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Protein

Neuraminidase

Gene

NA

Organism
Influenza A virus (strain A/Duck/England/1/1956 H11N6)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

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

Protein has several cofactor binding sites:
  • Note: Binds 1 Ca2+ ion per subunit.2 Publications
  • Ca2+UniRule annotation2 Publications

Activity 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 sitei118SubstrateUniRule annotation1
Active sitei151Proton donor/acceptorUniRule annotation1
Binding sitei152SubstrateUniRule annotation1
Binding sitei293SubstrateUniRule annotation1
Metal bindingi294Calcium; via carbonyl oxygenUniRule annotation2 Publications1
Metal bindingi298Calcium; via carbonyl oxygenUniRule annotation2 Publications1
Metal bindingi325CalciumUniRule annotation2 Publications1
Metal bindingi348Calcium; via carbonyl oxygen2 Publications1
Binding sitei372SubstrateUniRule annotation1
Active sitei406NucleophileUniRule 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/Duck/England/1/1956 H11N6)
Taxonomic identifieri383550 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA negative-strand virusesOrthomyxoviridaeAlphainfluenzavirus
Virus hostiAves [TaxID: 8782]
Proteomesi
  • UP000155465 Componenti: Genome

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 6IntravirionUniRule annotation6
Transmembranei7 – 27HelicalUniRule annotationAdd BLAST21
Topological domaini28 – 470Virion surfaceUniRule annotationAdd BLAST443

GO - Cellular componenti

Keywords - Cellular componenti

Host cell membrane, Host membrane, Membrane, Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002801271 – 470NeuraminidaseAdd BLAST470

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi51N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Glycosylationi54N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Glycosylationi62N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Glycosylationi67N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Glycosylationi70N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Glycosylationi86N-linked (GlcNAc...) asparagine; by hostUniRule annotation1 Publication1
Disulfide bondi92 ↔ 419UniRule annotation
Disulfide bondi124 ↔ 129UniRule annotation
Glycosylationi146N-linked (GlcNAc...) asparagine; by hostUniRule annotation2 Publications1
Disulfide bondi176 ↔ 194
Disulfide bondi184 ↔ 231UniRule annotation
Glycosylationi201N-linked (GlcNAc...) asparagine; by hostUniRule annotation1 Publication1
Disulfide bondi233 ↔ 238UniRule annotation
Disulfide bondi279 ↔ 292UniRule annotation
Disulfide bondi281 ↔ 290UniRule annotation
Disulfide bondi319 ↔ 337UniRule annotation
Glycosylationi402N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Disulfide bondi423 ↔ 449UniRule annotation

Post-translational modificationi

N-glycosylated.UniRule annotation2 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein

Interactioni

Subunit structurei

Homotetramer.UniRule annotation2 Publications

Structurei

Secondary structure

1470
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliQ6XV27
SMRiQ6XV27
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ6XV27

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni11 – 33Involved in apical transport and lipid raft associationUniRule annotationAdd BLAST23
Regioni36 – 88Hypervariable stalk regionUniRule annotationAdd BLAST53
Regioni91 – 470Head of neuraminidaseUniRule annotationAdd BLAST380
Regioni277 – 278Substrate 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

Phylogenomic databases

OrthoDBiVOG0900006X

Family and domain databases

HAMAPiMF_04071 INFV_NRAM, 1 hit
InterProiView protein in InterPro
IPR001860 Glyco_hydro_34
IPR036278 Sialidase_sf
PfamiView protein in Pfam
PF00064 Neur, 1 hit
SUPFAMiSSF50939 SSF50939, 1 hit

Sequencei

Sequence statusi: Complete.

Q6XV27-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MNPNQKIICI SATGMTLSVV SLLVGIANLG LNIGLHYKVG DTPNVNIPNV
60 70 80 90 100
NGTNSTTTII NNNTQNNFTN ITNIIQSKGG ERTFLNLTKP LCEVNSWHIL
110 120 130 140 150
SKDNAIRIGE DAHILVTREP YLSCDPQGCR MFALSQGTTL RGRHANGTIH
160 170 180 190 200
DRSPFRALIS WEMGQAPSPY NTRVECIGWS STSCHDGMSR MSICMSGPNN
210 220 230 240 250
NASAVVWYGG RPITEIPSWA GNILRTQESE CVCHKGVCPV VMTDGPANNR
260 270 280 290 300
AATKIIYFKE GKIQKIEELA GNAQHIEECS CYGAGGVIKC ICRDNWKGAN
310 320 330 340 350
RPVITIDPEM MTHTSKYLCS KVLTDTSRPN DPTNGNCDAP ITGGSPDPGV
360 370 380 390 400
KGFAFLDGEN SWLGRTISKD SRSGYEMLKV PNAETDIQSG PISNQVIVNN
410 420 430 440 450
QNWSGYSGAF IDYWANKECF NPCFYVELIR GRPKESSVLW TSNSIVALCG
460 470
SKKRLGSWSW HDGAEIIYFE
Length:470
Mass (Da):51,470
Last modified:July 5, 2004 - v1
Checksum:iC3C30CB83D15E0E7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY207549 Genomic DNA Translation: AAO62063.1
AB288846 Genomic RNA Translation: BAF43436.1
CY014681 Genomic RNA Translation: ABI84548.1
K01039 Genomic RNA Translation: AAA43389.1

Similar proteinsi

Entry informationi

Entry nameiNRAM_I56A2
AccessioniPrimary (citable) accession number: Q6XV27
Secondary accession number(s): Q83982
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 20, 2007
Last sequence update: July 5, 2004
Last modified: September 12, 2018
This is version 79 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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