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Q67344

- NRAM_I82A7

UniProt

Q67344 - NRAM_I82A7

Protein

Neuraminidase

Gene

NA

Organism
Influenza A virus (strain A/Swine/Hong Kong/127/1982 H3N2)
Status
Reviewed - Annotation score: 5 out of 5- Protein inferred from homologyi
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    • History
      Entry version 78 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      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 sitei95 – 951SubstrateBy similarity
    Active sitei128 – 1281Proton donor/acceptorBy similarity
    Binding sitei129 – 1291SubstrateBy similarity
    Binding sitei269 – 2691SubstrateBy similarity
    Metal bindingi270 – 2701Calcium; via carbonyl oxygenBy similarity
    Metal bindingi274 – 2741Calcium; via carbonyl oxygenBy similarity
    Metal bindingi301 – 3011CalciumBy similarity
    Binding sitei348 – 3481SubstrateBy similarity
    Active sitei383 – 3831NucleophileBy 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/Swine/Hong Kong/127/1982 H3N2)
    Taxonomic identifieri384483 [NCBI]
    Taxonomic lineageiVirusesssRNA negative-strand virusesOrthomyxoviridaeInfluenzavirus A
    Virus hostiAves [TaxID: 8782]
    Cetacea (whales) [TaxID: 9721]
    Homo sapiens (Human) [TaxID: 9606]
    Phocidae (true seals) [TaxID: 9709]
    Sus scrofa (Pig) [TaxID: 9823]

    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 – 446446NeuraminidasePRO_0000280158Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi38 – 381N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi47 – 471N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi63 – 631N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi69 ↔ 394By similarity
    Disulfide bondi101 ↔ 106By similarity
    Glycosylationi123 – 1231N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi152 ↔ 170By similarity
    Disulfide bondi160 ↔ 207By similarity
    Glycosylationi177 – 1771N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi209 ↔ 214By similarity
    Glycosylationi211 – 2111N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi255 ↔ 268By similarity
    Disulfide bondi257 ↔ 266By similarity
    Disulfide bondi295 ↔ 314By similarity
    Glycosylationi379 – 3791N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi398 ↔ 424By similarity

    Post-translational modificationi

    N-glycosylated.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Interactioni

    Subunit structurei

    Homotetramer.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliQ67344.
    SMRiQ67344. Positions 59-446.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni13 – 6755Hypervariable stalk regionBy similarityAdd
    BLAST
    Regioni68 – 446379Head of neuraminidaseBy similarityAdd
    BLAST
    Regioni253 – 2542Substrate bindingBy similarity

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi308 – 3125Poly-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

    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: Fragment.

    Q67344-1 [UniParc]FASTAAdd to Basket

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    MQIAILVTTV TLHFNQYECD SLADNQVMPC EPIIIERNIT EIIYLTNTTI    50
    EKEICPKLME YRNWSRPQCK ITGFAPFSKD NSIRLSAGGD IWVTREPYVS 100
    CDPGKCYQFA LGQGTTLDNK HSNDTIHDRI PHRTLLMNEL GVPFHLGTRQ 150
    VCIAWSSSSC HDGKAWLHVC VTGDDKNATA SFIYDGRLVD SMGSWSQNIL 200
    RTQESECVCI NGTCTVVMTD GSASGRADTR ILFIEEGKIV HISPLSGSAQ 250
    HVEECSCYPR YPSVRCICRD NWKGSNRPIV DINIKDYSID SRYVCSGLVG 300
    DTPRNNDRSS SSDCKNPNND KGNHGVKGWA FDDGNDVWMG RTISKDSRSG 350
    YETFKVIDGW STPNSKSQIN RQVIVDRDNR SGYSGIFSVE SKGCINRCFY 400
    VELIRGRKQE TRVWWTSSSI VVFCGTSGTY GKGSWPDGAN INFMPI 446
    Length:446
    Mass (Da):49,915
    Last modified:November 1, 1996 - v1
    Checksum:iB3E31B09E6728A9D
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-terminal residuei1 – 11

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D21194 Genomic RNA. Translation: BAA04730.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D21194 Genomic RNA. Translation: BAA04730.1 .

    3D structure databases

    ProteinModelPortali Q67344.
    SMRi Q67344. Positions 59-446.
    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. "Genetic analysis of porcine H3N2 viruses originating in Southern China."
      Nerome K., Kanegae Y., Shortridge K.F., Sugita S., Ishida M.
      J. Gen. Virol. 76:613-624(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    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_I82A7
    AccessioniPrimary (citable) accession number: Q67344
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 6, 2007
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 78 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.

    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