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Q2VC95

- NRAM_I80A2

UniProt

Q2VC95 - NRAM_I80A2

Protein

Neuraminidase

Gene

NA

Organism
Influenza A virus (strain A/Seal/Massachusetts/1/1980 H7N7)
Status
Reviewed - Annotation score: 5 out of 5- Protein inferred from homologyi
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    • History
      Entry version 53 (01 Oct 2014)
      Sequence version 1 (10 Jan 2006)
      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 bindingi323 – 3231CalciumBy similarity
    Binding sitei370 – 3701SubstrateBy similarity
    Active sitei404 – 4041NucleophileBy 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

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Neuraminidase (EC:3.2.1.18)
    Gene namesi
    Name:NA
    OrganismiInfluenza A virus (strain A/Seal/Massachusetts/1/1980 H7N7)
    Taxonomic identifieri384493 [NCBI]
    Taxonomic lineageiVirusesssRNA negative-strand virusesOrthomyxoviridaeInfluenzavirus A
    Virus hostiAves [TaxID: 8782]
    Equus caballus (Horse) [TaxID: 9796]
    Homo sapiens (Human) [TaxID: 9606]
    Phocidae (true seals) [TaxID: 9709]
    ProteomesiUP000008576: Genome

    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_0000280149Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi32 – 321N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi46 – 461N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi55 – 551N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi56 – 561N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi66 – 661N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi67 – 671N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi86 – 861N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi90 ↔ 418By similarity
    Disulfide bondi122 ↔ 127By similarity
    Glycosylationi144 – 1441N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi174 ↔ 192By similarity
    Disulfide bondi182 ↔ 229By similarity
    Glycosylationi199 – 1991N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi231 ↔ 236By similarity
    Glycosylationi233 – 2331N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi277 ↔ 290By similarity
    Disulfide bondi279 ↔ 288By similarity
    Disulfide bondi317 ↔ 335By similarity
    Glycosylationi400 – 4001N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi422 ↔ 449By similarity

    Post-translational modificationi

    N-glycosylated.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Interactioni

    Subunit structurei

    Homotetramer.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliQ2VC95.
    SMRiQ2VC95. Positions 85-469.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 66IntravirionSequence Analysis
    Topological domaini28 – 470443Virion surfaceSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei7 – 2721Helical; 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
    Regioni36 – 8853Hypervariable stalk regionBy similarityAdd
    BLAST
    Regioni89 – 470382Head of neuraminidaseBy similarityAdd
    BLAST
    Regioni275 – 2762Substrate 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.

    Q2VC95-1 [UniParc]FASTAAdd to Basket

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    MNPNQKLFAL SGVAIALSIF NLLIGISNVV LNVSLHLKNN NDQDKNWTCT    50
    SITQNNTTLI ENTYVNNTTV INKETEAAKQ NYLMLNKSLC KVEGWVVVAK 100
    DNAIRFGESE QVIVTREPYV SCDPLGCRMY ALHQGTTIRN KHSNGTIHDR 150
    TALRGLISTP LGSPPVVSNS DFLCVGWSST SCHDGIGRMT ICVQGNNDNA 200
    TATVYYDRRL TTTIKTWARN ILRTQESECV CHNGTCVVVM TDGSASSQAH 250
    TKVLYFHKGL IIKEEALKGS ARHIEECSCY GHDSKVTCVC RDNWQGANRP 300
    VIEIDMNAME HTSQYLCTGV LTDTSRPSDK SIGDCNNPIT GSPGAPGVKG 350
    FGFLDSSNTW LGRTISPRSR SGFEMLKIPN AGTDPNSRIT ERQEIVDSNN 400
    WSGYSGSFID YWDESSECYN PCFYVELIRG RPEEAKYVWW TSNSLVALCG 450
    SPVPVGSGSF PDGAQIQYFS 470
    Length:470
    Mass (Da):51,769
    Last modified:January 10, 2006 - v1
    Checksum:i777E7FC7A9695C2F
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DQ266095 Genomic RNA. Translation: ABB90268.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DQ266095 Genomic RNA. Translation: ABB90268.1 .

    3D structure databases

    ProteinModelPortali Q2VC95.
    SMRi Q2VC95. Positions 85-469.
    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. "The viral polymerase mediates adaptation of an avian influenza virus to a mammalian host."
      Gabriel G., Dauber B., Wolff T., Planz O., Klenk H.D., Stech J.
      Proc. Natl. Acad. Sci. U.S.A. 102:18590-18595(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
      Strain: SC35M mouse-adapted.
    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_I80A2
    AccessioniPrimary (citable) accession number: Q2VC95
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 6, 2007
    Last sequence update: January 10, 2006
    Last modified: October 1, 2014
    This is version 53 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.
    SC35 was derived from A/Seal/Massachussetts/1/80 (H7N7) by serial passages in chicken embryo cells, thereby acquiring a multibasic cleavage site in its hemagglutinin (HA) and becoming 100% lethal for chickens. SC35 was then passaged 11 times in mouse lung, yielding the mouse-adapted variant SC35M.

    Keywords - Technical termi

    Complete proteome

    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