IED ID | IndEnz0002009722 |
Enzyme Type ID | protease009722 |
Protein Name |
Spike glycoprotein S glycoprotein E2 Peplomer protein Cleaved into: Spike protein S1; Spike protein S2 Fragment |
Gene Name | S 2 |
Organism | Avian infectious bronchitis virus (strain D3896) (IBV) |
Taxonomic Lineage | Viruses Riboviria Orthornavirae Pisuviricota Pisoniviricetes Nidovirales Cornidovirineae Coronaviridae Orthocoronavirinae Gammacoronavirus Igacovirus Avian coronavirus Infectious bronchitis virus Avian infectious bronchitis virus (strain D3896) (IBV) |
Enzyme Sequence | MLEKSLLLVTLLFALCSANLFGNNSYVYYYQSAFRPPNGWHLHGGAYEVVNVSTESSNAGTTECTAGAIYWSKNFSAASVAMTAPQNGMLWSTAQFCTAHCNFTDFVVFVTHCYKSASGSCPLTGLIPQYHIRISAMKNSSLFYNLTVAVTKYPRFKSLQCVNNMTSVYLNGDLVFTSNETKDVSAAGVHFKAGGPITYKVMREVKALAYFVNGTAQDVILCDGSPTGLLACQYNTGNFSDGFYPFTNSSLVKEKFIVYRESSVNTTLELTNFTFSNVSNANPNTGGVHTIQLYQTSTAQSGHYNFNFSFLSSFTYKESDYMYGSYHPSCKFRLETINNGLWFNSLSVSLGYGPIQGGCKQSVFQNRATCCYAYSYNGPPLCKGVYRGELTKSFECGLLVFVTKTDGSRIQTRNEPFTLTQHNYNNITLDRCVEYNIYGRVGQGFITNVTNYAINYNYLADGGMAILDTSGAIDIFVVQGEYGLNYYKVNPCEDVNQQFVVSGGKLVGILTSRNETGSQPLENQFYIKIINGTRRSRRSITGNVTNCPYV |
Enzyme Length | 550 |
Uniprot Accession Number | P17662 |
Absorption | |
Active Site | |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | |
Enzyme Function | FUNCTION: S1 attaches the virion to the cell membrane by interacting with cell receptors, initiating the infection.; FUNCTION: S2 is a 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 coiled coil regions (heptad repeats) 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 (By similarity). {ECO:0000250}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Chain (3); Glycosylation (19); Non-terminal residue (1); Signal peptide (1); Site (1); Topological domain (1) |
Keywords | Cleavage on pair of basic residues;Coiled coil;Fusion of virus membrane with host endosomal membrane;Fusion of virus membrane with host membrane;Glycoprotein;Host membrane;Host-virus interaction;Membrane;Signal;Viral attachment to host cell;Viral envelope protein;Viral penetration into host cytoplasm;Virion;Virulence;Virus endocytosis by host;Virus entry into host cell |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: [Spike protein S2]: Virion membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Host endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Note=Accumulates in the endoplasmic reticulum-Golgi intermediate compartment, where it participates in virus particle assembly. Some S oligomers may be transported to the plasma membrane, where they may mediate cell-cell fusion (By similarity). {ECO:0000250}.; SUBCELLULAR LOCATION: [Spike protein S1]: Virion membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Host endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Accumulates in the endoplasmic reticulum-Golgi intermediate compartment, where it participates in virus particle assembly. Some S oligomers may be transported to the plasma membrane, where they may mediate cell-cell fusion. S1 is not anchored to the viral envelope, but associates with the extravirion surface through its binding to S2 (By similarity). {ECO:0000250}. |
Modified Residue | |
Post Translational Modification | PTM: Specific enzymatic cleavages in vivo yield mature proteins. The precursor is processed into S1 and S2 by host cell furin or furin-like protease to yield the mature S1 and S2 proteins. The cleavage site between S1 and S2 requires the optimal sequence [KR]-X-[KR]-R. Cleavage is not necessary for virus-cell fusion (By similarity). {ECO:0000250}. |
Signal Peptide | SIGNAL 1..18; /evidence=ECO:0000255 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 60,877 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |