Q6RI13 · Q6RI13_9BETC

  • Protein
    Spike glycoprotein
  • Gene
    S
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Evidence at transcript level
  • Annotation score
    4/5

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.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.

Features

Showing features for site.

113241002003004005006007008009001,0001,1001,2001,300
TypeIDPosition(s)Description
Site869-870Cleavage

GO annotations

AspectTerm
Cellular Componenthost cell endoplasmic reticulum-Golgi intermediate compartment membrane
Cellular Componenthost cell plasma membrane
Cellular Componentmembrane
Cellular Componentviral envelope
Cellular Componentvirion membrane
Biological Processendocytosis involved in viral entry into host cell
Biological Processfusion of virus membrane with host endosome membrane
Biological Processfusion of virus membrane with host plasma membrane
Biological Processreceptor-mediated virion attachment to host cell

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Spike glycoprotein
  • Short names
    S glycoprotein
  • Alternative names
    • E2
    • Peplomer protein
  • Cleaved into 3 chains

Gene names

    • Name
      S

Organism names

  • Taxonomic identifier
  • Organism
  • Strains
    • MHV-A59
    • A59
  • Taxonomic lineage
    Viruses > Riboviria > Orthornavirae > Pisuviricota > Pisoniviricetes > Nidovirales > Cornidovirineae > Coronaviridae > Orthocoronavirinae > Betacoronavirus > Embecovirus > Murine coronavirus

Accessions

  • Primary accession
    Q6RI13
  • Secondary accessions
    • Q66WN1

Proteomes

Subcellular Location

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.

TypeIDPosition(s)Description
Transmembrane1266-1289Helical
Topological domain1287-1324Cytoplasmic

Keywords

PTM/Processing

Features

Showing features for disulfide bond, chain.

TypeIDPosition(s)Description
Disulfide bond329↔354
Disulfide bond372↔425
ChainPRO_5039966248714-1324Spike protein S2
ChainPRO_5039966247870-1324Spike protein S2'
Disulfide bond894↔905

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

Interaction

Subunit

Homotrimer; each monomer consists of a S1 and a S2 subunit. The resulting peplomers protrude from the virus surface as spikes.

Structure

3D structure databases

Family & Domains

Features

Showing features for domain, region, coiled coil, motif.

TypeIDPosition(s)Description
Domain15-296BetaCoV S1-NTD
Domain327-566BetaCoV S1-CTD
Region870-891Fusion peptide 1
Region889-909Fusion peptide 2
Domain946-1051Coronavirus spike (S) glycoprotein S2 subunit heptad repeat 1 (HR1) region profile
Region970-1020Heptad repeat 1
Coiled coil999-1043
Domain1194-1277Coronavirus spike (S) glycoprotein S2 subunit heptad repeat 2 (HR2) region profile
Coiled coil1227-1255
Motif1320-1324KxHxx

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

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,324
  • Mass (Da)
    145,937
  • Last updated
    2004-07-05 v1
  • Checksum
    5506AA9D92C2360F
MLFVFILFLPSCLGYIGDFRCIQLVNSNGANVSAPSISTETVEVSQGLGTYYVLDRVYLNATLLLTGYYPVDGSKFRNLALTGTNSVSLSWFQPPYLSQFNDGIFAKVQNLKTSTPSGATAYFPTIVIGSLFGYTSYTVVIEPYNGVIMASVCQYTICQLPYTDCKPNTNGNKLIGFWHTDVKPPICVLKRNFTLNVNADAFYFHFYQHGGTFYAYYADKPSATTFLFSVYIGDILTQYYVLPFICNPTAGSTFAPRYWVTPLVKRQYLFNFNQKGVITSAVDCASSYTSEIKCKTQSMLPSTGVYELSGYTVQPVGVVYRRVANLPACNIEEWLTARSVPSPLNWERKTFQNCNFNLSSLLRYVQAESLFCNNIDASKVYGRCFGSISVDKFAVPRSRQVDLQLGNSGFLQTANYKIDTAATSCQLHYTLPKNNVTINNHNPSSWNRRYGFNDAGVFGKNQHDVVYAQQCFTVRSSYCPCAQPDIVSPCTTQTKPKSAFVNVGDHCEGLGVLEDNCGNADPHKGCICANNSFIGWSHDTCLVNDRCQIFANILLNGINSGTTCSTDLQLPNTEVVTGICVKYDLYGITGQGVFKEVKADYYNSWQTLLYDVNGNLNGFRDLTTNKTYTIRSCYSGRVSAAFHKDAPEPALLYRNINCSYVFSNNISREENPLNYFDSYLGCVVNADNRTDEALPNCDLRMGAGLCVDYSKSRRAHRSVSTGYRLTTFEPYTPMLVNDSVQSVDGLYEMQIPTNFTIGHHEEFIQTRSPKVTIDCAAFVCGDNTACRQQLVEYGSFCVNVNAILNEVNNLLDNMQLQVASALMQGVTISSRLPDGISGPIDDINFSPLLGCIGSTCAEDGNGPSAIRGRSAIEDLLFDKVKLSDVGFVEAYNNCTGGQEVRDLLCVQSFNGIKVLPPVLSESQISGYTTGATAAAMFPPWSAAAGVPFSLSVQYRINGLGVTMNVLSENQKMIASAFNNALGAIQDGFDATNSALGKIQSVVNANAEALNNLLNQLSNRFGAISASLQEILTRLEAVEAKAQIDRLINGRLTALNAYISKQLSDSTLIKVSAAQAIEKVNECVKSQTTRINFCGNGNHILSLVQNAPYGLYFIHFSYVPISFTTANVSPGLCISGDRGLAPKAGYFVQDDGEWKFTGSSYYYPEPITDKNSVIMSSCAVNYTKAPEVFLNTSIPNPPDFKEELDKWFKNQTSIAPDLSLDFEKLNVTLLDLTYEMNRIQDAIKKLNESYINLKEVGTYEMYVKWPWYVWLLIGLAGVAVCVLLFFICCCTGCGSCCFKKCGNCCDEYGGHQDSIVIHNISSHED

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AY497328
EMBL· GenBank· DDBJ
AAR92025.1
EMBL· GenBank· DDBJ
mRNA
AY700211
EMBL· GenBank· DDBJ
AAU06356.1
EMBL· GenBank· DDBJ
Genomic RNA

Similar Proteins

Disclaimer

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