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P31510

- NRAM_I85A8

UniProt

P31510 - NRAM_I85A8

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Protein

Neuraminidase

Gene
NA
Organism
Influenza A virus (strain A/Ruddy Turnstone/New Jersey/60/1985 H4N9)
Status
Reviewed - Annotation score: 5 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.

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.

Cofactori

Binds 1 calcium ion per subunit By similarity.

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei119 – 1191Substrate By similarity
Active sitei152 – 1521Proton donor/acceptor By similarity
Binding sitei153 – 1531Substrate By similarity
Binding sitei294 – 2941Substrate By similarity
Metal bindingi295 – 2951Calcium; via carbonyl oxygen By similarity
Metal bindingi299 – 2991Calcium; via carbonyl oxygen By similarity
Metal bindingi326 – 3261Calcium By similarity
Metal bindingi348 – 3481Calcium; via carbonyl oxygen By similarity
Binding sitei372 – 3721Substrate By similarity
Active sitei406 – 4061Nucleophile By similarity

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

Glycosidase, Hydrolase

Keywords - Ligandi

Calcium, Metal-binding

Protein family/group databases

CAZyiGH34. Glycoside Hydrolase Family 34.

Names & Taxonomyi

Protein namesi
Recommended name:
Neuraminidase (EC:3.2.1.18)
Gene namesi
Name:NA
OrganismiInfluenza A virus (strain A/Ruddy Turnstone/New Jersey/60/1985 H4N9)
Taxonomic identifieri31662 [NCBI]
Taxonomic lineageiVirusesssRNA negative-strand virusesOrthomyxoviridaeInfluenzavirus A
Virus hostiAves [TaxID: 8782]

Subcellular locationi

Virion membrane By similarity. Host apical cell membrane; Single-pass type II membrane protein By similarity
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 By similarity.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 66Intravirion Reviewed prediction
Transmembranei7 – 3529Helical; Signal-anchor for type II membrane protein; Reviewed predictionAdd
BLAST
Topological domaini36 – 470435Virion surface Reviewed predictionAdd
BLAST

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 membrane, Host membrane, Membrane, Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 470470NeuraminidasePRO_0000078715Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi42 – 421N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi52 – 521N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi63 – 631N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi66 – 661N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi87 – 871N-linked (GlcNAc...); by host Reviewed prediction
Disulfide bondi93 ↔ 419 By similarity
Disulfide bondi125 ↔ 130 By similarity
Glycosylationi147 – 1471N-linked (GlcNAc...); by host Reviewed prediction
Disulfide bondi177 ↔ 195 By similarity
Disulfide bondi185 ↔ 232 By similarity
Glycosylationi202 – 2021N-linked (GlcNAc...); by host Reviewed prediction
Disulfide bondi234 ↔ 239 By similarity
Disulfide bondi280 ↔ 293 By similarity
Disulfide bondi282 ↔ 291 By similarity
Disulfide bondi320 ↔ 338 By similarity
Disulfide bondi423 ↔ 449 By similarity

Post-translational modificationi

N-glycosylated By similarity.

Keywords - PTMi

Disulfide bond, Glycoprotein

Interactioni

Subunit structurei

Homotetramer By similarity.

Structurei

3D structure databases

ProteinModelPortaliP31510.
SMRiP31510. Positions 83-470.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni11 – 3323Involved in apical transport and lipid raft association By similarityAdd
BLAST
Regioni36 – 8954Hypervariable stalk regionAdd
BLAST
Regioni90 – 470381Head of neuraminidaseAdd
BLAST
Regioni278 – 2792Substrate binding By similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi345 – 3484Poly-Asn

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 By similarity.

Sequence similaritiesi

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

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.

P31510-1 [UniParc]FASTAAdd to Basket

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MNPNQKILFA SATAIVIGTI AVLIGIVNLG LNIGLHLKPS CNCSRSQPEA    50
TNASQTIINN YYNKTNITQI SNTNIQVEER ASREFNNLTK GLCTINSWHI 100
YGKDNAVRIG EDSDVLVTRE PYVSCDPDEC RFYALSQGTT IRGKHSNGTI 150
HDRSQYRALI SWPLSSPPTV YNSRVECIGW SSTSCHDGRA RMSICISGPN 200
NNASAVIWYN RRPVTEINTW ARNILRTQES ECVCHNGVCP VVFTDGSATG 250
PAETRIYYFK EGKILKWEPL TGTAKHIEEC SCYGEQARVT CTCRDNWQGS 300
NRPVIQIDPV AMTHTSQYIC SPVLTDNPRP NDPTVGKCND PYPGNNNNGV 350
KGFSYLDGGN TWLGRTISTA SRSGYEMLKV PNALTDDRSK PTQGQTIVLN 400
TDWSGYSGSF MDYWAEGECY RACFYVELIR GRPKEDRVWW TSNSIVSMCS 450
STEFLGQWNW PDGAKIEYFL 470
Length:470
Mass (Da):52,487
Last modified:July 1, 1993 - v1
Checksum:i28C5BECE89DBEA45
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M37511 Genomic RNA. Translation: AAA43426.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M37511 Genomic RNA. Translation: AAA43426.1 .

3D structure databases

ProteinModelPortali P31510.
SMRi P31510. Positions 83-470.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi GH34. Glycoside Hydrolase Family 34.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 2.120.10.10. 1 hit.
InterProi IPR001860. Glyco_hydro_34.
IPR011040. Sialidases.
[Graphical view ]
Pfami PF00064. Neur. 1 hit.
[Graphical view ]
SUPFAMi SSF50939. SSF50939. 1 hit.
ProtoNeti Search...

Publicationsi

  1. Air G.M., Laver W.G., Webster R.G.
    Submitted (AUG-1990) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  2. "Assembly and budding of influenza virus."
    Nayak D.P., Hui E.K., Barman S.
    Virus Res. 106:147-165(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  3. "Neuraminidase inhibitors for influenza."
    Moscona A.
    N. Engl. J. Med. 353:1363-1373(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  4. "Sialobiology of influenza: molecular mechanism of host range variation of influenza viruses."
    Suzuki Y.
    Biol. Pharm. Bull. 28:399-408(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.

Entry informationi

Entry nameiNRAM_I85A8
AccessioniPrimary (citable) accession number: P31510
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: September 3, 2014
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

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.

Documents

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

External Data

Dasty 3

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