Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q6DPK0

- NRAM_I02A3

UniProt

Q6DPK0 - NRAM_I02A3

Protein

Neuraminidase

Gene

NA

Organism
Influenza A virus (strain A/Chicken/Hong Kong/37.4/2002 H5N1 genotype X2)
Status
Reviewed - Annotation score: 5 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 57 (01 Oct 2014)
      Sequence version 2 (22 Jul 2008)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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 sitei273 – 2731SubstrateBy similarity
    Metal bindingi274 – 2741Calcium; via carbonyl oxygenBy similarity
    Metal bindingi278 – 2781Calcium; via carbonyl oxygenBy similarity
    Metal bindingi304 – 3041CalciumBy similarity
    Binding sitei348 – 3481SubstrateBy similarity
    Active sitei382 – 3821NucleophileBy 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/Hong Kong/37.4/2002 H5N1 genotype X2)
    Taxonomic identifieri284172 [NCBI]
    Taxonomic lineageiVirusesssRNA negative-strand virusesOrthomyxoviridaeInfluenzavirus A
    Virus hostiAves [TaxID: 8782]
    Felis catus (Cat) (Felis silvestris catus) [TaxID: 9685]
    Homo sapiens (Human) [TaxID: 9606]
    Panthera pardus (Leopard) (Felis pardus) [TaxID: 9691]
    Panthera tigris (Tiger) [TaxID: 9694]
    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 – 449449NeuraminidasePRO_0000310936Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi68 – 681N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi72 ↔ 397By similarity
    Disulfide bondi104 ↔ 109By similarity
    Glycosylationi126 – 1261N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi164 ↔ 211By similarity
    Disulfide bondi213 ↔ 218By similarity
    Glycosylationi215 – 2151N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi259 ↔ 272By similarity
    Disulfide bondi261 ↔ 270By similarity
    Disulfide bondi298 ↔ 315By similarity
    Disulfide bondi401 ↔ 426By similarity

    Post-translational modificationi

    N-glycosylated.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Interactioni

    Subunit structurei

    Homotetramer.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliQ6DPK0.
    SMRiQ6DPK0. Positions 63-447.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 66IntravirionSequence Analysis
    Topological domaini28 – 449422Virion 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 – 7035Hypervariable stalk regionBy similarityAdd
    BLAST
    Regioni71 – 449379Head of neuraminidaseBy similarityAdd
    BLAST
    Regioni257 – 2582Substrate 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.

    Q6DPK0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNPNRKIITI GSICMVIGIV SLMLQIGNII SIWVSHSIQT ENHHQAEPIS    50
    NTNFLTEKAV ASVTLAGNSS LCPISGWAIH SKDNGIRIGS KGDVFVIREP 100
    FISCSHLECR TFFLTQGALL NDKHSNGTAK DRSPHRTLMS CPVGEAPSPY 150
    NSRFESVAWS ASACHDGTSW LTIAISGPDN GAVAVLKYNG IITDTIKSWR 200
    NNILRTQESE CACVNGSCFT VMTDGPSNGQ ASYKIFKMEK GKVVKSVELD 250
    APNYHYEECS CYPDAGEVTC VCRDNWHGSN RPWVSFNQNL EYQIGYICSG 300
    VFGDNPRPND GTGSCGPMSL NGAYGVKGFS FKYGNGVWIG RTKSTNSRSG 350
    FEMIWDPNGW TGTDSNFSVK QDIVAITDWS GYSGSFVQHP ELTGLDCIRP 400
    CFWVELIRGR PKESTIWTSG SSISFCGVNS DTVGWSWPDG AELPFTIDK 449
    Length:449
    Mass (Da):49,075
    Last modified:July 22, 2008 - v2
    Checksum:i6B7ED2862D623468
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY651459 Genomic RNA. Translation: AAT73341.2.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY651459 Genomic RNA. Translation: AAT73341.2 .

    3D structure databases

    ProteinModelPortali Q6DPK0.
    SMRi Q6DPK0. Positions 63-447.
    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. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    2. Cited for: SEQUENCE REVISION.

    Entry informationi

    Entry nameiNRAM_I02A3
    AccessioniPrimary (citable) accession number: Q6DPK0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 13, 2007
    Last sequence update: July 22, 2008
    Last modified: October 1, 2014
    This is version 57 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