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Q8JSD9

- NRAM_I47A0

UniProt

Q8JSD9 - NRAM_I47A0

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Protein
Neuraminidase
Gene
NA
Organism
Influenza A virus (strain A/Fort Monmouth/1/1947 H1N1)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at transcript 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.

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 sitei118 – 1181Substrate By similarity
Active sitei151 – 1511Proton donor/acceptor By similarity
Binding sitei152 – 1521Substrate By similarity
Binding sitei293 – 2931Substrate By similarity
Metal bindingi294 – 2941Calcium; via carbonyl oxygen By similarity
Metal bindingi298 – 2981Calcium; via carbonyl oxygen By similarity
Metal bindingi324 – 3241Calcium By similarity
Binding sitei368 – 3681Substrate By similarity
Active sitei402 – 4021Nucleophile 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
  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-RKQ8JSD9.

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/Fort Monmouth/1/1947 H1N1)
Taxonomic identifieri380282 [NCBI]
Taxonomic lineageiVirusesssRNA negative-strand virusesOrthomyxoviridaeInfluenzavirus A
Virus hostiAves [TaxID: 8782]
Homo sapiens (Human) [TaxID: 9606]
Sus scrofa (Pig) [TaxID: 9823]

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. 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.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 66Intravirion Reviewed prediction
Transmembranei7 – 2721Helical; Signal-anchor for type II membrane protein; Reviewed prediction
Add
BLAST
Topological domaini28 – 469442Virion 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 – 469469Neuraminidase
PRO_0000280130Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi44 – 441N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi58 – 581N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi63 – 631N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi68 – 681N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi88 – 881N-linked (GlcNAc...); by host Reviewed prediction
Disulfide bondi92 ↔ 417 By similarity
Disulfide bondi124 ↔ 129 By similarity
Glycosylationi146 – 1461N-linked (GlcNAc...); by host Reviewed prediction
Disulfide bondi184 ↔ 231 By similarity
Disulfide bondi233 ↔ 238 By similarity
Glycosylationi235 – 2351N-linked (GlcNAc...); by host Reviewed prediction
Disulfide bondi279 ↔ 292 By similarity
Disulfide bondi281 ↔ 290 By similarity
Disulfide bondi318 ↔ 335 By similarity
Glycosylationi365 – 3651N-linked (GlcNAc...); by host Reviewed prediction
Disulfide bondi421 ↔ 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

ProteinModelPortaliQ8JSD9.
SMRiQ8JSD9. Positions 83-467.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni11 – 3323Involved in apical transport and lipid raft association By similarity
Add
BLAST
Regioni36 – 9055Hypervariable stalk region By similarity
Add
BLAST
Regioni91 – 469379Head of neuraminidase By similarity
Add
BLAST
Regioni277 – 2782Substrate binding By 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.

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.

Q8JSD9-1 [UniParc]FASTAAdd to Basket

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MNPNQKIITI GSICMVVGII SLILQIGNIV SIWISHSIQT GNQNHTGTCD    50
QSIITYKNST WVNQTYVNIS NTNVVAGKDT TSVILAGNSS LCPIRGWAIY 100
SKDNGVRIGS KGDVFVIREP FISCSHLECK TFFLTQGALL NDKHSNGTVK 150
DRSPYRALMS CPVGEAPSPY NSRFESVAWS ASACHDGMGW LTIGISGPDD 200
GAVAVLKYNG IITETIKSWR KEILRTQESE CVCVNGSCFT IMTDGPSGGP 250
ASYKIFKIEK GKVTKSIELD APNSHYEECS CYPDTSKVMC VCRDNWHGSN 300
RPWVSFDQNL DYQMGYICSG VFGDNPRPKD GKGSCGPVNV DGADGVKGFS 350
YRYGNGGWIG RTKSNSSRKG FEMIWDPNGW TDPDSNFLVK QDIVAMTDWS 400
GYSGSFVQHP ELTGLDCMRP CFWVELIRGR PKENTIWTSG SSISFCGVNS 450
DTVDWSWPDD AELPLNIDK 469
Length:469
Mass (Da):51,499
Last modified:October 1, 2002 - v1
Checksum:i74E0E3A8BB7F08BC
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti68 – 725Missing in strain: A/Fort Monmouth/1/1947-MA.
Natural varianti130 – 1301K → R in strain: A/Fort Monmouth/1/1947-MA.
Natural varianti339 – 3391N → Y in strain: A/Fort Monmouth/1/1947-MA.
Natural varianti344 – 3441D → N in strain: A/Fort Monmouth/1/1947-MA.
Natural varianti352 – 3521R → K in strain: A/Fort Monmouth/1/1947-MA.
Natural varianti357 – 3571G → V in strain: A/Fort Monmouth/1/1947-MA.
Natural varianti369 – 3691K → Q in strain: A/Fort Monmouth/1/1947-MA.
Natural varianti382 – 3832DP → ET in strain: A/Fort Monmouth/1/1947-MA.
Natural varianti388 – 3892LV → FT in strain: A/Fort Monmouth/1/1947-MA.
Natural varianti393 – 3931I → V in strain: A/Fort Monmouth/1/1947-MA.
Natural varianti396 – 3961M → V in strain: A/Fort Monmouth/1/1947-MA.
Natural varianti460 – 4601D → G in strain: A/Fort Monmouth/1/1947-MA.
Natural varianti465 – 4662LN → FT in strain: A/Fort Monmouth/1/1947-MA.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti365 – 3651N → I in CAB40420. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF494253 Genomic RNA. Translation: AAM76693.1.
Y14193 Genomic RNA. Translation: CAB40419.1.
Y14194 Genomic RNA. Translation: CAB40420.1.
AF250357 mRNA. Translation: AAF77037.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF494253 Genomic RNA. Translation: AAM76693.1 .
Y14193 Genomic RNA. Translation: CAB40419.1 .
Y14194 Genomic RNA. Translation: CAB40420.1 .
AF250357 mRNA. Translation: AAF77037.1 .

3D structure databases

ProteinModelPortali Q8JSD9.
SMRi Q8JSD9. Positions 83-467.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi GH34. Glycoside Hydrolase Family 34.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

SABIO-RK Q8JSD9.

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. "Genetic analysis of mouse-adapted influenza A virus identifies roles for the NA, PB1, and PB2 genes in virulence."
    Brown E.G., Bailly J.E.
    Virus Res. 61:63-76(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    Strain: A/Fort Monmouth/1/1947-MA.
  2. "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].
    Strain: A/Fort Monmouth/1/1947-MA.
  3. "The total influenza vaccine failure of 1947 revisited: major intrasubtypic antigenic change can explain failure of vaccine in a post-World War II epidemic."
    Kilbourne E.D., Smith C., Brett I., Pokorny B.A., Johansson B., Cox N.
    Proc. Natl. Acad. Sci. U.S.A. 99:10748-10752(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  4. "Assembly and budding of influenza virus."
    Nayak D.P., Hui E.K., Barman S.
    Virus Res. 106:147-165(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  5. "Neuraminidase inhibitors for influenza."
    Moscona A.
    N. Engl. J. Med. 353:1363-1373(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  6. "Sialobiology of influenza: molecular mechanism of host range variation of influenza viruses."
    Suzuki Y.
    Biol. Pharm. Bull. 28:399-408(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.

Entry informationi

Entry nameiNRAM_I47A0
AccessioniPrimary (citable) accession number: Q8JSD9
Secondary accession number(s): Q9WMK7, Q9WMK8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 6, 2007
Last sequence update: October 1, 2002
Last modified: September 3, 2014
This is version 65 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.

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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