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Q75VQ4

- NRAM_I68A0

UniProt

Q75VQ4 - NRAM_I68A0

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Protein

Neuraminidase

Gene

NA

Organism
Influenza A virus (strain A/Aichi/2/1968 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

Enzyme and pathway databases

SABIO-RKQ75VQ4.

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/Aichi/2/1968 H3N2)
Taxonomic identifieri387139 [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_0000280119Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi61 – 611N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi69 – 691N-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
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

ProteinModelPortaliQ75VQ4.
SMRiQ75VQ4. Positions 82-469.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 99IntravirionSequence Analysis
Topological domaini31 – 469439Virion surfaceSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei10 – 3021Helical; 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
Regioni36 – 9055Hypervariable stalk regionBy similarityAdd
BLAST
Regioni91 – 469379Head of neuraminidaseBy similarityAdd
BLAST
Regioni276 – 2772Substrate bindingBy 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.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.

Q75VQ4-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNPNQKIITI GSVSLTIATV CFLMQIAILV TTVTLHFKQY ECDSPASNQV
60 70 80 90 100
MPCEPIIIER NITEIVYLNN TTIDKEKCPK VVEYRNWSKP QCQITGFAPF
110 120 130 140 150
SKDNSIRLSA GGDIWVTREP YVSCDHGKCY QFALGQGTTL DNKHSNDTIH
160 170 180 190 200
DRIPHRTLLM NELGVPFHLG TRQVCIAWSS SSCHDGKAWL HVCITGDDKN
210 220 230 240 250
ATASFIYDGR LVDSIGSWSQ NILRTQESEC VCINGTCTVV MTDGSASGRA
260 270 280 290 300
DTRILFIEEG KIVHISPLSG SAQHVEECSC YPRYPGVRCI CRDNWKGSNR
310 320 330 340 350
PVVDINMEDY SIDSSYVCSG LVGDTPRNDD RSSNSNCRNP NNERGNQGVK
360 370 380 390 400
GWAFDNGDDV WMGRTISKDL RSGYETFKVI GGWSTPNSKS QINRQVIVDS
410 420 430 440 450
DNRSGYSGIF SVEGKSCINR CFYVELIRGR KQETRVWWTS NSIVVFCGTS
460
GTYGTGSWPD GANINFMPI
Length:469
Mass (Da):52,186
Last modified:July 5, 2004 - v1
Checksum:i868C7625A7D60CC7
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB124658 Genomic RNA. Translation: BAD16642.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB124658 Genomic RNA. Translation: BAD16642.1 .

3D structure databases

ProteinModelPortali Q75VQ4.
SMRi Q75VQ4. Positions 82-469.
ModBasei Search...
MobiDBi Search...

Chemistry

BindingDBi Q75VQ4.
ChEMBLi CHEMBL1287607.

Protein family/group databases

CAZyi GH34. Glycoside Hydrolase Family 34.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

SABIO-RK Q75VQ4.

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. "Evolutional analysis of human influenza A virus N2 neuraminidase genes based on the transition of the low-pH stability of sialidase activity."
    Suzuki T., Takahashi T., Saito T., Guo C.T., Hidari K.I.-P.J., Miyamoto D., Suzuki Y.
    FEBS Lett. 557:228-232(2004) [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_I68A0
AccessioniPrimary (citable) accession number: Q75VQ4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 6, 2007
Last sequence update: July 5, 2004
Last modified: October 29, 2014
This is version 64 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