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Protein

Neuraminidase

Gene

NA

Organism
Influenza A virus (strain swl A/California/04/2009 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. 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.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 1; via carbonyl oxygenCombined sources
Metal bindingi298 – 2981Calcium 1; via carbonyl oxygenCombined sources
Metal bindingi324 – 3241Calcium 1Combined sources
Metal bindingi342 – 3421Calcium 1; via carbonyl oxygenCombined sources
Metal bindingi344 – 3441Calcium 1; via carbonyl oxygenCombined sources
Metal bindingi376 – 3761Calcium 2Combined sources
Metal bindingi378 – 3781Calcium 2Combined sources
Metal bindingi384 – 3841Calcium 2Combined sources
Metal bindingi386 – 3861Calcium 2; via carbonyl oxygenCombined sources

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

GlycosidaseUniRule annotationSAAS annotation, Hydrolase

Keywords - Ligandi

CalciumUniRule annotationCombined sourcesSAAS annotation, Metal-bindingUniRule annotationCombined sourcesSAAS 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 (strain swl A/California/04/2009 H1N1)Imported
Taxonomic identifieri641501 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA negative-strand virusesOrthomyxoviridaeInfluenzavirus A
Virus hostiAves [TaxID: 8782]
Homo sapiens (Human) [TaxID: 9606]
Sus scrofa (Pig) [TaxID: 9823]

Subcellular locationi

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei7 – 3428HelicalSequence analysisAdd
BLAST

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 sourcesCAR_5006991053
Disulfide bondi92 ↔ 417Combined sources
Disulfide bondi124 ↔ 129Combined sources
Glycosylationi146 – 1461N-linked (GlcNAc...)Combined sourcesCAR_5006991049
Disulfide bondi184 ↔ 231Combined sources
Disulfide bondi233 ↔ 238Combined sources
Glycosylationi235 – 2351N-linked (GlcNAc...)Combined sourcesCAR_5006991051
Disulfide bondi279 ↔ 292Combined sources
Disulfide bondi281 ↔ 290Combined sources
Disulfide bondi318 ↔ 335Combined sources
Disulfide bondi421 ↔ 446Combined sources

Post-translational modificationi

N-glycosylated.UniRule annotation

Keywords - PTMi

Disulfide bondSAAS annotation, GlycoproteinUniRule annotation

Interactioni

Subunit structurei

Homotetramer.UniRule annotationSAAS annotation

Protein-protein interaction databases

DIPiDIP-59036N.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3NSSX-ray1.90A/B82-469[»]
3TI3X-ray1.80A/B82-469[»]
3TI4X-ray1.60A/B82-469[»]
3TI5X-ray1.90A/B82-469[»]
3TI6X-ray1.69A/B82-469[»]
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 34 family.UniRule annotationSAAS annotation

Keywords - Domaini

Transmembrane, Transmembrane helixSequence analysisSAAS 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.

C3W5S3-1 [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
SKDNSVRIGS KGDVFVIREP FISCSPLECR TFFLTQGALL NDKHSNGTIK
160 170 180 190 200
DRSPYRTLMS CPIGEVPSPY NSRFESVAWS ASACHDGINW LTIGISGPDN
210 220 230 240 250
GAVAVLKYNG IITDTIKSWR NNILRTQESE CACVNGSCFT VMTDGPSNGQ
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 TGTDNNFSIK QDIVGINEWS
410 420 430 440 450
GYSGSFVQHP ELTGLDCIRP CFWVELIRGR PKENTIWTSG SSISFCGVNS
460
DTVGWSWPDG AELPFTIDK
Length:469
Mass (Da):51,597
Last modified:June 16, 2009 - v1
Checksum:i24712B3623B0E964
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FJ966084 Viral cRNA. Translation: ACP41107.1.
FJ969517 Viral cRNA. Translation: ACP44158.1.
JF915186 Viral cRNA. Translation: AEE69012.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FJ966084 Viral cRNA. Translation: ACP41107.1.
FJ969517 Viral cRNA. Translation: ACP44158.1.
JF915186 Viral cRNA. Translation: AEE69012.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3NSSX-ray1.90A/B82-469[»]
3TI3X-ray1.80A/B82-469[»]
3TI4X-ray1.60A/B82-469[»]
3TI5X-ray1.90A/B82-469[»]
3TI6X-ray1.69A/B82-469[»]
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-59036N.

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. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: A/California/04/2009Imported.
  2. "Antigenic and genetic characteristics of swine-origin 2009 A(H1N1) influenza viruses circulating in humans."
    Garten R.J., Davis C.T., Russell C.A., Shu B., Lindstrom S., Balish A., Sessions W.M., Xu X., Skepner E., Deyde V., Okomo-Adhiambo M., Gubareva L., Barnes J., Smith C.B., Emery S.L., Hillman M.J., Rivailler P., Smagala J.
    , de Graaf M., Burke D.F., Fouchier R.A., Pappas C., Alpuche-Aranda C.M., Lopez-Gatell H., Olivera H., Lopez I., Myers C.A., Faix D., Blair P.J., Yu C., Keene K.M., Dotson P.D.Jr., Boxrud D., Sambol A.R., Abid S.H., St George K., Bannerman T., Moore A.L., Stringer D.J., Blevins P., Demmler-Harrison G.J., Ginsberg M., Kriner P., Waterman S., Smole S., Guevara H.F., Belongia E.A., Clark P.A., Beatrice S.T., Donis R., Katz J., Finelli L., Bridges C.B., Shaw M., Jernigan D.B., Uyeki T.M., Smith D.J., Klimov A.I., Cox N.J.
    Science 325:197-201(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: A/California/04/2009Imported.
  3. "The 2009 pandemic H1N1 neuraminidase N1 lacks the 150-cavity in its active site."
    Li Q., Qi J., Zhang W., Vavricka C.J., Shi Y., Wei J., Feng E., Shen J., Chen J., Liu D., He J., Yan J., Liu H., Jiang H., Teng M., Li X., Gao G.F.
    Nat. Struct. Mol. Biol. 17:1266-1268(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 82-469 IN COMPLEX WITH CALCIUM, DISULFIDE BONDS, GLYCOSYLATION AT ASN-88 AND ASN-146.
  4. "2009 Pandemic H1N1 Influenza Virus Causes Disease and Upregulation of Genes Related to Inflammatory and Immune Responses, Cell Death, and Lipid Metabolism in Pigs."
    Ma W., Belisle S.E., Mosier D., Li X., Stigger-Rosser E., Liu Q., Qiao C., Elder J., Webby R., Katze M.G., Richt J.A.
    J. Virol. 85:11626-11637(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: A/California/04/2009Imported.
  5. "Structural and functional analysis of laninamivir and its octanoate prodrug reveals group specific mechanisms for influenza NA inhibition."
    Vavricka C.J., Li Q., Wu Y., Qi J., Wang M., Liu Y., Gao F., Liu J., Feng E., He J., Wang J., Liu H., Jiang H., Gao G.F.
    PLoS Pathog. 7:e1002249-e1002249(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 82-469 IN COMPLEX WITH CALCIUM, DISULFIDE BONDS, GLYCOSYLATION AT ASN-88; ASN-146 AND ASN-235.

Entry informationi

Entry nameiC3W5S3_I09A0
AccessioniPrimary (citable) accession number: C3W5S3
Entry historyi
Integrated into UniProtKB/TrEMBL: June 16, 2009
Last sequence update: June 16, 2009
Last modified: May 11, 2016
This is version 54 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

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.