Identification |
HMDB Protein ID
| HMDBP14051 |
Secondary Accession Numbers
| None |
Name
| Fusion glycoprotein F0 |
Synonyms
|
Not Available
|
Gene Name
| F |
Protein Type
| Unknown |
Biological Properties |
General Function
| Not Available |
Specific Function
| Inactive precursor that is cleaved at two sites by a furin-like protease to give rise to the mature F1 and F2 fusion glycoproteins.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. F protein is involved in the entry into the host cell through the interaction with host IGFR1. This interaction activates PRKCZ/PKCzeta that recruits host NCL/nucleolin to the apical cell surface where it can bind fusion glycoprotein F1. Later in infection, F protein expressed at the plasma membrane of infected cells can mediate fusion with adjacent cells to form syncytia, a cytopathic effect that could lead to tissue necrosis. F protein may trigger p53-dependent apoptosis.Major determinant of the species specificity of RSV infection. The trimer of F1-F2 (F protein) also facilitates the attachment to host cell by binding to host heparan sulfate. F protein is involved in the entry into the host cell through the interaction with host IGFR1. This interaction activates PRKCZ/PKCzeta that recruits host NCL/nucleolin to the apical cell surface where it can bind fusion glycoprotein F1. Later in infection, F protein expressed at the plasma membrane of infected cells can mediate fusion with adjacent cells to form syncytia, a cytopathic effect that could lead to tissue necrosis. F protein seems to trigger p53-dependent apoptosis. |
Pathways
|
Not Available
|
Reactions
| Not Available |
GO Classification
|
Biological Process |
viral entry into host cell via membrane fusion with the plasma membrane |
entry receptor-mediated virion attachment to host cell |
positive regulation of syncytium formation by virus |
Cellular Component |
host cell Golgi membrane |
virion membrane |
host cell plasma membrane |
viral envelope |
integral to membrane |
|
Cellular Location
|
Not Available
|
Gene Properties |
Chromosome Location
| Not Available |
Locus
| Not Available |
SNPs
| Not Available |
Gene Sequence
|
Not Available
|
Protein Properties |
Number of Residues
| Not Available |
Molecular Weight
| 63333.525 |
Theoretical pI
| Not Available |
Pfam Domain Function
|
|
Signals
|
|
Transmembrane Regions
|
|
Protein Sequence
|
Not Available
|
External Links |
GenBank ID Protein
| Not Available |
UniProtKB/Swiss-Prot ID
| P11209 |
UniProtKB/Swiss-Prot Entry Name
| FUS_HRSVR |
PDB IDs
|
|
GenBank Gene ID
| Not Available |
GeneCard ID
| Not Available |
GenAtlas ID
| Not Available |
HGNC ID
| Not Available |
References |
General References
| - Baybutt HN, Pringle CR: Molecular cloning and sequencing of the F and 22K membrane protein genes of the RSS-2 strain of respiratory syncytial virus. J Gen Virol. 1987 Nov;68 ( Pt 11):2789-96. doi: 10.1099/0022-1317-68-11-2789. [PubMed:3681264 ]
- Zhao X, Singh M, Malashkevich VN, Kim PS: Structural characterization of the human respiratory syncytial virus fusion protein core. Proc Natl Acad Sci U S A. 2000 Dec 19;97(26):14172-7. doi: 10.1073/pnas.260499197. [PubMed:11106388 ]
|