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P16201

- NRAM_INBOR

UniProt

P16201 - NRAM_INBOR

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Protein

Neuraminidase

Gene
NA
Organism
Influenza B virus (strain B/Oregon/5/1980)
Status
Reviewed - Annotation score: 4 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.

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 – 1161Substrate By similarity
Active sitei149 – 1491Proton donor/acceptor By similarity
Binding sitei150 – 1501Substrate By similarity
Binding sitei292 – 2921Substrate By similarity
Metal bindingi293 – 2931Calcium; via carbonyl oxygen By similarity
Metal bindingi297 – 2971Calcium; via carbonyl oxygen By similarity
Metal bindingi324 – 3241Calcium By similarity
Metal bindingi344 – 3441Calcium; via carbonyl oxygen By similarity
Metal bindingi346 – 3461Calcium; via carbonyl oxygen By similarity
Binding sitei374 – 3741Substrate By similarity
Active sitei409 – 4091Nucleophile By 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

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

Subcellular locationi

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.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 66Intravirion Reviewed prediction
Transmembranei7 – 3529Helical; Signal-anchor for type II membrane protein; Reviewed predictionAdd
BLAST
Topological domaini36 – 466431Virion surface Reviewed predictionAdd
BLAST

GO - Cellular componenti

  1. host cell plasma membrane Source: UniProtKB-SubCell
  2. integral component of membrane Source: UniProtKB-KW
  3. virion membrane Source: UniProtKB-SubCell
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_0000078737Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi56 – 561N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi64 – 641N-linked (GlcNAc...); by host Reviewed prediction
Disulfide bondi87 ↔ 420 By similarity
Disulfide bondi122 ↔ 127 By similarity
Glycosylationi144 – 1441N-linked (GlcNAc...); by host Reviewed prediction
Disulfide bondi182 ↔ 229 By similarity
Disulfide bondi231 ↔ 236 By similarity
Disulfide bondi277 ↔ 291 By similarity
Disulfide bondi279 ↔ 289 By similarity
Glycosylationi284 – 2841N-linked (GlcNAc...); by host Reviewed prediction
Disulfide bondi318 ↔ 337 By similarity
Disulfide bondi424 ↔ 447 By similarity

Post-translational modificationi

N-glycosylated By similarity.

Keywords - PTMi

Disulfide bond, Glycoprotein

Interactioni

Subunit structurei

Homotetramer By similarity.

Structurei

3D structure databases

ProteinModelPortaliP16201.
SMRiP16201. Positions 77-466.

Family & Domainsi

Region

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

Sequence similaritiesi

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.

P16201-1 [UniParc]FASTAAdd to Basket

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MLPSTIQTLT LFLTSGGVLL SLYVSASLSY LLYSDILLKF STTKITAPTM    50
SLDCANISNV QAVNRSATKE MTFLLPEPEW TYPRLSCQGS TFQKALLISP 100
HRFGEARGNS APLIIREPFI ACGPKECKHF ALTHYAAQPG GYYNGTRKDR 150
NKLRHLISVK LGKIPTVENS IFHMAAWSGS ACHDGREWTY IGVDGPDSNA 200
LIKIKYGEAY TDTYHSYANN ILRTQESACN CIGGDCYLMI TDGSASGISK 250
CRFLKIREGR IIKEIFPTGR VEHTEECTCG FASNKTIECA CRDNSYTAKR 300
PFVKLNVETD TAEIRLMCTE TYLDTPRPDD GSITGPCESN GDKGLGGIKG 350
GFVHQRMASK IGRWYSRTMS KTERMGMELY VKYDGDPWTD SDALAPSGVM 400
VSMKEPGWYS FGFEIKDKKC DVPCIGIEMV HDGGKETWHS AATAIYCLMG 450
SGQLLWDTVT GVDMAL 466
Length:466
Mass (Da):51,462
Last modified:April 1, 1990 - v1
Checksum:iD3F357AC5B3E1CDE
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M30636 Genomic RNA. Translation: AAA43741.1.
PIRiF46347.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M30636 Genomic RNA. Translation: AAA43741.1 .
PIRi F46347.

3D structure databases

ProteinModelPortali P16201.
SMRi P16201. 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_INBOR
AccessioniPrimary (citable) accession number: P16201
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: September 3, 2014
This is version 91 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

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