Detail Information for IndEnz0010001410
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