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Protein

Neuraminidase

Gene

NA

Organism
Influenza A virus (strain A/Tern/Australia/G70C/1975 H11N9)
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 annotation1 Publication

Cofactori

Protein has several cofactor binding sites:

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 annotation1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei119SubstrateUniRule annotation1
Active sitei152Proton donor/acceptorUniRule annotation1
Binding sitei153SubstrateUniRule annotation1
Binding sitei294SubstrateUniRule annotation1
Metal bindingi295Calcium; via carbonyl oxygenUniRule annotation4 Publications1
Metal bindingi299Calcium; via carbonyl oxygenUniRule annotation4 Publications1
Metal bindingi326CalciumUniRule annotation4 Publications1
Metal bindingi348Calcium; via carbonyl oxygenUniRule annotation4 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/Tern/Australia/G70C/1975 H11N9)
Taxonomic identifieri384509 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA negative-strand virusesOrthomyxoviridaeAlphainfluenzavirus
Virus hostiAves [TaxID: 8782]

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 14IntravirionUniRule annotationAdd BLAST14
Transmembranei15 – 35HelicalUniRule annotationAdd BLAST21
Topological domaini36 – 470Virion surfaceUniRule annotationAdd BLAST435

GO - Cellular componenti

Keywords - Cellular componenti

Host cell membrane, Host membrane, Membrane, Virion

Pathology & Biotechi

Chemistry databases

DrugBankiDB02600 5-N-Acetyl-3-(1-Ethylpropyl)-1-Cyclohexene-1-Carboxylic Acid
DB03655 Bcx-1812
DB03721 N-acetyl-alpha-neuraminic acid

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000787211 – 470NeuraminidaseAdd BLAST470

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi42N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Glycosylationi52N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Glycosylationi63N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Glycosylationi66N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Glycosylationi87N-linked (GlcNAc...) asparagine; by hostUniRule annotation3 Publications1
Disulfide bondi93 ↔ 419UniRule annotation
Disulfide bondi125 ↔ 130UniRule annotation
Glycosylationi147N-linked (GlcNAc...) asparagine; by hostUniRule annotation3 Publications1
Disulfide bondi177 ↔ 195
Disulfide bondi185 ↔ 232UniRule annotation
Glycosylationi202N-linked (GlcNAc...) asparagine; by hostUniRule annotation3 Publications1
Disulfide bondi234 ↔ 239UniRule annotation
Disulfide bondi280 ↔ 293UniRule annotation
Disulfide bondi282 ↔ 291UniRule annotation
Disulfide bondi320 ↔ 338UniRule annotation
Disulfide bondi423 ↔ 449UniRule annotation

Post-translational modificationi

N-glycosylated.UniRule annotation3 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PRIDEiP03472

PTM databases

iPTMnetiP03472

Interactioni

Subunit structurei

Homotetramer.UniRule annotation4 Publications

Chemistry databases

BindingDBiP03472

Structurei

Secondary structure

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

3D structure databases

ProteinModelPortaliP03472
SMRiP03472
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP03472

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni11 – 33Involved in apical transport and lipid raft associationUniRule annotationAdd BLAST23
Regioni36 – 89Hypervariable stalk regionUniRule annotationAdd BLAST54
Regioni92 – 470Head of neuraminidaseUniRule annotationAdd BLAST379
Regioni278 – 279Substrate bindingUniRule annotation2

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi345 – 348Poly-Asn4

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
IPR036278 Sialidase_sf
PfamiView protein in Pfam
PF00064 Neur, 1 hit
SUPFAMiSSF50939 SSF50939, 1 hit

Sequencei

Sequence statusi: Complete.

P03472-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MNPNQKILCT SATALVIGTI AVLIGITNLG LNIGLHLKPS CNCSHSQPEA
60 70 80 90 100
TNASQTIINN YYNDTNITQI SNTNIQVEER AIRDFNNLTK GLCTINSWHI
110 120 130 140 150
YGKDNAVRIG EDSDVLVTRE PYVSCDPDEC RFYALSQGTT IRGKHSNGTI
160 170 180 190 200
HDRSQYRALI SWPLSSPPTV YNSRVECIGW SSTSCHDGKT RMSICISGPN
210 220 230 240 250
NNASAVIWYN RRPVTEINTW ARNILRTQES ECVCHNGVCP VVFTDGSATG
260 270 280 290 300
PAETRIYYFK EGKILKWEPL AGTAKHIEEC SCYGERAEIT CTCRDNWQGS
310 320 330 340 350
NRPVIRIDPV AMTHTSQYIC SPVLTDNPRP NDPTVGKCND PYPGNNNNGV
360 370 380 390 400
KGFSYLDGVN TWLGRTISIA SRSGYEMLKV PNALTDDKSK PTQGQTIVLN
410 420 430 440 450
TDWSGYSGSF MDYWAEGECY RACFYVELIR GRPKEDKVWW TSNSIVSMCS
460 470
STEFLGQWDW PDGAKIEYFL
Length:470
Mass (Da):52,469
Last modified:July 21, 1986 - v1
Checksum:iF114226CF93E1370
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti377M → I in AAA43574 (PubMed:3660585).1
Sequence conflicti387 – 388DK → ER in AAA43574 (PubMed:3660585).2

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M11445 Genomic RNA Translation: AAA43353.1
M17813 Genomic RNA Translation: AAA43574.1
PIRiA00884 NMIV9

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M11445 Genomic RNA Translation: AAA43353.1
M17813 Genomic RNA Translation: AAA43574.1
PIRiA00884 NMIV9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1A14X-ray2.50N83-470[»]
1BJIX-ray2.00A83-470[»]
1F8BX-ray1.80A83-470[»]
1F8CX-ray1.70A83-470[»]
1F8DX-ray1.40A83-470[»]
1F8EX-ray1.40A83-470[»]
1INYX-ray2.40A83-470[»]
1L7FX-ray1.80A83-470[»]
1L7GX-ray1.85A83-470[»]
1L7HX-ray1.85A83-470[»]
1MWEX-ray1.70A83-470[»]
1NCAX-ray2.50N82-470[»]
1NCBX-ray2.50N82-470[»]
1NCCX-ray2.50N82-470[»]
1NMCX-ray2.50A/N83-470[»]
1NNAX-ray2.50A84-470[»]
1NNBX-ray2.80A84-470[»]
1NNCX-ray1.80A83-470[»]
1XOEX-ray2.20A84-470[»]
1XOGX-ray2.80A84-470[»]
2C4AX-ray2.15A83-470[»]
2C4LX-ray2.15A83-470[»]
2QWAX-ray1.70A83-470[»]
2QWBX-ray2.00A83-470[»]
2QWCX-ray1.60A83-470[»]
2QWDX-ray2.00A83-470[»]
2QWEX-ray2.00A83-470[»]
2QWFX-ray1.90A83-470[»]
2QWGX-ray1.80A83-470[»]
2QWHX-ray1.80A83-470[»]
2QWIX-ray2.00A83-470[»]
2QWJX-ray2.00A83-470[»]
2QWKX-ray1.80A83-470[»]
3NN9X-ray2.30A83-470[»]
3W09X-ray2.00A83-470[»]
4DGRX-ray1.55A82-470[»]
4NN9X-ray2.30A83-470[»]
4WEGX-ray2.10A83-470[»]
5NN9X-ray2.30A83-470[»]
5W26X-ray1.90A83-470[»]
5W2UX-ray2.00A83-470[»]
5W2WX-ray1.85A83-470[»]
5W2YX-ray2.39A83-470[»]
6HCXX-ray1.30A83-470[»]
6HEBX-ray1.75A83-470[»]
6HFCX-ray1.29A83-470[»]
6HG0X-ray1.30A83-470[»]
6NN9X-ray2.30A83-470[»]
7NN9X-ray2.00A83-470[»]
ProteinModelPortaliP03472
SMRiP03472
ModBaseiSearch...
MobiDBiSearch...

Chemistry databases

BindingDBiP03472
DrugBankiDB02600 5-N-Acetyl-3-(1-Ethylpropyl)-1-Cyclohexene-1-Carboxylic Acid
DB03655 Bcx-1812
DB03721 N-acetyl-alpha-neuraminic acid

Protein family/group databases

CAZyiGH34 Glycoside Hydrolase Family 34

PTM databases

iPTMnetiP03472

Proteomic databases

PRIDEiP03472

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP03472

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
IPR036278 Sialidase_sf
PfamiView protein in Pfam
PF00064 Neur, 1 hit
SUPFAMiSSF50939 SSF50939, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiNRAM_I75A5
AccessioniPrimary (citable) accession number: P03472
Secondary accession number(s): Q84070
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: October 10, 2018
This is version 141 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

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
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Main funding by: National Institutes of Health

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