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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

Protein namei

  • Recommended name:
    Neuraminidase (EC:3.2.1.18)

Gene namei

  • Name:NA

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.

Post-translational modificationi

  • N-glycosylated.

Subunit structurei

  • Homotetramer.

Cofactori

Catalytic activityi

  • Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-(2->8)- glycosidic linkages of terminal sialic acid residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates.

Sequence similaritiesi

Subcellular locationi

Enzyme 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.

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.

Transmembranei

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

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)

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)

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)

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)

Active sitei

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

Keywordsi

GO (Gene Ontology) termsi

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