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P67907

- NRAM_INBME

UniProt

P67907 - NRAM_INBME

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Protein

Neuraminidase

Gene

NA

Organism
Influenza B virus (strain B/Memphis/6/1986)
Status
Reviewed - 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 Ca(2+) 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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei115 – 1151SubstrateBy similarity
Active sitei148 – 1481Proton donor/acceptorBy similarity
Binding sitei149 – 1491SubstrateBy similarity
Binding sitei291 – 2911SubstrateBy similarity
Metal bindingi292 – 2921Calcium; via carbonyl oxygenBy similarity
Metal bindingi296 – 2961Calcium; via carbonyl oxygenBy similarity
Metal bindingi323 – 3231CalciumBy similarity
Metal bindingi343 – 3431Calcium; via carbonyl oxygenBy similarity
Metal bindingi345 – 3451Calcium; via carbonyl oxygenBy similarity
Binding sitei373 – 3731SubstrateBy similarity
Active sitei408 – 4081NucleophileBy similarity

GO - Molecular functioni

  1. exo-alpha-(2->3)-sialidase activity Source: UniProtKB-EC
  2. exo-alpha-(2->6)-sialidase activity Source: UniProtKB-EC
  3. exo-alpha-(2->8)-sialidase activity Source: UniProtKB-EC
  4. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. carbohydrate metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Ligandi

Calcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Neuraminidase (EC:3.2.1.18)
Gene namesi
Name:NA
OrganismiInfluenza B virus (strain B/Memphis/6/1986)
Taxonomic identifieri11538 [NCBI]
Taxonomic lineageiVirusesssRNA negative-strand virusesOrthomyxoviridaeInfluenzavirus B
Virus hostiHomo sapiens (Human) [TaxID: 9606]

Subcellular locationi

Virion membrane By similarity. Host apical cell membrane By similarity; 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).By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 66IntravirionSequence Analysis
Transmembranei7 – 3529Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini36 – 465430Virion surfaceSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. host cell plasma membrane Source: UniProtKB-KW
  2. integral component of membrane Source: UniProtKB-KW
  3. virion membrane Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Host cell membrane, Host membrane, Membrane, Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 465465NeuraminidasePRO_0000078735Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi55 – 551N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi63 – 631N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi86 ↔ 419By similarity
Disulfide bondi121 ↔ 126By similarity
Glycosylationi143 – 1431N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi181 ↔ 228By similarity
Disulfide bondi230 ↔ 235By similarity
Disulfide bondi276 ↔ 290By similarity
Disulfide bondi278 ↔ 288By similarity
Glycosylationi283 – 2831N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi294 – 2941N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi317 ↔ 336By similarity
Disulfide bondi423 ↔ 446By similarity

Post-translational modificationi

N-glycosylated.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Interactioni

Subunit structurei

Homotetramer.By similarity

Structurei

3D structure databases

ProteinModelPortaliP67907.
SMRiP67907. Positions 76-465.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni39 – 6830Hypervariable stalk regionAdd
BLAST
Regioni69 – 465397Head of neuraminidaseAdd
BLAST
Regioni274 – 2752Substrate bindingBy similarity

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.

P67907-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLPSTIQTLT LFLTSGGVLL SLYVSASLSY LLYSDILLKF SPKITAPTMT
60 70 80 90 100
LDCANASNVQ AVNRSATKEM TFLLPEPEWT YPRLSCQGST FQKALLISPH
110 120 130 140 150
RFGEARGNSA PLIIREPFIA CGPKECKHFA LTHYAAQPGG YYNGTREDRN
160 170 180 190 200
KLRHLISVKL GKIPTVENSI FHMAAWSGSA CHDGREWTYI GVDGPDSNAL
210 220 230 240 250
IKIKYGEAYT DTYHSYANNI LRTQESACNC IGGDCYLMIT DGSASGISEC
260 270 280 290 300
RFLKIREGRI IKEIFPTGRV EHTEECTCGF ASNKTIECAC RDNNYTAKRP
310 320 330 340 350
FVKLNVETDT AEIRLMCTET YLDTPRPDDG SITGPCESNG DKGRGGIKGG
360 370 380 390 400
FVHQRMASKI GRWYSRTMSK TERMGMELYV KYDGDPWTDS DALAPSGVMV
410 420 430 440 450
SIKEPGWYSF GFEIKDKKCD VPCIGIEMVH DGGKKTWHSA ATAIYCLMGS
460
GQLLWDTVTG VDMAL
Length:465
Mass (Da):51,382
Last modified:October 11, 2004 - v1
Checksum:iFD402484907888CA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M30634 Genomic RNA. Translation: AAA43737.1.
PIRiC46347.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M30634 Genomic RNA. Translation: AAA43737.1 .
PIRi C46347.

3D structure databases

ProteinModelPortali P67907.
SMRi P67907. Positions 76-465.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 2.120.10.10. 1 hit.
InterProi IPR001860. Glyco_hydro_34.
IPR011040. Sialidases.
[Graphical view ]
Pfami PF00064. Neur. 1 hit.
[Graphical view ]
SUPFAMi SSF50939. SSF50939. 1 hit.
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiNRAM_INBME
AccessioniPrimary (citable) accession number: P67907
Secondary accession number(s): P16193, P16197
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: November 26, 2014
This is version 59 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

External Data

Dasty 3