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Protein

Neuraminidase

Gene

NA

Organism
Influenza A virus (A/Memphis/31/98(H3N2))
Status
Unreviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the removal of terminal sialic acid residues from viral and cellular glycoconjugates.UniRule annotation
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 (By similarity).SAAS annotation

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 annotationSAAS annotation

Cofactori

Ca2+UniRule annotationNote: Binds 1 Ca2+ ion per subunit.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei86 – 861N-acetyl-D-glucosamineCombined sources
Binding sitei200 – 2001N-acetyl-D-glucosamineCombined sources
Binding sitei234 – 2341N-acetyl-D-glucosamineCombined sources
Binding sitei284 – 2841N-acetyl-D-glucosamineCombined sources
Binding sitei391 – 3911MannoseCombined sources
Binding sitei437 – 4371N-acetyl-D-glucosamineCombined sources
Binding sitei454 – 4541N-acetyl-D-glucosamine; via carbonyl oxygenCombined sources

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

GlycosidaseUniRule annotationSAAS annotation, Hydrolase

Keywords - Ligandi

CalciumUniRule annotationSAAS annotation, Metal-bindingUniRule annotationSAAS annotation

Protein family/group databases

CAZyiGH34. Glycoside Hydrolase Family 34.

Names & Taxonomyi

Protein namesi
Recommended name:
NeuraminidaseUniRule annotationSAAS annotation (EC:3.2.1.18UniRule annotationSAAS annotation)
Gene namesi
Name:NAUniRule annotation
OrganismiInfluenza A virus (A/Memphis/31/98(H3N2))Imported
Taxonomic identifieri228928 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA negative-strand virusesOrthomyxoviridaeInfluenzavirus A

Subcellular locationi

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

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Host cell membraneUniRule annotationSAAS annotation, Host membrane, Membrane, VirionUniRule annotationSAAS annotation

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi92 ↔ 417Combined sources
Disulfide bondi124 ↔ 129Combined sources
Disulfide bondi175 ↔ 193Combined sources
Disulfide bondi183 ↔ 230Combined sources
Disulfide bondi232 ↔ 237Combined sources
Disulfide bondi278 ↔ 291Combined sources
Disulfide bondi280 ↔ 289Combined sources
Disulfide bondi318 ↔ 337Combined sources
Disulfide bondi421 ↔ 447Combined sources

Post-translational modificationi

N-glycosylated.UniRule annotation

Keywords - PTMi

Disulfide bondSAAS annotation, GlycoproteinUniRule annotation

Interactioni

Subunit structurei

Homotetramer.UniRule annotationSAAS annotation

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2AEQX-ray3.00A75-469[»]
ProteinModelPortaliQ80DL0.
SMRiQ80DL0. Positions 82-469.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ80DL0.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni393 – 3942N-acetyl-D-glucosamine bindingCombined sources

Sequence similaritiesi

Belongs to the glycosyl hydrolase 34 family.UniRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helixSAAS annotation

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.

Q80DL0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNPNQKIITI GSVSLTIATI CFLMQIAILV TTVTLHFKQY ECSSPPNNQV
60 70 80 90 100
MLCEPTIIER NITEIVYLTN TTIEKEICPK LAEYRNWSKP QCKITGFAPF
110 120 130 140 150
SKDNSIRLSA GGDIWVTREP YVSCDPDKCY QFALGQGTTL NNRHSNDTVH
160 170 180 190 200
DRTPYRTLLM NELGVPFHLG TKQVCIAWSS SSCHDGKAWL HVCVTGHDEN
210 220 230 240 250
ATASFIYDGR LVDSIGSWSK KILRTQESEC VCINGTCTVV MTDGSASGRA
260 270 280 290 300
DTKILFIEEG KIVHISPLSG SAQHVEECSC YPRYPGVRCV CRDNWKGSNR
310 320 330 340 350
PIVDINVKDY SIVSSYVCSG LVGDTPRKND SSSSSHCLNP NNEEGGHGVK
360 370 380 390 400
GWAFDDGNDV WMGRTISEKF RSGYETFKVI EGWSKPNSKL QINRQVIVDR
410 420 430 440 450
GNRSGYSGIF SVEGKSCINR CFYVELIRGR KQETEVWWTS NSIVVFCGTS
460
GTYGTGSWPD GADINLMPI
Length:469
Mass (Da):52,110
Last modified:June 1, 2003 - v1
Checksum:i46B453F12B0D2754
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY271795 Genomic RNA. Translation: AAP23239.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY271795 Genomic RNA. Translation: AAP23239.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2AEQX-ray3.00A75-469[»]
ProteinModelPortaliQ80DL0.
SMRiQ80DL0. Positions 82-469.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH34. Glycoside Hydrolase Family 34.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiQ80DL0.

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...

Publicationsi

  1. "Antibody epitopes on the neuraminidase of a recent H3N2 influenza virus (A/Memphis/31/98)."
    Gulati U., Hwang C.C., Venkatramani L., Gulati S., Stray S.J., Lee J.T., Laver W.G., Bochkarev A., Zlotnick A., Air G.M.
    J. Virol. 76:12274-12280(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
  2. Gulati U., Air G.M.
    Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
  3. "An epidemiologically significant epitope of a 1998 human influenza virus neuraminidase forms a highly hydrated interface in the NA-antibody complex."
    Venkatramani L., Bochkareva E., Lee J.T., Gulati U., Graeme Laver W., Bochkarev A., Air G.M.
    J. Mol. Biol. 356:651-663(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 75-469 IN COMPLEX WITH MANNOSE AND N-ACETYL-D-GLUCOSAMINE, DISULFIDE BONDS.

Entry informationi

Entry nameiQ80DL0_9INFA
AccessioniPrimary (citable) accession number: Q80DL0
Entry historyi
Integrated into UniProtKB/TrEMBL: June 1, 2003
Last sequence update: June 1, 2003
Last modified: June 24, 2015
This is version 69 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

External Data

Dasty 3

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 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.