Detail Information for IndEnz0002003573
IED ID IndEnz0002003573
Enzyme Type ID protease003573
Protein Name Fusion glycoprotein F0
Cleaved into: Fusion glycoprotein F2
F2
; p27
Intervening segment
Pep27
Peptide 27
; Fusion glycoprotein F1
F1
Gene Name F
Organism Bovine respiratory syncytial virus (strain A51908) (BRS)
Taxonomic Lineage Viruses Riboviria Orthornavirae Negarnaviricota Haploviricotina Monjiviricetes Mononegavirales Pneumoviridae Orthopneumovirus Bovine orthopneumovirus Bovine respiratory syncytial virus (strain A51908) (BRS)
Enzyme Sequence MATTTMRMIISIILISTYVPHITLCQNITEEFYQSTCSAVSRGYLSALRTGWYTSVVTIELSKIQKNVCNGTDSKVKLIKQELERYNNAVAELQSLMQNEPTSSSRAKRGIPESIHYTRNSTKKFYGLMGKKRKRRFLGFLLGIGSAIASGVAVSKVLHLEGEVNKIKNALLSTNKAVVSLSNGVSVLTSKVLDLKNYIDKELLPKVNNHDCRISNIATVIEFQQKNNRLLEIAREFSVNAGITTPLSTYMLTNSELLSIINDMPITNDQKKLMSVCQIVRQQSYSIMSVLREVIAYVVQLPLYGVIDTPCWKLHTSPLCTTDNKEGSNICLTRTDRGWYCDNAGSVSFFPQAETCKVQSNRVFCDTMNSLTLPTDVNLCNTDIFNSKYDCKIMTSKTDISSSVITSIGAIVSCYGKTKCTASNKNRGIIKTFSNGCDYVSNKGVDTVSVGNTLYYVNKLEGKALYIKGEPIINYYNPLVFPSDEFDASIAQVNAKINQSLAFIRRSDELLHSVDVGKSTTNVVITTIIIVIVVVILMLITVGLLFYCKTRSTPIMLGKDQLSSINNLSFSK
Enzyme Length 572
Uniprot Accession Number P29791
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number
Enzyme Function FUNCTION: [Fusion glycoprotein F0]: Inactive precursor that is cleaved at two sites by a furin-like protease to give rise to the mature F1 and F2 fusion glycoproteins. {ECO:0000250|UniProtKB:P03420}.; FUNCTION: [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 and entry into the host cell. 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. {ECO:0000250|UniProtKB:P03420}.; FUNCTION: [Fusion glycoprotein F2]: Major determinant of the species specificity of RSV infection. The trimer of F1-F2 (F protein) also facilitates the attachment and entry into the host cell. 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. {ECO:0000250|UniProtKB:P03420}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Chain (3); Coiled coil (3); Disulfide bond (7); Glycosylation (4); Lipidation (1); Natural variant (20); Peptide (1); Region (1); Signal peptide (1); Site (2); Topological domain (2); Transmembrane (1)
Keywords Cleavage on pair of basic residues;Coiled coil;Disulfide bond;Fusion of virus membrane with host cell membrane;Fusion of virus membrane with host membrane;Glycoprotein;Host Golgi apparatus;Host cell membrane;Host membrane;Host-virus interaction;Lipoprotein;Membrane;Palmitate;Reference proteome;Signal;Syncytium formation induced by viral infection;Transmembrane;Transmembrane helix;Viral attachment to host cell;Viral attachment to host entry receptor;Viral envelope protein;Viral penetration into host cytoplasm;Virion;Virus entry into host cell
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: [Fusion glycoprotein F0]: Host Golgi apparatus membrane {ECO:0000250|UniProtKB:P03420}; Single-pass membrane protein {ECO:0000250|UniProtKB:P03420}.; SUBCELLULAR LOCATION: [Fusion glycoprotein F1]: Virion membrane {ECO:0000250|UniProtKB:P03420}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P03420}. Host cell membrane {ECO:0000250|UniProtKB:P03420}; Single-pass membrane protein {ECO:0000250|UniProtKB:P03420}. Note=Localized at the host apical membrane. {ECO:0000250|UniProtKB:P03420}.; SUBCELLULAR LOCATION: [Fusion glycoprotein F2]: Virion membrane {ECO:0000250|UniProtKB:P03420}. Host cell membrane {ECO:0000250|UniProtKB:P03420}. Note=Localized at the host apical membrane. {ECO:0000250|UniProtKB:P03420}.
Modified Residue
Post Translational Modification PTM: [Fusion glycoprotein F0]: The F glycoprotein is synthesized as a F0 inactive precursor that is heavily N-glycosylated and processed at two sites by a host furin-like protease probably in the Golgi. The cleavage site between p27 and F1 may occur after endocytosis to yield the mature F1 and F2 proteins. Both cleavages are required for membrane fusion and p27 is released from the processed protein. {ECO:0000250|UniProtKB:P03420}.
Signal Peptide SIGNAL 1..25; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 63,443
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda