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Showing Protein Neuraminidase (HMDBP14393)

IdentificationBiological propertiesGene propertiesProtein propertiesExternal linksReferencesXMLShow 0 metabolites
Identification
HMDB Protein ID HMDBP14393
Secondary Accession Numbers None
Name Neuraminidase
Synonyms Not Available
Gene Name NA
Protein Type Unknown
Biological Properties
General Function Not Available
Specific 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.
Pathways Not Available
Reactions Not Available
GO Classification
Biological Process
virion attachment to host cell
viral entry into host cell via membrane fusion with the plasma membrane
viral budding from plasma membrane
induction by virus of host immune response
intracellular transport of viral protein in host cell
uncoating of virus
viral genome packaging
viral release from host cell
virion assembly
carbohydrate metabolic process
receptor-mediated endocytosis of virus by host cell
Cellular Component
extracellular region
virion membrane
host cell plasma membrane
integral to membrane
Molecular Function
metal ion binding
exo-alpha-(2->3)-sialidase activity
exo-alpha-(2->6)-sialidase activity
exo-alpha-(2->8)-sialidase activity
Cellular Location Not Available
Gene Properties
Chromosome Location Not Available
Locus Not Available
SNPs Not Available
Gene Sequence Not Available
Protein Properties
Number of Residues 454
Molecular Weight 50120.235
Theoretical pI 7.136
Pfam Domain Function
Signals Not Available
Transmembrane Regions
  • 7-27;
Protein Sequence Not Available
GenBank ID Protein Not Available
UniProtKB/Swiss-Prot ID P03468
UniProtKB/Swiss-Prot Entry Name NRAM_I34A1
PDB IDs
GenBank Gene ID Not Available
GeneCard ID Not Available
GenAtlas ID Not Available
HGNC ID Not Available
References
General References
  1. Schickli JH, Flandorfer A, Nakaya T, Martinez-Sobrido L, Garcia-Sastre A, Palese P: Plasmid-only rescue of influenza A virus vaccine candidates. Philos Trans R Soc Lond B Biol Sci. 2001 Dec 29;356(1416):1965-73. [PubMed:11779399 ]
  2. de Wit E, Spronken MI, Bestebroer TM, Rimmelzwaan GF, Osterhaus AD, Fouchier RA: Efficient generation and growth of influenza virus A/PR/8/34 from eight cDNA fragments. Virus Res. 2004 Jul;103(1-2):155-61. [PubMed:15163504 ]
  3. Moscona A: Neuraminidase inhibitors for influenza. N Engl J Med. 2005 Sep 29;353(13):1363-73. doi: 10.1056/NEJMra050740. [PubMed:16192481 ]
  4. Nayak DP, Hui EK, Barman S: Assembly and budding of influenza virus. Virus Res. 2004 Dec;106(2):147-65. doi: 10.1016/j.virusres.2004.08.012. [PubMed:15567494 ]
  5. Suzuki Y: Sialobiology of influenza: molecular mechanism of host range variation of influenza viruses. Biol Pharm Bull. 2005 Mar;28(3):399-408. doi: 10.1248/bpb.28.399. [PubMed:15744059 ]
  6. Blok J, Air GM: Sequence variation at the 3' end of the neuraminidase gene from 39 influenza type A viruses. Virology. 1982 Sep;121(2):211-29. doi: 10.1016/0042-6822(82)90162-3. [PubMed:6927853 ]
  7. Fields S, Winter G, Brownlee GG: Structure of the neuraminidase gene in human influenza virus A/PR/8/34. Nature. 1981 Mar 19;290(5803):213-7. doi: 10.1038/290213a0. [PubMed:7010182 ]