Q6RI13 · Q6RI13_9BETC
- ProteinSpike glycoprotein
- GeneS
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids1324 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score4/5
Function
function
Spike protein S1: attaches the virion to the cell membrane by interacting with host receptor, initiating the infection.
Spike protein S2': Acts as a viral fusion peptide which is unmasked following S2 cleavage occurring upon virus endocytosis.
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 three 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.
Features
Showing features for site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 869-870 | Cleavage | ||||
Sequence: RS |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | host cell endoplasmic reticulum-Golgi intermediate compartment membrane | |
Cellular Component | host cell plasma 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 | fusion of virus membrane with host plasma membrane | |
Biological Process | receptor-mediated virion attachment to host cell |
Keywords
- Biological process
Names & Taxonomy
Protein names
- Recommended nameSpike glycoprotein
- Short namesS glycoprotein
- Alternative names
- Cleaved into 3 chains
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageViruses > Riboviria > Orthornavirae > Pisuviricota > Pisoniviricetes > Nidovirales > Cornidovirineae > Coronaviridae > Orthocoronavirinae > Betacoronavirus > Embecovirus > Murine coronavirus
Accessions
- Primary accessionQ6RI13
- Secondary accessions
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Virion membrane ; Single-pass type I membrane protein
Host endoplasmic reticulum-Golgi intermediate compartment membrane ; Single-pass type I membrane protein
Host cell 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 are transported to the host plasma membrane, where they may mediate cell-cell fusion.
Features
Showing features for transmembrane, topological domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 1266-1289 | Helical | ||||
Sequence: WYVWLLIGLAGVAVCVLLFFICCC | ||||||
Topological domain | 1287-1324 | Cytoplasmic | ||||
Sequence: CCCTGCGSCCFKKCGNCCDEYGGHQDSIVIHNISSHED |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for disulfide bond, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Disulfide bond | 329↔354 | |||||
Sequence: CNIEEWLTARSVPSPLNWERKTFQNC | ||||||
Disulfide bond | 372↔425 | |||||
Sequence: CNNIDASKVYGRCFGSISVDKFAVPRSRQVDLQLGNSGFLQTANYKIDTAATSC | ||||||
Chain | PRO_5039966248 | 714-1324 | Spike protein S2 | |||
Sequence: RAHRSVSTGYRLTTFEPYTPMLVNDSVQSVDGLYEMQIPTNFTIGHHEEFIQTRSPKVTIDCAAFVCGDNTACRQQLVEYGSFCVNVNAILNEVNNLLDNMQLQVASALMQGVTISSRLPDGISGPIDDINFSPLLGCIGSTCAEDGNGPSAIRGRSAIEDLLFDKVKLSDVGFVEAYNNCTGGQEVRDLLCVQSFNGIKVLPPVLSESQISGYTTGATAAAMFPPWSAAAGVPFSLSVQYRINGLGVTMNVLSENQKMIASAFNNALGAIQDGFDATNSALGKIQSVVNANAEALNNLLNQLSNRFGAISASLQEILTRLEAVEAKAQIDRLINGRLTALNAYISKQLSDSTLIKVSAAQAIEKVNECVKSQTTRINFCGNGNHILSLVQNAPYGLYFIHFSYVPISFTTANVSPGLCISGDRGLAPKAGYFVQDDGEWKFTGSSYYYPEPITDKNSVIMSSCAVNYTKAPEVFLNTSIPNPPDFKEELDKWFKNQTSIAPDLSLDFEKLNVTLLDLTYEMNRIQDAIKKLNESYINLKEVGTYEMYVKWPWYVWLLIGLAGVAVCVLLFFICCCTGCGSCCFKKCGNCCDEYGGHQDSIVIHNISSHED | ||||||
Chain | PRO_5039966247 | 870-1324 | Spike protein S2' | |||
Sequence: SAIEDLLFDKVKLSDVGFVEAYNNCTGGQEVRDLLCVQSFNGIKVLPPVLSESQISGYTTGATAAAMFPPWSAAAGVPFSLSVQYRINGLGVTMNVLSENQKMIASAFNNALGAIQDGFDATNSALGKIQSVVNANAEALNNLLNQLSNRFGAISASLQEILTRLEAVEAKAQIDRLINGRLTALNAYISKQLSDSTLIKVSAAQAIEKVNECVKSQTTRINFCGNGNHILSLVQNAPYGLYFIHFSYVPISFTTANVSPGLCISGDRGLAPKAGYFVQDDGEWKFTGSSYYYPEPITDKNSVIMSSCAVNYTKAPEVFLNTSIPNPPDFKEELDKWFKNQTSIAPDLSLDFEKLNVTLLDLTYEMNRIQDAIKKLNESYINLKEVGTYEMYVKWPWYVWLLIGLAGVAVCVLLFFICCCTGCGSCCFKKCGNCCDEYGGHQDSIVIHNISSHED | ||||||
Disulfide bond | 894↔905 | |||||
Sequence: CTGGQEVRDLLC |
Post-translational modification
Specific enzymatic cleavages in vivo yield mature proteins. The precursor is processed into S1 and S2 by host cell furin or another cellular protease to yield the mature S1 and S2 proteins. Additionally, a second cleavage leads to the release of a fusion peptide after viral attachment to host cell receptor.
The cytoplasmic Cys-rich domain is palmitoylated. Spike glycoprotein is digested within host endosomes.
Keywords
- PTM
Interaction
Subunit
Homotrimer; each monomer consists of a S1 and a S2 subunit. The resulting peplomers protrude from the virus surface as spikes.
Family & Domains
Features
Showing features for domain, region, coiled coil, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 15-296 | BetaCoV S1-NTD | ||||
Sequence: YIGDFRCIQLVNSNGANVSAPSISTETVEVSQGLGTYYVLDRVYLNATLLLTGYYPVDGSKFRNLALTGTNSVSLSWFQPPYLSQFNDGIFAKVQNLKTSTPSGATAYFPTIVIGSLFGYTSYTVVIEPYNGVIMASVCQYTICQLPYTDCKPNTNGNKLIGFWHTDVKPPICVLKRNFTLNVNADAFYFHFYQHGGTFYAYYADKPSATTFLFSVYIGDILTQYYVLPFICNPTAGSTFAPRYWVTPLVKRQYLFNFNQKGVITSAVDCASSYTSEIKCKT | ||||||
Domain | 327-566 | BetaCoV S1-CTD | ||||
Sequence: PACNIEEWLTARSVPSPLNWERKTFQNCNFNLSSLLRYVQAESLFCNNIDASKVYGRCFGSISVDKFAVPRSRQVDLQLGNSGFLQTANYKIDTAATSCQLHYTLPKNNVTINNHNPSSWNRRYGFNDAGVFGKNQHDVVYAQQCFTVRSSYCPCAQPDIVSPCTTQTKPKSAFVNVGDHCEGLGVLEDNCGNADPHKGCICANNSFIGWSHDTCLVNDRCQIFANILLNGINSGTTCST | ||||||
Region | 870-891 | Fusion peptide 1 | ||||
Sequence: SAIEDLLFDKVKLSDVGFVEAY | ||||||
Region | 889-909 | Fusion peptide 2 | ||||
Sequence: EAYNNCTGGQEVRDLLCVQSF | ||||||
Domain | 946-1051 | Coronavirus spike (S) glycoprotein S2 subunit heptad repeat 1 (HR1) region profile | ||||
Sequence: VPFSLSVQYRINGLGVTMNVLSENQKMIASAFNNALGAIQDGFDATNSALGKIQSVVNANAEALNNLLNQLSNRFGAISASLQEILTRLEAVEAKAQIDRLINGRL | ||||||
Region | 970-1020 | Heptad repeat 1 | ||||
Sequence: QKMIASAFNNALGAIQDGFDATNSALGKIQSVVNANAEALNNLLNQLSNRF | ||||||
Coiled coil | 999-1043 | |||||
Sequence: QSVVNANAEALNNLLNQLSNRFGAISASLQEILTRLEAVEAKAQI | ||||||
Domain | 1194-1277 | Coronavirus spike (S) glycoprotein S2 subunit heptad repeat 2 (HR2) region profile | ||||
Sequence: PNPPDFKEELDKWFKNQTSIAPDLSLDFEKLNVTLLDLTYEMNRIQDAIKKLNESYINLKEVGTYEMYVKWPWYVWLLIGLAGV | ||||||
Coiled coil | 1227-1255 | |||||
Sequence: TLLDLTYEMNRIQDAIKKLNESYINLKEV | ||||||
Motif | 1320-1324 | KxHxx | ||||
Sequence: SSHED |
Domain
Fusion peptide 1 (FP1) and fusion peptide 2 (FP2) function cooperatively and have a membrane-ordering effect on lipid headgroups and shallow hydrophobic regions of target bilayers. They are considered as two domains of an extended, bipartite FP. The membrane-ordering activity is calcium-dependent and also dependent on correct folding, which is maintained by an internal disulfide bond in FP2.
Sequence similarities
Belongs to the betacoronaviruses spike protein family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,324
- Mass (Da)145,937
- Last updated2004-07-05 v1
- Checksum5506AA9D92C2360F