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P16191

- NRAM_INBHK

UniProt

P16191 - NRAM_INBHK

Protein

Neuraminidase

Gene

NA

Organism
Influenza B virus (strain B/Hong Kong/8/1973)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 93 (01 Oct 2014)
      Sequence version 1 (01 Apr 1990)
      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 sitei116 – 1161SubstrateBy similarity
    Active sitei149 – 1491Proton donor/acceptorBy similarity
    Binding sitei150 – 1501SubstrateBy similarity
    Binding sitei292 – 2921SubstrateBy similarity
    Metal bindingi293 – 2931Calcium; via carbonyl oxygenBy similarity
    Metal bindingi297 – 2971Calcium; via carbonyl oxygenBy similarity
    Metal bindingi324 – 3241CalciumBy similarity
    Metal bindingi346 – 3461Calcium; via carbonyl oxygenBy similarity
    Binding sitei374 – 3741SubstrateBy similarity
    Active sitei409 – 4091NucleophileBy 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

    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 B virus (strain B/Hong Kong/8/1973)
    Taxonomic identifieri11531 [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 – 466466NeuraminidasePRO_0000078731Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi56 – 561N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi64 – 641N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi87 ↔ 420By similarity
    Disulfide bondi122 ↔ 127By similarity
    Glycosylationi144 – 1441N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi182 ↔ 229By similarity
    Disulfide bondi231 ↔ 236By similarity
    Disulfide bondi277 ↔ 291By similarity
    Disulfide bondi279 ↔ 289By similarity
    Glycosylationi284 – 2841N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi318 ↔ 337By similarity
    Disulfide bondi424 ↔ 447By similarity

    Post-translational modificationi

    N-glycosylated.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Interactioni

    Subunit structurei

    Homotetramer.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliP16191.
    SMRiP16191. Positions 77-466.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 66IntravirionSequence Analysis
    Topological domaini36 – 466431Virion 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 – 6931Hypervariable stalk regionAdd
    BLAST
    Regioni70 – 466397Head of neuraminidaseAdd
    BLAST
    Regioni275 – 2762Substrate 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.

    P16191-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLPSTIQTLT LFLTSGGVLL SLYVSASLSY LLYSDILLKF SSTKRTAPTM    50
    SLDCANVSNV QAVNRSATKE MTFLLPEPEW TYPRLSCQGS TFQKALLISP 100
    HRFGETRGNS APLIIREPFV ACGPKECRHF ALTHYAAQPG GYYNGTRKDR 150
    NKLRHLISVK LGKIPTVENS IFHMAAWSGS ACHDGREWTY VGVDGPDSNA 200
    LIKIKYGEAY TDTYHSYANN ILRTQESACN CIGGDCYLMI TDGSASGISK 250
    CRFLKIREGR IIKEIFPTGR VEHTEECTCG FASNKTIECA CRDNSYTAKR 300
    PFVKLNVETD TAEIRLMCTE TYLDTPRPDD GSITGPCESN GDKGLGGIKG 350
    GFVHQRMASK IGRWYSRTMS KTERMGMELY VKYDGDPWTD SDALAPSGVM 400
    VSMKEPGWYS FGFEIKDKKC DVPCIGIEMV HDGGKETWHS AATAIYCLMG 450
    SGQLLWDTVT GVDMAL 466
    Length:466
    Mass (Da):51,507
    Last modified:April 1, 1990 - v1
    Checksum:i790D08EB36F10AC3
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M30631 Genomic RNA. Translation: AAA43729.1.
    PIRiH46347.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M30631 Genomic RNA. Translation: AAA43729.1 .
    PIRi H46347.

    3D structure databases

    ProteinModelPortali P16191.
    SMRi P16191. Positions 77-466.
    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. "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_INBHK
    AccessioniPrimary (citable) accession number: P16191
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: April 1, 1990
    Last modified: October 1, 2014
    This is version 93 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