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The annotation and conditions in this rule are derived from the following entries: P06821 (M2_I34A1)

If a protein meets these conditions... i

Common conditions

Special conditions

    • Subsequence at position 20 - 20 aligns to "N" in entry P06821
    • Subsequence at position 20 - 20 aligns to "N" in entry P06821
    • Subsequence at position @NTER@ - 22 aligns to entry P06821 (individually applies "Virion surface")
    • Subsequence at position 41 - 41 aligns to "W" in entry P06821 (individually applies "Seems to be involved in pH gating")
    • Subsequence at position 50 - 50 aligns to "C" in entry P06821 (individually applies "S-palmitoyl cysteine; by host")
    • Subsequence at position 19 - 19 aligns to "C" in entry P06821 (individually applies "Interchain (with @RESIDUE_NAME_AT_POS|Cys|19|@)")
    • Subsequence at position 17 - 17 aligns to "C" in entry P06821 (individually applies "Interchain (with @RESIDUE_NAME_AT_POS|Cys|17|@)")
    • Subsequence at position 82 - 82 aligns to "S" in entry P06821 (individually applies "Phosphoserine; by host")
    • Subsequence at position 64 - 64 aligns to "S" in entry P06821 (individually applies "Phosphoserine; by host")
    • Subsequence at position 37 - 37 aligns to "H" in entry P06821 (individually applies "Essential for channel activity, possibly by being protonated during channel activation, and by forming the channel gate and the selective filter")
    • Subsequence at position 44 - @CTER@ aligns to entry P06821 (individually applies "Intravirion")
    • Subsequence at position 93 - 93 aligns to "S" in entry P06821 (individually applies "Phosphoserine; by host")

... then these annotations are applied i

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:
    Matrix protein 2
    Alternative name(s):
    Proton channel protein M2

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:M

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

  • Homotetramer; composed of two disulfide-linked dimers held together by non-covalent interactions. May interact with matrix protein 1.

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> describes the function(s) of a protein.<p><a href='/help/function' target='_top'>More...</a></p>Functioni

  • Forms a proton-selective ion channel that is necessary for the efficient release of the viral genome during virus entry. After attaching to the cell surface, the virion enters the cell by endocytosis. Acidification of the endosome triggers M2 ion channel activity. The influx of protons into virion interior is believed to disrupt interactions between the viral ribonucleoprotein (RNP), matrix protein 1 (M1), and lipid bilayers, thereby freeing the viral genome from interaction with viral proteins and enabling RNA segments to migrate to the host cell nucleus, where influenza virus RNA transcription and replication occur. Also plays a role in viral proteins secretory pathway. Elevates the intravesicular pH of normally acidic compartments, such as trans-Golgi network, preventing newly formed hemagglutinin from premature switching to the fusion-active conformation.

<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 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 'Function' section describes relevant information that doesn't fall into the scope of any other subsections, but is thought to be valuable enough to be cited in UniProtKB.<p><a href='/help/miscellaneous' target='_top'>More...</a></p>Miscellaneousi

  • When the channel is activated, one or more imidazole moities of @RESIDUE_NAME_AT_POS|His|37|@i probably become bi-protonated.

<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

  • Cytoplasmic tail plays an important role in virion assembly and morphogenesis.

<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei

  • Phosphoserine; by host (to residues corresponding to position 82)
  • Phosphoserine; by host (to residues corresponding to position 64)
  • Phosphoserine; by host (to residues corresponding to position 93)

<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

  • Seems to be involved in pH gating (to residues corresponding to position 41)
  • Essential for channel activity, possibly by being protonated during channel activation, and by forming the channel gate and the selective filter (to residues corresponding to position 37)

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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

  • S-palmitoyl cysteine; by host (to residues corresponding to position 50)

<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'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

  • Virion surface (to residues corresponding to positions @NTER@i - 22)
  • Intravirion (to residues corresponding to positions 44 - @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

  • Interchain (with @RESIDUE_NAME_AT_POS|Cys|19|@i) (to residues corresponding to position 19)
  • Interchain (with @RESIDUE_NAME_AT_POS|Cys|17|@i) (to residues corresponding to position 17)

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi

  • N-linked (GlcNAc...) asparagine; by host (to residues corresponding to position 20)

<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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