A0A679DU09 · A0A679DU09_9BETC

  • Protein
    Spike glycoprotein
  • Gene
    S
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • 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.

113631002003004005006007008009001,0001,1001,2001,300
TypeIDPosition(s)Description
Site913-914Cleavage

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
  • Strain
    • IWT-22
  • Taxonomic lineage
    Viruses > Riboviria > Orthornavirae > Pisuviricota > Pisoniviricetes > Nidovirales > Cornidovirineae > Coronaviridae > Orthocoronavirinae > Betacoronavirus > Embecovirus > Betacoronavirus 1

Accessions

  • Primary accession
    A0A679DU09

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
Transmembrane1308-1331Helical
Topological domain1329-1363Cytoplasmic

Keywords

PTM/Processing

Features

Showing features for disulfide bond, chain.

TypeIDPosition(s)Description
Disulfide bond331↔356
Disulfide bond374↔427
ChainPRO_5025742219765-1363Spike protein S2
ChainPRO_5025742218914-1363Spike protein S2'
Disulfide bond938↔949

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.

Family & Domains

Features

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

TypeIDPosition(s)Description
Domain15-298BetaCoV S1-NTD
Domain329-617BetaCoV S1-CTD
Region914-935Fusion peptide 1
Region933-953Fusion peptide 2
Domain990-1095Coronavirus spike (S) glycoprotein S2 subunit heptad repeat 1 (HR1) region profile
Region1014-1064Heptad repeat 1
Coiled coil1043-1087
Domain1238-1319Coronavirus spike (S) glycoprotein S2 subunit heptad repeat 2 (HR2) region profile
Coiled coil1269-1297
Motif1359-1363KxHxx

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
    1,363
  • Mass (Da)
    150,509
  • Last updated
    2020-06-17 v1
  • Checksum
    0A4184E4A01F0CCB
MFLILLISLPTAFAVIGDLKCTTVSINDVDTGVPSISTDTVDVTNGLGTYYVLDRVYLNTTLLLNGYYPTSGFTYRNMALKGTLLLSTLWFKPPFLSDFTNGIFAKVKNTKVIKDGVMYSEFPAITIGSTFVNTSYSVVVQPHTTILGNKLQGFLEISVCQYTMCEYPNTICNPNLGNQRVELWHWDTGVVSCLYKRNFTYDVNADYLYFHFYQEGGTFYAYFTDTGVVTKFLFNVYLGTVLSHYYVMPLTCNSALTLEYWVTPLTSKQYLLAFNQDGVIFNAVDCKSDFMSEIKCKTLSIAPSTGVYELNGYTVQPIADVYRRIPNLPDCNIEAWLNDKSVPSPLNWERKTFSNCNFNMSSLMSFIQADSFTCNNIDAAKIYGMCFSSITIDKFAIPNGRKVDLQLGNLGYLQSFNYRIDTTATSCQLYYNLPAANVSVSRFNPSTWNRRFGFTEQSVFKPQPAGVFADHDVVYAQHCFKAPTNFCPCKLDGSLCVGSGSGIDAGYKNTGIGTCPAGTNYLTCHNAAQCDCLCTPDPITSKATGPHKCPQTKYLVGIGEHCSGLAIKSDHCGGNPCSCQPQAFLGWSVDSCLQGDRCNIFANFILHDVNSGTTCSTDLQKSNTDIILGVCVNYDLYGITGQGIFVEVNATYYNSWQNLLYDSNGNLYGFRDYLTNRTFMIRSCYSGRVSAAFHANSSEPALLFRNIKCNYVFNNTLSRQLQPINYFDSYLGCVVNADNSTSSVVQTCDLTVGSGYCVDYSTKRRSRRSITTGYRFTNFEPFTVNSVNDSLEPVGGLYEIQIPSEFTIGNMEEFIQTSSPKVTIDCSAFVCGDYAACKSQLVEYGSFCDNINAILTEVNELLDTTQLQVANSLMNGVTLSTKLKDGVNFNVDDINFSPVLGCLGSDCNKVSSRSAIEDLLFSKVKLSDVGFVEAYNNCTGGAEIRDLICVQSYNGIKVLPPLLSENQISGYTLAATSASLFPPWSAAAGVPFYLNVQYRINGIGVTMDVLSQNQKLIANAFNNALGAIQEGFDATNSALVKIQAVVNANAEALNNLLQQLSNRFGAISSSLQEILSRLDALEAQAQIDRLINGRLTALNAYVSQQLSDSTLVKFSAAQAMEKVNECVKSQSSRINFCGNGNHIISLVQNAPYGLYFIHFSYVPTKYVTAKVSPGLCIAGDRGIAPKSGYFVNVNNTWMFTGSGYYYPEPITGNNVVVMSTCAVNYTKAPDVMLNISTPNLPDFKEELDQWFKNQTSVAPDLSLDYINVTFLDLQDEMNRLQEAIKVLNQSYINLKDIGTYEYYVKWPWYVWLLIGFAGVAMLVLLFFICCCTGCGTSCFKKCGGCCDDYTGHQELVIKTSHED

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LC494148
EMBL· GenBank· DDBJ
BBM61137.1
EMBL· GenBank· DDBJ
Genomic RNA

Similar Proteins

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