A3EX94 · SPIKE_BCHK4

Function

function

Spike protein S1

Attaches the virion to the cell membrane by interacting with host receptor, initiating the infection.

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.

Spike protein S2'

Acts as a viral fusion peptide which is unmasked following S2 cleavage occurring upon virus endocytosis.

Features

Showing features for site.

113521002003004005006007008009001,0001,1001,2001,300
TypeIDPosition(s)Description
Site749-750Cleavage
Site886-887Cleavage

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
    • ORF names
      2

Organism names

Accessions

  • Primary accession
    A3EX94

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 topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain13-1297Extracellular
Transmembrane1298-1318Helical
Topological domain1319-1352Cytoplasmic

Keywords

PTM/Processing

Features

Showing features for signal, chain, glycosylation, disulfide bond.

TypeIDPosition(s)Description
Signal1-12
ChainPRO_000044406113-746Spike protein S1
ChainPRO_000029032113-1352Spike glycoprotein
Glycosylation30N-linked (GlcNAc...) asparagine; by host
Glycosylation71N-linked (GlcNAc...) asparagine; by host
Glycosylation111N-linked (GlcNAc...) asparagine; by host
Glycosylation132N-linked (GlcNAc...) asparagine; by host
Glycosylation162N-linked (GlcNAc...) asparagine; by host
Glycosylation172N-linked (GlcNAc...) asparagine; by host
Disulfide bond191↔242
Glycosylation227N-linked (GlcNAc...) asparagine; by host
Glycosylation241N-linked (GlcNAc...) asparagine; by host
Disulfide bond344↔354
Glycosylation384N-linked (GlcNAc...) asparagine; by host
Disulfide bond388↔412
Glycosylation415N-linked (GlcNAc...) asparagine; by host
Disulfide bond430↔483
Disulfide bond442↔590
Glycosylation492N-linked (GlcNAc...) asparagine; by host
Glycosylation624N-linked (GlcNAc...) asparagine; by host
Glycosylation723N-linked (GlcNAc...) asparagine; by host
ChainPRO_0000290323750-1235Spike protein S2
Glycosylation762N-linked (GlcNAc...) asparagine; by host
Glycosylation773N-linked (GlcNAc...) asparagine; by host
Glycosylation784N-linked (GlcNAc...) asparagine; by host
Glycosylation869N-linked (GlcNAc...) asparagine; by host
ChainPRO_0000444062887-1352Spike protein S2'
Disulfide bond911↔924
Glycosylation1144N-linked (GlcNAc...) asparagine; by host
Glycosylation1147N-linked (GlcNAc...) asparagine; by host
Glycosylation1174N-linked (GlcNAc...) asparagine; by host
Glycosylation1226N-linked (GlcNAc...) asparagine; by host
Glycosylation1242N-linked (GlcNAc...) asparagine; by host
Glycosylation1257N-linked (GlcNAc...) asparagine; by host
Glycosylation1278N-linked (GlcNAc...) asparagine; by host
Glycosylation1289N-linked (GlcNAc...) asparagine; by host

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 databases

Interaction

Subunit

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

Structure

Family & Domains

Features

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

TypeIDPosition(s)Description
Domain21-356BetaCoV S1-NTD
Domain386-592BetaCoV S1-CTD
Region887-908Fusion peptide 1
Region906-928Fusion peptide 2
Region993-1043Heptad repeat 1
Coiled coil1022-1066
Region1247-1286Heptad repeat 2
Coiled coil1259-1287
Motif1350-1352KxHxx

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
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    1,352
  • Mass (Da)
    149,029
  • Last updated
    2007-03-20 v1
  • Checksum
    2E75232D7E4E693A
MTLLMCLLMSLLIFVRGCDSQFVDMSPASNTSECLESQVDAAAFSKLMWPYPIDPSKVDGIIYPLGRTYSNITLAYTGLFPLQGDLGSQYLYSVSHAVGHDGDPTKAYISNYSLLVNDFDNGFVVRIGAAANSTGTIVISPSVNTKIKKAYPAFILGSSLTNTSAGQPLYANYSLTIIPDGCGTVLHAFYCILKPRTVNRCPSGTGYVSYFIYETVHNDCQSTINRNASLNSFKSFFDLVNCTFFNSWDITADETKEWFGITQDTQGVHLYSSRKGDLYGGNMFRFATLPVYEGIKYYTVIPRSFRSKANKREAWAAFYVYKLHQLTYLLDFSVDGYIRRAIDCGHDDLSQLHCSYTSFEVDTGVYSVSSYEASATGTFIEQPNATECDFSPMLTGVAPQVYNFKRLVFSNCNYNLTKLLSLFAVDEFSCNGISPDSIARGCYSTLTVDYFAYPLSMKSYIRPGSAGNIPLYNYKQSFANPTCRVMASVLANVTITKPHAYGYISKCSRLTGANQDVETPLYINPGEYSICRDFSPGGFSEDGQVFKRTLTQFEGGGLLIGVGTRVPMTDNLQMSFIISVQYGTGTDSVCPMLDLGDSLTITNRLGKCVDYSLYGVTGRGVFQNCTAVGVKQQRFVYDSFDNLVGYYSDDGNYYCVRPCVSVPVSVIYDKSTNLHATLFGSVACEHVTTMMSQFSRLTQSNLRRRDSNIPLQTAVGCVIGLSNNSLVVSDCKLPLGQSLCAVPPVSTFRSYSASQFQLAVLNYTSPIVVTPINSSGFTAAIPTNFSFSVTQEYIETSIQKVTVDCKQYVCNGFTRCEKLLVEYGQFCSKINQALHGANLRQDESVYSLYSNIKTTSTQTLEYGLNGDFNLTLLQVPQIGGSSSSYRSAIEDLLFDKVTIADPGYMQGYDDCMKQGPQSARDLICAQYVSGYKVLPPLYDPNMEAAYTSSLLGSIAGAGWTAGLSSFAAIPFAQSMFYRLNGVGITQQVLSENQKLIANKFNQALGAMQTGFTTSNLAFSKVQDAVNANAQALSKLASELSNTFGAISSSISDILARLDTVEQDAQIDRLINGRLISLNAFVSQQLVRSETAARSAQLASDKVNECVKSQSKRNGFCGSGTHIVSFVVNAPNGFYFFHVGYVPTNYTNVTAAYGLCNNNNPPLCIAPIDGYFITNQTTTYSVDTEWYYTGSSFYKPEPITQANSRYVSSDVKFDKLENNLPPPLLENSTDVDFKDELEEFFKNVTSHGPNFAEISKINTTLLDLSDEMAMLQEVVKQLNDSYIDLKELGNYTYYNKWPWYVWLGFIAGLVALLLCVFFLLCCTGCGTSCLGKMKCKNCCDSYEEYDVEKIHVH

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
EF065505
EMBL· GenBank· DDBJ
ABN10839.1
EMBL· GenBank· DDBJ
Genomic RNA

Genome annotation databases

Similar Proteins

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