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P16199

- NRAM_INBMF

UniProt

P16199 - NRAM_INBMF

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Protein
Neuraminidase
Gene
NA
Organism
Influenza B virus (strain B/Memphis/3/1989)
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 sitei115 – 1151Substrate By similarity
Active sitei148 – 1481Proton donor/acceptor By similarity
Binding sitei149 – 1491Substrate By similarity
Binding sitei291 – 2911Substrate By similarity
Metal bindingi292 – 2921Calcium; via carbonyl oxygen By similarity
Metal bindingi296 – 2961Calcium; via carbonyl oxygen By similarity
Metal bindingi323 – 3231Calcium By similarity
Metal bindingi343 – 3431Calcium; via carbonyl oxygen By similarity
Metal bindingi345 – 3451Calcium; via carbonyl oxygen By similarity
Binding sitei373 – 3731Substrate By similarity
Active sitei408 – 4081Nucleophile 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
Complete GO annotation...

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/Memphis/3/1989)
Taxonomic identifieri98827 [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 prediction
Add
BLAST
Topological domaini36 – 465430Virion surface Reviewed prediction
Add
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 – 465465Neuraminidase
PRO_0000078736Add
BLAST

Amino acid modifications

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

Post-translational modificationi

N-glycosylated By similarity.

Keywords - PTMi

Disulfide bond, Glycoprotein

Interactioni

Subunit structurei

Homotetramer By similarity.

Structurei

3D structure databases

ProteinModelPortaliP16199.
SMRiP16199. Positions 76-465.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni39 – 6830Hypervariable stalk region
Add
BLAST
Regioni69 – 465397Head of neuraminidase
Add
BLAST
Regioni274 – 2752Substrate 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.

P16199-1 [UniParc]FASTAAdd to Basket

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MLPSTIQTLT LFLTSGGVLL SLYVSASLSY LLYSDILLRF SSKITAPTMT    50
LDCANASNVQ AVNRSATKEM TFLLPEPEWT YPRLSCQGST FQKALLISPH 100
RFGEARGNSA PLIIREPFIA CGPKECKHFA LTHYAAQPGG YYNGTREDRN 150
KLRHLISVKL GKIPTVENSI FHMAAWSGSA CHDGREWTYI GVDGPDSNAL 200
IKIKYGEAYT DTYHSYANNI LRTQESACNC IGGDCYLMIT DGSASGISEC 250
RFLKIREGRI IKEIFPTGRV EHTEECTCGF ASNKTIECAC RDNSYTAKRP 300
FVKLNVETDT AEIRLMCTET YLDTPRPDDG SITGPCESDG DKGRGGIKGG 350
FVHQRMASKI GRWYSRTMSK TERMGMELYV KYDGDPWTDS DALAPSGVMV 400
SMKEPGWYSF GFEIKDKKCD VPCIGIEMVH DGGKKTWHSA ATAIYCLMGS 450
GQLLWDTVTG VDMAL 465
Length:465
Mass (Da):51,392
Last modified:April 1, 1990 - v1
Checksum:i2507A2270957F19B
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M30635 Genomic RNA. Translation: AAA43739.1.
PIRiA46347.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M30635 Genomic RNA. Translation: AAA43739.1 .
PIRi A46347.

3D structure databases

ProteinModelPortali P16199.
SMRi P16199. Positions 76-465.
ModBasei Search...

Chemistry

BindingDBi P16199.

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_INBMF
AccessioniPrimary (citable) accession number: P16199
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: September 3, 2014
This is version 93 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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