O36634 (FUS_HRSVB) Reviewed, UniProtKB/Swiss-Prot
Last modified February 19, 2014. Version 59. History...
Names and origin
|Protein names||Recommended name:|
Fusion glycoprotein F0
Short name=Protein F
|Organism||Human respiratory syncytial virus B (strain B1) [Reference proteome]|
|Taxonomic identifier||79692 [NCBI]|
|Taxonomic lineage||Viruses › ssRNA negative-strand viruses › Mononegavirales › Paramyxoviridae › Pneumovirinae › Pneumovirus ›|
|Virus host||Homo sapiens (Human) [TaxID: 9606]|
|Sequence length||574 AA.|
|Sequence processing||The displayed sequence is further processed into a mature form.|
|Protein existence||Inferred from homology|
General annotation (Comments)
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.
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.
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.
Belongs to the paramyxoviruses fusion glycoprotein family.
Sequence annotation (Features)
|Feature key||Position(s)||Length||Description||Graphical view||Feature identifier|
|Signal peptide||1 – 25||25||Potential|
|Chain||26 – 574||549||Fusion glycoprotein F0||PRO_0000390376|
|Chain||26 – 136||111||Fusion glycoprotein F2||PRO_0000390377|
|Chain||137 – 574||438||Fusion glycoprotein F1||PRO_0000390378|
|Transmembrane||530 – 550||21||Helical; Potential|
|Coiled coil||73 – 100||28||Potential|
Amino acid modifications
|Glycosylation||27||1||N-linked (GlcNAc...); by host Potential|
|Glycosylation||70||1||N-linked (GlcNAc...); by host Potential|
|Glycosylation||116||1||N-linked (GlcNAc...); by host Potential|
|Glycosylation||120||1||N-linked (GlcNAc...); by host Potential|
|Glycosylation||126||1||N-linked (GlcNAc...); by host Potential|
|Glycosylation||500||1||N-linked (GlcNAc...); by host Potential|
|Disulfide bond||69 ↔ 212||Interchain (between F2 and F1 chains) By similarity|
|Disulfide bond||358 ↔ 367||By similarity|
|Disulfide bond||382 ↔ 393||By similarity|
|||"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].
|AF013254 Genomic RNA. Translation: AAB82436.1.|
|RefSeq||NP_056863.1. NC_001781.1. |
3D structure databases
Protocols and materials databases
Genome annotation databases
Family and domain databases
|InterPro||IPR000776. Fusion_F0_Paramyxovir. |
|Pfam||PF00523. Fusion_gly. 1 hit. |
|Accession||Primary (citable) accession number: O36634|
|Entry status||Reviewed (UniProtKB/Swiss-Prot)|
|Annotation program||Viral Protein Annotation Program|
Index of protein domains and families