| IED ID | IndEnz0010001410 |
| Enzyme Type ID | esterase001410 |
| Protein Name |
Fusion glycoprotein F0 Protein 3 P3 Cleaved into: Fusion glycoprotein F1; Fusion glycoprotein F2 |
| Gene Name | Segment-5 |
| Organism | Infectious salmon anemia virus (isolate Atlantic salmon/Norway/810/9/99) (ISAV) |
| Taxonomic Lineage | Viruses Riboviria Orthornavirae Negarnaviricota Polyploviricotina Insthoviricetes Articulavirales Orthomyxoviridae Isavirus Salmon isavirus Infectious salmon anemia virus (isolate Atlantic salmon/Norway/810/9/99) (ISAV) |
| Enzyme Sequence | MAFLTILVLFLFKEVLCEPCICENPTCLGITIPQAGFVRSAPGGVLLTETITERPQLTEWTTSRPKLEETLWLDGETKNGKVSQTLFEAIQGTQMENCAVKAVLDTTFVNLTKQDIVLGKIKVSEFGGDSDISKCGRKGLKVFICGGTVGYVTRGCPPEECKGKKGRMMALEPTTDCGVEKGLTTDRIKTGMLDITSCCTQHGCTKGIRVEVPSPVLVSSKCQEVTFRVVPFHSVPDKLGFARTSSFTLKANFVNKHGWSKYNFNLRGFPGEEFIKCCGFTLGVGGAWFQAYLNGMVQGDGAASADDVKEKLNGIIDQINKANTLLEGEIEAVRRIAYMNQASSLQNQVEIGLIGEYLNISSWLETTTLTKTEEGLMKNGWCQSNTHCWCPPKPTIVPTIGYVDSIKEVTGTSWWMVMIHYIIVGLIVIVVVVFGLKLWGCLRR |
| Enzyme Length | 444 |
| Uniprot Accession Number | Q8V3T9 |
| 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 target 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 target cell membranes. Directs fusion of viral and cellular membranes leading to delivery of the nucleocapsid into the cytoplasm. The trimer of F1-F2 (F protein) probably interacts with HE at the virion surface. Upon HE 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. {ECO:0000269|PubMed:16160182, ECO:0000269|PubMed:26082488}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (3); Glycosylation (2); Region (1); Signal peptide (1); Site (1); Topological domain (2); Transmembrane (1) |
| Keywords | Disulfide bond;Glycoprotein;Host membrane;Membrane;Reference proteome;Signal;Transmembrane;Transmembrane helix;Virion |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Virion membrane {ECO:0000269|PubMed:14990725}. Host membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000255}. |
| Modified Residue | |
| Post Translational Modification | PTM: 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. {ECO:0000269|PubMed:16160182}. |
| Signal Peptide | SIGNAL 1..17; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 48,773 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |