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P67923

- NRAM_INBLN

UniProt

P67923 - NRAM_INBLN

Protein

Neuraminidase

Gene

NA

Organism
Influenza B virus (strain B/Leningrad/179/1986)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 57 (01 Oct 2014)
      Sequence version 1 (11 Oct 2004)
      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 By similarity.By similarity

    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 sitei115 – 1151SubstrateBy similarity
    Active sitei148 – 1481Proton donor/acceptorBy similarity
    Binding sitei149 – 1491SubstrateBy similarity
    Binding sitei291 – 2911SubstrateBy similarity
    Metal bindingi292 – 2921Calcium; via carbonyl oxygenBy similarity
    Metal bindingi296 – 2961Calcium; via carbonyl oxygenBy similarity
    Metal bindingi323 – 3231CalciumBy similarity
    Metal bindingi343 – 3431Calcium; via carbonyl oxygenBy similarity
    Metal bindingi345 – 3451Calcium; via carbonyl oxygenBy similarity
    Binding sitei373 – 3731SubstrateBy similarity
    Active sitei408 – 4081NucleophileBy 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

    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 B virus (strain B/Leningrad/179/1986)
    Taxonomic identifieri11536 [NCBI]
    Taxonomic lineageiVirusesssRNA negative-strand virusesOrthomyxoviridaeInfluenzavirus B
    Virus hostiHomo sapiens (Human) [TaxID: 9606]

    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. 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 – 465465NeuraminidasePRO_0000078733Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi55 – 551N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi63 – 631N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi86 ↔ 419By similarity
    Disulfide bondi121 ↔ 126By similarity
    Glycosylationi143 – 1431N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi181 ↔ 228By similarity
    Disulfide bondi230 ↔ 235By similarity
    Disulfide bondi276 ↔ 290By similarity
    Disulfide bondi278 ↔ 288By similarity
    Glycosylationi283 – 2831N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi294 – 2941N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi317 ↔ 336By similarity
    Disulfide bondi423 ↔ 446By similarity

    Post-translational modificationi

    N-glycosylated.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Interactioni

    Subunit structurei

    Homotetramer.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliP67923.
    SMRiP67923. Positions 76-465.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 66IntravirionSequence Analysis
    Topological domaini36 – 465430Virion surfaceSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei7 – 3529Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni39 – 6830Hypervariable stalk regionAdd
    BLAST
    Regioni69 – 465397Head of neuraminidaseAdd
    BLAST
    Regioni274 – 2752Substrate bindingBy 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.

    P67923-1 [UniParc]FASTAAdd to Basket

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    MLPSTIQTLT LFLTSGGVLL SLYVSASLSY LLYSDILLKF SPKITAPTMT    50
    LDCANASNVQ AVNRSATKEM TFLLPEPEWT YPRLSCQGST FQKALLISPH 100
    RFGEARGNSA PLIIREPFIA CGPKECKHFA LTHYAAQPGG YYNGTREDRN 150
    KLRHLISVKL GKIPTVENSI FHMAAWSGSA CHDGREWTYI GVDGPDSNAL 200
    IKIKYGEAYT DTYHSYANNI LRTQESACNC IGGDCYLMIT DGSASGISEC 250
    RFLKIREGRI IKEIFPTGRV EHTEECTCGF ASNKTIECAC RDNNYTAKRP 300
    FVKLNVETDT AEIRLMCTET YLDTPRPDDG SITGPCESNG DKGRGGIKGG 350
    FVHQRMASKI GRWYSRTMSK TERMGMELYV KYDGDPWTDS DALAPSGVMV 400
    SIKEPGWYSF GFEIKDKKCD VPCIGIEMVH DGGKKTWHSA ATAIYCLMGS 450
    GQLLWDTVTG VDMAL 465
    Length:465
    Mass (Da):51,382
    Last modified:October 11, 2004 - v1
    Checksum:iFD402484907888CA
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M30632 Genomic RNA. Translation: AAA43731.1.
    PIRiC46347.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M30632 Genomic RNA. Translation: AAA43731.1 .
    PIRi C46347.

    3D structure databases

    ProteinModelPortali P67923.
    SMRi P67923. Positions 76-465.
    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. "Antigenic, sequence, and crystal variation in influenza B neuraminidase."
      Air G.M., Laver W.G., Luo M., Stray S.J., Legrone G., Webster R.G.
      Virology 177:578-587(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    2. "Neuraminidase inhibitors for influenza."
      Moscona A.
      N. Engl. J. Med. 353:1363-1373(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.

    Entry informationi

    Entry nameiNRAM_INBLN
    AccessioniPrimary (citable) accession number: P67923
    Secondary accession number(s): P16193, P16197
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 11, 2004
    Last sequence update: October 11, 2004
    Last modified: October 1, 2014
    This is version 57 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 B 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