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Q9WAA1

- NRAM_I97A0

UniProt

Q9WAA1 - NRAM_I97A0

Protein

Neuraminidase

Gene

NA

Organism
Influenza A virus (strain A/Chicken/Hong Kong/220/1997 H5N1 genotype Gs/Gd)
Status
Reviewed - Annotation score: 5 out of 5- Protein inferred from homologyi
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    • History
      Entry version 77 (01 Oct 2014)
      Sequence version 1 (01 Nov 1999)
      Previous versions | rss
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    Functioni

    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 activityi

    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.

    Cofactori

    Binds 1 calcium ion per subunit.By similarity

    Enzyme regulationi

    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.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei99 – 991SubstrateBy similarity
    Active sitei132 – 1321Proton donor/acceptorBy similarity
    Binding sitei133 – 1331SubstrateBy similarity
    Binding sitei274 – 2741SubstrateBy similarity
    Metal bindingi275 – 2751Calcium; via carbonyl oxygenBy similarity
    Metal bindingi279 – 2791Calcium; via carbonyl oxygenBy similarity
    Metal bindingi305 – 3051CalciumBy similarity
    Binding sitei349 – 3491SubstrateBy similarity
    Active sitei383 – 3831NucleophileBy similarity

    GO - Molecular functioni

    1. exo-alpha-(2->3)-sialidase activity Source: UniProtKB-EC
    2. exo-alpha-(2->6)-sialidase activity Source: UniProtKB-EC
    3. exo-alpha-(2->8)-sialidase activity Source: UniProtKB-EC
    4. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. carbohydrate metabolic process Source: InterPro

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Ligandi

    Calcium, Metal-binding

    Protein family/group databases

    CAZyiGH34. Glycoside Hydrolase Family 34.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Neuraminidase (EC:3.2.1.18)
    Gene namesi
    Name:NA
    OrganismiInfluenza A virus (strain A/Chicken/Hong Kong/220/1997 H5N1 genotype Gs/Gd)
    Taxonomic identifieri100834 [NCBI]
    Taxonomic lineageiVirusesssRNA negative-strand virusesOrthomyxoviridaeInfluenzavirus A
    Virus hostiAves [TaxID: 8782]
    Felis catus (Cat) (Felis silvestris catus) [TaxID: 9685]
    Homo sapiens (Human) [TaxID: 9606]
    Panthera pardus (Leopard) (Felis pardus) [TaxID: 9691]
    Panthera tigris (Tiger) [TaxID: 9694]
    Sus scrofa (Pig) [TaxID: 9823]

    Subcellular locationi

    Virion membrane By similarity. Host apical cell membrane By similarity; 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.By similarity

    GO - Cellular componenti

    1. host cell plasma membrane Source: UniProtKB-SubCell
    2. integral component of membrane Source: UniProtKB-KW
    3. virion membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Host cell membrane, Host membrane, Membrane, Virion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 450450NeuraminidasePRO_0000280123Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi50 – 501N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi69 – 691N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi73 ↔ 398By similarity
    Disulfide bondi105 ↔ 110By similarity
    Glycosylationi127 – 1271N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi165 ↔ 212By similarity
    Disulfide bondi214 ↔ 219By similarity
    Glycosylationi216 – 2161N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi260 ↔ 273By similarity
    Disulfide bondi262 ↔ 271By similarity
    Disulfide bondi299 ↔ 316By similarity
    Disulfide bondi402 ↔ 427By similarity

    Post-translational modificationi

    N-glycosylated.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Interactioni

    Subunit structurei

    Homotetramer.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliQ9WAA1.
    SMRiQ9WAA1. Positions 64-448.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 66IntravirionSequence Analysis
    Topological domaini28 – 450423Virion surfaceSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei7 – 2721Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni11 – 3323Involved in apical transport and lipid raft associationBy similarityAdd
    BLAST
    Regioni36 – 7136Hypervariable stalk regionBy similarityAdd
    BLAST
    Regioni72 – 450379Head of neuraminidaseBy similarityAdd
    BLAST
    Regioni258 – 2592Substrate bindingBy similarity

    Domaini

    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.By similarity

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 34 family.Curated

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Family and domain databases

    Gene3Di2.120.10.10. 1 hit.
    InterProiIPR001860. Glyco_hydro_34.
    IPR011040. Sialidases.
    [Graphical view]
    PfamiPF00064. Neur. 1 hit.
    [Graphical view]
    SUPFAMiSSF50939. SSF50939. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q9WAA1-1 [UniParc]FASTAAdd to Basket

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    MNPNQKIITI GSICMVVGII SLMLQIGNII SVWVSHIIQT WHPNQPEPCN    50
    QSINFYTEQA AASVTLAGNS SLCPISGWAI YSKDNSIRIG SKGDVFVIRE 100
    PFISCSHLEC RTFFLTQGAL LNDKHSNGTV KDRSPYRTLM SCPVGEAPSP 150
    YKSRFESVAW SASACHDGIS WLTIGISGPD NGAVAVLKYN GIITDTIKSW 200
    RNNILRTQES ECACVNGSCF TVMTDGPSNE QASYKIFKIE KGRVVKSVEL 250
    NAPNYHYEEC SCYPDAGEIT CVCRDNWHGS NRPWVSFNQN LEYQIGYICS 300
    GVFGDSPRPN DGTGSCGPVS LNGAYGVKGF SFKYGNGVWI GRTKSTSSRS 350
    GFEMIWDPNG WTETDSSFSL KQDIIAITDW SGYSGSFIQH PELTGLNCMR 400
    PCFWVELIRG RPKEKTIWTS GSSISFCGVN SDTVGWSWPD GAELPFTIDK 450
    Length:450
    Mass (Da):49,531
    Last modified:November 1, 1999 - v1
    Checksum:i7E13E0EDE7A3CF3A
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti152 – 1521K → N.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF046081 Genomic RNA. Translation: AAC32079.1.
    AF098547 Genomic RNA. Translation: AAF02310.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF046081 Genomic RNA. Translation: AAC32079.1 .
    AF098547 Genomic RNA. Translation: AAF02310.1 .

    3D structure databases

    ProteinModelPortali Q9WAA1.
    SMRi Q9WAA1. Positions 64-448.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GH34. Glycoside Hydrolase Family 34.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    Gene3Di 2.120.10.10. 1 hit.
    InterProi IPR001860. Glyco_hydro_34.
    IPR011040. Sialidases.
    [Graphical view ]
    Pfami PF00064. Neur. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50939. SSF50939. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Comparisons of highly virulent H5N1 influenza A viruses isolated from humans and chickens from Hong Kong."
      Suarez D.L., Perdue M.L., Cox N., Rowe T., Bender C., Huang J., Swayne D.E.
      J. Virol. 72:6678-6688(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    2. "Rapid evolution of H5N1 influenza viruses in chickens in Hong Kong."
      Zhou N.N., Shortridge K.F., Claas E.C.J., Krauss S.L., Webster R.G.
      J. Virol. 73:3366-3374(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    3. "Assembly and budding of influenza virus."
      Nayak D.P., Hui E.K., Barman S.
      Virus Res. 106:147-165(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    4. "Neuraminidase inhibitors for influenza."
      Moscona A.
      N. Engl. J. Med. 353:1363-1373(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    5. "Sialobiology of influenza: molecular mechanism of host range variation of influenza viruses."
      Suzuki Y.
      Biol. Pharm. Bull. 28:399-408(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.

    Entry informationi

    Entry nameiNRAM_I97A0
    AccessioniPrimary (citable) accession number: Q9WAA1
    Secondary accession number(s): Q9PZN0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 6, 2007
    Last sequence update: November 1, 1999
    Last modified: October 1, 2014
    This is version 77 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programViral Protein Annotation Program

    Miscellaneousi

    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.

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3