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The annotation and conditions in this rule are derived from the following entries: P03468 (NRAM_I34A1), P27907 (NRAM_INBBE)

If a protein meets these conditions... i

Common conditions

Special conditions

    • Subsequence at position 11 - 33 aligns to entry P03468 (individually applies "Involved in apical transport and lipid raft association")
    • Subsequence at position 36 - 75 aligns to entry P03468 (individually applies "Hypervariable stalk region")
    • Subsequence at position 76 - @CTER@ aligns to entry P03468 (individually applies "Head of neuraminidase")
    • Subsequence at position 77 - 402 aligns to "C-x*-C" in entry P03468 (individually applies "")
    • Subsequence at position 103 - 103 aligns to "R" in entry P03468 (individually applies "Substrate")
    • Subsequence at position 109 - 114 aligns to "C-x*-C" in entry P03468 (individually applies "")
    • Subsequence at position 136 - 136 aligns to "D" in entry P03468 (individually applies "Proton donor/acceptor")
    • Subsequence at position 137 - 137 aligns to "R" in entry P03468 (individually applies "Substrate")
    • Subsequence at position 169 - 216 aligns to "C-x*-C" in entry P03468 (individually applies "")
    • Subsequence at position 218 - 223 aligns to "C-x*-C" in entry P03468 (individually applies "")
    • Subsequence at position 262 - 263 aligns to "E-E" in entry P03468 (individually applies "Substrate binding")
    • Subsequence at position 264 - 277 aligns to "C-x*-C" in entry P03468 (individually applies "")
    • Subsequence at position 266 - 275 aligns to "C-x*-C" in entry P03468 (individually applies "")
    • Subsequence at position 278 - 278 aligns to "R" in entry P03468 (individually applies "Substrate")
    • Subsequence at position 279 - 279 aligns to "D" in entry P03468 (individually applies "Calcium; via carbonyl oxygen")
    • Subsequence at position 283 - 283 aligns to "G" in entry P03468 (individually applies "Calcium; via carbonyl oxygen")
    • Subsequence at position 303 - 320 aligns to "C-x*-C" in entry P03468 (individually applies "")
    • Subsequence at position 309 - 309 aligns to "D" in entry P03468 (individually applies "Calcium")
    • Subsequence at position 329 - 329 aligns to "N" in entry P03468 (individually applies "Calcium; via carbonyl oxygen")
    • Subsequence at position 353 - 353 aligns to "R" in entry P03468 (individually applies "Substrate")
    • Subsequence at position 387 - 387 aligns to "Y" in entry P03468 (individually applies "Nucleophile")
    • Subsequence at position 406 - 431 aligns to "C-x*-C" in entry P03468 (individually applies "")
    • Predicted transmembrane

... 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:
    Neuraminidase (EC:3.2.1.18)

<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:NA

<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

  • Intact N-terminus is essential for virion morphogenesis. Possess two apical sorting signals, one in the ectodomain, which is likely to be a glycan, and the other in the transmembrane domain. The transmembrane domain also plays a role in lipid raft association.

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

  • Inhibited by the neuraminidase inhibitors zanamivir (Relenza) and oseltamivir (Tamiflu). These drugs interfere with the release of progeny virus from infected cells and are effective against all influenza strains. Resistance to neuraminidase inhibitors is quite rare.

<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 provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

<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

  • Homotetramer.

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

  • Catalyzes the removal of terminal sialic acid residues from viral and cellular glycoconjugates. Cleaves off the terminal sialic acids on the glycosylated HA during virus budding to facilitate virus release. Additionally helps virus spread through the circulation by further removing sialic acids from the cell surface. These cleavages prevent self-aggregation and ensure the efficient spread of the progeny virus from cell to cell. Otherwise, infection would be limited to one round of replication. Described as a receptor-destroying enzyme because it cleaves a terminal sialic acid from the cellular receptors. May facilitate viral invasion of the upper airways by cleaving the sialic acid moities on the mucin of the airway epithelial cells. Likely to plays a role in the budding process through its association with lipid rafts during intracellular transport. May additionally display a raft-association independent effect on budding. Plays a role in the determination of host range restriction on replication and virulence. Sialidase activity in late endosome/lysosome traffic seems to enhance virus replication.

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<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

  • N-glycosylated.

<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 ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei

  • Proton donor/acceptor (to residues corresponding to position 136)
  • Nucleophile (to residues corresponding to position 387)

<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei

  • Substrate (to residues corresponding to position 103)
  • Substrate (to residues corresponding to position 137)
  • Substrate (to residues corresponding to position 278)
  • Substrate (to residues corresponding to position 353)

<p>This subsection of the ‘Function’ 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

  • Calcium; via carbonyl oxygen (to residues corresponding to position 279)
  • Calcium; via carbonyl oxygen (to residues corresponding to position 283)
  • Calcium (to residues corresponding to position 309)
  • Calcium; via carbonyl oxygen (to residues corresponding to position 329)

<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

  • Involved in apical transport and lipid raft association (to residues corresponding to positions 11 - 33)
  • Hypervariable stalk region (to residues corresponding to positions 36 - 75)
  • Head of neuraminidase (to residues corresponding to positions 76 - @CTER@i)
  • Substrate binding (to residues corresponding to positions 262 - 263)

<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 77 - 402)
  • (to residues corresponding to positions 109 - 114)
  • (to residues corresponding to positions 169 - 216)
  • (to residues corresponding to positions 218 - 223)
  • (to residues corresponding to positions 264 - 277)
  • (to residues corresponding to positions 266 - 275)
  • (to residues corresponding to positions 303 - 320)
  • (to residues corresponding to positions 406 - 431)
  • (to residues corresponding to positions 86 - 419)

<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei

  • Helical (to residues corresponding to positions @FROM@i - @TO@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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