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P67923 (NRAM_INBLN) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 55. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Neuraminidase

EC=3.2.1.18
Gene names
Name:NA
OrganismInfluenza B virus (strain B/Leningrad/179/1986)
Taxonomic identifier11536 [NCBI]
Taxonomic lineageVirusesssRNA negative-strand virusesOrthomyxoviridaeInfluenzavirus B
Virus hostHomo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length465 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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.

Catalytic activity

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.

Enzyme regulation

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.

Subunit structure

Homotetramer By similarity.

Subcellular location

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. In the virion, forms a mushroom-shaped spike on the surface of the membrane By similarity.

Post-translational modification

N-glycosylated By similarity.

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.

Sequence similarities

Belongs to the glycosyl hydrolase 34 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 465465Neuraminidase
PRO_0000078733

Regions

Topological domain1 – 66Intravirion Potential
Transmembrane7 – 3529Helical; Signal-anchor for type II membrane protein; Potential
Topological domain36 – 465430Virion surface Potential
Region39 – 6830Hypervariable stalk region
Region69 – 465397Head of neuraminidase

Sites

Active site1481 Potential
Active site2741 Potential
Active site4081 Potential
Binding site1151Substrate Potential
Binding site2911Substrate Potential
Binding site3731Substrate Potential

Amino acid modifications

Glycosylation551N-linked (GlcNAc...); by host Potential
Glycosylation631N-linked (GlcNAc...); by host Potential
Glycosylation1431N-linked (GlcNAc...); by host Potential
Glycosylation2831N-linked (GlcNAc...); by host Potential
Glycosylation2941N-linked (GlcNAc...); by host Potential
Disulfide bond86 ↔ 419 By similarity
Disulfide bond121 ↔ 126 By similarity
Disulfide bond181 ↔ 228 By similarity
Disulfide bond230 ↔ 235 By similarity
Disulfide bond276 ↔ 290 By similarity
Disulfide bond278 ↔ 288 By similarity
Disulfide bond317 ↔ 336 By similarity
Disulfide bond423 ↔ 446 By similarity

Sequences

Sequence LengthMass (Da)Tools
P67923 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: FD402484907888CA

FASTA46551,382
        10         20         30         40         50         60 
MLPSTIQTLT LFLTSGGVLL SLYVSASLSY LLYSDILLKF SPKITAPTMT LDCANASNVQ 

        70         80         90        100        110        120 
AVNRSATKEM TFLLPEPEWT YPRLSCQGST FQKALLISPH RFGEARGNSA PLIIREPFIA 

       130        140        150        160        170        180 
CGPKECKHFA LTHYAAQPGG YYNGTREDRN KLRHLISVKL GKIPTVENSI FHMAAWSGSA 

       190        200        210        220        230        240 
CHDGREWTYI GVDGPDSNAL IKIKYGEAYT DTYHSYANNI LRTQESACNC IGGDCYLMIT 

       250        260        270        280        290        300 
DGSASGISEC RFLKIREGRI IKEIFPTGRV EHTEECTCGF ASNKTIECAC RDNNYTAKRP 

       310        320        330        340        350        360 
FVKLNVETDT AEIRLMCTET YLDTPRPDDG SITGPCESNG DKGRGGIKGG FVHQRMASKI 

       370        380        390        400        410        420 
GRWYSRTMSK TERMGMELYV KYDGDPWTDS DALAPSGVMV SIKEPGWYSF GFEIKDKKCD 

       430        440        450        460 
VPCIGIEMVH DGGKKTWHSA ATAIYCLMGS GQLLWDTVTG VDMAL 

« Hide

References

[1]"Antigenic, sequence, and crystal variation in influenza B neuraminidase."
Air G.M., Laver W.G., Luo M., Stray S.J., Legrone G., Webster R.G.
Virology 177:578-587(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[2]"Neuraminidase inhibitors for influenza."
Moscona A.
N. Engl. J. Med. 353:1363-1373(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M30632 Genomic RNA. Translation: AAA43731.1.
PIRC46347.

3D structure databases

ProteinModelPortalP67923.
SMRP67923. Positions 76-465.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D2.120.10.10. 1 hit.
InterProIPR001860. Glyco_hydro_34.
IPR011040. Sialidases.
[Graphical view]
PfamPF00064. Neur. 1 hit.
[Graphical view]
SUPFAMSSF50939. SSF50939. 1 hit.
ProtoNetSearch...

Entry information

Entry nameNRAM_INBLN
AccessionPrimary (citable) accession number: P67923
Secondary accession number(s): P16193, P16197
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: February 19, 2014
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries