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Q9IGQ6

- NRAM_I18A0

UniProt

Q9IGQ6 - NRAM_I18A0

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Protein

Neuraminidase

Gene

NA

Organism
Influenza A virus (strain A/Brevig Mission/1/1918 H1N1) (Influenza A virus (strain A/South Carolina/1/1918 H1N1))
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. Likely to plays a role in the budding process through its association with lipid rafts during intracellular transport. May additionally display a raft-association independent effect on budding. Plays a role in the determination of host range restriction on replication and virulence. Sialidase activity in late endosome/lysosome traffic seems to enhance virus replication (By similarity).By similarity
Unlike other strains, A/WSN/33 neuraminidase binds and activates plasminogen into plasmin in the vicinity of HA so that activated plasmin cleaves HA rendering the virus infectious.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 sitei118 – 1181Substrate
Active sitei151 – 1511Proton donor/acceptorBy similarity
Binding sitei152 – 1521Substrate
Binding sitei293 – 2931Substrate
Metal bindingi294 – 2941Calcium; via carbonyl oxygen1 Publication
Metal bindingi298 – 2981Calcium; via carbonyl oxygen1 Publication
Metal bindingi324 – 3241Calcium1 Publication
Metal bindingi344 – 3441Calcium; via carbonyl oxygen1 Publication
Binding sitei368 – 3681Substrate
Active sitei402 – 4021NucleophileBy 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

Enzyme and pathway databases

SABIO-RKQ9IGQ6.

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 A virus (strain A/Brevig Mission/1/1918 H1N1) (Influenza A virus (strain A/South Carolina/1/1918 H1N1))
Taxonomic identifieri88776 [NCBI]
Taxonomic lineageiVirusesssRNA negative-strand virusesOrthomyxoviridaeInfluenzavirus A
Virus hostiAves [TaxID: 8782]
Homo sapiens (Human) [TaxID: 9606]
Sus scrofa (Pig) [TaxID: 9823]
ProteomesiUP000008430: Genome

Subcellular locationi

Virion membrane. Host apical cell membrane; Single-pass type II membrane protein
Note: Preferentially accumulates at the apical plasma membrane in infected polarized epithelial cells, which is the virus assembly site. Uses lipid rafts for cell surface transport and apical sorting. 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 – 469469NeuraminidasePRO_0000310569Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi88 – 881N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi92 ↔ 4171 Publication
Disulfide bondi124 ↔ 1291 Publication
Glycosylationi146 – 1461N-linked (GlcNAc...); by host1 Publication
Disulfide bondi184 ↔ 2311 Publication
Disulfide bondi233 ↔ 2381 Publication
Glycosylationi235 – 2351N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi279 ↔ 2921 Publication
Disulfide bondi281 ↔ 2901 Publication
Disulfide bondi318 ↔ 3351 Publication
Disulfide bondi421 ↔ 4461 Publication

Post-translational modificationi

N-glycosylated.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PRIDEiQ9IGQ6.

Interactioni

Subunit structurei

Homotetramer.1 Publication

Structurei

Secondary structure

1
469
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi95 – 1028
Helixi105 – 1095
Beta strandi115 – 12410
Beta strandi129 – 14214
Helixi143 – 1453
Turni146 – 1494
Beta strandi157 – 1626
Turni169 – 1713
Beta strandi173 – 1775
Beta strandi179 – 1857
Beta strandi190 – 1978
Beta strandi203 – 2086
Beta strandi211 – 2177
Beta strandi219 – 2224
Beta strandi228 – 2303
Beta strandi232 – 2343
Beta strandi237 – 2459
Beta strandi247 – 2493
Beta strandi252 – 2598
Beta strandi262 – 2687
Beta strandi277 – 2848
Beta strandi287 – 2937
Beta strandi302 – 3065
Beta strandi312 – 3165
Beta strandi324 – 3263
Beta strandi350 – 3534
Beta strandi356 – 3616
Beta strandi365 – 37612
Turni377 – 3815
Beta strandi388 – 39912
Beta strandi403 – 4086
Helixi410 – 4134
Beta strandi416 – 42914
Turni430 – 4323
Beta strandi433 – 4364
Beta strandi438 – 45013

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3B7EX-ray1.45A/B83-467[»]
3BEQX-ray1.64A/B83-467[»]
3CYEX-ray1.65A/B83-469[»]
ProteinModelPortaliQ9IGQ6.
SMRiQ9IGQ6. Positions 83-467.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9IGQ6.

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 66IntravirionSequence Analysis
Topological domaini28 – 469442Virion surfaceSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei7 – 2721HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni11 – 3323Involved in apical transport and lipid raft associationBy similarityAdd
BLAST
Regioni36 – 9055Hypervariable stalk regionBy similarityAdd
BLAST
Regioni91 – 469379Head of neuraminidaseBy similarityAdd
BLAST
Regioni277 – 2782Substrate bindingBy similarity

Domaini

Intact N-terminus is essential for virion morphogenesis. Possess two apical sorting signals, one in the ectodomain, which is likely to be a glycan, and the other in the transmembrane domain. The transmembrane domain also plays a role in lipid raft association (By similarity).By 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.

Q9IGQ6-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNPNQKIITI GSICMVVGII SLILQIGNII SIWVSHSIQT GNQNHPETCN
60 70 80 90 100
QSIITYENNT WVNQTYVNIS NTNVVAGQDA TSVILTGNSS LCPISGWAIY
110 120 130 140 150
SKDNGIRIGS KGDVFVIREP FISCSHLECR TFFLTQGALL NDKHSNGTVK
160 170 180 190 200
DRSPYRTLMS CPVGEAPSPY NSRFESVAWS ASACHDGMGW LTIGISGPDN
210 220 230 240 250
GAVAVLKYNG IITDTIKSWR NNILRTQESE CACVNGSCFT IMTDGPSNGQ
260 270 280 290 300
ASYKILKIEK GKVTKSIELN APNYHYEECS CYPDTGKVMC VCRDNWHGSN
310 320 330 340 350
RPWVSFDQNL DYQIGYICSG VFGDNPRPND GTGSCGPVSS NGANGIKGFS
360 370 380 390 400
FRYDNGVWIG RTKSTSSRSG FEMIWDPNGW TETDSSFSVR QDIVAITDWS
410 420 430 440 450
GYSGSFVQHP ELTGLDCMRP CFWVELIRGQ PKENTIWTSG SSISFCGVNS
460
DTVGWSWPDG AELPFSIDK
Length:469
Mass (Da):51,406
Last modified:October 1, 2000 - v1
Checksum:i28888692D4394159
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF250356 mRNA. Translation: AAF77036.1.
U94893 Genomic DNA. Translation: AAC57065.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF250356 mRNA. Translation: AAF77036.1 .
U94893 Genomic DNA. Translation: AAC57065.1 .

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3B7E X-ray 1.45 A/B 83-467 [» ]
3BEQ X-ray 1.64 A/B 83-467 [» ]
3CYE X-ray 1.65 A/B 83-469 [» ]
ProteinModelPortali Q9IGQ6.
SMRi Q9IGQ6. Positions 83-467.
ModBasei Search...
MobiDBi Search...

Chemistry

BindingDBi Q9IGQ6.
ChEMBLi CHEMBL1795169.

Protein family/group databases

CAZyi GH34. Glycoside Hydrolase Family 34.

Proteomic databases

PRIDEi Q9IGQ6.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

SABIO-RK Q9IGQ6.

Miscellaneous databases

EvolutionaryTracei Q9IGQ6.
PROi Q9IGQ6.

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. "Characterization of the 1918 'Spanish' influenza virus neuraminidase gene."
    Reid A.H., Fanning T.G., Janczewski T.A., Taubenberger J.K.
    Proc. Natl. Acad. Sci. U.S.A. 97:6785-6790(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Initial genetic characterization of the 1918 'Spanish' influenza virus."
    Taubenberger J.K., Reid A.H., Krafft A.E., Bijwaard K.E., Fanning T.G.
    Science 275:1793-1796(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 12-23.
    Strain: A/South Carolina/1/18.
  3. "Structural characterization of the 1918 influenza virus H1N1 neuraminidase."
    Xu X., Zhu X., Dwek R.A., Stevens J., Wilson I.A.
    J. Virol. 82:10493-10501(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 83-467 IN COMPLEX WITH CALCIUM AND INHIBITOR ZANAMIVIR, COFACTOR, SUBUNIT, GLYCOSYLATION AT ASN-146, DISULFIDE BOND.

Entry informationi

Entry nameiNRAM_I18A0
AccessioniPrimary (citable) accession number: Q9IGQ6
Secondary accession number(s): O10421
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: October 1, 2000
Last modified: October 29, 2014
This is version 77 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 A 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.
South Carolina isolate has been sequenced from formalid fixed-lung tissues of a 21-year-old male which died in 1918 at Ft. Jackson, SC. Brevig Mission isolate has been sequenced from lung tissues of an Inuit woman buried in the permafrost in a gravesite near Brevig Mission, Alaska. This sample was recovered by John Hultin, retired pathologist.

Keywords - Technical termi

3D-structure, Complete proteome

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