Neuraminidase
Details
- Name
- Neuraminidase
- Synonyms
- 3.2.1.18
- Gene Name
- NA
- Organism
- Influenza A virus (strain A/Tokyo/3/1967 H2N2)
- Amino acid sequence
>lcl|BSEQ0011033|Neuraminidase MNPNQKIITIGSVSLTIATVCFLMQIAILVTTVTLHFKQHECDSPASNQVMPCEPIIIER NITEIVYLNNTTIEKEICPKVVEYRNWSKPQCQITGFAPFSKDNSIRLSAGGDIWVTREP YVSCDPVKCYQFALGQGTTLDNKHSNDTVHDRIPHRTLLMNELGVPFHLGTRQVCIAWSS SSCHDGKAWLHVCITGDDKNATASFIYDGRLVDSIGSWSQNILRTQESECVCINGTCTVV MTDGSASGRADTRILFIEEGKIVHISPLAGSAQHVEECSCYPRYPGVRCICRDNWKGSNR PVVDINMEDYSIDSSYVCSGLVGDTPRNDDRSSNSNCRNPNNERGTQGVKGWAFDNGNDL WMGRTISKDLRSGYETFKVIGGWSTPNSKSQINRQVIVDSDNRSGYSGIFSVEGKSCINR CFYVELIRGRKQETRVWWTSNSIVVFCGTSGTYGTGSWPDGANINFMPI
- Number of residues
- 469
- Molecular Weight
- 52130.36
- Theoretical pI
- 6.79
- GO Classification
- Functionsexo-alpha-(2->3)-sialidase activity / exo-alpha-(2->6)-sialidase activity / exo-alpha-(2->8)-sialidase activity / metal ion bindingProcessescarbohydrate metabolic processComponentshost cell plasma membrane / integral component of membrane / virion membrane
- General Function
- Metal ion binding
- 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 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.
- Pfam Domain Function
- Neur (PF00064)
- Transmembrane Regions
- 7-35
- Cellular Location
- Virion membrane
- Gene sequence
>lcl|BSEQ0002913|1410 bp ATGAATCCAAATCAAAAGATAATAACAATTGGCTCTGTCTCTCTCACCATTGCAACAGTA TGCTTTCTCATGCAGATTGCCATCTTGGTAACTACTGTAACATTGCACTTTAAGCAACAT GAGTGCGACTCCCCCGCGAGCAACCAAGTAATGCCGTGTGAACCAATAATAATAGAAAGG AACATAACAGAGATAGTGTATTTGAATAACACCACCATAGAGAAAGAGATATGCCCCAAA GTAGTGGAATACAGAAATTGGTCAAAGCCGCAATGTCAAATTACAGGATTTGCACCTTTT TCTAAGGACAATTCAATCCGGCTTTCTGCTGGTGGGGACATTTGGGTGACGAGAGAACCT TATGTGTCATGCGATCCTGTCAAGTGTTATCAATTTGCACTCGGGCAGGGGACCACACTA GACAACAAACATTCAAATGACACAGTACATGATAGAATCCCTCATCGAACCCTATTAATG AATGAGTTGGGTGTTCCATTTCACTTAGGAACCAGGCAAGTGTGTATAGCATGGTCCAGC TCAAGTTGTCACGATGGAAAAGCATGGCTGCATGTTTGTATCACTGGGGATGATAAAAAT GCAACTGCTAGCTTCATTTATGACGGGAGGCTTGTGGACAGTATTGGTTCATGGTCTCAA AATATCCTCAGAACCCAGGAGTCGGAATGCGTTTGTATCAATGGGACTTGCACAGTAGTA ATGACTGATGGAAGTGCTTCAGGAAGAGCCGATACTAGAATACTATTCATTGAAGAGGGG AAAATTGTCCATATTAGCCCATTGGCAGGAAGTGCTCAGCATGTAGAGGAGTGTTCCTGT TATCCTCGATATCCTGGCGTCAGATGTATCTGCAGAGACAACTGGAAAGGCTCTAATAGG CCCGTCGTAGACATAAATATGGAAGATTATAGCATTGATTCCAGTTATGTGTGCTCAGGG CTTGTTGGCGACACACCTAGAAACGATGACAGATCTAGCAATAGCAATTGCAGGAATCCT AACAATGAGAGAGGGACTCAAGGAGTGAAAGGCTGGGCCTTTGACAATGGAAATGACTTG TGGATGGGAAGAACAATCAGCAAGGATTTACGCTCAGGTTATGAAACTTTCAAAGTCATT GGTGGTTGGTCCACACCTAATTCCAAATCGCAGATCAATAGACAAGTCATAGTTGACAGT GATAATCGGTCAGGTTACTCTGGTATTTTCTCTGTTGAGGGCAAAAGCTGCATCAATAGG TGCTTTTATGTGGAGTTGATAAGGGGAAGGAAACAGGAGACTAGAGTATGGTGGACCTCA AACAGTATTGTTGTGTTTTGTGGCACTTCAGGTACCTATGGAACAGGCTCATGGCCTGAT GGGGCGAACATCAATTTCATGCCTATATAA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P06820 UniProtKB Entry Name NRAM_I67A0 GenBank Protein ID 1480200 GenBank Gene ID K01393 - General References
- Lentz MR, Air GM, Laver WG, Webster RG: Sequence of the neuraminidase gene of influenza virus A/Tokyo/3/67 and previously uncharacterized monoclonal variants. Virology. 1984 May;135(1):257-65. [Article]
- Lindstrom SE, Cox NJ, Klimov A: Genetic analysis of human H2N2 and early H3N2 influenza viruses, 1957-1972: evidence for genetic divergence and multiple reassortment events. Virology. 2004 Oct 10;328(1):101-19. [Article]
- Nayak DP, Hui EK, Barman S: Assembly and budding of influenza virus. Virus Res. 2004 Dec;106(2):147-65. [Article]
- Moscona A: Neuraminidase inhibitors for influenza. N Engl J Med. 2005 Sep 29;353(13):1363-73. [Article]
- Suzuki Y: Sialobiology of influenza: molecular mechanism of host range variation of influenza viruses. Biol Pharm Bull. 2005 Mar;28(3):399-408. [Article]
- Varghese JN, Colman PM: Three-dimensional structure of the neuraminidase of influenza virus A/Tokyo/3/67 at 2.2 A resolution. J Mol Biol. 1991 Sep 20;221(2):473-86. [Article]
- White CL, Janakiraman MN, Laver WG, Philippon C, Vasella A, Air GM, Luo M: A sialic acid-derived phosphonate analog inhibits different strains of influenza virus neuraminidase with different efficiencies. J Mol Biol. 1995 Feb 3;245(5):623-34. [Article]
- Jedrzejas MJ, Singh S, Brouillette WJ, Laver WG, Air GM, Luo M: Structures of aromatic inhibitors of influenza virus neuraminidase. Biochemistry. 1995 Mar 14;34(10):3144-51. [Article]
Drug Relations
- Drug Relations
DrugBank ID Name Drug group Pharmacological action? Actions Details DB02268 4-(Acetylamino)-3-Amino Benzoic Acid experimental unknown Details DB02829 4-(Acetylamino)-3-[(Aminoacetyl)Amino]Benzoic Acid experimental unknown Details DB04565 4-(Acetylamino)-3-[(Hydroxyacetyl)Amino]Benzoic Acid experimental unknown Details DB08570 4-(ACETYLAMINO)-3-HYDROXY-5-NITROBENZOIC ACID experimental unknown Details DB08571 4-(ACETYLAMINO)-5-AMINO-3-HYDROXYBENZOIC ACID experimental unknown Details