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Q6XV27

- NRAM_I56A2

UniProt

Q6XV27 - NRAM_I56A2

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Protein

Neuraminidase

Gene

NA

Organism
Influenza A virus (strain A/Duck/England/1/1956 H11N6)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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

Ca2+2 PublicationsNote: Binds 1 Ca(2+) ion per subunit.2 Publications

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 – 1181Substrate
Active sitei151 – 1511Proton donor/acceptorBy similarity
Binding sitei152 – 1521Substrate
Binding sitei293 – 2931Substrate
Metal bindingi294 – 2941Calcium; via carbonyl oxygen2 Publications
Metal bindingi298 – 2981Calcium; via carbonyl oxygen2 Publications
Metal bindingi325 – 3251Calcium2 Publications
Metal bindingi348 – 3481Calcium; via carbonyl oxygen2 Publications
Binding sitei372 – 3721Substrate
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/England/1/1956 H11N6)
Taxonomic identifieri383550 [NCBI]
Taxonomic lineageiVirusesssRNA negative-strand virusesOrthomyxoviridaeInfluenzavirus A
Virus hostiAves [TaxID: 8782]
ProteomesiUP000008435: Genome

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 – 2721Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini28 – 470443Virion 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_0000280127Add
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 host1 Publication
Disulfide bondi92 ↔ 419
Disulfide bondi124 ↔ 129
Glycosylationi146 – 1461N-linked (GlcNAc...); by host2 Publications
Disulfide bondi176 ↔ 194
Disulfide bondi184 ↔ 231
Glycosylationi201 – 2011N-linked (GlcNAc...); by host1 Publication
Disulfide bondi233 ↔ 238
Disulfide bondi279 ↔ 292
Disulfide bondi281 ↔ 290
Disulfide bondi319 ↔ 337
Glycosylationi402 – 4021N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi423 ↔ 449

Post-translational modificationi

N-glycosylated.2 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein

Interactioni

Subunit structurei

Homotetramer.2 Publications

Structurei

Secondary structure

1
470
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi95 – 1028Combined sources
Helixi105 – 1095Combined sources
Beta strandi115 – 12511Combined sources
Beta strandi128 – 14215Combined sources
Helixi143 – 1453Combined sources
Turni146 – 1494Combined sources
Beta strandi157 – 1626Combined sources
Beta strandi173 – 18513Combined sources
Beta strandi187 – 19711Combined sources
Helixi199 – 2013Combined sources
Beta strandi203 – 2086Combined sources
Beta strandi211 – 2177Combined sources
Beta strandi219 – 2224Combined sources
Beta strandi237 – 2459Combined sources
Beta strandi247 – 2493Combined sources
Beta strandi252 – 2598Combined sources
Beta strandi262 – 2687Combined sources
Beta strandi277 – 2848Combined sources
Beta strandi287 – 2937Combined sources
Beta strandi295 – 2973Combined sources
Beta strandi302 – 3076Combined sources
Turni308 – 3114Combined sources
Beta strandi312 – 3176Combined sources
Beta strandi320 – 3223Combined sources
Beta strandi325 – 3273Combined sources
Beta strandi337 – 3393Combined sources
Beta strandi362 – 3654Combined sources
Beta strandi367 – 37913Combined sources
Turni381 – 3855Combined sources
Beta strandi392 – 40312Combined sources
Beta strandi407 – 4115Combined sources
Beta strandi415 – 4206Combined sources
Beta strandi422 – 43110Combined sources
Turni432 – 4343Combined sources
Beta strandi441 – 45313Combined sources
Helixi466 – 4694Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1V0ZX-ray1.84A/B/C/D82-470[»]
1W1XX-ray2.00A/B/C/D82-470[»]
1W20X-ray2.08A/B/C/D82-470[»]
1W21X-ray2.08A/B/C/D82-470[»]
2CMLX-ray2.15A/B/C/D82-470[»]
ProteinModelPortaliQ6XV27.
SMRiQ6XV27. Positions 82-470.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ6XV27.

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 – 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.

Q6XV27-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNPNQKIICI SATGMTLSVV SLLVGIANLG LNIGLHYKVG DTPNVNIPNV
60 70 80 90 100
NGTNSTTTII NNNTQNNFTN ITNIIQSKGG ERTFLNLTKP LCEVNSWHIL
110 120 130 140 150
SKDNAIRIGE DAHILVTREP YLSCDPQGCR MFALSQGTTL RGRHANGTIH
160 170 180 190 200
DRSPFRALIS WEMGQAPSPY NTRVECIGWS STSCHDGMSR MSICMSGPNN
210 220 230 240 250
NASAVVWYGG RPITEIPSWA GNILRTQESE CVCHKGVCPV VMTDGPANNR
260 270 280 290 300
AATKIIYFKE GKIQKIEELA GNAQHIEECS CYGAGGVIKC ICRDNWKGAN
310 320 330 340 350
RPVITIDPEM MTHTSKYLCS KVLTDTSRPN DPTNGNCDAP ITGGSPDPGV
360 370 380 390 400
KGFAFLDGEN SWLGRTISKD SRSGYEMLKV PNAETDIQSG PISNQVIVNN
410 420 430 440 450
QNWSGYSGAF IDYWANKECF NPCFYVELIR GRPKESSVLW TSNSIVALCG
460 470
SKKRLGSWSW HDGAEIIYFE
Length:470
Mass (Da):51,470
Last modified:July 5, 2004 - v1
Checksum:iC3C30CB83D15E0E7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY207549 Genomic DNA. Translation: AAO62063.1.
AB288846 Genomic RNA. Translation: BAF43436.1.
CY014681 Genomic RNA. Translation: ABI84548.1.
K01039 Genomic RNA. Translation: AAA43389.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY207549 Genomic DNA. Translation: AAO62063.1 .
AB288846 Genomic RNA. Translation: BAF43436.1 .
CY014681 Genomic RNA. Translation: ABI84548.1 .
K01039 Genomic RNA. Translation: AAA43389.1 .

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1V0Z X-ray 1.84 A/B/C/D 82-470 [» ]
1W1X X-ray 2.00 A/B/C/D 82-470 [» ]
1W20 X-ray 2.08 A/B/C/D 82-470 [» ]
1W21 X-ray 2.08 A/B/C/D 82-470 [» ]
2CML X-ray 2.15 A/B/C/D 82-470 [» ]
ProteinModelPortali Q6XV27.
SMRi Q6XV27. 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...

Miscellaneous databases

EvolutionaryTracei Q6XV27.
PROi Q6XV27.

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. "Genetic analysis of multiple N3, N4, and N6 influenza A virus neuraminidase genes."
    Webby R.J., Humberd J.L., Krauss S.L.
    Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  3. "Sequence variation at the 3' end of the neuraminidase gene from 39 influenza type A viruses."
    Blok J., Air G.M.
    Virology 121:211-229(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-71.
  4. "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.
  5. "Neuraminidase inhibitors for influenza."
    Moscona A.
    N. Engl. J. Med. 353:1363-1373(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  6. "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.
  7. "The crystal structure of influenza type A virus neuraminidase of the N6 subtype at 1.85 A resolution."
    Rudino-Pinera E., Crennell S.J., Webster R.G., Laver W.G., Garman E.F.
    Submitted (APR-2004) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.84 ANGSTROMS) OF 82-470 IN COMPLEX WITH CALCIUM AND SUBSTRATE ANALOG, COFACTOR, SUBUNIT, DISULFIDE BONDS, GLYCOSYLATION AT ASN-86; ASN-146 AND ASN-201.
  8. "The crystal structure of type A influenza virus neuraminidase of the N6 subtype reveals the existence of two separate Neu5Ac binding sites."
    Rudino-Pinera E., Tunnah P., Crennell S.J., Webster R.G., Laver W.G., Garman E.F.
    Submitted (MAY-2006) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 82-470 IN COMPLEX WITH CALCIUM AND ZANAMIVIR, COFACTOR, SUBUNIT, DISULFIDE BONDS, GLYCOSYLATION AT ASN-146.

Entry informationi

Entry nameiNRAM_I56A2
AccessioniPrimary (citable) accession number: Q6XV27
Secondary accession number(s): Q83982
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 20, 2007
Last sequence update: July 5, 2004
Last modified: November 26, 2014
This is version 65 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.

Keywords - Technical termi

3D-structure, Complete proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3