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The annotation and conditions in this rule are derived from the following entries: P59594 (SPIKE_CVHSA)

If a protein meets these conditions... i

Common conditions

Special conditions

    • Subsequence at position 667 - 668 aligns to "R-S" in entry P59594 (individually applies "Cleavage")
    • Subsequence at position 14 - 667 aligns to entry P59594 (individually applies "Spike protein S1")
    • Subsequence at position 902 - 952 aligns to entry P59594 (individually applies "Heptad repeat 1")
    • Subsequence at position 323 - 348 aligns to "C-x*-C" in entry P59594 (individually applies "")
    • Subsequence at position 1145 - 1184 aligns to entry P59594 (individually applies "Heptad repeat 2")
    • Subsequence at position 1157 - 1185 aligns to entry P59594 (individually applies "")
    • Subsequence at position 760 - 761 aligns to "R-S" in entry P59594 (individually applies "Cleavage")
    • Subsequence at position 668 - @CTER@ aligns to entry P59594 (individually applies "Spike protein S2")
    • Subsequence at position 1251 - @CTER@ aligns to entry P59594 (individually applies "KxHxx")
    • Subsequence at position 931 - 975 aligns to entry P59594 (individually applies "")
    • Subsequence at position 14 - 1195 aligns to entry P59594 (individually applies "Extracellular")
    • Subsequence at position 306 - 527 aligns to entry P59594 (individually applies "Receptor-binding domain")
    • Subsequence at position 798 - @CTER@ aligns to entry P59594 (individually applies "Spike protein S2'")
    • Subsequence at position 366 - 419 aligns to "C-x*-C" in entry P59594 (individually applies "")
    • Subsequence at position 797 - 798 aligns to "R-S" in entry P59594 (individually applies "Cleavage")
    • Subsequence at position 1217 - @CTER@ aligns to entry P59594 (individually applies "Cytoplasmic")
    • Subsequence at position 770 - 788 aligns to entry P59594 (individually applies "Fusion peptide")

... then these annotations are applied i

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namei

  • Recommended name:
    Spike glycoprotein
    Short name:
    S glycoprotein
    Alternative name(s):
    E2
    Peplomer protein

Cleaved chain(s) or included domain(s)i

  • Cleaved chain:
    Recommended name:
    Spike protein S1
  • Cleaved chain:
    Recommended name:
    Spike protein S2
  • Cleaved chain:
    Recommended name:
    Spike protein S2'

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namei

  • Name:S

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

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

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

  • 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.

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> describes the function(s) of a protein.<p><a href='/help/function' target='_top'>More...</a></p>Functioni

  • 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.

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni

  • Heptad repeat 1 (to residues corresponding to positions 902 - 952)
  • Heptad repeat 2 (to residues corresponding to positions 1145 - 1184)
  • Receptor-binding domain (to residues corresponding to positions 306 - 527)
  • Fusion peptide (to residues corresponding to positions 770 - 788)

<p>This subsection of the ‘Family and domains’ section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili

  • (to residues corresponding to positions 1157 - 1185)
  • (to residues corresponding to positions 931 - 975)

<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>Chaini

  • Spike protein S1 (to residues corresponding to positions 14 - 667)
  • Spike protein S2 (to residues corresponding to positions 668 - @CTER@i)
  • Spike protein S2' (to residues corresponding to positions 798 - @CTER@i)

<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei

  • Cleavage (to residues corresponding to positions 667 - 668)
  • Cleavage (to residues corresponding to positions 760 - 761)
  • Cleavage (to residues corresponding to positions 797 - 798)

<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi

  • KxHxx (to residues corresponding to positions 1251 - @CTER@i)

<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi

  • (to residues corresponding to positions 323 - 348)
  • (to residues corresponding to positions 366 - 419)

<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini

  • Extracellular (to residues corresponding to positions 14 - 1195)
  • Cytoplasmic (to residues corresponding to positions 1217 - @CTER@i)

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO (Gene Ontology) termsi

  • GO:0016021 integral component of membrane
  • GO:0019031 viral envelope
  • GO:0019064 fusion of virus membrane with host plasma membrane
  • GO:0039654 fusion of virus membrane with host endosome membrane
  • GO:0044173 host cell endoplasmic reticulum-Golgi intermediate compartment membrane
  • GO:0046813 receptor-mediated virion attachment to host cell
  • GO:0055036 virion membrane
  • GO:0075509 endocytosis involved in viral entry into host cell
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