P17662 · SPIKE_IBVD3
- ProteinSpike glycoprotein
- GeneS
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids550 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
S1 attaches the virion to the cell membrane by interacting with cell receptors, initiating the infection.
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).
Features
Showing features for site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 538-539 | Cleavage; by host | ||||
Sequence: RS |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | host cell endoplasmic reticulum-Golgi intermediate compartment membrane | |
Cellular Component | membrane | |
Cellular Component | viral envelope | |
Cellular Component | virion membrane | |
Biological Process | endocytosis involved in viral entry into host cell | |
Biological Process | fusion of virus membrane with host endosome membrane | |
Biological Process | virion attachment to host cell |
Keywords
- Biological process
Names & Taxonomy
Protein names
- Recommended nameSpike glycoprotein
- Short namesS glycoprotein
- Alternative names
- Cleaved into 2 chains
Gene names
Organism names
- Taxonomic lineageViruses > Riboviria > Orthornavirae > Pisuviricota > Pisoniviricetes > Nidovirales > Cornidovirineae > Coronaviridae > Orthocoronavirinae > Gammacoronavirus > Igacovirus > Avian coronavirus
- Virus hosts
Accessions
- Primary accessionP17662
Subcellular Location
UniProt Annotation
GO Annotation
Spike protein S2
Virion membrane ; Single-pass type I membrane protein
Host endoplasmic reticulum-Golgi intermediate compartment membrane ; Single-pass type I membrane protein
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).
Spike protein S1
Virion membrane ; Peripheral membrane protein
Host endoplasmic reticulum-Golgi intermediate compartment membrane ; Peripheral membrane protein
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).
Features
Showing features for topological domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 19-550 | Extracellular | ||||
Sequence: NLFGNNSYVYYYQSAFRPPNGWHLHGGAYEVVNVSTESSNAGTTECTAGAIYWSKNFSAASVAMTAPQNGMLWSTAQFCTAHCNFTDFVVFVTHCYKSASGSCPLTGLIPQYHIRISAMKNSSLFYNLTVAVTKYPRFKSLQCVNNMTSVYLNGDLVFTSNETKDVSAAGVHFKAGGPITYKVMREVKALAYFVNGTAQDVILCDGSPTGLLACQYNTGNFSDGFYPFTNSSLVKEKFIVYRESSVNTTLELTNFTFSNVSNANPNTGGVHTIQLYQTSTAQSGHYNFNFSFLSSFTYKESDYMYGSYHPSCKFRLETINNGLWFNSLSVSLGYGPIQGGCKQSVFQNRATCCYAYSYNGPPLCKGVYRGELTKSFECGLLVFVTKTDGSRIQTRNEPFTLTQHNYNNITLDRCVEYNIYGRVGQGFITNVTNYAINYNYLADGGMAILDTSGAIDIFVVQGEYGLNYYKVNPCEDVNQQFVVSGGKLVGILTSRNETGSQPLENQFYIKIINGTRRSRRSITGNVTNCPYV |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for signal, chain, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-18 | |||||
Sequence: MLEKSLLLVTLLFALCSA | ||||||
Chain | PRO_0000037169 | 19-538 | Spike protein S1 | |||
Sequence: NLFGNNSYVYYYQSAFRPPNGWHLHGGAYEVVNVSTESSNAGTTECTAGAIYWSKNFSAASVAMTAPQNGMLWSTAQFCTAHCNFTDFVVFVTHCYKSASGSCPLTGLIPQYHIRISAMKNSSLFYNLTVAVTKYPRFKSLQCVNNMTSVYLNGDLVFTSNETKDVSAAGVHFKAGGPITYKVMREVKALAYFVNGTAQDVILCDGSPTGLLACQYNTGNFSDGFYPFTNSSLVKEKFIVYRESSVNTTLELTNFTFSNVSNANPNTGGVHTIQLYQTSTAQSGHYNFNFSFLSSFTYKESDYMYGSYHPSCKFRLETINNGLWFNSLSVSLGYGPIQGGCKQSVFQNRATCCYAYSYNGPPLCKGVYRGELTKSFECGLLVFVTKTDGSRIQTRNEPFTLTQHNYNNITLDRCVEYNIYGRVGQGFITNVTNYAINYNYLADGGMAILDTSGAIDIFVVQGEYGLNYYKVNPCEDVNQQFVVSGGKLVGILTSRNETGSQPLENQFYIKIINGTRRSRR | ||||||
Chain | PRO_0000037168 | 19-550 | Spike glycoprotein | |||
Sequence: NLFGNNSYVYYYQSAFRPPNGWHLHGGAYEVVNVSTESSNAGTTECTAGAIYWSKNFSAASVAMTAPQNGMLWSTAQFCTAHCNFTDFVVFVTHCYKSASGSCPLTGLIPQYHIRISAMKNSSLFYNLTVAVTKYPRFKSLQCVNNMTSVYLNGDLVFTSNETKDVSAAGVHFKAGGPITYKVMREVKALAYFVNGTAQDVILCDGSPTGLLACQYNTGNFSDGFYPFTNSSLVKEKFIVYRESSVNTTLELTNFTFSNVSNANPNTGGVHTIQLYQTSTAQSGHYNFNFSFLSSFTYKESDYMYGSYHPSCKFRLETINNGLWFNSLSVSLGYGPIQGGCKQSVFQNRATCCYAYSYNGPPLCKGVYRGELTKSFECGLLVFVTKTDGSRIQTRNEPFTLTQHNYNNITLDRCVEYNIYGRVGQGFITNVTNYAINYNYLADGGMAILDTSGAIDIFVVQGEYGLNYYKVNPCEDVNQQFVVSGGKLVGILTSRNETGSQPLENQFYIKIINGTRRSRRSITGNVTNCPYV | ||||||
Glycosylation | 23 | N-linked (GlcNAc...) asparagine; by host | ||||
Sequence: N | ||||||
Glycosylation | 74 | N-linked (GlcNAc...) asparagine; by host | ||||
Sequence: N | ||||||
Glycosylation | 102 | N-linked (GlcNAc...) asparagine; by host | ||||
Sequence: N | ||||||
Glycosylation | 139 | N-linked (GlcNAc...) asparagine; by host | ||||
Sequence: N | ||||||
Glycosylation | 145 | N-linked (GlcNAc...) asparagine; by host | ||||
Sequence: N | ||||||
Glycosylation | 164 | N-linked (GlcNAc...) asparagine; by host | ||||
Sequence: N | ||||||
Glycosylation | 179 | N-linked (GlcNAc...) asparagine; by host | ||||
Sequence: N | ||||||
Glycosylation | 213 | N-linked (GlcNAc...) asparagine; by host | ||||
Sequence: N | ||||||
Glycosylation | 238 | N-linked (GlcNAc...) asparagine; by host | ||||
Sequence: N | ||||||
Glycosylation | 248 | N-linked (GlcNAc...) asparagine; by host | ||||
Sequence: N | ||||||
Glycosylation | 265 | N-linked (GlcNAc...) asparagine; by host | ||||
Sequence: N | ||||||
Glycosylation | 272 | N-linked (GlcNAc...) asparagine; by host | ||||
Sequence: N | ||||||
Glycosylation | 277 | N-linked (GlcNAc...) asparagine; by host | ||||
Sequence: N | ||||||
Glycosylation | 307 | N-linked (GlcNAc...) asparagine; by host | ||||
Sequence: N | ||||||
Glycosylation | 426 | N-linked (GlcNAc...) asparagine; by host | ||||
Sequence: N | ||||||
Glycosylation | 448 | N-linked (GlcNAc...) asparagine; by host | ||||
Sequence: N | ||||||
Glycosylation | 514 | N-linked (GlcNAc...) asparagine; by host | ||||
Sequence: N | ||||||
Glycosylation | 531 | N-linked (GlcNAc...) asparagine; by host | ||||
Sequence: N | ||||||
Chain | PRO_0000037170 | 539-550 | Spike protein S2 | |||
Sequence: SITGNVTNCPYV | ||||||
Glycosylation | 543 | N-linked (GlcNAc...) asparagine; by host | ||||
Sequence: N |
Post-translational modification
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).
Keywords
- PTM
PTM databases
Interaction
Subunit
Homotrimer; each monomer consists of a S1 and a S2 subunit. The resulting peplomers protrude from the virus surface as spikes (By similarity).
Family & Domains
Sequence similarities
Belongs to the coronaviruses spike protein family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusFragment
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length550
- Mass (Da)60,877
- Last updated1991-08-01 v2
- ChecksumD6FFEA93C78C4F95
Features
Showing features for non-terminal residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Non-terminal residue | 550 | |||||
Sequence: V |