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Q20NV8

- NRAM_I80AD

UniProt

Q20NV8 - NRAM_I80AD

Protein

Neuraminidase

Gene

NA

Organism
Influenza A virus (strain A/Gull/Minnesota/945/1980 H13N6)
Status
Reviewed - Annotation score: 5 out of 5- Protein inferred from homologyi
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    • History
      Entry version 48 (01 Oct 2014)
      Sequence version 1 (18 Apr 2006)
      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 sitei119 – 1191SubstrateBy similarity
    Active sitei152 – 1521Proton donor/acceptorBy similarity
    Binding sitei153 – 1531SubstrateBy similarity
    Binding sitei294 – 2941SubstrateBy similarity
    Metal bindingi295 – 2951Calcium; via carbonyl oxygenBy similarity
    Metal bindingi299 – 2991Calcium; via carbonyl oxygenBy similarity
    Metal bindingi326 – 3261CalciumBy similarity
    Binding sitei373 – 3731SubstrateBy similarity
    Active sitei407 – 4071NucleophileBy 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

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Neuraminidase (EC:3.2.1.18)
    Gene namesi
    Name:NA
    OrganismiInfluenza A virus (strain A/Gull/Minnesota/945/1980 H13N6)
    Taxonomic identifieri385597 [NCBI]
    Taxonomic lineageiVirusesssRNA negative-strand virusesOrthomyxoviridaeInfluenzavirus A
    Virus hostiAves [TaxID: 8782]
    ProteomesiUP000008581: Genome

    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 – 471471NeuraminidasePRO_0000280135Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi51 – 511N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi54 – 541N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi63 – 631N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi68 – 681N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi71 – 711N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi87 – 871N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi93 ↔ 420By similarity
    Disulfide bondi125 ↔ 130By similarity
    Glycosylationi147 – 1471N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi177 ↔ 195By similarity
    Disulfide bondi185 ↔ 232By similarity
    Glycosylationi202 – 2021N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi234 ↔ 239By similarity
    Disulfide bondi280 ↔ 293By similarity
    Disulfide bondi282 ↔ 291By similarity
    Disulfide bondi320 ↔ 338By similarity
    Glycosylationi403 – 4031N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi424 ↔ 450By similarity

    Post-translational modificationi

    N-glycosylated.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Interactioni

    Subunit structurei

    Homotetramer.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliQ20NV8.
    SMRiQ20NV8. Positions 83-471.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 66IntravirionSequence Analysis
    Topological domaini28 – 471444Virion 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 – 9156Hypervariable stalk regionBy similarityAdd
    BLAST
    Regioni92 – 471380Head of neuraminidaseBy similarityAdd
    BLAST
    Regioni278 – 2792Substrate 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.

    Q20NV8-1 [UniParc]FASTAAdd to Basket

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    MNPNQKIICI SATGMTLSVV SLLVGIANLG LNIGLHYKVG YTPDVNTPNV    50
    NGTNSTTTTI INNNTQNNFT NITNIIQNKN EERTFLNLTK PLCEVNSWHI 100
    LSKDNAIRIG EDANILVTRE PYLSCDPQGC RMFALSQGTT LKGRHANGTI 150
    HDRSPFRALV SWEMGQAPSP YNAKIECIGW SSTSCHDGIS RMSICMSGPN 200
    NNASAVVWYG GRPVTEIPSW AGNILRTQES ECVCHKGICP VVMTDGPANN 250
    KAATKIIYFK EGKIQKIEEL TGTAQHIEEC SCYGAKEVIK CICRDNWKGA 300
    NRPVITIDPD MMTHTSKYLC SKILTDTSRP NDPNNGNCDA PITGGGPDPG 350
    VKGFAFLDGE NSWLGRTISK DSRSGYEVLK VPNAETNTQS GPITHQIIVN 400
    NQNWSGYSGA FIDYWANKEC FNPCFYVELI RGRPKESSVL WTSNSIVALC 450
    GSRERLGSWS WHDGAEITYF K 471
    Length:471
    Mass (Da):51,775
    Last modified:April 18, 2006 - v1
    Checksum:iE43232C661501B40
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CY005860 Genomic RNA. Translation: ABB21764.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CY005860 Genomic RNA. Translation: ABB21764.1 .

    3D structure databases

    ProteinModelPortali Q20NV8.
    SMRi Q20NV8. Positions 83-471.
    ModBasei Search...
    MobiDBi Search...

    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. "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.
    3. "Neuraminidase inhibitors for influenza."
      Moscona A.
      N. Engl. J. Med. 353:1363-1373(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    4. "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_I80AD
    AccessioniPrimary (citable) accession number: Q20NV8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 6, 2007
    Last sequence update: April 18, 2006
    Last modified: October 1, 2014
    This is version 48 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.

    Keywords - Technical termi

    Complete proteome

    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