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O36634

- FUS_HRSVB

UniProt

O36634 - FUS_HRSVB

Protein

Fusion glycoprotein F0

Gene

F

Organism
Human respiratory syncytial virus B (strain B1)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 60 (01 Oct 2014)
      Sequence version 1 (01 Jan 1998)
      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 (protein F) interacts with glycoprotein G at the virion surface. Upon binding of G to heparan sulfate, the hydrophobic fusion peptide is unmasked and interacts with the cellular membrane, inducing the fusion between host cell and virion membranes. Notably, RSV fusion protein is able to interact directly with heparan sulfate and therefore actively participates in virus attachment. Furthermore, the F2 subunit was identifed as the major determinant of RSV host cell specificity. Later in infection, proteins F expressed at the plasma membrane of infected cells mediate fusion with adjacent cells to form syncytia, a cytopathic effect that could lead to tissue necrosis. The fusion protein is also able to trigger p53-dependent apoptosis By similarity.By similarity

    GO - Biological processi

    1. fusion of virus membrane with host plasma membrane Source: UniProtKB-KW
    2. positive regulation of syncytium formation by virus Source: UniProtKB-KW

    Keywords - Biological processi

    Fusion of virus membrane with host cell membrane, Fusion of virus membrane with host membrane, Syncytium formation induced by viral infection, Viral penetration into host cytoplasm, Virus entry into host cell

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Fusion glycoprotein F0
    Short name:
    Protein F
    Cleaved into the following 2 chains:
    Gene namesi
    Name:F
    OrganismiHuman respiratory syncytial virus B (strain B1)
    Taxonomic identifieri79692 [NCBI]
    Taxonomic lineageiVirusesssRNA negative-strand virusesMononegaviralesParamyxoviridaePneumovirinaePneumovirus
    Virus hostiHomo sapiens (Human) [TaxID: 9606]
    ProteomesiUP000002472: Genome

    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 – 2525Sequence AnalysisAdd
    BLAST
    Chaini26 – 574549Fusion glycoprotein F0PRO_0000390376Add
    BLAST
    Chaini26 – 136111Fusion glycoprotein F2PRO_0000390377Add
    BLAST
    Chaini137 – 574438Fusion glycoprotein F1PRO_0000390378Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi27 – 271N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi69 ↔ 212Interchain (between F2 and F1 chains)By similarity
    Glycosylationi70 – 701N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi116 – 1161N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi120 – 1201N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi126 – 1261N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi358 ↔ 367By similarity
    Disulfide bondi382 ↔ 393By similarity
    Glycosylationi500 – 5001N-linked (GlcNAc...); by hostSequence Analysis

    Post-translational modificationi

    The F glycoprotein is synthesized as a inactive precursor that is heavily N-glycosylated and processed by host cell furin in the Golgi to yield the mature F1 and F2 proteins. The cleavage site between F1 and F2 requires the minimal sequence [KR]-X-[KR]-R.

    Keywords - PTMi

    Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Lipoprotein, Palmitate

    Interactioni

    Subunit structurei

    Homotrimer of disulfide-linked F1-F2 By similarity. Interacts with glycoprotein G. Interacts with host RHOA; this interaction facilitates virus-induced syncytium formation By similarity.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliO36634.
    ModBaseiSearch...
    MobiDBiSearch...

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei530 – 55021HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili73 – 10028Sequence 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.

    O36634-1 [UniParc]FASTAAdd to Basket

    « Hide

    MELLIHRLSA IFLTLAINAL YLTSSQNITE EFYQSTCSAV SRGYFSALRT    50
    GWYTSVITIE LSNIKETKCN GTDTKVKLIK QELDKYKNAV TELQLLMQNT 100
    PAANNRARRE APQYMNYTIN TTKNLNVSIS KKRKRRFLGF LLGVGSAIAS 150
    GIAVSKVLHL EGEVNKIKNA LLSTNKAVVS LSNGVSVLTS KVLDLKNYIN 200
    NQLLPIVNQQ SCRISNIETV IEFQQKNSRL LEINREFSVN AGVTTPLSTY 250
    MLTNSELLSL INDMPITNDQ KKLMSSNVQI VRQQSYSIMS IIKEEVLAYV 300
    VQLPIYGVID TPCWKLHTSP LCTTNIKEGS NICLTRTDRG WYCDNAGSVS 350
    FFPQADTCKV QSNRVFCDTM NSLTLPSEVS LCNTDIFNSK YDCKIMTSKT 400
    DISSSVITSL GAIVSCYGKT KCTASNKNRG IIKTFSNGCD YVSNKGVDTV 450
    SVGNTLYYVN KLEGKNLYVK GEPIINYYDP LVFPSDEFDA SISQVNEKIN 500
    QSLAFIRRSD ELLHNVNTGK STTNIMITTI IIVIIVVLLS LIAIGLLLYC 550
    KAKNTPVTLS KDQLSGINNI AFSK 574
    Length:574
    Mass (Da):63,710
    Last modified:January 1, 1998 - v1
    Checksum:i29A127B128BF5E92
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF013254 Genomic RNA. Translation: AAB82436.1.
    RefSeqiNP_056863.1. NC_001781.1.

    Genome annotation databases

    GeneIDi1489825.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF013254 Genomic RNA. Translation: AAB82436.1 .
    RefSeqi NP_056863.1. NC_001781.1.

    3D structure databases

    ProteinModelPortali O36634.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 1489825.

    Family and domain databases

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

    Publicationsi

    1. "Respiratory syncytial virus (RSV) SH and G proteins are not essential for viral replication in vitro: clinical evaluation and molecular characterization of a cold-passaged, attenuated RSV subgroup B mutant."
      Karron R.A., Buonagurio D.A., Georgiu A.F., Whitehead S.S., Adamus J.E., Clements-Mann M.L., Harris D.O., Randolph V.B., Udem S.A., Murphy B.R., Sidhu M.S.
      Proc. Natl. Acad. Sci. U.S.A. 94:13961-13966(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].

    Entry informationi

    Entry nameiFUS_HRSVB
    AccessioniPrimary (citable) accession number: O36634
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 2009
    Last sequence update: January 1, 1998
    Last modified: October 1, 2014
    This is version 60 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, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3