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Q6TXB9

- NRAM_I85A5

UniProt

Q6TXB9 - NRAM_I85A5

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Protein

Neuraminidase

Gene

NA

Organism
Influenza A virus (strain A/Equine/Santiago/1/1985 H3N8)
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 sitei116 – 1161SubstrateBy similarity
Active sitei149 – 1491Proton donor/acceptorBy similarity
Binding sitei150 – 1501SubstrateBy similarity
Binding sitei291 – 2911SubstrateBy similarity
Metal bindingi292 – 2921Calcium; via carbonyl oxygenBy similarity
Metal bindingi296 – 2961Calcium; via carbonyl oxygenBy similarity
Metal bindingi322 – 3221CalciumBy similarity
Binding sitei368 – 3681SubstrateBy similarity
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

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/Equine/Santiago/1/1985 H3N8)
Taxonomic identifieri11414 [NCBI]
Taxonomic lineageiVirusesssRNA negative-strand virusesOrthomyxoviridaeInfluenzavirus A
Virus hostiAves [TaxID: 8782]
Equus caballus (Horse) [TaxID: 9796]

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. 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 – 470470NeuraminidasePRO_0000265109Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi46 – 461N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi54 – 541N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi90 ↔ 417By similarity
Disulfide bondi122 ↔ 127By similarity
Glycosylationi144 – 1441N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi182 ↔ 229By similarity
Disulfide bondi231 ↔ 236By similarity
Disulfide bondi277 ↔ 290By similarity
Disulfide bondi279 ↔ 288By similarity
Glycosylationi293 – 2931N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi316 ↔ 335By similarity
Glycosylationi398 – 3981N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi421 ↔ 446By similarity

Post-translational modificationi

N-glycosylated.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Interactioni

Subunit structurei

Homotetramer.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ6TXB9.
SMRiQ6TXB9. Positions 82-467.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 66IntravirionSequence Analysis

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
Regioni11 – 3323Involved in apical transport and lipid raft associationBy similarityAdd
BLAST
Regioni39 – 8850Hypervariable stalk regionAdd
BLAST
Regioni89 – 470382Head of neuraminidaseAdd
BLAST
Regioni275 – 2762Substrate bindingBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi439 – 4424Poly-Ser

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.

Q6TXB9-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNPNQKIITI GSASLGILIL NVILHVVSII VTVLVLNNNG TGLNCNGTII
60 70 80 90 100
REYNETVRVE RVIQWYNTNT IEYIERPSNE YYMNNTEPLC EAQGFAPFSK
110 120 130 140 150
DNGIRIGSRG HVFVIREPFV SCSPSECRTF FLTQGSLLND KHSNGTVKDR
160 170 180 190 200
SPYRTLMSVK IGQSPNVYQA RFESVAWSAT ACHDGKKWMT VGVTGPDNQA
210 220 230 240 250
VAVVNYGGVP VDIINSWAGD ILRTQESSCT CIKGDCYWVM TDGPANRQAK
260 270 280 290 300
YRIFKAKDGR IIGQTDISFN GGHIEECSCY PNEGKVECVC RDNWTGTNRP
310 320 330 340 350
ILVISPDLSY TVGYLCAGIP TDTPRGEDSQ FTGSCTSPLG NKGYGVKGFG
360 370 380 390 400
FRQGTDVWAG RTISRTSRSG FEIIKIRNGW TQNSKDQIRR QVIIDNPNWS
410 420 430 440 450
GYSGSFTLPV ELTKKGCLVP CFWVEMIRGK PEETTIWTSS SSIVMCGVDH
460 470
KIASWSWHDG AILPFDIDKM
Length:470
Mass (Da):52,133
Last modified:July 5, 2004 - v1
Checksum:iC36E595800C1866C
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY383754 mRNA. Translation: AAQ90290.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY383754 mRNA. Translation: AAQ90290.1 .

3D structure databases

ProteinModelPortali Q6TXB9.
SMRi Q6TXB9. Positions 82-467.
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. "Isolation, sequencing and phylogenetic analysis of the hemagglutinin, neuraminidase and nucleoprotein genes of the Chilean equine influenza virus subtypes H7N7 and H3N8."
    Muller I., Jaureguiberry B., Valenzuela P.D.T.
    Biol. Res. 38:55-67(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  2. "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.
  3. "Neuraminidase inhibitors for influenza."
    Moscona A.
    N. Engl. J. Med. 353:1363-1373(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  4. "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_I85A5
AccessioniPrimary (citable) accession number: Q6TXB9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: July 5, 2004
Last modified: October 29, 2014
This is version 62 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