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Protein

Neuraminidase

Gene
N/A
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

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

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

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)
OrganismiInfluenza A virus (A/Memphis/31/98(H3N2))Imported
Taxonomic identifieri228928 [NCBI]
Taxonomic lineageiVirusesssRNA negative-strand virusesOrthomyxoviridaeInfluenzavirus A

Subcellular locationi

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

GO - Cellular componenti

  1. host cell plasma membrane Source: UniProtKB-SubCell
  2. integral component of membrane Source: UniProtKB-KW
  3. virion membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

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

PTM / Processingi

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

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:May 31, 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(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
  2. Gulati U., Air G.M.
    Submitted (MAR-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(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 75-469 IN COMPLEX WITH MANNOSE AND N-ACETYL-D-GLUCOSAMINE, ACTIVE SITE.

Entry informationi

Entry nameiQ80DL0_9INFA
AccessioniPrimary (citable) accession number: Q80DL0
Entry historyi
Integrated into UniProtKB/TrEMBL: May 31, 2003
Last sequence update: May 31, 2003
Last modified: March 3, 2015
This is version 66 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.