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[1]
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NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=A/WSN/33;
PubMed=7077751 [NCBI, ExPASy, EBI, Israel, Japan]
Hiti A.L.,
Nayak D.P.;
"Complete nucleotide sequence of the neuraminidase gene of human influenza virus A/WSN/33.";
J. Virol. 41:730-734(1982).
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[2]
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NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=A/NWS/33, A/WS/33, and A/WSN/33;
DOI=10.1007/BF01701815; PubMed=8560787 [NCBI, ExPASy, EBI, Israel, Japan]
Ward A.C.;
"Changes in the neuraminidase of neurovirulent influenza virus strains.";
Virus Genes 10:253-260(1995).
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[3]
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SUBCELLULAR LOCATION.
DOI=10.1128/JVI.74.14.6538-6545.2000; PubMed=10864667 [NCBI, ExPASy, EBI, Israel, Japan]
Barman S.,
Nayak D.P.;
"Analysis of the transmembrane domain of influenza virus neuraminidase, a type II transmembrane glycoprotein, for apical sorting and raft association.";
J. Virol. 74:6538-6545(2000).
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[4]
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FUNCTION.
STRAIN=A/WSN/33;
DOI=10.1128/JVI.79.18.11705-11715.2005; PubMed=16140748 [NCBI, ExPASy, EBI, Israel, Japan]
Suzuki T.,
Takahashi T.,
Guo C.T.,
Hidari K.I.,
Miyamoto D.,
Goto H.,
Kawaoka Y.,
Suzuki Y.;
"Sialidase activity of influenza A virus in an endocytic pathway enhances viral replication.";
J. Virol. 79:11705-11715(2005).
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[5]
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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).
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[6]
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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).
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[7]
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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).
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- 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.
- FUNCTION: Unlike other strains, A/WSN/33 neuraminidase binds and activates plasminogen into plasmin in the vicinity of HA so that activated plasmin cleaves HA rendering the virus infectious.
- 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.
- SUBCELLULAR LOCATION: Virion membrane. Apical cell membrane; Single-pass type II membrane protein. 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.
- 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.
- 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].
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Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms.
Distributed under the Creative Commons Attribution-NoDerivs License.
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| Length: 453 AA [This is the length of the unprocessed precursor] |
Molecular weight: 49687 Da [This is the MW of the unprocessed precursor] |
CRC64: 76E63E3A97D1EFEC [This is a checksum on the sequence] |
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10 20 30 40 50 60
MNPNQKIITI GSICMVVGII SLILQIGNII SIWISHSIQT GNQNHTGICN QGIITYNVVA
70 80 90 100 110 120
GQDSTSVILT GNSSLCPIRG WAIHSKDNGI RIGSKGDVFV IREPFISCSH LECRTFFLTQ
130 140 150 160 170 180
GALLNDKHSN GTVKDRSPYR ALMSCPVGEA PSPYNSRFES VAWSASACHD GMGWLTIGIS
190 200 210 220 230 240
GPDNGAVAVL KYNGIITETI KSWRKKILRT QESECTCVNG SCFTIMTDGP SNGLASYKIF
250 260 270 280 290 300
KIEKGKVTKS IELNAPNSHY EECSCYPDTG KVMCVCRDNW HGSNRPWVSF DQNLDYQIGY
310 320 330 340 350 360
ICSGVFGDNP RPKDGPGSCG PVSADGANGV KGFSYRYGNG VWIGRTKSDS SRHGFEMIWD
370 380 390 400 410 420
PNGWTETDSR FSVRQDVVAM TDRSGYSGSF VQHPELTGLD CMRPCFWVEL IRGRPEEETI
430 440 450
WTSGSIISFC GVNSDTVDWS WPDGAELPFT IDK
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P03470 in FASTA format |
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