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Q6DPI6

- NRAM_I02A7

UniProt

Q6DPI6 - NRAM_I02A7

Protein

Neuraminidase

Gene

NA

Organism
Influenza A virus (strain A/Teal/China/2978.1/2002 H5N1 genotype W)
Status
Reviewed - Annotation score: 5 out of 5- Protein inferred from homologyi
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    • History
      Entry version 57 (01 Oct 2014)
      Sequence version 2 (22 Jul 2008)
      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 sitei103 – 1031SubstrateBy similarity
    Active sitei136 – 1361Proton donor/acceptorBy similarity
    Binding sitei137 – 1371SubstrateBy similarity
    Binding sitei278 – 2781SubstrateBy similarity
    Metal bindingi279 – 2791Calcium; via carbonyl oxygenBy similarity
    Metal bindingi283 – 2831Calcium; via carbonyl oxygenBy similarity
    Metal bindingi309 – 3091CalciumBy similarity
    Binding sitei353 – 3531SubstrateBy similarity
    Active sitei387 – 3871NucleophileBy 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/Teal/China/2978.1/2002 H5N1 genotype W)
    Taxonomic identifieri284215 [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
    Chaini‹1 – 454›454NeuraminidasePRO_0000310940Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi43 – 431N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi48 – 481N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi53 – 531N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi73 – 731N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi77 ↔ 402By similarity
    Disulfide bondi109 ↔ 114By similarity
    Glycosylationi131 – 1311N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi169 ↔ 216By similarity
    Disulfide bondi218 ↔ 223By similarity
    Glycosylationi220 – 2201N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi264 ↔ 277By similarity
    Disulfide bondi266 ↔ 275By similarity
    Disulfide bondi303 ↔ 320By similarity
    Disulfide bondi406 ↔ 431By similarity

    Post-translational modificationi

    N-glycosylated.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Interactioni

    Subunit structurei

    Homotetramer.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliQ6DPI6.
    SMRiQ6DPI6. Positions 68-452.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini14 – 454441Virion surfaceSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei‹1 – 13›13HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni21 – 7555Hypervariable stalk regionBy similarityAdd
    BLAST
    Regioni76 – 454379Head of neuraminidaseBy similarityAdd
    BLAST
    Regioni262 – 2632Substrate 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: Fragment.

    Q6DPI6-1 [UniParc]FASTAAdd to Basket

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    VIGIVSLMLQ IGNIISIWVS HSIQTGNQHQ AEPCIQSIIT YENNTWVNQT    50
    YVNISNTNFL TEKTVASVTL AGNSSLCPIS GWAVYSKDNG IRIGSKGDVF 100
    VIREPFISCS HLECRTFFLT QGALLNDKHS NGTVKDRSPH RTLMSCPVGE 150
    APSPYNSRFE SVAWSASACH DGTNWLTIGI SGPDNGAVAV LKYNGIITDT 200
    IKSWRNNILR TQESECACVN GSCFTVMTDG PSNGQASYKI FRIEKGKVVK 250
    SVELNAPNYH YEECSCYPDA GEITCVCRDN WHGSNRPWVS FNQNLEYQIG 300
    YICSGIFGDN PRPNDGTGSC GPVSSNGAYG IKGFSYKYGN GVWIGRTKST 350
    NSRSGFEMIW DPNGWTGTDS NFSVKQDIVA ITDWSGYSGS FVQHPELTGL 400
    DCIRPCFWVE LIRGRPKEST IWTSGSSISF CGVNSDTVGW SWPDGAELPF 450
    TIDK 454
    Length:454
    Mass (Da):49,799
    Last modified:July 22, 2008 - v2
    Checksum:i09163590DFA4E0F0
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-terminal residuei1 – 11

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY651473 Genomic RNA. Translation: AAT73355.2.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY651473 Genomic RNA. Translation: AAT73355.2 .

    3D structure databases

    ProteinModelPortali Q6DPI6.
    SMRi Q6DPI6. Positions 68-452.
    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. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    2. Cited for: SEQUENCE REVISION.

    Entry informationi

    Entry nameiNRAM_I02A7
    AccessioniPrimary (citable) accession number: Q6DPI6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 13, 2007
    Last sequence update: July 22, 2008
    Last modified: October 1, 2014
    This is version 57 of the entry and version 2 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