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O91745

- NRAM_I96A1

UniProt

O91745 - NRAM_I96A1

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Protein

Neuraminidase

Gene

NA

Organism
Influenza A virus (strain A/Niigata/137/1996 H3N2)
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 sitei118 – 1181SubstrateBy similarity
Active sitei151 – 1511Proton donor/acceptorBy similarity
Binding sitei152 – 1521SubstrateBy similarity
Binding sitei292 – 2921SubstrateBy similarity
Metal bindingi293 – 2931Calcium; via carbonyl oxygenBy similarity
Metal bindingi297 – 2971Calcium; via carbonyl oxygenBy similarity
Metal bindingi324 – 3241CalciumBy similarity
Binding sitei371 – 3711SubstrateBy similarity
Active sitei406 – 4061NucleophileBy 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/Niigata/137/1996 H3N2)
Taxonomic identifieri109049 [NCBI]
Taxonomic lineageiVirusesssRNA negative-strand virusesOrthomyxoviridaeInfluenzavirus A
Virus hostiAves [TaxID: 8782]
Cetacea (whales) [TaxID: 9721]
Homo sapiens (Human) [TaxID: 9606]
Phocidae (true seals) [TaxID: 9709]
Sus scrofa (Pig) [TaxID: 9823]

Subcellular locationi

Virion membrane By similarity. Host apical cell membrane By similarity; 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.By similarity

GO - Cellular componenti

  1. host cell plasma membrane Source: UniProtKB-KW
  2. integral component of membrane Source: UniProtKB-KW
  3. virion membrane Source: InterPro
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_0000078709Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi61 – 611N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi70 – 701N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi86 – 861N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi92 ↔ 417By similarity
Disulfide bondi124 ↔ 129By similarity
Glycosylationi146 – 1461N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi175 ↔ 193By similarity
Disulfide bondi183 ↔ 230By similarity
Glycosylationi200 – 2001N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi232 ↔ 237By similarity
Glycosylationi234 – 2341N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi278 ↔ 291By similarity
Disulfide bondi280 ↔ 289By similarity
Disulfide bondi318 ↔ 337By similarity
Glycosylationi329 – 3291N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi402 – 4021N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi421 ↔ 447By similarity

Post-translational modificationi

N-glycosylated.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Interactioni

Subunit structurei

Homotetramer.By similarity

Structurei

3D structure databases

ProteinModelPortaliO91745.
SMRiO91745. Positions 82-469.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 66IntravirionSequence Analysis
Topological domaini36 – 469434Virion surfaceSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei7 – 3529Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni11 – 3323Involved in apical transport and lipid raft associationBy similarityAdd
BLAST
Regioni276 – 2772Substrate bindingBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi179 – 1824Poly-Ser
Compositional biasi331 – 3355Poly-Ser

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.By similarity

Sequence similaritiesi

Belongs to the glycosyl hydrolase 34 family.Curated

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.

O91745-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNPNQKIITI GSVSLTIATI CFLMQIAILV TTVTLHFKQY ECNSPPNNQV
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 YPRYSGVRCV CRDNWKGSNR
310 320 330 340 350
PIVDINVKDY SIVSSYVCSG LVGDTPRKND SSSSSHCLNP NNEEGGHGVK
360 370 380 390 400
GWAFDDGNDV WMGRTISEKL RSGYETFKVI GGWSKPNSKL QINRQVIVDR
410 420 430 440 450
GNRSGYSGIF SVEGKSCINR CFYVELIRGR KQETEVWWTS NSIVVFCGTS
460
GTYGTGSWPD GADINLMPI
Length:469
Mass (Da):52,021
Last modified:November 1, 1998 - v1
Checksum:iD5F1F00128023210
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF038262 Genomic RNA. Translation: AAC63470.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF038262 Genomic RNA. Translation: AAC63470.1 .

3D structure databases

ProteinModelPortali O91745.
SMRi O91745. Positions 82-469.
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. "Phylogenetic analysis of the entire genome of influenza A (H3N2) viruses from Japan: evidence for genetic reassortment of the six internal genes."
    Lindstrom S.E., Hiromoto Y., Nerome R., Omoe K., Sugita S., Yamazaki Y., Takahashi T., Nerome K.
    J. Virol. 72:8021-8031(1998) [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_I96A1
AccessioniPrimary (citable) accession number: O91745
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1998
Last modified: October 29, 2014
This is version 87 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