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Q07599

- NRAM_I63A3

UniProt

Q07599 - NRAM_I63A3

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Protein

Neuraminidase

Gene
NA
Organism
Influenza A virus (strain A/Duck/Ukraine/1/1963 H3N8)
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

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 sitei116 – 1161Substrate By similarity
Active sitei149 – 1491Proton donor/acceptor By similarity
Binding sitei150 – 1501Substrate By similarity
Binding sitei291 – 2911Substrate By similarity
Metal bindingi292 – 2921Calcium; via carbonyl oxygen By similarity
Metal bindingi296 – 2961Calcium; via carbonyl oxygen By similarity
Metal bindingi322 – 3221Calcium By similarity
Binding sitei368 – 3681Substrate By similarity
Active sitei402 – 4021Nucleophile 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/Duck/Ukraine/1/1963 H3N8)
Taxonomic identifieri385580 [NCBI]
Taxonomic lineageiVirusesssRNA negative-strand virusesOrthomyxoviridaeInfluenzavirus A
Virus hostiAves [TaxID: 8782]
Equus caballus (Horse) [TaxID: 9796]

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

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 – 470470NeuraminidasePRO_0000078688Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi46 – 461N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi54 – 541N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi84 – 841N-linked (GlcNAc...); by host Reviewed prediction
Disulfide bondi90 ↔ 417 By similarity
Disulfide bondi122 ↔ 127 By similarity
Glycosylationi144 – 1441N-linked (GlcNAc...); by host Reviewed prediction
Disulfide bondi182 ↔ 229 By similarity
Disulfide bondi231 ↔ 236 By similarity
Disulfide bondi277 ↔ 290 By similarity
Disulfide bondi279 ↔ 288 By similarity
Disulfide bondi316 ↔ 335 By similarity
Glycosylationi398 – 3981N-linked (GlcNAc...); by host Reviewed prediction
Disulfide bondi421 ↔ 446 By similarity

Post-translational modificationi

N-glycosylated By similarity.

Keywords - PTMi

Disulfide bond, Glycoprotein

Interactioni

Subunit structurei

Homotetramer By similarity.

Protein-protein interaction databases

DIPiDIP-60415N.

Structurei

Secondary structure

1
470
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi96 – 1005
Helixi103 – 1064
Turni107 – 1093
Beta strandi112 – 12211
Beta strandi127 – 13711
Helixi141 – 1444
Beta strandi155 – 1606
Helixi167 – 1693
Beta strandi171 – 1755
Beta strandi177 – 1837
Beta strandi185 – 19511
Helixi197 – 1993
Beta strandi201 – 21515
Beta strandi217 – 2204
Beta strandi222 – 2243
Beta strandi226 – 2283
Beta strandi230 – 2323
Beta strandi235 – 2439
Beta strandi245 – 2473
Beta strandi250 – 2578
Beta strandi260 – 2667
Beta strandi275 – 2828
Beta strandi285 – 2917
Beta strandi294 – 2985
Beta strandi300 – 3045
Beta strandi310 – 3145
Beta strandi317 – 3193
Beta strandi322 – 3243
Helixi328 – 3303
Beta strandi335 – 3373
Beta strandi350 – 3534
Beta strandi356 – 3616
Beta strandi363 – 37614
Turni377 – 3815
Beta strandi387 – 39913
Beta strandi403 – 4086
Helixi410 – 4134
Beta strandi415 – 42915
Turni430 – 4323
Beta strandi433 – 4364
Beta strandi438 – 4469
Helixi466 – 4683

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2HT5X-ray2.40A81-470[»]
2HT7X-ray2.60A81-470[»]
2HT8X-ray2.40A81-470[»]
2HTQX-ray2.20A81-470[»]
2HTRX-ray2.50A81-470[»]
2HTUX-ray2.20A81-470[»]
3O9JX-ray2.00A81-467[»]
3O9KX-ray2.49A81-467[»]
4D8SX-ray2.40A81-470[»]
4GB1X-ray2.62A81-470[»]
4KS1X-ray2.20A81-470[»]
4M3MX-ray2.10A80-469[»]
4MJUX-ray2.35A81-469[»]
4MJVX-ray2.65A81-470[»]
ProteinModelPortaliQ07599.
SMRiQ07599. Positions 81-467.

Miscellaneous databases

EvolutionaryTraceiQ07599.

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 – 470382Head of neuraminidaseAdd
BLAST
Regioni275 – 2762Substrate binding By similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi439 – 4424Poly-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.

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.

Q07599-1 [UniParc]FASTAAdd to Basket

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MNPNQKIITI GSISLGLVVF NVLLHVVSII VTVLVLGKGG NNGICNETVV    50
REYNETVRIE KVTQWHNTNV VEYVPYWNGG TYMNNTEAIC DAKGFAPFSK 100
DNGIRIGSRG HIFVIREPFV SCSPIECRTF FLTQGSLLND KHSNGTVKDR 150
SPFRTLMSVE VGQSPNVYQA RFEAVAWSAT ACHDGKKWMT VGVTGPDSKA 200
VAVIHYGGVP TDVVNSWAGD ILRTQESSCT CIQGDCYWVM TDGPANRQAQ 250
YRIYKANQGR IIGQTDISFN GGHIEECSCY PNDGKVECVC RDGWTGTNRP 300
VLVISPDLSY RVGYLCAGIP SDTPRGEDTQ FTGSCTSPMG NQGYGVKGFG 350
FRQGTDVWMG RTISRTSRSG FEILRIKNGW TQTSKEQIRK QVVVDNLNWS 400
GYSGSFTLPV ELSGKDCLVP CFWVEMIRGK PEEKTIWTSS SSIVMCGVDY 450
EVADWSWHDG AILPFDIDKM 470
Length:470
Mass (Da):51,960
Last modified:October 1, 1994 - v1
Checksum:iB46D54A03AC84CCE
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L06576 Unassigned RNA. Translation: AAA16234.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L06576 Unassigned RNA. Translation: AAA16234.1 .

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2HT5 X-ray 2.40 A 81-470 [» ]
2HT7 X-ray 2.60 A 81-470 [» ]
2HT8 X-ray 2.40 A 81-470 [» ]
2HTQ X-ray 2.20 A 81-470 [» ]
2HTR X-ray 2.50 A 81-470 [» ]
2HTU X-ray 2.20 A 81-470 [» ]
3O9J X-ray 2.00 A 81-467 [» ]
3O9K X-ray 2.49 A 81-467 [» ]
4D8S X-ray 2.40 A 81-470 [» ]
4GB1 X-ray 2.62 A 81-470 [» ]
4KS1 X-ray 2.20 A 81-470 [» ]
4M3M X-ray 2.10 A 80-469 [» ]
4MJU X-ray 2.35 A 81-469 [» ]
4MJV X-ray 2.65 A 81-470 [» ]
ProteinModelPortali Q07599.
SMRi Q07599. Positions 81-467.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-60415N.

Protein family/group databases

CAZyi GH34. Glycoside Hydrolase Family 34.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei Q07599.
PROi Q07599.

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 N8 neuraminidase gene of influenza A viruses."
    Saito T., Kawaoka Y., Webster R.G.
    Virology 193:868-876(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
  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_I63A3
AccessioniPrimary (citable) accession number: Q07599
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
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.

Keywords - Technical termi

3D-structure

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

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