| IED ID | IndEnz0002005545 |
| Enzyme Type ID | protease005545 |
| Protein Name |
Fusion glycoprotein F0 Protein F Cleaved into: Fusion glycoprotein F2; Fusion glycoprotein F1 |
| Gene Name | F |
| Organism | Sendai virus (strain Harris) (SeV) |
| Taxonomic Lineage | Viruses Riboviria Orthornavirae Negarnaviricota Haploviricotina Monjiviricetes Mononegavirales Paramyxoviridae Orthoparamyxovirinae Respirovirus Murine respirovirus Sendai virus (strain Harris) (SeV) |
| Enzyme Sequence | MTAYIQRSQCISTSLLVVLTTLVSCQIPRDRLSNIGVIVDEGKSLKIAGSHESRYIVLSLVPGVDLENGCGTAQVIQYKSLLNRLLIPLRDALDLQEALITVTNDTTQNAGVPQSRFFGAVIGTIALGVATSAQITAGIALAEAREAKRDIALIKESMTKTHKSVELLQNAVGEQILALKTLQDFVNDEIKPAISELGCETAALRLGIKLTQHYFGLLTAFGSNFGTIGEKSRTLQALSSLYSANITEIMTTIRTGQSNIYDVIYTEQIKGTVIDVDLERYMVTLSVKIPILSEVPGVLIHKASSISYNIDGEEWYVTVPSHILSRASFLGGADITDCVESRLTYICPRDPAQLIPDSQQKCILGDTTRCPVTKVVDSLIPKFAFVNGGVVANRIASTCTCGTGRRPISQDRSKGVAFLTHDNCGLIGVNGVELYANRRGHDATWGVQNLTVGPAIAIRPVDISLNLADATNFLQDSKAELEKARKILSEVGRWYNSRETVITIIVVMVVILVVIIVIVIVLYRLKRSMLMGNPDERIPRDTYTLEPKIRHMYTNGGFDAMAEKR |
| Enzyme Length | 565 |
| Uniprot Accession Number | P04856 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: 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) interacts with HN tetramer 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). {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (3); Coiled coil (2); Disulfide bond (4); Glycosylation (3); Region (2); Signal peptide (1); Site (1); Topological domain (2); Transmembrane (1) |
| Keywords | Coiled coil;Disulfide bond;Fusion of virus membrane with host cell membrane;Fusion of virus membrane with host membrane;Glycoprotein;Host cell membrane;Host membrane;Membrane;Signal;Transmembrane;Transmembrane helix;Viral envelope protein;Viral penetration into host cytoplasm;Virion;Virus entry into host cell |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Virion membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Host cell membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | PTM: In natural infection, inactive F0 is matured into F1 and F2 outside the cell by one or more trypsin-like, arginine-specific endoprotease secreted by the bronchial epithelial cells. One identified protease that may be involved in this process is tryptase Clara. Unlike most paramyxoviruses, Sendai F0 processing occurs on the cell surface and induces a conformational change in the protein that unmasks the fusion peptide. F0 maturation is a primary determinant for organ tropism and pathogenicity. F1 and F2 display interchain and intrachain disulfide bonds, that are necessary for correct folding and intracellular transport (By similarity). {ECO:0000250}.; PTM: N-glycosylated; glycans consist of a mixture of high mannose-type oligosaccharides and of complex-type oligosaccharides. Glycosylation at Asn-245 is essential for membrane localization and F0 cleavage (By similarity). {ECO:0000250}. |
| Signal Peptide | SIGNAL 1..25; /evidence=ECO:0000250 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 61,666 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |