Neuraminidase
Details
- Name
- Neuraminidase
- Kind
- protein
- Synonyms
- 3.2.1.18
- Gene Name
- NA
- UniProtKB Entry
- P03472Swiss-Prot
- Organism
- Influenza A virus (strain A/Tern/Australia/G70C/1975 H11N9)
- NCBI Taxonomy ID
- 384509
- Amino acid sequence
>lcl|BSEQ0011188|Neuraminidase MNPNQKILCTSATALVIGTIAVLIGITNLGLNIGLHLKPSCNCSHSQPEATNASQTIINN YYNDTNITQISNTNIQVEERAIRDFNNLTKGLCTINSWHIYGKDNAVRIGEDSDVLVTRE PYVSCDPDECRFYALSQGTTIRGKHSNGTIHDRSQYRALISWPLSSPPTVYNSRVECIGW SSTSCHDGKTRMSICISGPNNNASAVIWYNRRPVTEINTWARNILRTQESECVCHNGVCP VVFTDGSATGPAETRIYYFKEGKILKWEPLAGTAKHIEECSCYGERAEITCTCRDNWQGS NRPVIRIDPVAMTHTSQYICSPVLTDNPRPNDPTVGKCNDPYPGNNNNGVKGFSYLDGVN TWLGRTISIASRSGYEMLKVPNALTDDKSKPTQGQTIVLNTDWSGYSGSFMDYWAEGECY RACFYVELIRGRPKEDKVWWTSNSIVSMCSSTEFLGQWDWPDGAKIEYFL
- Number of residues
- 470
- Molecular Weight
- 52468.405
- Theoretical pI
- 6.57
- 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
- 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.
- Specific Function
- exo-alpha-(2->3)-sialidase activity
- Pfam Domain Function
- Neur (PF00064)
- Signal Regions
- Not Available
- Transmembrane Regions
- 7-35
- Cellular Location
- Virion membrane
- Gene sequence
>lcl|BSEQ0003306|1413 bp ATGAATCCAAATCAGAAGATTCTATGCACTTCTGCCACTGCTCTCGTAATAGGCACAATT GCAGTACTCATAGGAATAACGAACTTAGGATTGAACATAGGACTACATCTGAAACCGAGC TGCAATTGCTCACACTCACAACCCGAAGCAACCAATGCAAGCCAAACAATAATAAATAAC TATTATAATGACACAAACATCACCCAGATAAGTAATACCAACATTCAGGTAGAGGAAAGG GCAATTAGAGATTTCAATAACTTGACCAAAGGGCTCTGTACTATAAATTCATGGCACATA TATGGGAAAGACAATGCGGTGAGAATTGGGGAGGACTCAGATGTTTTAGTCACAAGAGAA CCCTATGTCTCCTGTGACCCAGATGAGTGCAGGTTCTATGCTCTCAGCCAAGGGACAACA ATCAGAGGAAAACACTCAAATGGAACAATACACGATAGGTCTCAATATCGTGCCCTGATA AGCTGGCCATTGTCATCACCGCCCACAGTATACAACAGCAGAGTGGAATGCATTGGATGG TCAAGTACTAGTTGTCATGATGGCAAAACCAGGATGTCAATATGCATATCAGGCCCGAAC AATAACGCATCAGCAGTGATCTGGTACAATAGAAGGCCTGTGACAGAAATCAACACATGG GCCCGAAACATACTAAGGACACAAGAATCTGAATGCGTATGCCACAACGGTGTCTGCCCG GTAGTGTTCACAGATGGGTCTGCCACTGGACCTGCAGAAACAAGAATATACTATTTTAAA GAAGGGAAGATCTTAAAATGGGAACCTCTGGCTGGAACTGCTAAGCATATCGAAGAATGC TCATGCTACGGAGAGCGAGCAGAGATTACTTGCACGTGTAGGGATAATTGGCAAGGCTCA AATAGACCAGTAATTCGGATAGATCCAGTGGCGATGACACATACTAGTCAGTATATATGT AGCCCTGTTCTCACAGATAACCCCCGACCGAATGACCCAACTGTAGGTAAGTGTAACGAC CCTTATCCAGGCAATAACAACAATGGGGTCAAAGGGTTTTCATATCTGGATGGAGTTAAT ACTTGGCTAGGGAGGACAATAAGCATAGCTTCAAGATCCGGATATGAGATGCTAAAGGTG CCAAATGCATTGACAGACGATAAGTCAAAGCCCACTCAAGGTCAGACAATCGTCTTAAAC ACTGACTGGAGTGGTTACAGTGGGTCCTTCATGGACTATTGGGCTGAGGGGGAATGCTAC CGAGCGTGTTTTTACGTGGAGTTAATACGTGGGAGACCTAAGGAGGATAAAGTGTGGTGG ACCAGTAATAGTATAGTATCGATGTGTTCCAGCACAGAATTCCTTGGACAATGGGACTGG CCTGATGGGGCTAAAATAGAGTACTTCCTCTAA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P03472 UniProtKB Entry Name NRAM_I75A5 GenBank Protein ID 324416 GenBank Gene ID M11445 PDB ID(s) 1A14, 1BJI, 1F8B, 1F8C, 1F8D, 1F8E, 1INY, 1L7F, 1L7G, 1L7H, 1MWE, 1NCA, 1NCB, 1NCC, 1NMC, 1NNA, 1NNB, 1NNC, 1XOE, 1XOG, 2C4A, 2C4L, 2QWA, 2QWB, 2QWC, 2QWD, 2QWE, 2QWF, 2QWG, 2QWH, 2QWI, 2QWJ, 2QWK, 3NN9, 3W09, 4DGR, 4NN9, 4WEG, 5NN9, 6NN9, 7NN9 - General References
- Air GM, Ritchie LR, Laver WG, Colman PM: Gene and protein sequence of an influenza neuraminidase with hemagglutinin activity. Virology. 1985 Aug;145(1):117-22. [Article]
- Air GM, Webster RG, Colman PM, Laver WG: Distribution of sequence differences in influenza N9 neuraminidase of tern and whale viruses and crystallization of the whale neuraminidase complexed with antibodies. Virology. 1987 Oct;160(2):346-54. [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]
- Baker AT, Varghese JN, Laver WG, Air GM, Colman PM: Three-dimensional structure of neuraminidase of subtype N9 from an avian influenza virus. Proteins. 1987;2(2):111-7. [Article]
- Bossart-Whitaker P, Carson M, Babu YS, Smith CD, Laver WG, Air GM: Three-dimensional structure of influenza A N9 neuraminidase and its complex with the inhibitor 2-deoxy 2,3-dehydro-N-acetyl neuraminic acid. J Mol Biol. 1993 Aug 20;232(4):1069-83. [Article]
- Varghese JN, Epa VC, Colman PM: Three-dimensional structure of the complex of 4-guanidino-Neu5Ac2en and influenza virus neuraminidase. Protein Sci. 1995 Jun;4(6):1081-7. [Article]
- Varghese JN, Colman PM, van Donkelaar A, Blick TJ, Sahasrabudhe A, McKimm-Breschkin JL: Structural evidence for a second sialic acid binding site in avian influenza virus neuraminidases. Proc Natl Acad Sci U S A. 1997 Oct 28;94(22):11808-12. [Article]
- Kim JH, Resende R, Wennekes T, Chen HM, Bance N, Buchini S, Watts AG, Pilling P, Streltsov VA, Petric M, Liggins R, Barrett S, McKimm-Breschkin JL, Niikura M, Withers SG: Mechanism-based covalent neuraminidase inhibitors with broad-spectrum influenza antiviral activity. Science. 2013 Apr 5;340(6128):71-5. doi: 10.1126/science.1232552. Epub 2013 Feb 21. [Article]
Associated Data
- Drug Relations
Drug Drug group Pharmacological action? Type Actions Details (2R,4S,5R,6R)-5-Acetamido-4-amino-6-(diethylcarbamoyl)oxane-2-carboxylic acid experimental unknown target Details Oseltamivir acid experimental unknown target Details 5-[1-(Acetylamino)-3-Methylbutyl]-2,5-Anhydro-3,4-Dideoxy-4-(Methoxycarbonyl)Pentonic Acid experimental unknown target Details Des(carbamimidoyl) zanamivir experimental unknown target Details 2,4-deoxy-4-guanidino-5-N-acetyl-neuraminic acid experimental unknown target Details 4-Acetyl-4-guanidino-6-methyl(propyl)carboxamide-4,5-dihydro-2H-pyran-2-carboxylic acid experimental unknown target Details Peramivir approved, investigational yes target Details N-acetyl-alpha-neuraminic acid experimental unknown target Details 2-deoxy-2,3-dehydro-N-acetylneuraminic acid experimental unknown target Details 9-Amino-2-deoxy-2,3-dehydro-n-acetyl-neuraminic acid experimental unknown target Details