P17662 · SPIKE_IBVD3

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.

155050100150200250300350400450500550
TypeIDPosition(s)Description
Site538-539Cleavage; by host

GO annotations

AspectTerm
Cellular Componenthost cell endoplasmic reticulum-Golgi intermediate compartment 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 Processvirion attachment to host cell

Keywords

Names & Taxonomy

Protein names

Gene names

    • Name
      S
    • ORF names
      2

Organism names

Accessions

  • Primary accession
    P17662

Subcellular Location

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.

TypeIDPosition(s)Description
Topological domain19-550Extracellular

Keywords

PTM/Processing

Features

Showing features for signal, chain, glycosylation.

TypeIDPosition(s)Description
Signal1-18
ChainPRO_000003716919-538Spike protein S1
ChainPRO_000003716819-550Spike glycoprotein
Glycosylation23N-linked (GlcNAc...) asparagine; by host
Glycosylation74N-linked (GlcNAc...) asparagine; by host
Glycosylation102N-linked (GlcNAc...) asparagine; by host
Glycosylation139N-linked (GlcNAc...) asparagine; by host
Glycosylation145N-linked (GlcNAc...) asparagine; by host
Glycosylation164N-linked (GlcNAc...) asparagine; by host
Glycosylation179N-linked (GlcNAc...) asparagine; by host
Glycosylation213N-linked (GlcNAc...) asparagine; by host
Glycosylation238N-linked (GlcNAc...) asparagine; by host
Glycosylation248N-linked (GlcNAc...) asparagine; by host
Glycosylation265N-linked (GlcNAc...) asparagine; by host
Glycosylation272N-linked (GlcNAc...) asparagine; by host
Glycosylation277N-linked (GlcNAc...) asparagine; by host
Glycosylation307N-linked (GlcNAc...) asparagine; by host
Glycosylation426N-linked (GlcNAc...) asparagine; by host
Glycosylation448N-linked (GlcNAc...) asparagine; by host
Glycosylation514N-linked (GlcNAc...) asparagine; by host
Glycosylation531N-linked (GlcNAc...) asparagine; by host
ChainPRO_0000037170539-550Spike protein S2
Glycosylation543N-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 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 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).

Structure

3D structure databases

Family & Domains

Sequence similarities

Belongs to the coronaviruses spike protein family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Fragment
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    550
  • Mass (Da)
    60,877
  • Last updated
    1991-08-01 v2
  • Checksum
    D6FFEA93C78C4F95
MLEKSLLLVTLLFALCSANLFGNNSYVYYYQSAFRPPNGWHLHGGAYEVVNVSTESSNAGTTECTAGAIYWSKNFSAASVAMTAPQNGMLWSTAQFCTAHCNFTDFVVFVTHCYKSASGSCPLTGLIPQYHIRISAMKNSSLFYNLTVAVTKYPRFKSLQCVNNMTSVYLNGDLVFTSNETKDVSAAGVHFKAGGPITYKVMREVKALAYFVNGTAQDVILCDGSPTGLLACQYNTGNFSDGFYPFTNSSLVKEKFIVYRESSVNTTLELTNFTFSNVSNANPNTGGVHTIQLYQTSTAQSGHYNFNFSFLSSFTYKESDYMYGSYHPSCKFRLETINNGLWFNSLSVSLGYGPIQGGCKQSVFQNRATCCYAYSYNGPPLCKGVYRGELTKSFECGLLVFVTKTDGSRIQTRNEPFTLTQHNYNNITLDRCVEYNIYGRVGQGFITNVTNYAINYNYLADGGMAILDTSGAIDIFVVQGEYGLNYYKVNPCEDVNQQFVVSGGKLVGILTSRNETGSQPLENQFYIKIINGTRRSRRSITGNVTNCPYV

Features

Showing features for non-terminal residue.

TypeIDPosition(s)Description
Non-terminal residue550

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
X52084
EMBL· GenBank· DDBJ
CAA36302.1
EMBL· GenBank· DDBJ
Genomic RNA

Similar Proteins

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