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A3KF10

- NRAM_I56A1

UniProt

A3KF10 - NRAM_I56A1

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Protein

Neuraminidase

Gene

NA

Organism
Influenza A virus (strain A/Duck/Czechoslovakia/1956 H4N6)
Status
Reviewed - Annotation score: 4 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 (By similarity).By similarity

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

Ca2+By similarityNote: Binds 1 Ca(2+) 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 (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei118 – 1181SubstrateBy similarity
Active sitei151 – 1511Proton donor/acceptorBy similarity
Binding sitei152 – 1521SubstrateBy similarity
Binding sitei293 – 2931SubstrateBy similarity
Metal bindingi294 – 2941Calcium; via carbonyl oxygenBy similarity
Metal bindingi298 – 2981Calcium; via carbonyl oxygenBy similarity
Metal bindingi325 – 3251CalciumBy similarity
Binding sitei372 – 3721SubstrateBy 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/Duck/Czechoslovakia/1956 H4N6)
Taxonomic identifieri385590 [NCBI]
Taxonomic lineageiVirusesssRNA negative-strand virusesOrthomyxoviridaeInfluenzavirus A
Virus hostiAves [TaxID: 8782]
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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 66IntravirionSequence Analysis
Transmembranei7 – 3428Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini35 – 470436Virion surfaceSequence AnalysisAdd
BLAST

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 – 470470NeuraminidasePRO_0000402431Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi51 – 511N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi54 – 541N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi62 – 621N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi67 – 671N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi70 – 701N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi86 – 861N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi92 ↔ 419By similarity
Disulfide bondi124 ↔ 129By similarity
Glycosylationi146 – 1461N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi176 ↔ 194By similarity
Disulfide bondi184 ↔ 231By similarity
Glycosylationi201 – 2011N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi233 ↔ 238By similarity
Disulfide bondi279 ↔ 292By similarity
Disulfide bondi281 ↔ 290By similarity
Disulfide bondi319 ↔ 337By similarity
Glycosylationi402 – 4021N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi423 ↔ 449By similarity

Post-translational modificationi

N-glycosylated.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Interactioni

Subunit structurei

Homotetramer.By similarity

Structurei

3D structure databases

ProteinModelPortaliA3KF10.
SMRiA3KF10. Positions 82-470.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni11 – 3222Involved in apical transport and lipid raft associationBy similarityAdd
BLAST
Regioni35 – 9056Hypervariable stalk regionBy similarityAdd
BLAST
Regioni91 – 470380Head of neuraminidaseBy similarityAdd
BLAST
Regioni277 – 2782Substrate 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.

A3KF10-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNPNQKIICI SATGMTLSVV SLLIGIANLG LNIGLHYKVG DTPDVNIPNV
60 70 80 90 100
NRTNSTTTII NNNTQNNFTN ITNIIQNKNE ERTFLNLTKP LCEVNSWHIL
110 120 130 140 150
SKDNAIRIGE DAHILVTREP YLSCDPQGCR MFALSQGTTL RGRHANGTIH
160 170 180 190 200
DRSPFRALVS WEMGQAPSPY NAKVECIGWS STSCHDGISR MSICMSGPNN
210 220 230 240 250
NASAVVWYGG RPVTEIPSWA GNILRTQESE CVCHKGVCPV VMTDGPATNR
260 270 280 290 300
AATKIIYFKE GKIQKIEELT GKAQHIEECS CYGAGGVIKC ICRDNWKGAN
310 320 330 340 350
RPVITIDPEI MTHTSKYLCS KVLTDTSRPN DPTNGNCDAP ITGGSPDPGV
360 370 380 390 400
KGFAFLDGEN SWLGRTISKD SRSGYEMLKV PNAETDTQSG PISHQMIVNN
410 420 430 440 450
QNWSGYSGAF IDYWANKECF NPCFYVELIR GRPKESSVLW TSNSIVALCG
460 470
SRERLGSWSW HDGAEIIYFK
Length:470
Mass (Da):51,721
Last modified:April 3, 2007 - v1
Checksum:iA87E592B89234AE0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB295612 Genomic RNA. Translation: BAF48479.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB295612 Genomic RNA. Translation: BAF48479.1 .

3D structure databases

ProteinModelPortali A3KF10.
SMRi A3KF10. Positions 82-470.
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. "Evolution of the nucleoprotein gene of influenza A virus."
    Gorman O.T., Bean W.J., Kawaoka Y., Webster R.G.
    J. Virol. 64:1487-1497(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].

Entry informationi

Entry nameiNRAM_I56A1
AccessioniPrimary (citable) accession number: A3KF10
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 30, 2010
Last sequence update: April 3, 2007
Last modified: November 26, 2014
This is version 47 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