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P27907

- NRAM_INBBE

UniProt

P27907 - NRAM_INBBE

Protein

Neuraminidase

Gene

NA

Organism
Influenza B virus (strain B/Beijing/1/1987)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 96 (01 Oct 2014)
      Sequence version 1 (01 Aug 1992)
      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.1 Publication

    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 – 1151Substrate
    Active sitei148 – 1481Proton donor/acceptorBy similarity
    Binding sitei149 – 1491Substrate
    Binding sitei291 – 2911Substrate
    Metal bindingi292 – 2921Calcium; via carbonyl oxygen1 Publication
    Metal bindingi296 – 2961Calcium; via carbonyl oxygen1 Publication
    Metal bindingi323 – 3231Calcium1 Publication
    Metal bindingi343 – 3431Calcium; via carbonyl oxygen1 Publication
    Metal bindingi345 – 3451Calcium; via carbonyl oxygen1 Publication
    Binding sitei373 – 3731Substrate
    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

    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/Beijing/1/1987)
    Taxonomic identifieri11525 [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_0000078730Add
    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 ↔ 419
    Disulfide bondi121 ↔ 126
    Disulfide bondi181 ↔ 228
    Disulfide bondi230 ↔ 235
    Disulfide bondi276 ↔ 290
    Disulfide bondi278 ↔ 288
    Glycosylationi283 – 2831N-linked (GlcNAc...); by host1 Publication
    Disulfide bondi317 ↔ 336
    Disulfide bondi423 ↔ 446

    Post-translational modificationi

    N-glycosylated.1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Interactioni

    Subunit structurei

    Homotetramer.1 Publication

    Structurei

    Secondary structure

    1
    465
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi89 – 979
    Helixi99 – 1024
    Beta strandi111 – 12111
    Beta strandi126 – 14015
    Turni143 – 1464
    Beta strandi154 – 1596
    Turni166 – 1683
    Beta strandi170 – 1745
    Beta strandi176 – 1827
    Beta strandi187 – 1948
    Helixi196 – 1983
    Beta strandi200 – 2056
    Beta strandi208 – 2147
    Beta strandi216 – 2194
    Beta strandi229 – 2313
    Beta strandi234 – 2429
    Beta strandi244 – 2463
    Beta strandi248 – 2569
    Beta strandi259 – 2646
    Beta strandi267 – 2693
    Beta strandi274 – 29118
    Beta strandi293 – 2953
    Beta strandi300 – 3056
    Turni306 – 3094
    Beta strandi310 – 3156
    Beta strandi323 – 3253
    Beta strandi351 – 3555
    Beta strandi360 – 3667
    Beta strandi368 – 38417
    Turni386 – 3883
    Beta strandi394 – 40512
    Beta strandi409 – 4157
    Beta strandi417 – 43014
    Beta strandi439 – 4479
    Beta strandi449 – 4513

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1A4GX-ray2.20A/B76-465[»]
    1A4QX-ray1.90A/B76-465[»]
    1NSBX-ray2.20A/B76-465[»]
    1NSCX-ray1.70A/B76-465[»]
    1NSDX-ray1.80A/B76-465[»]
    ProteinModelPortaliP27907.
    SMRiP27907. Positions 76-465.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP27907.

    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 binding

    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.

    P27907-1 [UniParc]FASTAAdd to Basket

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    MLPSTIQTLT LFLTSGGVLL SLYVSASLSY LLYSDILLKF SSKITAPTMT    50
    LDCANASNVQ AVNRSATKEM TFLLPEPEWT YPRLSCQGST FQKALLISPH 100
    RFGEARGNSA PLIIREPFIA CGPKECKHFA LTHYAAQPGG YYNGTREDRN 150
    KLRHLISVKL GKIPTVENSI FHMAAWSGSA CHDGREWTYI GVDGPDSNAL 200
    IKIKYGEAYT DTYHSYANNI LRTQESACNC IGGDCYLMIT DGSASGISKC 250
    RFLKIREGRI IKEIFPTGRV EHTEECTCGF ASNKTIECAC RDNSYTAKRP 300
    FVKLNVETDT AEIRLMCTET YLDTPRPDDG SITGPCESNG DKGRGGIKGG 350
    FVHQRMASKI GRWYSRTMSK TERMGMELYV RYDGDPWTDS DALAHSGVMV 400
    SMKEPGWYSF GFEIKDKKCD VPCIGIEMVH DGGKKTWHSA ATAIYCLMGS 450
    GQLLWDTVTG VDMAL 465
    Length:465
    Mass (Da):51,430
    Last modified:August 1, 1992 - v1
    Checksum:i2FC60B895CBD430C
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M54967 Genomic RNA. Translation: AAA43733.1.
    PIRiB38520. NMIVB1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M54967 Genomic RNA. Translation: AAA43733.1 .
    PIRi B38520. NMIVB1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1A4G X-ray 2.20 A/B 76-465 [» ]
    1A4Q X-ray 1.90 A/B 76-465 [» ]
    1NSB X-ray 2.20 A/B 76-465 [» ]
    1NSC X-ray 1.70 A/B 76-465 [» ]
    1NSD X-ray 1.80 A/B 76-465 [» ]
    ProteinModelPortali P27907.
    SMRi P27907. Positions 76-465.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GH34. Glycoside Hydrolase Family 34.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P27907.

    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. "Sequence and crystallization of influenza virus B/Beijing/1/87 neuraminidase."
      Burmeister W.P., Daniels R.S., Dayan S., Gagnon J., Cusack S., Ruigrok R.W.
      Virology 180:266-272(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA], PARTIAL PROTEIN SEQUENCE.
    2. "Neuraminidase inhibitors for influenza."
      Moscona A.
      N. Engl. J. Med. 353:1363-1373(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    3. "The 2.2-A resolution crystal structure of influenza B neuraminidase and its complex with sialic acid."
      Burmeister W.P., Ruigrok R.W., Cusack S.
      EMBO J. 11:49-56(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 76-465 IN COMPLEX WITH CALCIUM AND SIALIC ACID, GLYCOSYLATION AT ASN-283, SUBUNIT, COFACTOR.
    4. "Dihydropyrancarboxamides related to zanamivir: a new series of inhibitors of influenza virus sialidases. 2. Crystallographic and molecular modeling study of complexes of 4-amino-4H-pyran-6-carboxamides and sialidase from influenza virus types A and B."
      Taylor N.R., Cleasby A., Singh O., Skarzynski T., Wonacott A.J., Smith P.W., Sollis S.L., Howes P.D., Cherry P.C., Bethell R., Colman P., Varghese J.
      J. Med. Chem. 41:798-807(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 76-465.

    Entry informationi

    Entry nameiNRAM_INBBE
    AccessioniPrimary (citable) accession number: P27907
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1992
    Last sequence update: August 1, 1992
    Last modified: October 1, 2014
    This is version 96 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.

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3