UniProt:P03468 NA

chain
  • chain:1-454
checksum 7C52E0A9FD93A98B
comment
  • FUNCTION 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 moieties 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.CATALYTIC ACTIVITY 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.COFACTOR 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.SUBUNIT Homotetramer.SUBCELLULAR LOCATION Preferentially accumulates at the apical plasma membrane in infected polarized epithelial cells, which is the virus assembly site. Uses lipid rafts for cell surface transport and apical sorting. In the virion, forms a mushroom-shaped spike on the surface of the membrane.DOMAIN Intact N-terminus is essential for virion morphogenesis. Possesses 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.PTM N-glycosylated.MISCELLANEOUS The influenza A genome consists of 8 RNA segments. Genetic variation of hemagglutinin and/or neuraminidase genes results in the emergence of new influenza strains. The mechanism of variation can be the result of point mutations or the result of genetic reassortment between segments of two different strains.SIMILARITY Belongs to the glycosyl hydrolase 34 family.
created [InstanceEdit:169110] Gillespie, ME, 2005-11-22 21:39:50
crossReference
databaseName UniProt
dbId 169106
description
  • recommendedName: fullName evidence="1"Neuraminidase ecNumber evidence="1"3.2.1.18
displayName UniProt:P03468 NA
geneName
  • NA
identifier P03468
isSequenceChanged false
keyword
  • 3D-structure
  • Calcium
  • Disulfide bond
  • Glycoprotein
  • Glycosidase
  • Host cell membrane
  • Host membrane
  • Hydrolase
  • Membrane
  • Metal-binding
  • Reference proteome
  • Signal-anchor
  • Transmembrane
  • Transmembrane helix
  • Virion
modified [InstanceEdit:9983091] Weiser, Joel, 2026-02-20
moleculeType Protein
name
  • NA
physicalEntity
referenceDatabase [ReferenceDatabase:2] UniProt
referenceGene
referenceTranscript
schemaClass ReferenceGeneProduct
secondaryIdentifier
  • NRAM_I34A1
  • A4GXH6
  • Q20N35
  • Q84043
  • Q8JUU4
sequenceLength 454
species [Species:9031716] Influenza A virus
stId uniprot:P03468
url http://purl.uniprot.org/uniprot/P03468
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