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Q6DPI6

- NRAM_I02A7

UniProt

Q6DPI6 - NRAM_I02A7

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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: 5 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.

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 sitei103 – 1031SubstrateBy similarity
Active sitei136 – 1361Proton donor/acceptorBy similarity
Binding sitei137 – 1371SubstrateBy similarity
Binding sitei278 – 2781SubstrateBy similarity
Metal bindingi279 – 2791Calcium; via carbonyl oxygenBy similarity
Metal bindingi283 – 2831Calcium; via carbonyl oxygenBy similarity
Metal bindingi309 – 3091CalciumBy similarity
Binding sitei353 – 3531SubstrateBy similarity
Active sitei387 – 3871NucleophileBy 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
Complete GO annotation...

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/Teal/China/2978.1/2002 H5N1 genotype W)
Taxonomic identifieri284215 [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-KW
  2. integral component of membrane Source: UniProtKB-KW
  3. virion membrane Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Host cell membrane, Host membrane, Membrane, Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini‹1 – 454›454NeuraminidasePRO_0000310940Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi43 – 431N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi48 – 481N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi53 – 531N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi73 – 731N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi77 ↔ 402By similarity
Disulfide bondi109 ↔ 114By similarity
Glycosylationi131 – 1311N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi169 ↔ 216By similarity
Disulfide bondi218 ↔ 223By similarity
Glycosylationi220 – 2201N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi264 ↔ 277By similarity
Disulfide bondi266 ↔ 275By similarity
Disulfide bondi303 ↔ 320By similarity
Disulfide bondi406 ↔ 431By similarity

Post-translational modificationi

N-glycosylated.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Interactioni

Subunit structurei

Homotetramer.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ6DPI6.
SMRiQ6DPI6. Positions 68-452.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini14 – 454441Virion surfaceSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei‹1 – 13›13HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni21 – 7555Hypervariable stalk regionBy similarityAdd
BLAST
Regioni76 – 454379Head of neuraminidaseBy similarityAdd
BLAST
Regioni262 – 2632Substrate 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: Fragment.

Q6DPI6 [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)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY651473 Genomic RNA. Translation: AAT73355.2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY651473 Genomic RNA. Translation: AAT73355.2 .

3D structure databases

ProteinModelPortali Q6DPI6.
SMRi Q6DPI6. Positions 68-452.
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_I02A7
AccessioniPrimary (citable) accession number: Q6DPI6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: July 22, 2008
Last modified: October 29, 2014
This is version 58 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