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Protein

Neuraminidase

Gene

NA

Organism
Influenza B virus (strain B/Lee/1940)
Status
Reviewed-Annotation score: 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 (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+3 PublicationsNote: Binds 1 Ca2+ ion per subunit.3 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)DescriptionActionsGraphical viewLength
Binding sitei116SubstrateBy similarity1
Active sitei149Proton donor/acceptorBy similarity1
Binding sitei150SubstrateBy similarity1
Binding sitei292SubstrateBy similarity1
Metal bindingi293Calcium; via carbonyl oxygen2 Publications1
Metal bindingi297Calcium; via carbonyl oxygen2 Publications1
Metal bindingi324Calcium2 Publications1
Metal bindingi346Calcium; via carbonyl oxygen2 Publications1
Binding sitei374SubstrateBy similarity1
Active sitei409NucleophileBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

SABIO-RKP03474.

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 B virus (strain B/Lee/1940)
Taxonomic identifieri518987 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA negative-strand virusesOrthomyxoviridaeInfluenzavirus B
Virus hostiHomo sapiens (Human) [TaxID: 9606]
Proteomesi
  • UP000008158 Componenti: Genome

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 6IntravirionSequence analysis6
Transmembranei7 – 35Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST29
Topological domaini36 – 466Virion surfaceSequence analysisAdd BLAST431

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Host cell membrane, Host membrane, Membrane, Virion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi117E → G: Reduced substrate binding. 1 Publication1
Mutagenesisi149D → E: Almost complete loss of enzymatic activity. 1 Publication1
Mutagenesisi150R → K: Reduced substrate binding. 1 Publication1
Mutagenesisi223R → K: Reduced substrate binding. 1 Publication1
Mutagenesisi275E → D: Almost complete loss of enzymatic activity. 1 Publication1
Mutagenesisi374R → K: 80% loss of catalytic efficiency. 1 Publication1
Mutagenesisi374R → N: 94% loss of catalytic efficiency. 1 Publication1
Mutagenesisi409Y → F: Complete loss of enzymatic activity. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL3377.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000787321 – 466NeuraminidaseAdd BLAST466

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi56N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi64N-linked (GlcNAc...); by hostSequence analysis1
Disulfide bondi87 ↔ 420
Disulfide bondi122 ↔ 127
Glycosylationi144N-linked (GlcNAc...); by hostSequence analysis1
Disulfide bondi182 ↔ 229
Disulfide bondi231 ↔ 236
Disulfide bondi277 ↔ 291
Disulfide bondi279 ↔ 289
Glycosylationi284N-linked (GlcNAc...); by hostSequence analysis1
Disulfide bondi318 ↔ 337
Disulfide bondi424 ↔ 447

Post-translational modificationi

N-glycosylated.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Interactioni

Subunit structurei

Homotetramer.3 Publications

Chemistry databases

BindingDBiP03474.

Structurei

Secondary structure

1466
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi88 – 90Combined sources3
Beta strandi92 – 98Combined sources7
Helixi100 – 102Combined sources3
Beta strandi106 – 108Combined sources3
Beta strandi119 – 122Combined sources4
Beta strandi127 – 133Combined sources7
Beta strandi137 – 139Combined sources3
Turni144 – 147Combined sources4
Beta strandi155 – 160Combined sources6
Turni167 – 169Combined sources3
Beta strandi171 – 175Combined sources5
Beta strandi177 – 183Combined sources7
Beta strandi185 – 195Combined sources11
Turni197 – 199Combined sources3
Beta strandi201 – 206Combined sources6
Beta strandi209 – 215Combined sources7
Beta strandi217 – 220Combined sources4
Beta strandi226 – 228Combined sources3
Beta strandi230 – 232Combined sources3
Beta strandi235 – 241Combined sources7
Beta strandi245 – 247Combined sources3
Beta strandi251 – 257Combined sources7
Beta strandi260 – 265Combined sources6
Beta strandi268 – 270Combined sources3
Beta strandi275 – 292Combined sources18
Beta strandi294 – 296Combined sources3
Beta strandi301 – 306Combined sources6
Turni307 – 310Combined sources4
Beta strandi311 – 316Combined sources6
Beta strandi324 – 326Combined sources3
Beta strandi352 – 356Combined sources5
Beta strandi361 – 367Combined sources7
Beta strandi369 – 385Combined sources17
Turni387 – 389Combined sources3
Beta strandi395 – 406Combined sources12
Beta strandi410 – 416Combined sources7
Beta strandi418 – 432Combined sources15
Beta strandi435 – 437Combined sources3
Beta strandi439 – 448Combined sources10
Beta strandi450 – 452Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1B9SX-ray2.50A77-466[»]
1B9TX-ray2.40A77-466[»]
1B9VX-ray2.35A77-466[»]
1INFX-ray2.40A77-466[»]
1INVX-ray2.40A77-466[»]
1IVBX-ray2.40A77-466[»]
1VCJX-ray2.40A78-466[»]
ProteinModelPortaliP03474.
SMRiP03474.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP03474.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni39 – 69Hypervariable stalk regionAdd BLAST31
Regioni70 – 466Head of neuraminidaseAdd BLAST397
Regioni275 – 276Substrate bindingBy similarity2

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.

P03474-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLPSTVQTLT LLLTSGGVLL SLYVSASLSY LLYSDVLLKF SSTKTTAPTM
60 70 80 90 100
SLECTNASNA QTVNHSATKE MTFPPPEPEW TYPRLSCQGS TFQKALLISP
110 120 130 140 150
HRFGEIKGNS APLIIREPFV ACGPKECRHF ALTHYAAQPG GYYNGTRKDR
160 170 180 190 200
NKLRHLVSVK LGKIPTVENS IFHMAAWSGS ACHDGREWTY IGVDGPDNDA
210 220 230 240 250
LVKIKYGEAY TDTYHSYAHN ILRTQESACN CIGGDCYLMI TDGSASGISK
260 270 280 290 300
CRFLKIREGR IIKEILPTGR VEHTEECTCG FASNKTIECA CRDNSYTAKR
310 320 330 340 350
PFVKLNVETD TAEIRLMCTK TYLDTPRPDD GSIAGPCESN GDKWLGGIKG
360 370 380 390 400
GFVHQRMASK IGRWYSRTMS KTNRMGMELY VKYDGDPWTD SDALTLSGVM
410 420 430 440 450
VSIEEPGWYS FGFEIKDKKC DVPCIGIEMV HDGGKDTWHS AATAIYCLMG
460
SGQLLWDTVT GVDMAL
Length:466
Mass (Da):51,442
Last modified:July 21, 1986 - v1
Checksum:iE6FF3E634F132263
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02095 Genomic RNA. Translation: AAA43749.1.
PIRiA00886. NMIV4.
RefSeqiNP_056663.1. NC_002209.1.

Genome annotation databases

GeneIDi26824004.
KEGGivg:26824004.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02095 Genomic RNA. Translation: AAA43749.1.
PIRiA00886. NMIV4.
RefSeqiNP_056663.1. NC_002209.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1B9SX-ray2.50A77-466[»]
1B9TX-ray2.40A77-466[»]
1B9VX-ray2.35A77-466[»]
1INFX-ray2.40A77-466[»]
1INVX-ray2.40A77-466[»]
1IVBX-ray2.40A77-466[»]
1VCJX-ray2.40A78-466[»]
ProteinModelPortaliP03474.
SMRiP03474.
ModBaseiSearch...
MobiDBiSearch...

Chemistry databases

BindingDBiP03474.
ChEMBLiCHEMBL3377.

Protein family/group databases

CAZyiGH34. Glycoside Hydrolase Family 34.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi26824004.
KEGGivg:26824004.

Enzyme and pathway databases

SABIO-RKP03474.

Miscellaneous databases

EvolutionaryTraceiP03474.
PROiP03474.

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.
ProtoNetiSearch...

Entry informationi

Entry nameiNRAM_INBLE
AccessioniPrimary (citable) accession number: P03474
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: November 2, 2016
This is version 124 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 B 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, Reference 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

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.