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Protein

Neuraminidase

Gene

NA

Organism
Influenza B virus (strain B/Oregon/5/1980)
Status
Reviewed-Annotation score: Annotation score: 5 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 (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 Ca2+ 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)DescriptionActionsGraphical viewLength
Binding sitei116SubstrateBy similarity1
Active sitei149Proton donor/acceptorBy similarity1
Binding sitei150SubstrateBy similarity1
Binding sitei292SubstrateBy similarity1
Metal bindingi293Calcium; via carbonyl oxygenBy similarity1
Metal bindingi297Calcium; via carbonyl oxygenBy similarity1
Metal bindingi324CalciumBy similarity1
Metal bindingi344Calcium; via carbonyl oxygenBy similarity1
Metal bindingi346Calcium; via carbonyl oxygenBy similarity1
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

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/Oregon/5/1980)
Taxonomic identifieri11541 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA negative-strand virusesOrthomyxoviridaeInfluenzavirus B
Virus hostiHomo sapiens (Human) [TaxID: 9606]

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000787371 – 466NeuraminidaseAdd BLAST466

Amino acid modifications

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

Post-translational modificationi

N-glycosylated.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Interactioni

Subunit structurei

Homotetramer.By similarity

Structurei

3D structure databases

ProteinModelPortaliP16201.
ModBaseiSearch...
MobiDBiSearch...

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

CDDicd15483. Influenza_NA. 1 hit.
Gene3Di2.120.10.10. 1 hit.
InterProiIPR001860. Glyco_hydro_34.
IPR033654. Sialidase_Influenza_A/B.
IPR011040. Sialidases.
[Graphical view]
PfamiPF00064. Neur. 1 hit.
[Graphical view]
SUPFAMiSSF50939. SSF50939. 1 hit.

Sequencei

Sequence statusi: Complete.

P16201-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLPSTIQTLT LFLTSGGVLL SLYVSASLSY LLYSDILLKF STTKITAPTM
60 70 80 90 100
SLDCANISNV QAVNRSATKE MTFLLPEPEW TYPRLSCQGS TFQKALLISP
110 120 130 140 150
HRFGEARGNS APLIIREPFI ACGPKECKHF ALTHYAAQPG GYYNGTRKDR
160 170 180 190 200
NKLRHLISVK LGKIPTVENS IFHMAAWSGS ACHDGREWTY IGVDGPDSNA
210 220 230 240 250
LIKIKYGEAY TDTYHSYANN ILRTQESACN CIGGDCYLMI TDGSASGISK
260 270 280 290 300
CRFLKIREGR IIKEIFPTGR VEHTEECTCG FASNKTIECA CRDNSYTAKR
310 320 330 340 350
PFVKLNVETD TAEIRLMCTE TYLDTPRPDD GSITGPCESN GDKGLGGIKG
360 370 380 390 400
GFVHQRMASK IGRWYSRTMS KTERMGMELY VKYDGDPWTD SDALAPSGVM
410 420 430 440 450
VSMKEPGWYS FGFEIKDKKC DVPCIGIEMV HDGGKETWHS AATAIYCLMG
460
SGQLLWDTVT GVDMAL
Length:466
Mass (Da):51,462
Last modified:April 1, 1990 - v1
Checksum:iD3F357AC5B3E1CDE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M30636 Genomic RNA. Translation: AAA43741.1.
PIRiF46347.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M30636 Genomic RNA. Translation: AAA43741.1.
PIRiF46347.

3D structure databases

ProteinModelPortaliP16201.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH34. Glycoside Hydrolase Family 34.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

CDDicd15483. Influenza_NA. 1 hit.
Gene3Di2.120.10.10. 1 hit.
InterProiIPR001860. Glyco_hydro_34.
IPR033654. Sialidase_Influenza_A/B.
IPR011040. Sialidases.
[Graphical view]
PfamiPF00064. Neur. 1 hit.
[Graphical view]
SUPFAMiSSF50939. SSF50939. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiNRAM_INBOR
AccessioniPrimary (citable) accession number: P16201
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: October 5, 2016
This is version 100 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.

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. 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.