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P09573

- NRAM_I83A6

UniProt

P09573 - NRAM_I83A6

Protein

Neuraminidase

Gene

NA

Organism
Influenza A virus (strain A/Chicken/Pennsylvania/1370/1983 H5N2)
Status
Reviewed - Annotation score: 5 out of 5- Protein inferred from homologyi
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    • History
      Entry version 99 (01 Oct 2014)
      Sequence version 2 (06 Mar 2007)
      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 sitei98 – 981SubstrateBy similarity
    Active sitei131 – 1311Proton donor/acceptorBy similarity
    Binding sitei132 – 1321SubstrateBy similarity
    Binding sitei272 – 2721SubstrateBy similarity
    Metal bindingi273 – 2731Calcium; via carbonyl oxygenBy similarity
    Metal bindingi277 – 2771Calcium; via carbonyl oxygenBy similarity
    Metal bindingi304 – 3041CalciumBy similarity
    Binding sitei351 – 3511SubstrateBy similarity
    Active sitei386 – 3861NucleophileBy 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/Chicken/Pennsylvania/1370/1983 H5N2)
    Taxonomic identifieri385617 [NCBI]
    Taxonomic lineageiVirusesssRNA negative-strand virusesOrthomyxoviridaeInfluenzavirus A
    Virus hostiAves [TaxID: 8782]

    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 – 449449NeuraminidasePRO_0000078680Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi48 – 481N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi66 – 661N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi72 ↔ 397By similarity
    Disulfide bondi104 ↔ 109By similarity
    Glycosylationi123 – 1231N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi126 – 1261N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi155 ↔ 173By similarity
    Disulfide bondi163 ↔ 210By similarity
    Glycosylationi180 – 1801N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi212 ↔ 217By similarity
    Glycosylationi214 – 2141N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi258 ↔ 271By similarity
    Disulfide bondi260 ↔ 269By similarity
    Disulfide bondi298 ↔ 317By similarity
    Glycosylationi382 – 3821N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi401 ↔ 427By similarity

    Post-translational modificationi

    N-glycosylated.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Interactioni

    Subunit structurei

    Homotetramer.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliP09573.
    SMRiP09573. Positions 62-449.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 66IntravirionSequence Analysis
    Topological domaini36 – 449414Virion 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
    Regioni11 – 3323Involved in apical transport and lipid raft associationBy similarityAdd
    BLAST
    Regioni36 – 7035Hypervariable stalk regionAdd
    BLAST
    Regioni71 – 449379Head of neuraminidaseAdd
    BLAST
    Regioni256 – 2572Substrate bindingBy similarity

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi311 – 3155Poly-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.

    P09573-1 [UniParc]FASTAAdd to Basket

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    MNPNQKIITI GSVSLTIATV CFLMQIAILA TNVTLHFRQN ERSIPAYNQT    50
    TPCKPIIIER NIKYRNWSKP QCQITGFAPF SKDNSIRLSA GGGIWVTREP 100
    YVSCDPSKCY QFALGQGTTL DNNHSNGTIH DRTPHRTLLM NELGVPFHLG 150
    TRQVCIAWSS SSCHDGKAWL HVCVTGDDRN ATASFIYNGM LVDSIGSWSQ 200
    NILRTQESEC VCINGTCTVV MTDGSASGKA DIRILFIREG KIVHISPLSG 250
    SAQHIEECSC YPRYPNVRCV CRDNWKGSNR PVIDINMADY SIDSSYVCSG 300
    LVGDTPRNDD SSSSSNCRDP NNERGNPGVK GWAFDIGDDV WMGRTISKDS 350
    RSGYETFRVI GGWATANSKS QTNRQVIVDN NNWSGYSGIF SVESKSCINR 400
    CFYVELIRGR PQETRVWWTS NSIVVFCGTS GTYGTGSWPD GANINFMPL 449
    Length:449
    Mass (Da):49,693
    Last modified:March 6, 2007 - v2
    Checksum:iDC716FBFB147ADA1
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti42 – 421R → G in AAA43424. (PubMed:2414922)Curated
    Sequence conflicti122 – 1221N → H in AAA43424. (PubMed:2414922)Curated
    Sequence conflicti160 – 1601S → R in AAA43424. (PubMed:2414922)Curated
    Sequence conflicti232 – 2321I → T in AAA43424. (PubMed:2414922)Curated
    Sequence conflicti263 – 2653RYP → KSYL in AAA43424. (PubMed:2414922)Curated
    Sequence conflicti283 – 2831I → KL in AAA43424. (PubMed:2414922)Curated
    Sequence conflicti361 – 3611G → S in AAA43424. (PubMed:2414922)Curated
    Sequence conflicti420 – 4201S → T in AAA43424. (PubMed:2414922)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M12051 Genomic RNA. Translation: AAA43424.1.
    CY015110 Genomic RNA. Translation: ABI85148.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M12051 Genomic RNA. Translation: AAA43424.1 .
    CY015110 Genomic RNA. Translation: ABI85148.1 .

    3D structure databases

    ProteinModelPortali P09573.
    SMRi P09573. Positions 62-449.
    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. "The neuraminidases of the virulent and avirulent A/Chicken/Pennsylvania/83 (H5N2) influenza A viruses: sequence and antigenic analyses."
      Deshpande K.L., Naeve C.W., Webster R.G.
      Virology 147:49-60(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    2. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    3. "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.
    4. "Neuraminidase inhibitors for influenza."
      Moscona A.
      N. Engl. J. Med. 353:1363-1373(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    5. "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_I83A6
    AccessioniPrimary (citable) accession number: P09573
    Secondary accession number(s): Q0A2D4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: March 6, 2007
    Last modified: October 1, 2014
    This is version 99 of the entry and version 2 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