|
|
|
|
|
|
[1]
|
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
DOI=10.1093/nar/10.16.5033; PubMed=6752886 [NCBI, ExPASy, EBI, Israel, Japan]
Bentley D.R.,
Brownlee G.G.;
"Sequence of the N2 neuraminidase from influenza virus A/NT/60/68.";
Nucleic Acids Res. 10:5033-5042(1982).
|
[2]
|
REVIEW.
DOI=10.1016/j.virusres.2004.08.012; PubMed=15567494 [NCBI, ExPASy, EBI, Israel, Japan]
Nayak D.P.,
Hui E.K.,
Barman S.;
"Assembly and budding of influenza virus.";
Virus Res. 106:147-165(2004).
|
[3]
|
REVIEW.
DOI=10.1056/NEJMra050740; PubMed=16192481 [NCBI, ExPASy, EBI, Israel, Japan]
Moscona A.;
"Neuraminidase inhibitors for influenza.";
N. Engl. J. Med. 353:1363-1373(2005).
|
[4]
|
REVIEW.
DOI=10.1248/bpb.28.399; PubMed=15744059 [NCBI, ExPASy, EBI, Israel, Japan]
Suzuki Y.;
"Sialobiology of influenza: molecular mechanism of host range variation of influenza viruses.";
Biol. Pharm. Bull. 28:399-408(2005).
|
|
|
|
- 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 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.
- 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: Binds 1 calcium ion (By similarity).
- ENZYME REGULATION: 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 (By similarity).
- SUBCELLULAR LOCATION: Virion membrane (By similarity). Apical cell membrane; Single-pass type II membrane protein (By similarity). Note=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 (By similarity).
- DOMAIN: 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 (By similarity).
- PTM: N-glycosylated (By similarity).
- MISCELLANEOUS: The influenza A genome consist 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 [view classification].
|
|
|
|
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms.
Distributed under the Creative Commons Attribution-NoDerivs License.
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
| Length: 469 AA [This is the length of the unprocessed precursor] |
Molecular weight: 52143 Da [This is the MW of the unprocessed precursor] |
CRC64: 5BF69A81412F7DE6 [This is a checksum on the sequence] |
|
10 20 30 40 50 60
MNPNQKIITI GSVSLTIATV CFLMQTAILV TTVTLHFKQY ECDSPASNQV MPCEPIIIER
70 80 90 100 110 120
NITEIVYLNN TTIEKEICPK VVEYRNWSKP QCQITGFAPF SKDNSIRLSA GGDIWVTREP
130 140 150 160 170 180
YVSCDHGKCY QFALGQGTTL DNKHSNDTIH DRIPHRTLLM NELGVPFHLG TRQVCIAWSS
190 200 210 220 230 240
SSCHDGKAWL HVCITGDDKN ATASFIYDGR LVDSIGSWSQ NILRTQESEC VCINGTCTVV
250 260 270 280 290 300
MTDGSASGRA DTRILFIEEG KIVHISPLSG SAQHVEECSC YPRYPGVRCI CRDNWKGSNR
310 320 330 340 350 360
PVVDINMEDY SIDSSYVCSG LVGDTPRNDD RSSNSNCRNP NNERGNQGVK GWAFDNGDDV
370 380 390 400 410 420
WMGRTISKDL RSGYETFKVI GGWSTPNSKS QINRQVIVDS DNRSGYSGIF SVEGKSCINR
430 440 450 460
CFYVELIRGR KQEARVWWTS NSIVVFCGTS GTYGTGSWPD GANINFMPI
|
P03473 in FASTA format |
|
ExPASy Home page
SIB Switzerland
