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Q9IGQ6

- NRAM_I18A0

UniProt

Q9IGQ6 - NRAM_I18A0

Protein

Neuraminidase

Gene

NA

Organism
Influenza A virus (strain A/Brevig Mission/1/1918 H1N1) (Influenza A virus (strain A/South Carolina/1/1918 H1N1))
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 76 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      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 By similarity.By similarity
    Unlike other strains, A/WSN/33 neuraminidase binds and activates plasminogen into plasmin in the vicinity of HA so that activated plasmin cleaves HA rendering the virus infectious.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 sitei118 – 1181Substrate
    Active sitei151 – 1511Proton donor/acceptorBy similarity
    Binding sitei152 – 1521Substrate
    Binding sitei293 – 2931Substrate
    Metal bindingi294 – 2941Calcium; via carbonyl oxygen1 Publication
    Metal bindingi298 – 2981Calcium; via carbonyl oxygen1 Publication
    Metal bindingi324 – 3241Calcium1 Publication
    Metal bindingi344 – 3441Calcium; via carbonyl oxygen1 Publication
    Binding sitei368 – 3681Substrate
    Active sitei402 – 4021NucleophileBy 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

    Enzyme and pathway databases

    SABIO-RKQ9IGQ6.

    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/Brevig Mission/1/1918 H1N1) (Influenza A virus (strain A/South Carolina/1/1918 H1N1))
    Taxonomic identifieri88776 [NCBI]
    Taxonomic lineageiVirusesssRNA negative-strand virusesOrthomyxoviridaeInfluenzavirus A
    Virus hostiAves [TaxID: 8782]
    Homo sapiens (Human) [TaxID: 9606]
    Sus scrofa (Pig) [TaxID: 9823]
    ProteomesiUP000008430: Genome

    Subcellular locationi

    Virion membrane. Host apical cell membrane; Single-pass type II membrane protein
    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 – 469469NeuraminidasePRO_0000310569Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi88 – 881N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi92 ↔ 4171 Publication
    Disulfide bondi124 ↔ 1291 Publication
    Glycosylationi146 – 1461N-linked (GlcNAc...); by host1 Publication
    Disulfide bondi184 ↔ 2311 Publication
    Disulfide bondi233 ↔ 2381 Publication
    Glycosylationi235 – 2351N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi279 ↔ 2921 Publication
    Disulfide bondi281 ↔ 2901 Publication
    Disulfide bondi318 ↔ 3351 Publication
    Disulfide bondi421 ↔ 4461 Publication

    Post-translational modificationi

    N-glycosylated.1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PRIDEiQ9IGQ6.

    Interactioni

    Subunit structurei

    Homotetramer.1 Publication

    Structurei

    Secondary structure

    1
    469
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi95 – 1028
    Helixi105 – 1095
    Beta strandi115 – 12410
    Beta strandi129 – 14214
    Helixi143 – 1453
    Turni146 – 1494
    Beta strandi157 – 1626
    Turni169 – 1713
    Beta strandi173 – 1775
    Beta strandi179 – 1857
    Beta strandi190 – 1978
    Beta strandi203 – 2086
    Beta strandi211 – 2177
    Beta strandi219 – 2224
    Beta strandi228 – 2303
    Beta strandi232 – 2343
    Beta strandi237 – 2459
    Beta strandi247 – 2493
    Beta strandi252 – 2598
    Beta strandi262 – 2687
    Beta strandi277 – 2848
    Beta strandi287 – 2937
    Beta strandi302 – 3065
    Beta strandi312 – 3165
    Beta strandi324 – 3263
    Beta strandi350 – 3534
    Beta strandi356 – 3616
    Beta strandi365 – 37612
    Turni377 – 3815
    Beta strandi388 – 39912
    Beta strandi403 – 4086
    Helixi410 – 4134
    Beta strandi416 – 42914
    Turni430 – 4323
    Beta strandi433 – 4364
    Beta strandi438 – 45013

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3B7EX-ray1.45A/B83-467[»]
    3BEQX-ray1.64A/B83-467[»]
    3CYEX-ray1.65A/B83-469[»]
    ProteinModelPortaliQ9IGQ6.
    SMRiQ9IGQ6. Positions 83-467.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9IGQ6.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 66IntravirionSequence Analysis
    Topological domaini28 – 469442Virion surfaceSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei7 – 2721HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni11 – 3323Involved in apical transport and lipid raft associationBy similarityAdd
    BLAST
    Regioni36 – 9055Hypervariable stalk regionBy similarityAdd
    BLAST
    Regioni91 – 469379Head of neuraminidaseBy similarityAdd
    BLAST
    Regioni277 – 2782Substrate 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.

    Q9IGQ6-1 [UniParc]FASTAAdd to Basket

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    MNPNQKIITI GSICMVVGII SLILQIGNII SIWVSHSIQT GNQNHPETCN    50
    QSIITYENNT WVNQTYVNIS NTNVVAGQDA TSVILTGNSS LCPISGWAIY 100
    SKDNGIRIGS KGDVFVIREP FISCSHLECR TFFLTQGALL NDKHSNGTVK 150
    DRSPYRTLMS CPVGEAPSPY NSRFESVAWS ASACHDGMGW LTIGISGPDN 200
    GAVAVLKYNG IITDTIKSWR NNILRTQESE CACVNGSCFT IMTDGPSNGQ 250
    ASYKILKIEK GKVTKSIELN APNYHYEECS CYPDTGKVMC VCRDNWHGSN 300
    RPWVSFDQNL DYQIGYICSG VFGDNPRPND GTGSCGPVSS NGANGIKGFS 350
    FRYDNGVWIG RTKSTSSRSG FEMIWDPNGW TETDSSFSVR QDIVAITDWS 400
    GYSGSFVQHP ELTGLDCMRP CFWVELIRGQ PKENTIWTSG SSISFCGVNS 450
    DTVGWSWPDG AELPFSIDK 469
    Length:469
    Mass (Da):51,406
    Last modified:October 1, 2000 - v1
    Checksum:i28888692D4394159
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF250356 mRNA. Translation: AAF77036.1.
    U94893 Genomic DNA. Translation: AAC57065.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF250356 mRNA. Translation: AAF77036.1 .
    U94893 Genomic DNA. Translation: AAC57065.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3B7E X-ray 1.45 A/B 83-467 [» ]
    3BEQ X-ray 1.64 A/B 83-467 [» ]
    3CYE X-ray 1.65 A/B 83-469 [» ]
    ProteinModelPortali Q9IGQ6.
    SMRi Q9IGQ6. Positions 83-467.
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    BindingDBi Q9IGQ6.
    ChEMBLi CHEMBL1795169.

    Protein family/group databases

    CAZyi GH34. Glycoside Hydrolase Family 34.

    Proteomic databases

    PRIDEi Q9IGQ6.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    SABIO-RK Q9IGQ6.

    Miscellaneous databases

    EvolutionaryTracei Q9IGQ6.
    PROi Q9IGQ6.

    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. "Characterization of the 1918 'Spanish' influenza virus neuraminidase gene."
      Reid A.H., Fanning T.G., Janczewski T.A., Taubenberger J.K.
      Proc. Natl. Acad. Sci. U.S.A. 97:6785-6790(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Initial genetic characterization of the 1918 'Spanish' influenza virus."
      Taubenberger J.K., Reid A.H., Krafft A.E., Bijwaard K.E., Fanning T.G.
      Science 275:1793-1796(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 12-23.
      Strain: A/South Carolina/1/18.
    3. "Structural characterization of the 1918 influenza virus H1N1 neuraminidase."
      Xu X., Zhu X., Dwek R.A., Stevens J., Wilson I.A.
      J. Virol. 82:10493-10501(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 83-467 IN COMPLEX WITH CALCIUM AND INHIBITOR ZANAMIVIR, COFACTOR, SUBUNIT, GLYCOSYLATION AT ASN-146, DISULFIDE BOND.

    Entry informationi

    Entry nameiNRAM_I18A0
    AccessioniPrimary (citable) accession number: Q9IGQ6
    Secondary accession number(s): O10421
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 13, 2007
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 76 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.
    South Carolina isolate has been sequenced from formalid fixed-lung tissues of a 21-year-old male which died in 1918 at Ft. Jackson, SC. Brevig Mission isolate has been sequenced from lung tissues of an Inuit woman buried in the permafrost in a gravesite near Brevig Mission, Alaska. This sample was recovered by John Hultin, retired pathologist.

    Keywords - Technical termi

    3D-structure, Complete proteome

    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