Detail Information for IndEnz0002010205
IED ID IndEnz0002010205
Enzyme Type ID protease010205
Protein Name Spike glycoprotein
S glycoprotein
E2
Peplomer protein

Cleaved into: Spike protein S1; Spike protein S2; Spike protein S2'
Gene Name S 2
Organism Avian infectious bronchitis virus (strain D274) (IBV)
Taxonomic Lineage Viruses Riboviria Orthornavirae Pisuviricota Pisoniviricetes Nidovirales Cornidovirineae Coronaviridae Orthocoronavirinae Gammacoronavirus Igacovirus Avian coronavirus Infectious bronchitis virus Avian infectious bronchitis virus (strain D274) (IBV)
Enzyme Sequence MLERSLLLATLLSALCSANLFGNNSYVYYYQSAFRPPDGWHLHGGAYEVVNVFTESSNAGTTGCTVGAIYWSKNFSAASVAMTAPQNGMSWSTEQFCTAHCNFTDFVVFVTHCYKSSHGSCPLTGLIPQNHIRISAMKNSSLFYNLTVAVTKYPRFKSLQCVNNMTSVYLNGDLVFTSNETKDVSAAGVHFKAGGPITYKVMREVKALAYFVNGTAQDVILCDGSPTGLLACQYNTGNFSDGFYPFTNSSLVKEKFIVYRESSVNTTLELTNFTFSNVSNATPNTGGVQTIQLYQTSTAQSGYYNLNFSFLSSFIYKASDYMYGSYHPSCKFRLETINNGLWFNSLSVSLGYGPIQGGCKQSVFANRATCCYAYSYNGPSLCKGVYRGELTKSFECGLLVFVTKTDGSRIQTRNEPFTLTQHNYNNITLDRCVEYNIYGRVGQGFITNVTNYAINYNYLADGGMAILDTSGAIDIFVVQGEYGLNYYKVNPCEDVNQQFVVSGGKLVGILTSRNETGSQPLENQFYIKIINGTRRSRRSITGNVTNCPYVTYGKFCIKPDGSISTIVPKELEHFVAPLLNVTENVLIPDSFNLTVTDEYIQTRMDKVQINCLQYVCGNSLECRKLFQQYGPVCDNILSVVNSVGQKEDMELLHFYSSTKPSGFNTPVLSNVSTGEFNISLLLTPPSSASGRSFIEDLLFTSVESVGLPTDDAYKKCTAGPLGFLKDLACAREYNGLLVLPPIITAEMQTLYTSSLVASMAFGGITSVGAIPFATQLQARINHLGITQSLLLKNQEKIAASFNKAIGHMQEGFRSTSLALQQIQDVVNKQSSILTETMASLNKNFGAISSVLQDIYQQLDSIQADAQVDRIITGRLSSLSVLASAKQAEYYRVSQQRELATQKINECVKSQSIRYSFCGNGRHVLTIPQNAPNGIVFIHFTYTPESFVNVTAIVGFCVNPANASQYAIVPANGRGIFIQVNGSYYITARDMYMPRDITAGDIVTLTSCQANYVSVNKTVITTFVDNDDFDFDDELSKWWNDTKHELPDFDEFNYTVPILDIGSEIDRIQGVIQGLNDSLIDLETLSILKTYIKWPWYVWLAIAFATIIFILILGWLFFMTGCCGCCCGCFGIIPLMSKCGKKSSYYTTFDNDVVT
Enzyme Length 1154
Uniprot Accession Number P12722
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number
Enzyme Function FUNCTION: [Spike protein S1]: Attaches the virion to the host cell membrane by interacting with sialic acids, initiating the infection. {ECO:0000255|HAMAP-Rule:MF_04098}.; FUNCTION: [Spike protein S2]: Mediates fusion of the virion and cellular membranes by acting as 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. {ECO:0000255|HAMAP-Rule:MF_04098}.; FUNCTION: [Spike protein S2']: Acts as a viral fusion peptide after S2 cleavage occurring upon virus endocytosis. {ECO:0000255|HAMAP-Rule:MF_04098}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Chain (4); Coiled coil (2); Glycosylation (30); Region (2); Signal peptide (1); Site (2); Topological domain (2); Transmembrane (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;Transmembrane;Transmembrane helix;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:0000255|HAMAP-Rule:MF_04098}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04098}. Host endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000255|HAMAP-Rule:MF_04098}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04098}. 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. {ECO:0000255|HAMAP-Rule:MF_04098}.; SUBCELLULAR LOCATION: [Spike protein S1]: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04098}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_04098}. Host endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000255|HAMAP-Rule:MF_04098}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_04098}. 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. {ECO:0000255|HAMAP-Rule:MF_04098}.
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. Additionally, a second cleavage leads to the release of a fusion peptide after viral attachment to host cell receptor. {ECO:0000255|HAMAP-Rule:MF_04098}.
Signal Peptide SIGNAL 1..18; /evidence=ECO:0000255|HAMAP-Rule:MF_04098
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 127,503
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda