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The annotation and conditions in this rule are derived from the following entries: P19240 (GLYC_MOPEI), P08669 (GLYC_LASSJ), P26313 (GLYC_JUNIN), P09991 (GLYC_LYCVA)

If a protein meets these conditions... i

Common conditions

Special conditions

    • Subsequence at position 2 - 2 aligns to "G" in entry P26313 (individually applies "N-myristoyl glycine; by host")
    • Subsequence at position 1 - 1 aligns to "M" in entry P26313 (individually applies "Removed; by host")
    • Subsequence at position 459 - 459 aligns to "H" in entry P26313 (individually applies "Zinc 1; via pros nitrogen")
    • Subsequence at position 279 - 292 aligns to "C-x*-C" in entry P26313 (individually applies "")
    • Subsequence at position 54 - 58 aligns to entry P26313 (individually applies "Extracellular")
    • Subsequence at position 135 - 164 aligns to "C-x*-C" in entry P26313 (individually applies "")
    • Subsequence at position 251 - 252 aligns to entry P26313 (individually applies "Cleavage; by host MBTPS1")
    • Subsequence at position 485 - 485 aligns to "H" in entry P26313 (individually applies "Zinc 2; via tele nitrogen")
    • Subsequence at position 118 - 155 aligns to "C-x*-C" in entry P26313 (individually applies "")
    • Subsequence at position 180 - 212 aligns to "C-x*-C" in entry P26313 (individually applies "")
    • Subsequence at position 455 - 455 aligns to "C" in entry P26313 (individually applies "Zinc 2")
    • Subsequence at position 33 - 33 aligns to entry P26313 (individually applies "Cytoplasmic")
    • Subsequence at position 446 - @CTER@ aligns to entry P26313 (individually applies "Cytoplasmic")
    • Subsequence at position 58 - 59 aligns to entry P26313 (individually applies "Cleavage; by host signal peptidase")
    • Subsequence at position 92 - 226 aligns to "C-x*-C" in entry P26313 (individually applies "")
    • Subsequence at position 449 - 449 aligns to "H" in entry P26313 (individually applies "Zinc 2; via tele nitrogen")
    • Subsequence at position 364 - 385 aligns to "C-x*-C" in entry P26313 (individually applies "")
    • Subsequence at position 467 - 467 aligns to "C" in entry P26313 (individually applies "Zinc 1")
    • Subsequence at position 469 - 469 aligns to "C" in entry P26313 (individually applies "Zinc 1")
    • Subsequence at position 447 - 447 aligns to "H" in entry P26313 (individually applies "Zinc 2; via tele nitrogen")
    • Subsequence at position 57 - 57 aligns to "C" in entry P26313 (individually applies "Zinc 1")
    • Subsequence at position 207 - 213 aligns to "C-x*-C" in entry P26313 (individually applies "")
    • Subsequence at position 301 - 310 aligns to "C-x*-C" in entry P26313 (individually applies "")
    • Subsequence at position 59 - 424 aligns to entry P26313 (individually applies "Extracellular")
    • Subsequence at position 2 - 17 aligns to entry P26313 (individually applies "Extracellular")

... 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:
    Pre-glycoprotein polyprotein GP complex
    Short name:
    Pre-GP-C

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

  • Cleaved chain:
    Recommended name:
    Stable signal peptide
    Short name:
    SSP
  • Cleaved chain:
    Recommended name:
    Glycoprotein G1
    Short name:
    GP1
  • Cleaved chain:
    Recommended name:
    Glycoprotein G2
    Short name:
    GP2

<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:GPC

<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 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

  • Glycoprotein G1: interacts with the host receptor.
  • Glycoprotein G2: class I viral fusion protein that directs fusion of viral and host endosomal membranes, leading to delivery of the nucleocapsid into the cytoplasm. Membrane fusion is mediated by irreversible conformational changes induced upon acidification in the endosome.
  • Stable signal peptide (SSP): cleaved and functions as a signal peptide. In addition, it is also retained as the third component of the GP complex. The SSP is required for efficient glycoprotein expression, post-translational maturation cleavage of GP1 and GP2, glycoprotein transport to the cell surface plasma membrane, formation of infectious virus particles, and acid pH-dependent glycoprotein-mediated cell fusion.

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

  • The cytoplasmic domain of GP2 plays a role in ER location. It also contains a zinc-binding domain that allows SSP retention in the GPC complex by accepting a cysteine from SSP as the fourth ligand.

<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. GP-C polyprotein is cleaved in the endoplasmic reticulum by the host protease MBTPS1. Only cleaved glycoprotein is incorporated into virions.
  • The SSP remains stably associated with the GP complex following cleavage by signal peptidase and plays crucial roles in the trafficking of GP through the secretory pathway.

<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

  • Glycoprotein G1: homotetramer; disulfide-linked. Glycoprotein G2: homotetramer. GP2 homotetramers bind through ionic interactions with GP1 homotetramers to form the GP complex together with the stable signal peptide. The GP-C polyprotein interacts with the host protease MBTPS1/SKI-1 resulting in the polyprotein processing.

<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 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; by host MBTPS1 (to residues corresponding to positions 251 - 252)
  • Cleavage; by host signal peptidase (to residues corresponding to positions 58 - 59)

<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 54 - 58)
  • Cytoplasmic (to residues corresponding to position 33)
  • Cytoplasmic (to residues corresponding to positions 446 - @CTER@i)
  • Extracellular (to residues corresponding to positions 59 - 424)
  • Extracellular (to residues corresponding to positions 2 - 17)

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methioninei

  • Removed; by host (to residues corresponding to position 1)

<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 279 - 292)
  • (to residues corresponding to positions 135 - 164)
  • (to residues corresponding to positions 118 - 155)
  • (to residues corresponding to positions 180 - 212)
  • (to residues corresponding to positions 92 - 226)
  • (to residues corresponding to positions 364 - 385)
  • (to residues corresponding to positions 207 - 213)
  • (to residues corresponding to positions 301 - 310)

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi

  • N-myristoyl glycine; by host (to residues corresponding to position 2)

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi

  • Zinc 1; via pros nitrogen (to residues corresponding to position 459)
  • Zinc 2; via tele nitrogen (to residues corresponding to position 485)
  • Zinc 2 (to residues corresponding to position 455)
  • Zinc 2; via tele nitrogen (to residues corresponding to position 449)
  • Zinc 1 (to residues corresponding to position 467)
  • Zinc 1 (to residues corresponding to position 469)
  • Zinc 2; via tele nitrogen (to residues corresponding to position 447)
  • Zinc 1 (to residues corresponding to position 57)

<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

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