| Identification |
|---|
| HMDB Protein ID
| HMDBP14378 |
| 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 |
| viral budding from plasma membrane |
| carbohydrate metabolic process |
| Cellular Component |
| 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
| Not Available |
| Molecular Weight
| 52185.31 |
| Theoretical pI
| Not Available |
| Pfam Domain Function
|
|
| Signals
|
Not Available
|
|
Transmembrane Regions
|
|
| Protein Sequence
|
Not Available
|
| External Links |
|---|
| GenBank ID Protein
| Not Available |
| UniProtKB/Swiss-Prot ID
| Q75VQ4 |
| UniProtKB/Swiss-Prot Entry Name
| NRAM_I68A0 |
| PDB IDs
|
Not Available |
| GenBank Gene ID
| Not Available |
| GeneCard ID
| Not Available |
| GenAtlas ID
| Not Available |
| HGNC ID
| Not Available |
| References |
|---|
| General References
| - Moscona A: Neuraminidase inhibitors for influenza. N Engl J Med. 2005 Sep 29;353(13):1363-73. doi: 10.1056/NEJMra050740. [PubMed:16192481 ]
- 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 ]
- 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 ]
- Suzuki T, Takahashi T, Saito T, Guo CT, Hidari KI, Miyamoto D, Suzuki Y: Evolutional analysis of human influenza A virus N2 neuraminidase genes based on the transition of the low-pH stability of sialidase activity. FEBS Lett. 2004 Jan 16;557(1-3):228-32. doi: 10.1016/s0014-5793(03)01503-5. [PubMed:14741372 ]
|
