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P27907 (NRAM_INBBE) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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/Beijing/1/1987)
Taxonomic identifier11525 [NCBI]
Taxonomic lineageVirusesssRNA negative-strand virusesOrthomyxoviridaeInfluenzavirus B
Virus hostHomo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length465 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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.

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_0000078730

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

Secondary structure

..................................................................... 465
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P27907 [UniParc].

Last modified August 1, 1992. Version 1.
Checksum: 2FC60B895CBD430C

FASTA46551,430
        10         20         30         40         50         60 
MLPSTIQTLT LFLTSGGVLL SLYVSASLSY LLYSDILLKF SSKITAPTMT 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 
DGSASGISKC RFLKIREGRI IKEIFPTGRV EHTEECTCGF ASNKTIECAC RDNSYTAKRP 

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

       370        380        390        400        410        420 
GRWYSRTMSK TERMGMELYV RYDGDPWTDS DALAHSGVMV SMKEPGWYSF GFEIKDKKCD 

       430        440        450        460 
VPCIGIEMVH DGGKKTWHSA ATAIYCLMGS GQLLWDTVTG VDMAL 

« Hide

References

[1]"Sequence and crystallization of influenza virus B/Beijing/1/87 neuraminidase."
Burmeister W.P., Daniels R.S., Dayan S., Gagnon J., Cusack S., Ruigrok R.W.
Virology 180:266-272(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA], PARTIAL PROTEIN SEQUENCE.
[2]"Neuraminidase inhibitors for influenza."
Moscona A.
N. Engl. J. Med. 353:1363-1373(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[3]"The 2.2-A resolution crystal structure of influenza B neuraminidase and its complex with sialic acid."
Burmeister W.P., Ruigrok R.W., Cusack S.
EMBO J. 11:49-56(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 76-465.
[4]"Dihydropyrancarboxamides related to zanamivir: a new series of inhibitors of influenza virus sialidases. 2. Crystallographic and molecular modeling study of complexes of 4-amino-4H-pyran-6-carboxamides and sialidase from influenza virus types A and B."
Taylor N.R., Cleasby A., Singh O., Skarzynski T., Wonacott A.J., Smith P.W., Sollis S.L., Howes P.D., Cherry P.C., Bethell R., Colman P., Varghese J.
J. Med. Chem. 41:798-807(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 76-465.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M54967 Genomic RNA. Translation: AAA43733.1.
PIRNMIVB1. B38520.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1A4GX-ray2.20A/B76-465[»]
1A4QX-ray1.90A/B76-465[»]
1NSBX-ray2.20A/B76-465[»]
1NSCX-ray1.70A/B76-465[»]
1NSDX-ray1.80A/B76-465[»]
ProteinModelPortalP27907.
SMRP27907. Positions 76-465.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH34. Glycoside Hydrolase Family 34.

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...

Other

EvolutionaryTraceP27907.

Entry information

Entry nameNRAM_INBBE
AccessionPrimary (citable) accession number: P27907
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: February 19, 2014
This is version 94 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries