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Protein

Neuraminidase

Gene

NA

Organism
Influenza A virus (strain A/Teal/China/2978.1/2002 H5N1 genotype W)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

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.UniRule annotation

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.

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.UniRule annotation

Cofactori

Ca2+UniRule annotation

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.UniRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei103SubstrateUniRule annotation1
Active sitei136Proton donor/acceptorUniRule annotation1
Binding sitei137SubstrateUniRule annotation1
Binding sitei278SubstrateUniRule annotation1
Metal bindingi279Calcium; via carbonyl oxygenUniRule annotation1
Metal bindingi283Calcium; via carbonyl oxygenUniRule annotation1
Metal bindingi309CalciumUniRule annotation1
Binding sitei353SubstrateUniRule annotation1
Active sitei387NucleophileUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionGlycosidase, Hydrolase
LigandCalcium, Metal-binding

Protein family/group databases

CAZyiGH34. Glycoside Hydrolase Family 34.

Names & Taxonomyi

Protein namesi
Recommended name:
NeuraminidaseUniRule annotation (EC:3.2.1.18UniRule annotation)
Gene namesi
Name:NAUniRule annotation
OrganismiInfluenza A virus (strain A/Teal/China/2978.1/2002 H5N1 genotype W)
Taxonomic identifieri284215 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA 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 UniRule annotation
  • Host apical cell membrane UniRule annotation; Single-pass type II membrane protein UniRule annotation

  • 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.UniRule annotation

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transmembranei‹1 – 13HelicalSequence analysisAdd BLAST›13
Topological domaini14 – 454Virion surfaceSequence analysisAdd BLAST441

GO - Cellular componenti

Keywords - Cellular componenti

Host cell membrane, Host membrane, Membrane, Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_0000310940‹1 – 454NeuraminidaseAdd BLAST›454

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi43N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Glycosylationi48N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Glycosylationi53N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Glycosylationi73N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Disulfide bondi77 ↔ 402UniRule annotation
Disulfide bondi109 ↔ 114UniRule annotation
Glycosylationi131N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Disulfide bondi169 ↔ 216UniRule annotation
Disulfide bondi218 ↔ 223UniRule annotation
Glycosylationi220N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Disulfide bondi264 ↔ 277UniRule annotation
Disulfide bondi266 ↔ 275UniRule annotation
Disulfide bondi303 ↔ 320UniRule annotation
Glycosylationi371N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Disulfide bondi406 ↔ 431UniRule annotation

Post-translational modificationi

N-glycosylated.UniRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliQ6DPI6.
SMRiQ6DPI6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni21 – 75Hypervariable stalk regionUniRule annotationAdd BLAST55
Regioni76 – 454Head of neuraminidaseUniRule annotationAdd BLAST379
Regioni262 – 263Substrate bindingUniRule annotation2

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.UniRule annotation

Sequence similaritiesi

Belongs to the glycosyl hydrolase 34 family.UniRule annotation

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Family and domain databases

CDDicd15483. Influenza_NA. 1 hit.
HAMAPiMF_04071. INFV_NRAM. 1 hit.
InterProiView protein in InterPro
IPR001860. Glyco_hydro_34.
IPR033654. Sialidase_Influenza_A/B.
IPR011040. Sialidases.
PfamiView protein in Pfam
PF00064. Neur. 1 hit.
SUPFAMiSSF50939. SSF50939. 1 hit.

Sequencei

Sequence statusi: Fragment.

Q6DPI6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
VIGIVSLMLQ IGNIISIWVS HSIQTGNQHQ AEPCIQSIIT YENNTWVNQT
60 70 80 90 100
YVNISNTNFL TEKTVASVTL AGNSSLCPIS GWAVYSKDNG IRIGSKGDVF
110 120 130 140 150
VIREPFISCS HLECRTFFLT QGALLNDKHS NGTVKDRSPH RTLMSCPVGE
160 170 180 190 200
APSPYNSRFE SVAWSASACH DGTNWLTIGI SGPDNGAVAV LKYNGIITDT
210 220 230 240 250
IKSWRNNILR TQESECACVN GSCFTVMTDG PSNGQASYKI FRIEKGKVVK
260 270 280 290 300
SVELNAPNYH YEECSCYPDA GEITCVCRDN WHGSNRPWVS FNQNLEYQIG
310 320 330 340 350
YICSGIFGDN PRPNDGTGSC GPVSSNGAYG IKGFSYKYGN GVWIGRTKST
360 370 380 390 400
NSRSGFEMIW DPNGWTGTDS NFSVKQDIVA ITDWSGYSGS FVQHPELTGL
410 420 430 440 450
DCIRPCFWVE LIRGRPKEST IWTSGSSISF CGVNSDTVGW SWPDGAELPF

TIDK
Length:454
Mass (Da):49,799
Last modified:July 22, 2008 - v2
Checksum:i09163590DFA4E0F0
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-terminal residuei11

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY651473 Genomic RNA. Translation: AAT73355.2.

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.

Entry informationi

Entry nameiNRAM_I02A7
AccessioniPrimary (citable) accession number: Q6DPI6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: July 22, 2008
Last modified: July 5, 2017
This is version 69 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families