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Protein

Neuraminidase

Gene

NA

Organism
Influenza A virus (strain A/Gull/Maryland/704/1977 H13N6)
Status
Reviewed-Annotation score: Annotation score: 4 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.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

Ca2+UniRule annotation

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.UniRule annotation

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 annotation1
Metal bindingi299Calcium; via carbonyl oxygenUniRule annotation1
Metal bindingi326CalciumUniRule annotation1
Binding sitei373SubstrateUniRule annotation1
Active sitei407NucleophileUniRule 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/Gull/Maryland/704/1977 H13N6)
Taxonomic identifieri384499 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA negative-strand virusesOrthomyxoviridaeInfluenzavirus A
Virus hostiAves [TaxID: 8782]
Proteomesi
  • UP000000828 Componenti: Genome

Subcellular locationi

  • Virion membrane UniRule annotation
  • Host apical cell membrane UniRule annotation; Single-pass type II membrane protein UniRule annotation
  • 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.UniRule annotation

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 6IntravirionUniRule annotation6
Transmembranei7 – 27HelicalUniRule annotationAdd BLAST21
Topological domaini28 – 471Virion surfaceUniRule annotationAdd BLAST444

GO - Cellular componenti

Keywords - Cellular componenti

Host cell membrane, Host membrane, Membrane, Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002801331 – 471NeuraminidaseAdd BLAST471

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi51N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Glycosylationi54N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Glycosylationi63N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Glycosylationi68N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Glycosylationi71N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Glycosylationi87N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Disulfide bondi93 ↔ 420UniRule annotation
Disulfide bondi125 ↔ 130UniRule annotation
Glycosylationi147N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Disulfide bondi185 ↔ 232UniRule annotation
Glycosylationi202N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Disulfide bondi234 ↔ 239UniRule annotation
Disulfide bondi280 ↔ 293UniRule annotation
Disulfide bondi282 ↔ 291UniRule annotation
Disulfide bondi320 ↔ 338UniRule annotation
Glycosylationi403N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Disulfide bondi424 ↔ 450UniRule annotation

Post-translational modificationi

N-glycosylated.UniRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliQ6XV23.
SMRiQ6XV23.
ModBaseiSearch...
MobiDBiSearch...

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 – 471Head of neuraminidaseUniRule annotationAdd BLAST380
Regioni278 – 279Substrate 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.
IPR011040. Sialidases.
PfamiView protein in Pfam
PF00064. Neur. 1 hit.
SUPFAMiSSF50939. SSF50939. 1 hit.

Sequencei

Sequence statusi: Complete.

Q6XV23-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNPNQKIICI SATGMTLSVV SLLIGIANLG LNIGLHYKVG DTPDVNTPNV
60 70 80 90 100
NGTNSTTTTI INNNTQNNFT NITNIIHNKN EERTFLNLTK PLCEVNSWHI
110 120 130 140 150
LSKDNAIRIG EEAHILVTRE PYLSCDPQGC RMFALSQGTT LRGRHANGTI
160 170 180 190 200
HDRSPFRALV SWEMGQAPSP YNAKIECIGW SSTSCHDGIS RMSICMSGPN
210 220 230 240 250
NNASAVVWYG GRPVTEIPSW AGNILRTQES ECVCHKGICP VVMTDGPANN
260 270 280 290 300
KAATKIIYFK EGKIQKIEEL TGNAQHIEEC SCYGAKEVIK CICRDNWKGA
310 320 330 340 350
NRPVITIDPE MMTHTSKYLC SKILTDTSRP NDPTNGNCDA PITGGNPDPG
360 370 380 390 400
VKGFAFLDGE NSWLGRTISK DSRSGYEMLK VPNAETNTQS GPITHQVIVN
410 420 430 440 450
NQNWSGYSGA FIDYWANKEC FNPCFYVELI RGRPKESSVL WTSNSIVALC
460 470
GSKERLGSWS WHDGAEIIYF K
Length:471
Mass (Da):51,888
Last modified:July 5, 2004 - v1
Checksum:i806ED70D97E7AA78
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY207553 Genomic DNA. Translation: AAO62067.1.
CY014696 Genomic RNA. Translation: ABI84569.1.

Similar proteinsi

Entry informationi

Entry nameiNRAM_I77AF
AccessioniPrimary (citable) accession number: Q6XV23
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 6, 2007
Last sequence update: July 5, 2004
Last modified: September 27, 2017
This is version 77 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

Complete proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families