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Protein

Neuraminidase

Gene

NA

Organism
Influenza A virus (strain A/Duck/Ukraine/1/1963 H3N8)
Status
Reviewed-Annotation score: Annotation score: 4 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.UniRule annotation

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.

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.UniRule annotation

Cofactori

Ca2+UniRule annotation

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.UniRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei116SubstrateUniRule annotation1
Active sitei149Proton donor/acceptorUniRule annotation1
Binding sitei150SubstrateUniRule annotation1
Binding sitei291SubstrateUniRule annotation1
Metal bindingi292Calcium; via carbonyl oxygenUniRule annotation1
Metal bindingi296Calcium; via carbonyl oxygenUniRule annotation1
Metal bindingi322CalciumUniRule annotation1
Binding sitei368SubstrateUniRule annotation1
Active sitei402NucleophileUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionGlycosidase, Hydrolase
LigandCalcium, Metal-binding

Enzyme and pathway databases

BRENDAi3.2.1.18. 7479.

Protein family/group databases

CAZyiGH34. Glycoside Hydrolase Family 34.

Names & Taxonomyi

Protein namesi
Recommended name:
NeuraminidaseUniRule annotation (EC:3.2.1.18UniRule annotation)
Gene namesi
Name:NAUniRule annotation
OrganismiInfluenza A virus (strain A/Duck/Ukraine/1/1963 H3N8)
Taxonomic identifieri385580 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA negative-strand virusesOrthomyxoviridaeInfluenzavirus A
Virus hostiAves [TaxID: 8782]
Equus caballus (Horse) [TaxID: 9796]
Proteomesi
  • UP000129778 Componenti: Chromosome

Subcellular locationi

  • Virion membrane UniRule annotation
  • Host apical cell membrane UniRule annotation; Single-pass type II membrane protein UniRule annotation

  • 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.UniRule annotation

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 14IntravirionUniRule annotationAdd BLAST14
Transmembranei15 – 35HelicalUniRule annotationAdd BLAST21
Topological domaini36 – 470Virion surfaceUniRule annotationAdd BLAST435

GO - Cellular componenti

Keywords - Cellular componenti

Host cell membrane, Host membrane, Membrane, Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000786881 – 470NeuraminidaseAdd BLAST470

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi46N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Glycosylationi54N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Glycosylationi84N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Disulfide bondi90 ↔ 417UniRule annotation
Disulfide bondi122 ↔ 127UniRule annotation
Glycosylationi144N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Disulfide bondi182 ↔ 229UniRule annotation
Disulfide bondi231 ↔ 236UniRule annotation
Disulfide bondi277 ↔ 290UniRule annotation
Disulfide bondi279 ↔ 288UniRule annotation
Disulfide bondi316 ↔ 335UniRule annotation
Glycosylationi398N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Disulfide bondi421 ↔ 446UniRule annotation

Post-translational modificationi

N-glycosylated.UniRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

DIPiDIP-60415N.

Structurei

Secondary structure

1470
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi96 – 100Combined sources5
Helixi103 – 106Combined sources4
Turni107 – 109Combined sources3
Beta strandi112 – 122Combined sources11
Beta strandi127 – 137Combined sources11
Helixi141 – 144Combined sources4
Beta strandi155 – 160Combined sources6
Helixi167 – 169Combined sources3
Beta strandi171 – 175Combined sources5
Beta strandi177 – 183Combined sources7
Beta strandi185 – 195Combined sources11
Helixi197 – 199Combined sources3
Beta strandi201 – 215Combined sources15
Beta strandi217 – 220Combined sources4
Beta strandi222 – 224Combined sources3
Beta strandi226 – 228Combined sources3
Beta strandi230 – 232Combined sources3
Beta strandi235 – 243Combined sources9
Beta strandi245 – 247Combined sources3
Beta strandi250 – 257Combined sources8
Beta strandi260 – 266Combined sources7
Beta strandi275 – 282Combined sources8
Beta strandi285 – 291Combined sources7
Beta strandi294 – 298Combined sources5
Beta strandi300 – 304Combined sources5
Beta strandi310 – 314Combined sources5
Beta strandi317 – 319Combined sources3
Beta strandi322 – 324Combined sources3
Helixi328 – 330Combined sources3
Beta strandi335 – 337Combined sources3
Beta strandi350 – 353Combined sources4
Beta strandi356 – 361Combined sources6
Beta strandi363 – 376Combined sources14
Turni377 – 381Combined sources5
Beta strandi387 – 399Combined sources13
Beta strandi403 – 408Combined sources6
Helixi410 – 413Combined sources4
Beta strandi415 – 429Combined sources15
Turni430 – 432Combined sources3
Beta strandi433 – 436Combined sources4
Beta strandi438 – 446Combined sources9
Helixi466 – 468Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ07599.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni11 – 32Involved in apical transport and lipid raft associationUniRule annotationAdd BLAST22
Regioni32 – 86Hypervariable stalk regionUniRule annotationAdd BLAST55
Regioni89 – 470Head of neuraminidaseUniRule annotationAdd BLAST382
Regioni275 – 276Substrate bindingUniRule annotation2

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi439 – 442Poly-Ser4

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.UniRule annotation

Sequence similaritiesi

Belongs to the glycosyl hydrolase 34 family.UniRule annotation

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Family and domain databases

HAMAPiMF_04071. INFV_NRAM. 1 hit.
InterProiView protein in InterPro
IPR001860. Glyco_hydro_34.
IPR011040. Sialidases.
PfamiView protein in Pfam
PF00064. Neur. 1 hit.
SUPFAMiSSF50939. SSF50939. 1 hit.

Sequencei

Sequence statusi: Complete.

Q07599-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNPNQKIITI GSISLGLVVF NVLLHVVSII VTVLVLGKGG NNGICNETVV
60 70 80 90 100
REYNETVRIE KVTQWHNTNV VEYVPYWNGG TYMNNTEAIC DAKGFAPFSK
110 120 130 140 150
DNGIRIGSRG HIFVIREPFV SCSPIECRTF FLTQGSLLND KHSNGTVKDR
160 170 180 190 200
SPFRTLMSVE VGQSPNVYQA RFEAVAWSAT ACHDGKKWMT VGVTGPDSKA
210 220 230 240 250
VAVIHYGGVP TDVVNSWAGD ILRTQESSCT CIQGDCYWVM TDGPANRQAQ
260 270 280 290 300
YRIYKANQGR IIGQTDISFN GGHIEECSCY PNDGKVECVC RDGWTGTNRP
310 320 330 340 350
VLVISPDLSY RVGYLCAGIP SDTPRGEDTQ FTGSCTSPMG NQGYGVKGFG
360 370 380 390 400
FRQGTDVWMG RTISRTSRSG FEILRIKNGW TQTSKEQIRK QVVVDNLNWS
410 420 430 440 450
GYSGSFTLPV ELSGKDCLVP CFWVEMIRGK PEEKTIWTSS SSIVMCGVDY
460 470
EVADWSWHDG AILPFDIDKM
Length:470
Mass (Da):51,960
Last modified:October 1, 1994 - v1
Checksum:iB46D54A03AC84CCE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L06576 Unassigned RNA. Translation: AAA16234.1.

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.

Entry informationi

Entry nameiNRAM_I63A3
AccessioniPrimary (citable) accession number: Q07599
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: June 7, 2017
This is version 112 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

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