Q6WB98 · FUS_HMPVC

Function

function

Fusion glycoprotein F0

Inactive precursor that is cleaved to give rise to the mature F1 and F2 fusion glycoproteins.

Fusion glycoprotein F1

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 coiled coil 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 cellular membranes leading to delivery of the nucleocapsid into the cytoplasm. This fusion is pH independent and occurs at the plasma or endosomal membrane. The trimer of F1-F2 (F protein) also facilitates the attachment to host cell by binding to host heparan sulfate.

Fusion glycoprotein F2

Major determinant of the species specificity of RSV infection (By similarity).
The trimer of F1-F2 (F protein) also facilitates the attachment to host cell by binding to host heparan sulfate (PubMed:22238303).

Miscellaneous

The cleavage peptide sequence for the hMPV F protein (RQSR) varies from the one described for other pneumoviruses, and differs from the furin protease motif (R/K-X-R/K-R).

GO annotations

AspectTerm
Cellular Componenthost cell plasma membrane
Cellular Componentmembrane
Cellular Componentviral envelope
Cellular Componentvirion membrane
Biological Processfusion of virus membrane with host plasma membrane
Biological Processsymbiont entry into host cell

Keywords

Names & Taxonomy

Protein names

Gene names

    • Name
      F

Organism names

Accessions

  • Primary accession
    Q6WB98

Proteomes

Subcellular Location

Virion membrane ; Single-pass type I membrane protein
Host cell membrane
; Single-pass membrane protein

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane492-512Helical

Keywords

PTM/Processing

Features

Showing features for signal, chain, disulfide bond, glycosylation.

TypeIDPosition(s)Description
Signal1-18
ChainPRO_000039480619-539Fusion glycoprotein F0
ChainPRO_000039480720-102Fusion glycoprotein F2
Disulfide bond28↔407Interchain (between F2 and F1 chains)
Glycosylation57N-linked (GlcNAc...) asparagine; by host
Disulfide bond60↔182Interchain (between F2 and F1 chains)
ChainPRO_0000394808103-539Fusion glycoprotein F1
Glycosylation172N-linked (GlcNAc...) asparagine; by host
Disulfide bond283↔311
Disulfide bond292↔301
Disulfide bond326↔335
Disulfide bond350↔361
Glycosylation353N-linked (GlcNAc...) asparagine; by host
Disulfide bond384↔390

Post-translational modification

Fusion glycoprotein F0

The F glycoprotein is synthesized as a F0 inactive precursor that is heavily N-glycosylated and processed.

Keywords

PTM databases

Interaction

Subunit

Fusion glycoprotein F1

Homotrimer. Heterodimer with fusion protein F2; disulfide-linked. As a heterodimer with F2, interacts with host heparan sulfate (PubMed:22238303).
As a heterodimer with F2, interacts with host integrin ITGAV/ITGB1 (PubMed:19164533).
Part of a complex composed of F1, F2 and G glycoproteins (By similarity).

Fusion glycoprotein F2

Homotrimer. Heterodimer with fusion protein F1; disulfide-linked. As a heterodimer with F1, interacts with host heparan sulfate (PubMed:22238303).
As a heterodimer with F2, interacts with host integrin ITGAV/ITGB1 (PubMed:19164533).
Part of a complex composed of F1, F2 and G glycoproteins (By similarity).

Family & Domains

Features

Showing features for region, motif.

TypeIDPosition(s)Description
Region103-127Fusion peptide
Motif329-331Cell attachment site
Region520-539Disordered

Domain

Fusion glycoprotein F0

The N-terminus is a hydrophobic fusion peptide that inserts into the target host membrane (By similarity).
It is buried in the center of the trimer cavity before cleavage. The coiled coil (heptad repeat) regions are probably involved in homotrimerization, heterodimerization and in the formation of a fusion-active hairpin structure (By similarity).

Fusion glycoprotein F1

The N-terminus is a hydrophobic fusion peptide that inserts into the target host membrane (By similarity).
It is buried in the center of the trimer cavity before cleavage. The coiled coil (heptad repeat) regions are probably involved in homotrimerization, heterodimerization and in the formation of a fusion-active hairpin structure (By similarity).

Sequence similarities

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    539
  • Mass (Da)
    58,477
  • Last updated
    2004-07-05 v1
  • Checksum
    2987E611786A64BA
MSWKVVIIFSLLITPQHGLKESYLEESCSTITEGYLSVLRTGWYTNVFTLEVGDVENLTCSDGPSLIKTELDLTKSALRELKTVSADQLAREEQIENPRQSRFVLGAIALGVATAAAVTAGVAIAKTIRLESEVTAIKNALKTTNEAVSTLGNGVRVLATAVRELKDFVSKNLTRAINKNKCDIDDLKMAVSFSQFNRRFLNVVRQFSDNAGITPAISLDLMTDAELARAVSNMPTSAGQIKLMLENRAMVRRKGFGILIGVYGSSVIYMVQLPIFGVIDTPCWIVKAAPSCSGKKGNYACLLREDQGWYCQNAGSTVYYPNEKDCETRGDHVFCDTAAGINVAEQSKECNINISTTNYPCKVSTGRHPISMVALSPLGALVACYKGVSCSIGSNRVGIIKQLNKGCSYITNQDADTVTIDNTVYQLSKVEGEQHVIKGRPVSSSFDPIKFPEDQFNVALDQVFENIENSQALVDQSNRILSSAEKGNTGFIIVIILIAVLGSSMILVSIFIIIKKTKKPTGAPPELSGVTNNGFIPHS

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AY297749
EMBL· GenBank· DDBJ
AAQ67695.1
EMBL· GenBank· DDBJ
Genomic RNA

Similar Proteins

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