P12570 (FUS_NDVU) Reviewed, UniProtKB/Swiss-Prot
Last modified April 3, 2013. Version 86. History...
Names and origin
|Protein names||Recommended name:|
Fusion glycoprotein F0
|Organism||Newcastle disease virus (strain Chicken/Northern Ireland/Ulster/67) (NDV)|
|Taxonomic identifier||11190 [NCBI]|
|Taxonomic lineage||Viruses › ssRNA negative-strand viruses › Mononegavirales › Paramyxoviridae › Paramyxovirinae › Avulavirus ›|
|Virus host||Gallus gallus (Chicken) [TaxID: 9031]|
|Sequence length||553 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 (F protein) probably interacts with HN 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.
Homotrimer of disulfide-linked F1-F2 By similarity.
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.
Belongs to the paramyxoviruses fusion glycoprotein family.
|Biological process||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
|Cellular component||Host cell membrane|
Viral envelope protein
|Gene Ontology (GO)|
|Biological_process||induction by virus of host cell-cell fusion|
Inferred from electronic annotation. Source: InterProviral entry into host cell via membrane fusion with the plasma membrane
Inferred from electronic annotation. Source: UniProtKB-KW
|Cellular_component||host cell plasma membrane|
Inferred from electronic annotation. Source: UniProtKB-SubCellintegral to membrane
Inferred from electronic annotation. Source: UniProtKB-KWviral envelope
Inferred from electronic annotation. Source: UniProtKB-KWvirion membrane
Inferred from electronic annotation. Source: UniProtKB-SubCell
|Complete GO annotation...|
Sequence annotation (Features)
|Feature key||Position(s)||Length||Description||Graphical view||Feature identifier|
|Signal peptide||1 – 31||31||Potential|
|Chain||32 – 553||522||Fusion glycoprotein F0||PRO_0000039324|
|Chain||32 – 116||85||Fusion glycoprotein F2||PRO_0000039325|
|Chain||117 – 553||437||Fusion glycoprotein F1||PRO_0000039326|
|Topological domain||32 – 500||469||Extracellular By similarity|
|Transmembrane||501 – 521||21||Helical; By similarity|
|Topological domain||522 – 553||32||Cytoplasmic By similarity|
|Region||117 – 141||25||Fusion peptide By similarity|
|Coiled coil||142 – 170||29||Potential|
|Coiled coil||466 – 491||26||Potential|
|Site||116 – 117||2||Cleavage; by host By similarity|
Amino acid modifications
|Lipidation||523||1||S-palmitoyl cysteine; by host Potential|
|Glycosylation||85||1||N-linked (GlcNAc...); by host Potential|
|Glycosylation||191||1||N-linked (GlcNAc...); by host Potential|
|Glycosylation||366||1||N-linked (GlcNAc...); by host Potential|
|Glycosylation||447||1||N-linked (GlcNAc...); by host Potential|
|Glycosylation||471||1||N-linked (GlcNAc...); by host Potential|
|Disulfide bond||76 ↔ 199||Interchain (between F2 and F1 chains) By similarity|
|Disulfide bond||338 ↔ 347||By similarity|
|Disulfide bond||362 ↔ 370||By similarity|
|Disulfide bond||394 ↔ 399||By similarity|
|||"Nucleotide sequence of the fusion and haemagglutinin-neuraminidase glycoprotein genes of Newcastle disease virus, strain Ulster: molecular basis for variations in pathogenicity between strains."|
Millar N.S., Chambers P., Emmerson P.T.
J. Gen. Virol. 69:613-620(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
|||"Newcastle disease virus evolution. II. Lack of gene recombination in generating virulent and avirulent strains."|
Toyoda T., Sakaguchi T., Hirota H., Gotoh B., Kuma K., Miyata T., Nagai Y.
Virology 169:273-282(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
|D00243 Genomic RNA. Translation: BAA00173.1.|
M24694 Genomic RNA. Translation: AAA46645.1.
|PIR||VGNZU1. A29823. |
3D structure databases
|SMR||P12570. Positions 33-454. |
Protocols and materials databases
Family and domain databases
|InterPro||IPR000776. Fusion_F0_Paramyxovir. |
|Pfam||PF00523. Fusion_gly. 1 hit. |
|Accession||Primary (citable) accession number: P12570|
|Entry status||Reviewed (UniProtKB/Swiss-Prot)|
|Annotation program||Viral Protein Annotation Program|
Index of protein domains and families