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Q07599

- NRAM_I63A3

UniProt

Q07599 - NRAM_I63A3

Protein

Neuraminidase

Gene

NA

Organism
Influenza A virus (strain A/Duck/Ukraine/1/1963 H3N8)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 98 (01 Oct 2014)
      Sequence version 1 (01 Oct 1994)
      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 sitei116 – 1161SubstrateBy similarity
    Active sitei149 – 1491Proton donor/acceptorBy similarity
    Binding sitei150 – 1501SubstrateBy similarity
    Binding sitei291 – 2911SubstrateBy similarity
    Metal bindingi292 – 2921Calcium; via carbonyl oxygenBy similarity
    Metal bindingi296 – 2961Calcium; via carbonyl oxygenBy similarity
    Metal bindingi322 – 3221CalciumBy similarity
    Binding sitei368 – 3681SubstrateBy similarity
    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

    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/Duck/Ukraine/1/1963 H3N8)
    Taxonomic identifieri385580 [NCBI]
    Taxonomic lineageiVirusesssRNA negative-strand virusesOrthomyxoviridaeInfluenzavirus A
    Virus hostiAves [TaxID: 8782]
    Equus caballus (Horse) [TaxID: 9796]

    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 – 470470NeuraminidasePRO_0000078688Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi46 – 461N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi54 – 541N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi84 – 841N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi90 ↔ 417By similarity
    Disulfide bondi122 ↔ 127By similarity
    Glycosylationi144 – 1441N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi182 ↔ 229By similarity
    Disulfide bondi231 ↔ 236By similarity
    Disulfide bondi277 ↔ 290By similarity
    Disulfide bondi279 ↔ 288By similarity
    Disulfide bondi316 ↔ 335By similarity
    Glycosylationi398 – 3981N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi421 ↔ 446By similarity

    Post-translational modificationi

    N-glycosylated.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Interactioni

    Subunit structurei

    Homotetramer.By similarity

    Protein-protein interaction databases

    DIPiDIP-60415N.

    Structurei

    Secondary structure

    1
    470
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi96 – 1005
    Helixi103 – 1064
    Turni107 – 1093
    Beta strandi112 – 12211
    Beta strandi127 – 13711
    Helixi141 – 1444
    Beta strandi155 – 1606
    Helixi167 – 1693
    Beta strandi171 – 1755
    Beta strandi177 – 1837
    Beta strandi185 – 19511
    Helixi197 – 1993
    Beta strandi201 – 21515
    Beta strandi217 – 2204
    Beta strandi222 – 2243
    Beta strandi226 – 2283
    Beta strandi230 – 2323
    Beta strandi235 – 2439
    Beta strandi245 – 2473
    Beta strandi250 – 2578
    Beta strandi260 – 2667
    Beta strandi275 – 2828
    Beta strandi285 – 2917
    Beta strandi294 – 2985
    Beta strandi300 – 3045
    Beta strandi310 – 3145
    Beta strandi317 – 3193
    Beta strandi322 – 3243
    Helixi328 – 3303
    Beta strandi335 – 3373
    Beta strandi350 – 3534
    Beta strandi356 – 3616
    Beta strandi363 – 37614
    Turni377 – 3815
    Beta strandi387 – 39913
    Beta strandi403 – 4086
    Helixi410 – 4134
    Beta strandi415 – 42915
    Turni430 – 4323
    Beta strandi433 – 4364
    Beta strandi438 – 4469
    Helixi466 – 4683

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2HT5X-ray2.40A81-470[»]
    2HT7X-ray2.60A81-470[»]
    2HT8X-ray2.40A81-470[»]
    2HTQX-ray2.20A81-470[»]
    2HTRX-ray2.50A81-470[»]
    2HTUX-ray2.20A81-470[»]
    3O9JX-ray2.00A81-467[»]
    3O9KX-ray2.49A81-467[»]
    4D8SX-ray2.40A81-470[»]
    4GB1X-ray2.62A81-470[»]
    4KS1X-ray2.20A81-470[»]
    4M3MX-ray2.10A80-469[»]
    4MJUX-ray2.35A81-469[»]
    4MJVX-ray2.65A81-470[»]
    ProteinModelPortaliQ07599.
    SMRiQ07599. Positions 81-467.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ07599.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 66IntravirionSequence Analysis

    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
    Regioni11 – 3323Involved in apical transport and lipid raft associationBy similarityAdd
    BLAST
    Regioni38 – 8851Hypervariable stalk regionAdd
    BLAST
    Regioni89 – 470382Head of neuraminidaseAdd
    BLAST
    Regioni275 – 2762Substrate bindingBy similarity

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi439 – 4424Poly-Ser

    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.

    Q07599-1 [UniParc]FASTAAdd to Basket

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    MNPNQKIITI GSISLGLVVF NVLLHVVSII VTVLVLGKGG NNGICNETVV    50
    REYNETVRIE KVTQWHNTNV VEYVPYWNGG TYMNNTEAIC DAKGFAPFSK 100
    DNGIRIGSRG HIFVIREPFV SCSPIECRTF FLTQGSLLND KHSNGTVKDR 150
    SPFRTLMSVE VGQSPNVYQA RFEAVAWSAT ACHDGKKWMT VGVTGPDSKA 200
    VAVIHYGGVP TDVVNSWAGD ILRTQESSCT CIQGDCYWVM TDGPANRQAQ 250
    YRIYKANQGR IIGQTDISFN GGHIEECSCY PNDGKVECVC RDGWTGTNRP 300
    VLVISPDLSY RVGYLCAGIP SDTPRGEDTQ FTGSCTSPMG NQGYGVKGFG 350
    FRQGTDVWMG RTISRTSRSG FEILRIKNGW TQTSKEQIRK QVVVDNLNWS 400
    GYSGSFTLPV ELSGKDCLVP CFWVEMIRGK PEEKTIWTSS SSIVMCGVDY 450
    EVADWSWHDG AILPFDIDKM 470
    Length:470
    Mass (Da):51,960
    Last modified:October 1, 1994 - v1
    Checksum:iB46D54A03AC84CCE
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L06576 Unassigned RNA. Translation: AAA16234.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L06576 Unassigned RNA. Translation: AAA16234.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2HT5 X-ray 2.40 A 81-470 [» ]
    2HT7 X-ray 2.60 A 81-470 [» ]
    2HT8 X-ray 2.40 A 81-470 [» ]
    2HTQ X-ray 2.20 A 81-470 [» ]
    2HTR X-ray 2.50 A 81-470 [» ]
    2HTU X-ray 2.20 A 81-470 [» ]
    3O9J X-ray 2.00 A 81-467 [» ]
    3O9K X-ray 2.49 A 81-467 [» ]
    4D8S X-ray 2.40 A 81-470 [» ]
    4GB1 X-ray 2.62 A 81-470 [» ]
    4KS1 X-ray 2.20 A 81-470 [» ]
    4M3M X-ray 2.10 A 80-469 [» ]
    4MJU X-ray 2.35 A 81-469 [» ]
    4MJV X-ray 2.65 A 81-470 [» ]
    ProteinModelPortali Q07599.
    SMRi Q07599. Positions 81-467.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-60415N.

    Protein family/group databases

    CAZyi GH34. Glycoside Hydrolase Family 34.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei Q07599.
    PROi Q07599.

    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. "Phylogenetic analysis of the N8 neuraminidase gene of influenza A viruses."
      Saito T., Kawaoka Y., Webster R.G.
      Virology 193:868-876(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE.
    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_I63A3
    AccessioniPrimary (citable) accession number: Q07599
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1994
    Last sequence update: October 1, 1994
    Last modified: October 1, 2014
    This is version 98 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

    3D-structure

    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