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P05803

- NRAM_I84A1

UniProt

P05803 - NRAM_I84A1

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Protein

Neuraminidase

Gene

NA

Organism
Influenza A virus (strain A/Whale/Maine/1/1984 H13N9)
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.

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+Note: Binds 1 Ca(2+) ion per subunit.

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 sitei119 – 1191SubstrateBy similarity
Active sitei152 – 1521Proton donor/acceptorBy similarity
Binding sitei153 – 1531SubstrateBy similarity
Binding sitei294 – 2941SubstrateBy similarity
Metal bindingi295 – 2951Calcium; via carbonyl oxygen1 Publication
Metal bindingi299 – 2991Calcium; via carbonyl oxygen1 Publication
Metal bindingi326 – 3261Calcium1 Publication
Metal bindingi348 – 3481Calcium; via carbonyl oxygen1 Publication
Binding sitei372 – 3721SubstrateBy similarity
Active sitei406 – 4061NucleophileBy 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/Whale/Maine/1/1984 H13N9)
Taxonomic identifieri11484 [NCBI]
Taxonomic lineageiVirusesssRNA negative-strand virusesOrthomyxoviridaeInfluenzavirus A
Virus hostiAves [TaxID: 8782]
Cetacea (whales) [TaxID: 9721]

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 – 470435Virion 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 – 470470NeuraminidasePRO_0000078725Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi42 – 421N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi52 – 521N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi63 – 631N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi66 – 661N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi87 – 871N-linked (GlcNAc...); by host2 Publications
Disulfide bondi93 ↔ 4191 Publication
Disulfide bondi125 ↔ 1301 Publication
Glycosylationi147 – 1471N-linked (GlcNAc...); by host1 Publication
Disulfide bondi177 ↔ 1951 Publication
Disulfide bondi185 ↔ 2321 Publication
Glycosylationi202 – 2021N-linked (GlcNAc...) (high mannose); by host1 Publication
Disulfide bondi234 ↔ 2391 Publication
Disulfide bondi280 ↔ 2931 Publication
Disulfide bondi282 ↔ 2911 Publication
Disulfide bondi320 ↔ 3381 Publication
Disulfide bondi423 ↔ 4491 Publication

Post-translational modificationi

N-glycosylated.2 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein

Interactioni

Subunit structurei

Homotetramer.2 Publications

Protein-protein interaction databases

MINTiMINT-1511103.

Structurei

Secondary structure

1
470
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi96 – 1049Combined sources
Helixi106 – 1105Combined sources
Beta strandi122 – 1265Combined sources
Beta strandi129 – 1357Combined sources
Beta strandi138 – 1436Combined sources
Helixi144 – 1463Combined sources
Turni147 – 1504Combined sources
Beta strandi158 – 1636Combined sources
Turni170 – 1723Combined sources
Beta strandi174 – 18613Combined sources
Beta strandi191 – 1988Combined sources
Beta strandi204 – 21815Combined sources
Beta strandi220 – 2234Combined sources
Beta strandi229 – 2313Combined sources
Beta strandi238 – 2469Combined sources
Beta strandi248 – 2503Combined sources
Beta strandi252 – 2609Combined sources
Beta strandi263 – 2697Combined sources
Beta strandi281 – 2855Combined sources
Beta strandi288 – 2925Combined sources
Beta strandi296 – 2983Combined sources
Beta strandi303 – 3086Combined sources
Turni309 – 3124Combined sources
Beta strandi313 – 3186Combined sources
Beta strandi326 – 3283Combined sources
Beta strandi338 – 3403Combined sources
Beta strandi354 – 3574Combined sources
Helixi358 – 3603Combined sources
Beta strandi362 – 3654Combined sources
Beta strandi369 – 37911Combined sources
Turni381 – 3855Combined sources
Beta strandi392 – 40312Combined sources
Beta strandi407 – 4104Combined sources
Beta strandi415 – 4206Combined sources
Beta strandi423 – 4319Combined sources
Turni432 – 4343Combined sources
Beta strandi437 – 4393Combined sources
Beta strandi441 – 45313Combined sources
Helixi466 – 4694Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1NCDX-ray2.90N83-470[»]
1NMAX-ray3.00N83-470[»]
1NMBX-ray2.20N1-470[»]
2B8HX-ray2.20A/B/C/D83-470[»]
ProteinModelPortaliP05803.
SMRiP05803. Positions 83-470.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP05803.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni11 – 3323Involved in apical transport and lipid raft associationBy similarityAdd
BLAST
Regioni36 – 8954Hypervariable stalk regionAdd
BLAST
Regioni90 – 470381Head of neuraminidaseAdd
BLAST
Regioni278 – 2792Substrate bindingBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi345 – 3484Poly-Asn

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.

P05803-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNPNQKILCT SATALVIGTI AVLIGIVNLG LNIGLHLKPS CNCSRSQPEA
60 70 80 90 100
TNASQTIINN YYNETNITQI SNTNIQVEER ASREFNNLTK GLCTINSWHI
110 120 130 140 150
YGKDNAVRIG EDSDVLVTRE PYVSCDPDEC RFYALSQGTT IRGKHSNGTI
160 170 180 190 200
HDRSQYRDLI SWPLSSPPTV YNSRVECIGW SSTSCHDGRA RMSICISGPN
210 220 230 240 250
NNASAVIWYN RRPVTEINTW ARNILRTQES ECVCQNGVCP VVFTDGSATG
260 270 280 290 300
PAETRIYYFK EGKILKWEPL TGTAKHIEEC SCYGEQAGVT CTCRDNWQGS
310 320 330 340 350
NRPVIQIDPV AMTHTSQYIC SPVLTDNPRP NDPTVGKCND PYPGNNNNGV
360 370 380 390 400
KGFSYLDGGN TWLGRTISIA SRSGYEMLKV PNALTDDRSK PTQGQTIVLN
410 420 430 440 450
TDWSGYSGSF MDYWAEGECY RACFYVELIR GRPKEDKVWW TSNSIVSMCS
460 470
STEFLGQWNW PDGAKIEYFL
Length:470
Mass (Da):52,394
Last modified:November 1, 1988 - v1
Checksum:iF2054DD47BBAB996
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M17812 Genomic RNA. Translation: AAA43575.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M17812 Genomic RNA. Translation: AAA43575.1 .

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1NCD X-ray 2.90 N 83-470 [» ]
1NMA X-ray 3.00 N 83-470 [» ]
1NMB X-ray 2.20 N 1-470 [» ]
2B8H X-ray 2.20 A/B/C/D 83-470 [» ]
ProteinModelPortali P05803.
SMRi P05803. Positions 83-470.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

MINTi MINT-1511103.

Protein family/group databases

CAZyi GH34. Glycoside Hydrolase Family 34.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P05803.
PROi P05803.

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. "Distribution of sequence differences in influenza N9 neuraminidase of tern and whale viruses and crystallization of the whale neuraminidase complexed with antibodies."
    Air G.M., Webster R.G., Colman P.M., Laver W.G.
    Virology 160:346-354(1987) [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.
  5. "The structure of a complex between the NC10 antibody and influenza virus neuraminidase and comparison with the overlapping binding site of the NC41 antibody."
    Malby R.L., Tulip W.R., Harley V.R., McKimm-Breschkin J.L., Laver W.G., Webster R.G., Colman P.M.
    Structure 2:733-746(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH CALCIUM; SUBSTRATE ANALOG AND THE NC10 ANTIBODY, SUBUNIT, DISULFIDE BONDS, GLYCOSYLATION AT ASN-87 AND ASN-147.
  6. "N9 neuraminidase complexes with antibodies NC41 and NC10: empirical free energy calculations capture specificity trends observed with mutant binding data."
    Tulip W.R., Harley V.R., Webster R.G., Novotny J.
    Biochemistry 33:7986-7997(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 83-470 IN COMPLEX WITH ANTIBODIES NC41 AND NC10, GLYCOSYLATION AT ASN-87 AND ASN-202.

Entry informationi

Entry nameiNRAM_I84A1
AccessioniPrimary (citable) accession number: P05803
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: November 1, 1988
Last modified: November 26, 2014
This is version 114 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.

Keywords - Technical termi

3D-structure

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