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The annotation and conditions in this rule are derived from the following entries: Q76R62 (HBSAG_HBVCJ)

If a protein meets these conditions... i

Common conditions

Special conditions

    • Subsequence at position 120 - 174 aligns to entry Q76R62 (individually applies "Pre-S2")
    • Subsequence at position 203 - 253 aligns to entry Q76R62 (individually applies "Intravirion; in external conformation")
    • Subsequence at position 275 - 348 aligns to entry Q76R62 (individually applies "Virion surface")
    • Subsequence at position 370 - 375 aligns to entry Q76R62 (individually applies "Intravirion")
    • Subsequence at position 399 - @CTER@ aligns to entry Q76R62 (individually applies "Virion surface")
    • Subsequence at position @NTER@ - @NTER@ aligns to "M" in entry Q76R62 (individually applies "Removed; by host")
    • Subsequence at position @PLUS|@NTER|+1@ - 119 aligns to entry Q76R62 (individually applies "Pre-S1")
    • Subsequence at position @PLUS|@NTER|+1@ - 174 aligns to entry Q76R62 (individually applies "Pre-S")
    • Subsequence at position @PLUS|@NTER|+1@ - 181 aligns to entry Q76R62 (individually applies "Virion surface; in external conformation")
    • Subsequence at position @PLUS|@NTER|+1@ - 253 aligns to entry Q76R62 (individually applies "Intravirion; in internal conformation")
    • Subsequence at position @PLUS|@NTER|+1@ - @PLUS|@NTER|+1@ aligns to "G" in entry Q76R62 (individually applies "N-myristoyl glycine; by host")

... 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:
    Large envelope protein
    Alternative name(s):
    L-HBsAg
    Short name:
    LHB
    L glycoprotein
    Major surface antigen
    Large S protein
    Large surface protein

<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 ‘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 large envelope protein is synthesized with the pre-S region at the cytosolic side of the endoplasmic reticulum and, hence will be within the virion after budding. Therefore the pre-S region is not N-glycosylated. Later a post-translational translocation of N-terminal pre-S and TM1 domains occur in about 50% of proteins at the virion surface. These molecules change their topology by an unknown mechanism, resulting in exposure of pre-S region at virion surface. For isoform M in contrast, the pre-S2 region is translocated cotranslationally to the endoplasmic reticulum lumen and is N-glycosylated.

<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/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

  • Isoform M is N-terminally acetylated by host at a ratio of 90%, and N-glycosylated by host at the pre-S2 region.
  • Myristoylated.

<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 <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

  • Li-HBsAg interacts with capsid protein and with HDV Large delta antigen. Isoform M associates with host chaperone CANX through its pre-S2 N glycan. This association may be essential for M proper secretion.

<p>This section describes the function(s) of a protein.<p><a href='/help/function' target='_top'>More...</a></p>Functioni

  • The large envelope protein exists in two topological conformations, one which is termed 'external' or Le-HBsAg and the other 'internal' or Li-HBsAg. In its external conformation the protein attaches the virus to cell receptors and thereby initiating infection. This interaction determines the species specificity and liver tropism. This attachment induces virion internalization predominantly through caveolin-mediated endocytosis. The large envelope protein also assures fusion between virion membrane and endosomal membrane. In its internal conformation the protein plays a role in virion morphogenesis and mediates the contact with the nucleocapsid like a matrix protein.
  • The middle envelope protein plays an important role in the budding of the virion. It is involved in the induction of budding in a nucleocapsid independent way. In this process the majority of envelope proteins bud to form subviral lipoprotein particles of 22 nm of diameter that do not contain a nucleocapsid.

<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

  • Intravirion; in external conformation (to residues corresponding to positions 203 - 253)
  • Virion surface (to residues corresponding to positions 275 - 348)
  • Intravirion (to residues corresponding to positions 370 - 375)
  • Virion surface (to residues corresponding to positions 399 - @CTER@i)
  • Virion surface; in external conformation (to residues corresponding to positions @PLUS|@NTER|+1@i - 181)
  • Intravirion; in internal conformation (to residues corresponding to positions @PLUS|@NTER|+1@i - 253)

<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

  • Pre-S2 (to residues corresponding to positions 120 - 174)
  • Pre-S1 (to residues corresponding to positions @PLUS|@NTER|+1@i - 119)
  • Pre-S (to residues corresponding to positions @PLUS|@NTER|+1@i - 174)

<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 @PLUS|@NTER|+1@i)

<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 @NTER@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

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