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P16203

- NRAM_INBSI

UniProt

P16203 - NRAM_INBSI

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Protein

Neuraminidase

Gene

NA

Organism
Influenza B virus (strain B/Singapore/222/1979)
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

Binds 1 calcium 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 sitei116 – 1161SubstrateBy similarity
Active sitei149 – 1491Proton donor/acceptorBy similarity
Binding sitei150 – 1501SubstrateBy similarity
Binding sitei292 – 2921SubstrateBy similarity
Metal bindingi293 – 2931Calcium; via carbonyl oxygenBy similarity
Metal bindingi297 – 2971Calcium; via carbonyl oxygenBy similarity
Metal bindingi324 – 3241CalciumBy similarity
Metal bindingi344 – 3441Calcium; via carbonyl oxygenBy similarity
Metal bindingi346 – 3461Calcium; via carbonyl oxygenBy similarity
Binding sitei374 – 3741SubstrateBy similarity
Active sitei409 – 4091NucleophileBy 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

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/Singapore/222/1979)
Taxonomic identifieri107417 [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

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 – 466466NeuraminidasePRO_0000078738Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi56 – 561N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi64 – 641N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi87 ↔ 420By similarity
Disulfide bondi122 ↔ 127By similarity
Glycosylationi144 – 1441N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi182 ↔ 229By similarity
Disulfide bondi231 ↔ 236By similarity
Disulfide bondi277 ↔ 291By similarity
Disulfide bondi279 ↔ 289By similarity
Glycosylationi284 – 2841N-linked (GlcNAc...); by hostSequence Analysis
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

ProteinModelPortaliP16203.
SMRiP16203. Positions 77-466.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 66IntravirionSequence Analysis
Topological domaini36 – 466431Virion surfaceSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei7 – 3529Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni39 – 6931Hypervariable stalk regionAdd
BLAST
Regioni70 – 466397Head of neuraminidaseAdd
BLAST
Regioni275 – 2762Substrate 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.

P16203 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLPSTIQTLT LFLTSGGVLL SLYVSASLSY LLYSDILLKF SPTKRTAPTM
60 70 80 90 100
SLDCANVSNV 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 SEALAPSGVM
410 420 430 440 450
VSMKEPGWYS FGFEIKDKKC DVPCIGIEMV HDGGKETWHS AATAIYCLMG
460
SGQLLWDTVT GVDMAL
Length:466
Mass (Da):51,501
Last modified:April 1, 1990 - v1
Checksum:i024F86FA5841BF76
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M30637 Genomic RNA. Translation: AAA43743.1.
PIRiG46347.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M30637 Genomic RNA. Translation: AAA43743.1 .
PIRi G46347.

3D structure databases

ProteinModelPortali P16203.
SMRi P16203. Positions 77-466.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi GH34. Glycoside Hydrolase Family 34.

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_INBSI
AccessioniPrimary (citable) accession number: P16203
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: October 29, 2014
This is version 94 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