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Q809V2

- NRAM_I01A2

UniProt

Q809V2 - NRAM_I01A2

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Protein

Neuraminidase

Gene

NA

Organism
Influenza A virus (strain A/Chicken/Hong Kong/FY150/2001 H5N1 genotype D)
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

Ca2+By similarityNote: Binds 1 Ca(2+) 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 sitei118 – 1181SubstrateBy similarity
Active sitei151 – 1511Proton donor/acceptorBy similarity
Binding sitei152 – 1521SubstrateBy similarity
Binding sitei293 – 2931SubstrateBy similarity
Metal bindingi294 – 2941Calcium; via carbonyl oxygenBy similarity
Metal bindingi298 – 2981Calcium; via carbonyl oxygenBy similarity
Metal bindingi324 – 3241CalciumBy similarity
Binding sitei368 – 3681SubstrateBy similarity
Active sitei402 – 4021NucleophileBy 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/Chicken/Hong Kong/FY150/2001 H5N1 genotype D)
Taxonomic identifieri222142 [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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 66IntravirionSequence Analysis
Transmembranei7 – 2721HelicalSequence AnalysisAdd
BLAST
Topological domaini28 – 469442Virion surfaceSequence AnalysisAdd
BLAST

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
Chaini1 – 469469NeuraminidasePRO_0000310932Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi50 – 501N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi58 – 581N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi63 – 631N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi68 – 681N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi88 – 881N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi92 ↔ 417By similarity
Disulfide bondi124 ↔ 129By similarity
Glycosylationi146 – 1461N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi184 ↔ 231By similarity
Disulfide bondi233 ↔ 238By similarity
Glycosylationi235 – 2351N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi279 ↔ 292By similarity
Disulfide bondi281 ↔ 290By similarity
Disulfide bondi318 ↔ 335By similarity
Glycosylationi386 – 3861N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi421 ↔ 446By similarity

Post-translational modificationi

N-glycosylated.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Interactioni

Subunit structurei

Homotetramer.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ809V2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni11 – 3323Involved in apical transport and lipid raft associationBy similarityAdd
BLAST
Regioni36 – 9055Hypervariable stalk regionBy similarityAdd
BLAST
Regioni91 – 469379Head of neuraminidaseBy similarityAdd
BLAST
Regioni277 – 2782Substrate 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.

Q809V2-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNPNQKIITI GSICMVIGIV SLMLQIGNII SIWVSHSIQT GNQHQAEPCN
60 70 80 90 100
QSIITYENNT WVNQTYVNIS NTNLLTEKAV ASVTLAGNSS LCPISGWAVY
110 120 130 140 150
SKDNGIRIGS KGDVFVIREP FISCSHLECR TFFLTQGALL NDKHSNGTVK
160 170 180 190 200
DRSPYRTLMS CPVGEAPSPY NSRFESVAWS ASACHDGTSW LTIGISGPDN
210 220 230 240 250
GAVAVLKYNG IITDTIKSWR NNILRTQESE CACVNGSCFT VMTDGPSNGQ
260 270 280 290 300
ASYKIFKIEK GKVVKSVELN APNYHYEECS CYPDAGEITC VCRDNWHGSN
310 320 330 340 350
RPWVSFNQNL EYQIGYICSG VFGDNPRPND GTGSCGPVSP NGAYGIKGFS
360 370 380 390 400
FKYGNGVWIG RTKSTNSRSG FEMIWDPNGW TGTDSNFSVK QDIVAITDWS
410 420 430 440 450
GYSGSFVQHP ELTGVDCIRP CFWVELIRGR PKESTIWTSG SSISFCGVNS
460
DTVGWSWPDG AELPFTIDK
Length:469
Mass (Da):51,318
Last modified:June 1, 2003 - v1
Checksum:i7CDB0E90A8D07702
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF509095 Genomic DNA. Translation: AAO52938.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF509095 Genomic DNA. Translation: AAO52938.1 .

3D structure databases

ProteinModelPortali Q809V2.
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].

Entry informationi

Entry nameiNRAM_I01A2
AccessioniPrimary (citable) accession number: Q809V2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: June 1, 2003
Last modified: November 26, 2014
This is version 68 of the entry and version 1 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