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P09573

- NRAM_I83A6

UniProt

P09573 - NRAM_I83A6

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Protein

Neuraminidase

Gene

NA

Organism
Influenza A virus (strain A/Chicken/Pennsylvania/1370/1983 H5N2)
Status
Reviewed - Annotation score: 5 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. 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

Ca2+By similarityNote: Binds 1 Ca(2+) 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 sitei98 – 981SubstrateBy similarity
Active sitei131 – 1311Proton donor/acceptorBy similarity
Binding sitei132 – 1321SubstrateBy similarity
Binding sitei272 – 2721SubstrateBy similarity
Metal bindingi273 – 2731Calcium; via carbonyl oxygenBy similarity
Metal bindingi277 – 2771Calcium; via carbonyl oxygenBy similarity
Metal bindingi304 – 3041CalciumBy similarity
Binding sitei351 – 3511SubstrateBy similarity
Active sitei386 – 3861NucleophileBy 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/Chicken/Pennsylvania/1370/1983 H5N2)
Taxonomic identifieri385617 [NCBI]
Taxonomic lineageiVirusesssRNA negative-strand virusesOrthomyxoviridaeInfluenzavirus A
Virus hostiAves [TaxID: 8782]

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 66IntravirionSequence Analysis
Transmembranei7 – 3529Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini36 – 449414Virion surfaceSequence AnalysisAdd
BLAST

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 – 449449NeuraminidasePRO_0000078680Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi48 – 481N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi66 – 661N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi72 ↔ 397By similarity
Disulfide bondi104 ↔ 109By similarity
Glycosylationi123 – 1231N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi126 – 1261N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi155 ↔ 173By similarity
Disulfide bondi163 ↔ 210By similarity
Glycosylationi180 – 1801N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi212 ↔ 217By similarity
Glycosylationi214 – 2141N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi258 ↔ 271By similarity
Disulfide bondi260 ↔ 269By similarity
Disulfide bondi298 ↔ 317By similarity
Glycosylationi382 – 3821N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi401 ↔ 427By similarity

Post-translational modificationi

N-glycosylated.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Interactioni

Subunit structurei

Homotetramer.By similarity

Structurei

3D structure databases

ProteinModelPortaliP09573.
SMRiP09573. Positions 62-449.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni11 – 3323Involved in apical transport and lipid raft associationBy similarityAdd
BLAST
Regioni36 – 7035Hypervariable stalk regionAdd
BLAST
Regioni71 – 449379Head of neuraminidaseAdd
BLAST
Regioni256 – 2572Substrate bindingBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi311 – 3155Poly-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.

P09573-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNPNQKIITI GSVSLTIATV CFLMQIAILA TNVTLHFRQN ERSIPAYNQT
60 70 80 90 100
TPCKPIIIER NIKYRNWSKP QCQITGFAPF SKDNSIRLSA GGGIWVTREP
110 120 130 140 150
YVSCDPSKCY QFALGQGTTL DNNHSNGTIH DRTPHRTLLM NELGVPFHLG
160 170 180 190 200
TRQVCIAWSS SSCHDGKAWL HVCVTGDDRN ATASFIYNGM LVDSIGSWSQ
210 220 230 240 250
NILRTQESEC VCINGTCTVV MTDGSASGKA DIRILFIREG KIVHISPLSG
260 270 280 290 300
SAQHIEECSC YPRYPNVRCV CRDNWKGSNR PVIDINMADY SIDSSYVCSG
310 320 330 340 350
LVGDTPRNDD SSSSSNCRDP NNERGNPGVK GWAFDIGDDV WMGRTISKDS
360 370 380 390 400
RSGYETFRVI GGWATANSKS QTNRQVIVDN NNWSGYSGIF SVESKSCINR
410 420 430 440
CFYVELIRGR PQETRVWWTS NSIVVFCGTS GTYGTGSWPD GANINFMPL
Length:449
Mass (Da):49,693
Last modified:March 6, 2007 - v2
Checksum:iDC716FBFB147ADA1
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti42 – 421R → G in AAA43424. (PubMed:2414922)Curated
Sequence conflicti122 – 1221N → H in AAA43424. (PubMed:2414922)Curated
Sequence conflicti160 – 1601S → R in AAA43424. (PubMed:2414922)Curated
Sequence conflicti232 – 2321I → T in AAA43424. (PubMed:2414922)Curated
Sequence conflicti263 – 2653RYP → KSYL in AAA43424. (PubMed:2414922)Curated
Sequence conflicti283 – 2831I → KL in AAA43424. (PubMed:2414922)Curated
Sequence conflicti361 – 3611G → S in AAA43424. (PubMed:2414922)Curated
Sequence conflicti420 – 4201S → T in AAA43424. (PubMed:2414922)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M12051 Genomic RNA. Translation: AAA43424.1.
CY015110 Genomic RNA. Translation: ABI85148.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M12051 Genomic RNA. Translation: AAA43424.1 .
CY015110 Genomic RNA. Translation: ABI85148.1 .

3D structure databases

ProteinModelPortali P09573.
SMRi P09573. Positions 62-449.
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. "The neuraminidases of the virulent and avirulent A/Chicken/Pennsylvania/83 (H5N2) influenza A viruses: sequence and antigenic analyses."
    Deshpande K.L., Naeve C.W., Webster R.G.
    Virology 147:49-60(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  3. "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.
  4. "Neuraminidase inhibitors for influenza."
    Moscona A.
    N. Engl. J. Med. 353:1363-1373(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  5. "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_I83A6
AccessioniPrimary (citable) accession number: P09573
Secondary accession number(s): Q0A2D4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: March 6, 2007
Last modified: November 26, 2014
This is version 101 of the entry and version 2 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