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Protein

Neuraminidase

Gene

NA

Organism
Influenza A virus (strain A/Chicken/Victoria/1/1985 H7N7)
Status
Reviewed-Annotation score: 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 Ca2+ 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)DescriptionActionsGraphical viewLength
Binding sitei117SubstrateBy similarity1
Active sitei150Proton donor/acceptorBy similarity1
Binding sitei151SubstrateBy similarity1
Binding sitei292SubstrateBy similarity1
Metal bindingi293Calcium; via carbonyl oxygenBy similarity1
Metal bindingi297Calcium; via carbonyl oxygenBy similarity1
Metal bindingi324CalciumBy similarity1
Binding sitei371SubstrateBy similarity1
Active sitei405NucleophileBy similarity1

GO - Molecular functioni

GO - Biological processi

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/Victoria/1/1985 H7N7)
Taxonomic identifieri402520 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA negative-strand virusesOrthomyxoviridaeInfluenzavirus A
Virus hostiAves [TaxID: 8782]
Equus caballus (Horse) [TaxID: 9796]
Homo sapiens (Human) [TaxID: 9606]
Phocidae (true seals) [TaxID: 9709]

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)DescriptionActionsGraphical viewLength
Topological domaini1 – 6IntravirionSequence analysis6
Transmembranei7 – 27Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST21
Topological domaini28 – 471Virion surfaceSequence analysisAdd BLAST444

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Host cell membrane, Host membrane, Membrane, Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002801261 – 471NeuraminidaseAdd BLAST471

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi32N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi47N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi56N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi57N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi67N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi68N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi87N-linked (GlcNAc...); by hostSequence analysis1
Disulfide bondi91 ↔ 419By similarity
Disulfide bondi123 ↔ 128By similarity
Glycosylationi145N-linked (GlcNAc...); by hostSequence analysis1
Disulfide bondi175 ↔ 193By similarity
Disulfide bondi183 ↔ 230By similarity
Glycosylationi200N-linked (GlcNAc...); by hostSequence analysis1
Disulfide bondi232 ↔ 237By similarity
Glycosylationi234N-linked (GlcNAc...); by hostSequence analysis1
Disulfide bondi278 ↔ 291By similarity
Disulfide bondi280 ↔ 289By similarity
Disulfide bondi318 ↔ 336By similarity
Glycosylationi401N-linked (GlcNAc...); by hostSequence analysis1
Disulfide bondi423 ↔ 450By similarity

Post-translational modificationi

N-glycosylated.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Interactioni

Subunit structurei

Homotetramer.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ0A2R1.
SMRiQ0A2R1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni11 – 33Involved in apical transport and lipid raft associationBy similarityAdd BLAST23
Regioni36 – 89Hypervariable stalk regionBy similarityAdd BLAST54
Regioni90 – 471Head of neuraminidaseBy similarityAdd BLAST382
Regioni276 – 277Substrate bindingBy similarity2

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.

Q0A2R1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNPNQKLFAL SGVAIALSVL NLLIGISNVG LNVSLHLKGA GTKQEENLTC
60 70 80 90 100
TTITQNNTTV VENTYVNNTT IITKEPEFRA PSYLLLNKSL CNVEGWVVVA
110 120 130 140 150
KDNAIRFGES EQIIVTREPY VSCDPSGCKM YALHQGTTIR NKHSNGTIHD
160 170 180 190 200
RTAFRGLIST HLGTPPTVSN SDFICVGWSS TSCHDGIGRM TICVQGNNDN
210 220 230 240 250
ATATVYYNRR LTTTIKTWAR NILRTQESEC VCHNGTCAVV MTDGSASSQA
260 270 280 290 300
YTKVMYFHKG LVIKEEPLKG SAKHIEECSC YGHNQKITCV CRDNWQGANR
310 320 330 340 350
PIIEIDMTTL EHTSRYVCTG VLTDTSRPGD KPSGDCSNPI TGSPGAPGVK
360 370 380 390 400
GFGFLNGDNT WLGRTISPRS RSGFEMLKIP NAGTDPNSKI VERQEIVDNN
410 420 430 440 450
NWSGYSGSFI DYWDDGNECY NPCFYVELIR GRPEEAKYVW WTSNSLIALC
460 470
GSPFPVGSGS FPDGAQIQYF S
Length:471
Mass (Da):51,671
Last modified:October 17, 2006 - v1
Checksum:i8359283CF1DC87AE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CY015021 Genomic RNA. Translation: ABI85021.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CY015021 Genomic RNA. Translation: ABI85021.1.

3D structure databases

ProteinModelPortaliQ0A2R1.
SMRiQ0A2R1.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH34. Glycoside Hydrolase Family 34.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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.
ProtoNetiSearch...

Entry informationi

Entry nameiNRAM_I85A3
AccessioniPrimary (citable) accession number: Q0A2R1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 6, 2007
Last sequence update: October 17, 2006
Last modified: November 2, 2016
This is version 53 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

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.