sequence cautioni

    The sequence AAA56660.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U03670 Genomic RNA. Translation: AAA56660.1. Different initiation.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U03670 Genomic RNA. Translation: AAA56660.1 . Different initiation.

    3D structure databases

    ProteinModelPortali P69358.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    InterProi IPR000776. Fusion_F0_Paramyxovir.
    [Graphical view ]
    Pfami PF00523. Fusion_gly. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Comparison of sequences of the H, F, and N coding genes of measles virus vaccine strains."
      Rota J.S., Wang Z.D., Rota P.A., Bellini W.J.
      Virus Res. 31:317-330(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].

    Entry informationi

    Entry nameiFUS_MEASZ
    AccessioniPrimary (citable) accession number: P69358
    Secondary accession number(s): P08300
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: August 1, 1988
    Last modified: October 1, 2014
    This is version 53 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