Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Neuraminidase

Gene

NA

Organism
Influenza A virus (A/Netherlands/2631_1202/2010(H1N1))
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
Metal bindingi294 – 2941Calcium; via carbonyl oxygen
Metal bindingi298 – 2981Calcium; via carbonyl oxygen
Metal bindingi324 – 3241Calcium
Metal bindingi342 – 3421Calcium; via carbonyl oxygen
Metal bindingi344 – 3441Calcium; via carbonyl oxygen

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

Names & Taxonomyi

Protein namesi
Recommended name:
NeuraminidaseUniRule annotationSAAS annotation (EC:3.2.1.18UniRule annotationSAAS annotation)
Gene namesi
Name:NAUniRule annotationImported
OrganismiInfluenza A virus (A/Netherlands/2631_1202/2010(H1N1))Imported
Taxonomic identifieri1027873 [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
Glycosylationi88 – 881N-linked (GlcNAc...)Combined sources
Disulfide bondi92 ↔ 417
Disulfide bondi124 ↔ 129
Glycosylationi146 – 1461N-linked (GlcNAc...)Combined sources
Disulfide bondi184 ↔ 231
Disulfide bondi233 ↔ 238
Glycosylationi235 – 2351N-linked (GlcNAc...)Combined sources
Disulfide bondi279 ↔ 292
Disulfide bondi281 ↔ 290
Disulfide bondi318 ↔ 335
Disulfide bondi421 ↔ 446

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
4B7JX-ray2.42A1-469[»]
4B7MX-ray2.50A/B1-469[»]
4B7NX-ray2.84A1-469[»]
ModBaseiSearch...
MobiDBiSearch...

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.

F8UU09-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNPNQKIITI GSVCMTIGMA NLILQIGNII SIWISHSIQL GNQNQIETCN
60 70 80 90 100
QSVITYENNT WVNQTYVNIS NTNFAAGQSV VSVKLAGNSS LCPVSGWAIY
110 120 130 140 150
SKDNSIRIGS KGDVFVIREP FISCSPLECR TFFLTQGALL NDKHSNGTIK
160 170 180 190 200
DRSPYRTLMS CPIGEVPSPY NSRFESVAWS ASACHDGINW LTIGISGPDN
210 220 230 240 250
GAVAVLKYNG IITDTIKSWR NNRLRTQESE CACVNGSCFT VMTDGPSDGQ
260 270 280 290 300
ASYKIFRIEK GKIVKSVEMN APNYHYEECS CYPDSSEITC VCRDNWHGSN
310 320 330 340 350
RPWVSFNQNL EYQIGYICSG IFGDNPRPND KTGSCGPVSS NGANGVKGFS
360 370 380 390 400
FKYGNGVWIG RTKSISSRNG FEMIWDPNGW TGTDNDFSIK QDIVGINEWS
410 420 430 440 450
GYSGSFVQHP ELTGLDCIRP CFWVELIRGR PKENTIWTSG SSISFCGVNS
460
DTVGWSWPDG AELPFTIDK
Length:469
Mass (Da):51,656
Last modified:September 21, 2011 - v1
Checksum:i48F0F60CD8119D39
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
JF906185 Viral cRNA. Translation: AEE69001.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
JF906185 Viral cRNA. Translation: AEE69001.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4B7JX-ray2.42A1-469[»]
4B7MX-ray2.50A/B1-469[»]
4B7NX-ray2.84A1-469[»]
ModBaseiSearch...
MobiDBiSearch...

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...

Publicationsi

  1. "Multidrug Resistant 2009 A/H1N1 Influenza Clinical Isolate with a Neuraminidase I223R Mutation Retains Its Virulence and Transmissibility in Ferrets."
    van der Vries E., Veldhuis Kroeze E.J., Stittelaar K.J., Linster M., Van der Linden A., Schrauwen E.J., Leijten L.M., van Amerongen G., Schutten M., Kuiken T., Osterhaus A.D., Fouchier R.A., Boucher C.A., Herfst S.
    PLoS Pathog. 7:E1002276-E1002276(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: A/Netherlands/2631_1202/2010Imported.
  2. "H1N1 2009 pandemic influenza virus: resistance of the I223R neuraminidase mutant explained by kinetic and structural analysis."
    van der Vries E., Collins P.J., Vachieri S.G., Xiong X., Liu J., Walker P.A., Haire L.F., Hay A.J., Schutten M., Osterhaus A.D., Martin S.R., Boucher C.A., Skehel J.J., Gamblin S.J.
    PLoS Pathog. 8:e1002914-e1002914(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.42 ANGSTROMS) IN COMPLEX WITH CALCIUM, DISULFIDE BONDS, GLYCOSYLATION AT ASN-88; ASN-146 AND ASN-235.

Entry informationi

Entry nameiF8UU09_9INFA
AccessioniPrimary (citable) accession number: F8UU09
Entry historyi
Integrated into UniProtKB/TrEMBL: September 21, 2011
Last sequence update: September 21, 2011
Last modified: June 24, 2015
This is version 24 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structure

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.