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P27907

- NRAM_INBBE

UniProt

P27907 - NRAM_INBBE

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Protein

Neuraminidase

Gene

NA

Organism
Influenza B virus (strain B/Beijing/1/1987)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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.1 Publication

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
Active sitei148 – 1481Proton donor/acceptorBy similarity
Binding sitei149 – 1491Substrate
Binding sitei291 – 2911Substrate
Metal bindingi292 – 2921Calcium; via carbonyl oxygen1 Publication
Metal bindingi296 – 2961Calcium; via carbonyl oxygen1 Publication
Metal bindingi323 – 3231Calcium1 Publication
Metal bindingi343 – 3431Calcium; via carbonyl oxygen1 Publication
Metal bindingi345 – 3451Calcium; via carbonyl oxygen1 Publication
Binding sitei373 – 3731Substrate
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

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/Beijing/1/1987)
Taxonomic identifieri11525 [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

Pathology & Biotechi

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 465465NeuraminidasePRO_0000078730Add
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 ↔ 419
Disulfide bondi121 ↔ 126
Disulfide bondi181 ↔ 228
Disulfide bondi230 ↔ 235
Disulfide bondi276 ↔ 290
Disulfide bondi278 ↔ 288
Glycosylationi283 – 2831N-linked (GlcNAc...); by host1 Publication
Disulfide bondi317 ↔ 336
Disulfide bondi423 ↔ 446

Post-translational modificationi

N-glycosylated.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Interactioni

Subunit structurei

Homotetramer.1 Publication

Structurei

Secondary structure

1
465
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi89 – 979
Helixi99 – 1024
Beta strandi111 – 12111
Beta strandi126 – 14015
Turni143 – 1464
Beta strandi154 – 1596
Turni166 – 1683
Beta strandi170 – 1745
Beta strandi176 – 1827
Beta strandi187 – 1948
Helixi196 – 1983
Beta strandi200 – 2056
Beta strandi208 – 2147
Beta strandi216 – 2194
Beta strandi229 – 2313
Beta strandi234 – 2429
Beta strandi244 – 2463
Beta strandi248 – 2569
Beta strandi259 – 2646
Beta strandi267 – 2693
Beta strandi274 – 29118
Beta strandi293 – 2953
Beta strandi300 – 3056
Turni306 – 3094
Beta strandi310 – 3156
Beta strandi323 – 3253
Beta strandi351 – 3555
Beta strandi360 – 3667
Beta strandi368 – 38417
Turni386 – 3883
Beta strandi394 – 40512
Beta strandi409 – 4157
Beta strandi417 – 43014
Beta strandi439 – 4479
Beta strandi449 – 4513

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP27907.
SMRiP27907. Positions 76-465.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP27907.

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 66IntravirionSequence Analysis
Topological domaini36 – 465430Virion 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 – 6830Hypervariable stalk regionAdd
BLAST
Regioni69 – 465397Head of neuraminidaseAdd
BLAST
Regioni274 – 2752Substrate binding

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.

P27907-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLPSTIQTLT LFLTSGGVLL SLYVSASLSY LLYSDILLKF SSKITAPTMT
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 DGSASGISKC
260 270 280 290 300
RFLKIREGRI IKEIFPTGRV EHTEECTCGF ASNKTIECAC RDNSYTAKRP
310 320 330 340 350
FVKLNVETDT AEIRLMCTET YLDTPRPDDG SITGPCESNG DKGRGGIKGG
360 370 380 390 400
FVHQRMASKI GRWYSRTMSK TERMGMELYV RYDGDPWTDS DALAHSGVMV
410 420 430 440 450
SMKEPGWYSF GFEIKDKKCD VPCIGIEMVH DGGKKTWHSA ATAIYCLMGS
460
GQLLWDTVTG VDMAL
Length:465
Mass (Da):51,430
Last modified:August 1, 1992 - v1
Checksum:i2FC60B895CBD430C
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M54967 Genomic RNA. Translation: AAA43733.1.
PIRiB38520. NMIVB1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M54967 Genomic RNA. Translation: AAA43733.1 .
PIRi B38520. NMIVB1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1A4G X-ray 2.20 A/B 76-465 [» ]
1A4Q X-ray 1.90 A/B 76-465 [» ]
1NSB X-ray 2.20 A/B 76-465 [» ]
1NSC X-ray 1.70 A/B 76-465 [» ]
1NSD X-ray 1.80 A/B 76-465 [» ]
ProteinModelPortali P27907.
SMRi P27907. Positions 76-465.
ModBasei Search...
MobiDBi Search...

Chemistry

DrugBanki DB00558. Zanamivir.

Protein family/group databases

CAZyi GH34. Glycoside Hydrolase Family 34.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P27907.

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. "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 (2.20 ANGSTROMS) OF 76-465 IN COMPLEX WITH CALCIUM AND SIALIC ACID, GLYCOSYLATION AT ASN-283, SUBUNIT, COFACTOR.
  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.

Entry informationi

Entry nameiNRAM_INBBE
AccessioniPrimary (citable) accession number: P27907
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: October 29, 2014
This is version 97 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.

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3