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Neuraminidase (EC 3.2.1.18)

 NRAM_I56A2              Reviewed;         470 AA.
Q6XV27; Q83982;
20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
25-OCT-2017, entry version 77.
RecName: Full=Neuraminidase {ECO:0000255|HAMAP-Rule:MF_04071};
EC=3.2.1.18 {ECO:0000255|HAMAP-Rule:MF_04071};
Name=NA {ECO:0000255|HAMAP-Rule:MF_04071};
Influenza A virus (strain A/Duck/England/1/1956 H11N6).
Viruses; ssRNA viruses; ssRNA negative-strand viruses;
Orthomyxoviridae; Influenzavirus A.
NCBI_TaxID=383550;
NCBI_TaxID=8782; Aves.
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
Webby R.J., Humberd J.L., Krauss S.L.;
"Genetic analysis of multiple N3, N4, and N6 influenza A virus
neuraminidase genes.";
Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=16439620; DOI=10.1126/science.1121586;
Obenauer J.C., Denson J., Mehta P.K., Su X., Mukatira S.,
Finkelstein D.B., Xu X., Wang J., Ma J., Fan Y., Rakestraw K.M.,
Webster R.G., Hoffmann E., Krauss S., Zheng J., Zhang Z., Naeve C.W.;
"Large-scale sequence analysis of avian influenza isolates.";
Science 311:1576-1580(2006).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-71.
PubMed=6927853; DOI=10.1016/0042-6822(82)90162-3;
Blok J., Air G.M.;
"Sequence variation at the 3' end of the neuraminidase gene from 39
influenza type A viruses.";
Virology 121:211-229(1982).
[4]
REVIEW.
PubMed=15567494; DOI=10.1016/j.virusres.2004.08.012;
Nayak D.P., Hui E.K., Barman S.;
"Assembly and budding of influenza virus.";
Virus Res. 106:147-165(2004).
[5]
REVIEW.
PubMed=16192481; DOI=10.1056/NEJMra050740;
Moscona A.;
"Neuraminidase inhibitors for influenza.";
N. Engl. J. Med. 353:1363-1373(2005).
[6]
REVIEW.
PubMed=15744059; DOI=10.1248/bpb.28.399;
Suzuki Y.;
"Sialobiology of influenza: molecular mechanism of host range
variation of influenza viruses.";
Biol. Pharm. Bull. 28:399-408(2005).
[7]
X-RAY CRYSTALLOGRAPHY (1.84 ANGSTROMS) OF 82-470 IN COMPLEX WITH
CALCIUM AND SUBSTRATE ANALOG, COFACTOR, SUBUNIT, DISULFIDE BONDS, AND
GLYCOSYLATION AT ASN-86; ASN-146 AND ASN-201.
Rudino-Pinera E., Crennell S.J., Webster R.G., Laver W.G.,
Garman E.F.;
"The crystal structure of influenza type A virus neuraminidase of the
N6 subtype at 1.85 A resolution.";
Submitted (APR-2004) to the PDB data bank.
[8]
X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 82-470 IN COMPLEX WITH
CALCIUM AND ZANAMIVIR, COFACTOR, SUBUNIT, DISULFIDE BONDS, AND
GLYCOSYLATION AT ASN-146.
Rudino-Pinera E., Tunnah P., Crennell S.J., Webster R.G., Laver W.G.,
Garman E.F.;
"The crystal structure of type A influenza virus neuraminidase of the
N6 subtype reveals the existence of two separate Neu5Ac binding
sites.";
Submitted (MAY-2006) to the PDB data bank.
-!- FUNCTION: 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. {ECO:0000255|HAMAP-
Rule:MF_04071}.
-!- CATALYTIC ACTIVITY: 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. {ECO:0000255|HAMAP-Rule:MF_04071}.
-!- COFACTOR:
Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000269|Ref.7,
ECO:0000269|Ref.8};
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
Evidence={ECO:0000255|HAMAP-Rule:MF_04071, ECO:0000269|Ref.7,
ECO:0000269|Ref.8};
-!- ENZYME REGULATION: 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. {ECO:0000255|HAMAP-
Rule:MF_04071}.
-!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_04071,
ECO:0000305|Ref.7, ECO:0000305|Ref.8}.
-!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-
Rule:MF_04071}. Host apical cell membrane {ECO:0000255|HAMAP-
Rule:MF_04071}; Single-pass type II membrane protein
{ECO:0000255|HAMAP-Rule:MF_04071}. 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.
{ECO:0000255|HAMAP-Rule:MF_04071}.
-!- DOMAIN: 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. {ECO:0000255|HAMAP-Rule:MF_04071}.
-!- PTM: N-glycosylated. {ECO:0000255|HAMAP-Rule:MF_04071,
ECO:0000269|Ref.7, ECO:0000269|Ref.8}.
-!- 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.
-!- SIMILARITY: Belongs to the glycosyl hydrolase 34 family.
{ECO:0000255|HAMAP-Rule:MF_04071}.
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EMBL; AY207549; AAO62063.1; -; Genomic_DNA.
EMBL; AB288846; BAF43436.1; -; Genomic_RNA.
EMBL; CY014681; ABI84548.1; -; Genomic_RNA.
EMBL; K01039; AAA43389.1; -; Genomic_RNA.
PDB; 1V0Z; X-ray; 1.84 A; A/B/C/D=82-470.
PDB; 1W1X; X-ray; 2.00 A; A/B/C/D=82-470.
PDB; 1W20; X-ray; 2.08 A; A/B/C/D=82-470.
PDB; 1W21; X-ray; 2.08 A; A/B/C/D=82-470.
PDB; 2CML; X-ray; 2.15 A; A/B/C/D=82-470.
PDBsum; 1V0Z; -.
PDBsum; 1W1X; -.
PDBsum; 1W20; -.
PDBsum; 1W21; -.
PDBsum; 2CML; -.
ProteinModelPortal; Q6XV27; -.
SMR; Q6XV27; -.
CAZy; GH34; Glycoside Hydrolase Family 34.
OrthoDB; VOG0900006X; -.
EvolutionaryTrace; Q6XV27; -.
PRO; PR:Q6XV27; -.
Proteomes; UP000155465; Genome.
GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
GO; GO:0052794; F:exo-alpha-(2->3)-sialidase activity; IEA:UniProtKB-EC.
GO; GO:0052795; F:exo-alpha-(2->6)-sialidase activity; IEA:UniProtKB-EC.
GO; GO:0052796; F:exo-alpha-(2->8)-sialidase activity; IEA:UniProtKB-EC.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
HAMAP; MF_04071; INFV_NRAM; 1.
InterPro; IPR001860; Glyco_hydro_34.
InterPro; IPR036278; Sialidase_sf.
Pfam; PF00064; Neur; 1.
SUPFAM; SSF50939; SSF50939; 1.
1: Evidence at protein level;
3D-structure; Calcium; Complete proteome; Disulfide bond;
Glycoprotein; Glycosidase; Host cell membrane; Host membrane;
Hydrolase; Membrane; Metal-binding; Signal-anchor; Transmembrane;
Transmembrane helix; Virion.
CHAIN 1 470 Neuraminidase.
/FTId=PRO_0000280127.
TOPO_DOM 1 6 Intravirion. {ECO:0000255|HAMAP-
Rule:MF_04071}.
TRANSMEM 7 27 Helical. {ECO:0000255|HAMAP-
Rule:MF_04071}.
TOPO_DOM 28 470 Virion surface. {ECO:0000255|HAMAP-
Rule:MF_04071}.
REGION 11 33 Involved in apical transport and lipid
raft association. {ECO:0000255|HAMAP-
Rule:MF_04071}.
REGION 36 88 Hypervariable stalk region.
{ECO:0000255|HAMAP-Rule:MF_04071}.
REGION 91 470 Head of neuraminidase.
{ECO:0000255|HAMAP-Rule:MF_04071}.
REGION 277 278 Substrate binding. {ECO:0000255|HAMAP-
Rule:MF_04071}.
ACT_SITE 151 151 Proton donor/acceptor.
{ECO:0000255|HAMAP-Rule:MF_04071}.
ACT_SITE 406 406 Nucleophile. {ECO:0000255|HAMAP-
Rule:MF_04071}.
METAL 294 294 Calcium; via carbonyl oxygen.
{ECO:0000255|HAMAP-Rule:MF_04071,
ECO:0000269|Ref.7, ECO:0000269|Ref.8}.
METAL 298 298 Calcium; via carbonyl oxygen.
{ECO:0000255|HAMAP-Rule:MF_04071,
ECO:0000269|Ref.7, ECO:0000269|Ref.8}.
METAL 325 325 Calcium. {ECO:0000255|HAMAP-
Rule:MF_04071, ECO:0000269|Ref.7,
ECO:0000269|Ref.8}.
METAL 348 348 Calcium; via carbonyl oxygen.
{ECO:0000269|Ref.7, ECO:0000269|Ref.8}.
BINDING 118 118 Substrate. {ECO:0000255|HAMAP-
Rule:MF_04071}.
BINDING 152 152 Substrate. {ECO:0000255|HAMAP-
Rule:MF_04071}.
BINDING 293 293 Substrate. {ECO:0000255|HAMAP-
Rule:MF_04071}.
BINDING 372 372 Substrate. {ECO:0000255|HAMAP-
Rule:MF_04071}.
CARBOHYD 51 51 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04071}.
CARBOHYD 54 54 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04071}.
CARBOHYD 62 62 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04071}.
CARBOHYD 67 67 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04071}.
CARBOHYD 70 70 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04071}.
CARBOHYD 86 86 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04071,
ECO:0000269|Ref.7}.
CARBOHYD 146 146 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04071,
ECO:0000269|Ref.7, ECO:0000269|Ref.8}.
CARBOHYD 201 201 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04071,
ECO:0000269|Ref.7}.
CARBOHYD 402 402 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04071}.
DISULFID 92 419 {ECO:0000255|HAMAP-Rule:MF_04071}.
DISULFID 124 129 {ECO:0000255|HAMAP-Rule:MF_04071}.
DISULFID 176 194
DISULFID 184 231 {ECO:0000255|HAMAP-Rule:MF_04071}.
DISULFID 233 238 {ECO:0000255|HAMAP-Rule:MF_04071}.
DISULFID 279 292 {ECO:0000255|HAMAP-Rule:MF_04071}.
DISULFID 281 290 {ECO:0000255|HAMAP-Rule:MF_04071}.
DISULFID 319 337 {ECO:0000255|HAMAP-Rule:MF_04071}.
DISULFID 423 449 {ECO:0000255|HAMAP-Rule:MF_04071}.
STRAND 95 102 {ECO:0000244|PDB:1V0Z}.
HELIX 105 109 {ECO:0000244|PDB:1V0Z}.
STRAND 115 125 {ECO:0000244|PDB:1V0Z}.
STRAND 128 142 {ECO:0000244|PDB:1V0Z}.
HELIX 143 145 {ECO:0000244|PDB:1V0Z}.
TURN 146 149 {ECO:0000244|PDB:1V0Z}.
STRAND 157 162 {ECO:0000244|PDB:1V0Z}.
STRAND 173 185 {ECO:0000244|PDB:1V0Z}.
STRAND 187 197 {ECO:0000244|PDB:1V0Z}.
HELIX 199 201 {ECO:0000244|PDB:1V0Z}.
STRAND 203 208 {ECO:0000244|PDB:1V0Z}.
STRAND 211 217 {ECO:0000244|PDB:1V0Z}.
STRAND 219 222 {ECO:0000244|PDB:1V0Z}.
STRAND 237 245 {ECO:0000244|PDB:1V0Z}.
STRAND 247 249 {ECO:0000244|PDB:1V0Z}.
STRAND 252 259 {ECO:0000244|PDB:1V0Z}.
STRAND 262 268 {ECO:0000244|PDB:1V0Z}.
STRAND 277 284 {ECO:0000244|PDB:1V0Z}.
STRAND 287 293 {ECO:0000244|PDB:1V0Z}.
STRAND 295 297 {ECO:0000244|PDB:1V0Z}.
STRAND 302 307 {ECO:0000244|PDB:1V0Z}.
TURN 308 311 {ECO:0000244|PDB:1V0Z}.
STRAND 312 317 {ECO:0000244|PDB:1V0Z}.
STRAND 320 322 {ECO:0000244|PDB:2CML}.
STRAND 325 327 {ECO:0000244|PDB:1V0Z}.
STRAND 337 339 {ECO:0000244|PDB:1V0Z}.
STRAND 362 365 {ECO:0000244|PDB:1V0Z}.
STRAND 367 379 {ECO:0000244|PDB:1V0Z}.
TURN 381 385 {ECO:0000244|PDB:1V0Z}.
STRAND 392 403 {ECO:0000244|PDB:1V0Z}.
STRAND 407 411 {ECO:0000244|PDB:1V0Z}.
STRAND 415 420 {ECO:0000244|PDB:1V0Z}.
STRAND 422 431 {ECO:0000244|PDB:1V0Z}.
TURN 432 434 {ECO:0000244|PDB:1V0Z}.
STRAND 441 453 {ECO:0000244|PDB:1V0Z}.
HELIX 466 469 {ECO:0000244|PDB:1V0Z}.
SEQUENCE 470 AA; 51470 MW; C3C30CB83D15E0E7 CRC64;
MNPNQKIICI SATGMTLSVV SLLVGIANLG LNIGLHYKVG DTPNVNIPNV NGTNSTTTII
NNNTQNNFTN ITNIIQSKGG ERTFLNLTKP LCEVNSWHIL SKDNAIRIGE DAHILVTREP
YLSCDPQGCR MFALSQGTTL RGRHANGTIH DRSPFRALIS WEMGQAPSPY NTRVECIGWS
STSCHDGMSR MSICMSGPNN NASAVVWYGG RPITEIPSWA GNILRTQESE CVCHKGVCPV
VMTDGPANNR AATKIIYFKE GKIQKIEELA GNAQHIEECS CYGAGGVIKC ICRDNWKGAN
RPVITIDPEM MTHTSKYLCS KVLTDTSRPN DPTNGNCDAP ITGGSPDPGV KGFAFLDGEN
SWLGRTISKD SRSGYEMLKV PNAETDIQSG PISNQVIVNN QNWSGYSGAF IDYWANKECF
NPCFYVELIR GRPKESSVLW TSNSIVALCG SKKRLGSWSW HDGAEIIYFE


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