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P08327

- NRAM_I74A1

UniProt

P08327 - NRAM_I74A1

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Protein

Neuraminidase

Gene
NA
Organism
Influenza A virus (strain A/Equine/Cor/16/1974 H7N7)
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 sitei115 – 1151Substrate By similarity
Active sitei148 – 1481Proton donor/acceptor By similarity
Binding sitei149 – 1491Substrate By similarity
Binding sitei290 – 2901Substrate By similarity
Metal bindingi291 – 2911Calcium; via carbonyl oxygen By similarity
Metal bindingi295 – 2951Calcium; via carbonyl oxygen By similarity
Metal bindingi322 – 3221Calcium By similarity
Binding sitei369 – 3691Substrate By similarity
Active sitei403 – 4031Nucleophile 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/Equine/Cor/16/1974 H7N7)
Taxonomic identifieri11397 [NCBI]
Taxonomic lineageiVirusesssRNA negative-strand virusesOrthomyxoviridaeInfluenzavirus A
Virus hostiAves [TaxID: 8782]
Equus caballus (Horse) [TaxID: 9796]
Homo sapiens (Human) [TaxID: 9606]
Phocidae (true seals) [TaxID: 9709]

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 – 469434Virion 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 – 469469NeuraminidasePRO_0000078694Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi46 – 461N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi55 – 551N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi66 – 661N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi85 – 851N-linked (GlcNAc...); by host Reviewed prediction
Disulfide bondi89 ↔ 417 By similarity
Disulfide bondi121 ↔ 126 By similarity
Glycosylationi143 – 1431N-linked (GlcNAc...); by host Reviewed prediction
Disulfide bondi173 ↔ 191 By similarity
Disulfide bondi181 ↔ 228 By similarity
Glycosylationi198 – 1981N-linked (GlcNAc...); by host Reviewed prediction
Disulfide bondi230 ↔ 235 By similarity
Glycosylationi232 – 2321N-linked (GlcNAc...); by host Reviewed prediction
Disulfide bondi276 ↔ 289 By similarity
Disulfide bondi278 ↔ 287 By similarity
Disulfide bondi316 ↔ 334 By similarity
Glycosylationi399 – 3991N-linked (GlcNAc...); by host Reviewed prediction
Disulfide bondi421 ↔ 448 By similarity

Post-translational modificationi

N-glycosylated By similarity.

Keywords - PTMi

Disulfide bond, Glycoprotein

Interactioni

Subunit structurei

Homotetramer By similarity.

Structurei

3D structure databases

ProteinModelPortaliP08327.
SMRiP08327. Positions 81-468.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni11 – 3323Involved in apical transport and lipid raft association By similarityAdd
BLAST
Regioni38 – 8851Hypervariable stalk regionAdd
BLAST
Regioni89 – 469381Head of neuraminidaseAdd
BLAST
Regioni274 – 2752Substrate binding By similarity

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.

P08327-1 [UniParc]FASTAAdd to Basket

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MNPNQKLFAS SGIAIVLGII NLLIGISNMS LNISLYSKGE SHKNNNLTCT    50
NINQNDTTMV NTYINNATII DKSTKIENPG YLLLNKSLCN VEGWVVIAKD 100
NAIRFGESEQ IIVTREPYVS CDPLSCKMYA LHQGTTIRNK HSNSTTHDRT 150
AFRGLISTPL GSPPTVSNSE FICVGWSSTS CHDGVNRMTI CVQGDNENAT 200
ATVYYNKRLT TTIKTWAKNI LRTQESECVC HNSTCVVVMT DGPANNQAFT 250
KVIYFHKGMI IKEESLKGSA KHIEECSCYG HNQRVTCVCR DNWQGANRPI 300
IEIDMNKLEH TSRYICTGVL TDTSRPKDKT IGECFNPITG SPGAPGIKGF 350
GFLNEDNTWL GRTISPRLRS GFEMLKIPNA GTDPESKIKE RQEIVSNDNW 400
SGYSGSFIDY WNDNSECYNP CFYVELIRGR PEEAKYVEWT SNSLIALCGS 450
PISVGSGSFP DGAQIKYFS 469
Length:469
Mass (Da):52,015
Last modified:August 1, 1988 - v1
Checksum:i45391CE693811E8E
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M14916 Genomic RNA. Translation: AAA43093.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M14916 Genomic RNA. Translation: AAA43093.1 .

3D structure databases

ProteinModelPortali P08327.
SMRi P08327. Positions 81-468.
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. "Nucleotide and deduced amino acid sequence of the influenza neuraminidase genes of two equine serotypes."
    Dale B., Brown R., Miller J., White R.T., Air G.M., Cordell B.
    Virology 155:460-468(1986) [PubMed] [Europe PMC] [Abstract]
    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_I74A1
AccessioniPrimary (citable) accession number: P08327
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: September 3, 2014
This is version 97 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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