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Neuraminidase (EC 3.2.1.18)

 NRAM_I67A0              Reviewed;         469 AA.
P06820; Q6XUB0;
01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 2.
07-JUN-2017, entry version 127.
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/Tokyo/3/1967 H2N2).
Viruses; ssRNA viruses; ssRNA negative-strand viruses;
Orthomyxoviridae; Influenzavirus A.
NCBI_TaxID=380960;
NCBI_TaxID=8782; Aves.
NCBI_TaxID=9606; Homo sapiens (Human).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=6203216; DOI=10.1016/0042-6822(84)90135-1;
Lentz M.R., Air G.M., Laver W.G., Webster R.G.;
"Sequence of the neuraminidase gene of influenza virus A/Tokyo/3/67
and previously uncharacterized monoclonal variants.";
Virology 135:257-265(1984).
[2]
SEQUENCE REVISION TO 420.
Air G.M.;
Submitted (JUL-1996) to UniProtKB.
[3]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=15380362; DOI=10.1016/j.virol.2004.06.009;
Lindstrom S.E., Cox N.J., Klimov A.;
"Genetic analysis of human H2N2 and early H3N2 influenza viruses,
1957-1972: evidence for genetic divergence and multiple reassortment
events.";
Virology 328:101-119(2004).
[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 (2.20 ANGSTROMS) OF 82-469 IN COMPLEX WITH
CALCIUM, GLYCOSYLATION AT ASN-86; ASN-146 AND ASN-200, COFACTOR,
SUBUNIT, AND DISULFIDE BOND.
PubMed=1920428; DOI=10.1016/0022-2836(91)80068-6;
Varghese J.N., Colman P.M.;
"Three-dimensional structure of the neuraminidase of influenza virus
A/Tokyo/3/67 at 2.2-A resolution.";
J. Mol. Biol. 221:473-486(1991).
[8]
X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 82-469 IN COMPLEX WITH
SUBSTRATE ANALOG AND CALCIUM, GLYCOSYLATION AT ASN-86; ASN-146;
ASN-200 AND ASN-234, COFACTOR, SUBUNIT, AND DISULFIDE BOND.
PubMed=7844831; DOI=10.1006/jmbi.1994.0051;
White C.L., Janakiraman M.N., Laver W.G., Philippon C., Vasella A.,
Air G.M., Luo M.;
"A sialic acid-derived phosphonate analog inhibits different strains
of influenza virus neuraminidase with different efficiencies.";
J. Mol. Biol. 245:623-634(1995).
[9]
X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 82-469 IN COMPLEX WITH
2-DEOXY-2,3-DEHYDRO-N-ACETYL-NEURAMINIC ACID AND CALCIUM, DISULFIDE
BONDS, GLYCOSYLATION AT ASN-86; ASN-146; ASN-200 AND ASN-234, AND
COFACTOR.
PubMed=7880809; DOI=10.1021/bi00010a003;
Jedrzejas M.J., Singh S., Brouillette W.J., Laver W.G., Air G.M.,
Luo M.;
"Structures of aromatic inhibitors of influenza virus neuraminidase.";
Biochemistry 34:3144-3151(1995).
-!- 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|PubMed:1920428,
ECO:0000269|PubMed:7844831, ECO:0000269|PubMed:7880809};
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
Evidence={ECO:0000255|HAMAP-Rule:MF_04071,
ECO:0000269|PubMed:1920428, ECO:0000269|PubMed:7844831,
ECO:0000269|PubMed:7880809};
-!- 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:0000269|PubMed:1920428, ECO:0000269|PubMed:7844831,
ECO:0000269|PubMed:7880809}.
-!- 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|PubMed:1920428, ECO:0000269|PubMed:7844831,
ECO:0000269|PubMed:7880809}.
-!- 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; K01393; AAB05621.1; -; Genomic_RNA.
EMBL; AY209929; AAO46245.1; -; Genomic_RNA.
PDB; 1ING; X-ray; 2.40 A; A/B=82-469.
PDB; 1INH; X-ray; 2.40 A; A/B=82-469.
PDB; 1INW; X-ray; 2.40 A; A=82-469.
PDB; 1INX; X-ray; 2.40 A; A=82-469.
PDB; 1IVC; X-ray; 2.40 A; A/B=82-469.
PDB; 1IVD; X-ray; 1.90 A; A/B=82-469.
PDB; 1IVE; X-ray; 2.40 A; A/B=82-469.
PDB; 1IVF; X-ray; 2.40 A; A/B=82-469.
PDB; 1IVG; X-ray; 1.90 A; A/B=82-469.
PDB; 1NN2; X-ray; 2.20 A; A=82-469.
PDB; 2BAT; X-ray; 2.00 A; A=82-469.
PDBsum; 1ING; -.
PDBsum; 1INH; -.
PDBsum; 1INW; -.
PDBsum; 1INX; -.
PDBsum; 1IVC; -.
PDBsum; 1IVD; -.
PDBsum; 1IVE; -.
PDBsum; 1IVF; -.
PDBsum; 1IVG; -.
PDBsum; 1NN2; -.
PDBsum; 2BAT; -.
ProteinModelPortal; P06820; -.
SMR; P06820; -.
BindingDB; P06820; -.
DrugBank; DB02829; 4-(Acetylamino)-3-[(Aminoacetyl)Amino]Benzoic Acid.
DrugBank; DB04565; 4-(Acetylamino)-3-[(Hydroxyacetyl)Amino]Benzoic Acid.
DrugBank; DB02268; 4-(Acetylamino)-3-Amino Benzoic Acid.
DrugBank; DB08570; 4-(ACETYLAMINO)-3-HYDROXY-5-NITROBENZOIC ACID.
DrugBank; DB08571; 4-(ACETYLAMINO)-5-AMINO-3-HYDROXYBENZOIC ACID.
CAZy; GH34; Glycoside Hydrolase Family 34.
BRENDA; 3.2.1.18; 7479.
SABIO-RK; P06820; -.
EvolutionaryTrace; P06820; -.
PRO; PR:P06820; -.
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.
GO; GO:0046761; P:viral budding from plasma membrane; IEA:InterPro.
CDD; cd15483; Influenza_NA; 1.
HAMAP; MF_04071; INFV_NRAM; 1.
InterPro; IPR001860; Glyco_hydro_34.
InterPro; IPR033654; Sialidase_Influenza_A/B.
InterPro; IPR011040; Sialidases.
Pfam; PF00064; Neur; 1.
SUPFAM; SSF50939; SSF50939; 1.
1: Evidence at protein level;
3D-structure; Calcium; Disulfide bond; Glycoprotein; Glycosidase;
Host cell membrane; Host membrane; Hydrolase; Membrane; Metal-binding;
Signal-anchor; Transmembrane; Transmembrane helix; Virion.
CHAIN 1 469 Neuraminidase.
/FTId=PRO_0000078720.
TOPO_DOM 1 9 Intravirion. {ECO:0000255|HAMAP-
Rule:MF_04071}.
TRANSMEM 10 30 Helical. {ECO:0000255|HAMAP-
Rule:MF_04071}.
TOPO_DOM 31 469 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 91 469 Head of neuraminidase.
{ECO:0000255|HAMAP-Rule:MF_04071}.
REGION 276 277 Substrate binding. {ECO:0000255|HAMAP-
Rule:MF_04071}.
COMPBIAS 179 182 Poly-Ser.
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 293 293 Calcium; via carbonyl oxygen.
{ECO:0000255|HAMAP-Rule:MF_04071,
ECO:0000269|PubMed:1920428,
ECO:0000269|PubMed:7844831,
ECO:0000269|PubMed:7880809}.
METAL 297 297 Calcium; via carbonyl oxygen.
{ECO:0000255|HAMAP-Rule:MF_04071,
ECO:0000269|PubMed:1920428,
ECO:0000269|PubMed:7844831,
ECO:0000269|PubMed:7880809}.
METAL 324 324 Calcium. {ECO:0000255|HAMAP-
Rule:MF_04071,
ECO:0000269|PubMed:1920428,
ECO:0000269|PubMed:7844831,
ECO:0000269|PubMed:7880809}.
METAL 345 345 Calcium; via carbonyl oxygen.
{ECO:0000255|HAMAP-Rule:MF_04071,
ECO:0000269|PubMed:1920428,
ECO:0000269|PubMed:7844831,
ECO:0000269|PubMed:7880809}.
METAL 346 346 Calcium; via carbonyl oxygen.
{ECO:0000255|HAMAP-Rule:MF_04071,
ECO:0000269|PubMed:1920428,
ECO:0000269|PubMed:7844831,
ECO:0000269|PubMed:7880809}.
METAL 347 347 Calcium; via carbonyl oxygen.
{ECO:0000269|PubMed:1920428,
ECO:0000269|PubMed:7844831,
ECO:0000269|PubMed:7880809}.
BINDING 118 118 Substrate. {ECO:0000255|HAMAP-
Rule:MF_04071}.
BINDING 152 152 Substrate. {ECO:0000255|HAMAP-
Rule:MF_04071}.
BINDING 292 292 Substrate. {ECO:0000255|HAMAP-
Rule:MF_04071}.
BINDING 371 371 Substrate. {ECO:0000255|HAMAP-
Rule:MF_04071}.
CARBOHYD 61 61 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04071}.
CARBOHYD 69 69 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|PubMed:1920428,
ECO:0000269|PubMed:7844831,
ECO:0000269|PubMed:7880809}.
CARBOHYD 146 146 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000269|PubMed:1920428,
ECO:0000269|PubMed:7844831,
ECO:0000269|PubMed:7880809}.
CARBOHYD 200 200 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000269|PubMed:1920428,
ECO:0000269|PubMed:7844831,
ECO:0000269|PubMed:7880809}.
CARBOHYD 234 234 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04071,
ECO:0000269|PubMed:7844831,
ECO:0000269|PubMed:7880809}.
CARBOHYD 402 402 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04071}.
DISULFID 92 417 {ECO:0000255|HAMAP-Rule:MF_04071}.
DISULFID 124 129 {ECO:0000255|HAMAP-Rule:MF_04071}.
DISULFID 175 193
DISULFID 183 230 {ECO:0000255|HAMAP-Rule:MF_04071}.
DISULFID 232 237 {ECO:0000255|HAMAP-Rule:MF_04071}.
DISULFID 278 291 {ECO:0000255|HAMAP-Rule:MF_04071}.
DISULFID 280 289 {ECO:0000255|HAMAP-Rule:MF_04071}.
DISULFID 318 337 {ECO:0000255|HAMAP-Rule:MF_04071}.
DISULFID 421 447 {ECO:0000255|HAMAP-Rule:MF_04071}.
CONFLICT 41 41 E -> D (in Ref. 3; AAO46245).
STRAND 96 102 {ECO:0000244|PDB:1IVD}.
HELIX 105 108 {ECO:0000244|PDB:1IVD}.
TURN 109 111 {ECO:0000244|PDB:1IVD}.
STRAND 121 124 {ECO:0000244|PDB:1IVD}.
STRAND 129 132 {ECO:0000244|PDB:1IVD}.
STRAND 137 139 {ECO:0000244|PDB:1IVD}.
TURN 144 149 {ECO:0000244|PDB:1IVD}.
STRAND 157 162 {ECO:0000244|PDB:1IVG}.
STRAND 172 176 {ECO:0000244|PDB:1IVG}.
STRAND 178 184 {ECO:0000244|PDB:1IVD}.
STRAND 186 196 {ECO:0000244|PDB:1IVD}.
STRAND 198 207 {ECO:0000244|PDB:1IVD}.
STRAND 210 216 {ECO:0000244|PDB:1IVD}.
STRAND 218 221 {ECO:0000244|PDB:1IVD}.
STRAND 227 229 {ECO:0000244|PDB:1IVD}.
STRAND 231 233 {ECO:0000244|PDB:1IVD}.
STRAND 236 244 {ECO:0000244|PDB:1IVD}.
STRAND 246 248 {ECO:0000244|PDB:2BAT}.
STRAND 250 267 {ECO:0000244|PDB:1IVD}.
STRAND 276 281 {ECO:0000244|PDB:1IVD}.
STRAND 284 292 {ECO:0000244|PDB:1IVD}.
STRAND 294 296 {ECO:0000244|PDB:1IVD}.
STRAND 301 305 {ECO:0000244|PDB:1IVD}.
TURN 307 309 {ECO:0000244|PDB:1IVD}.
STRAND 312 316 {ECO:0000244|PDB:1IVG}.
STRAND 319 321 {ECO:0000244|PDB:1ING}.
STRAND 324 326 {ECO:0000244|PDB:1ING}.
STRAND 330 332 {ECO:0000244|PDB:1IVD}.
STRAND 337 339 {ECO:0000244|PDB:1IVD}.
STRAND 353 356 {ECO:0000244|PDB:1IVD}.
STRAND 359 366 {ECO:0000244|PDB:1IVD}.
STRAND 368 371 {ECO:0000244|PDB:1IVD}.
STRAND 374 381 {ECO:0000244|PDB:1IVD}.
TURN 382 384 {ECO:0000244|PDB:1IVD}.
STRAND 385 387 {ECO:0000244|PDB:1IVD}.
STRAND 390 393 {ECO:0000244|PDB:1IVD}.
STRAND 407 413 {ECO:0000244|PDB:1IVD}.
STRAND 415 429 {ECO:0000244|PDB:1IVD}.
TURN 430 432 {ECO:0000244|PDB:1IVD}.
STRAND 435 437 {ECO:0000244|PDB:1IVG}.
STRAND 439 451 {ECO:0000244|PDB:1IVD}.
TURN 464 466 {ECO:0000244|PDB:1IVD}.
SEQUENCE 469 AA; 52131 MW; DF9F74BFFA3FEBC9 CRC64;
MNPNQKIITI GSVSLTIATV CFLMQIAILV TTVTLHFKQH ECDSPASNQV MPCEPIIIER
NITEIVYLNN TTIEKEICPK VVEYRNWSKP QCQITGFAPF SKDNSIRLSA GGDIWVTREP
YVSCDPVKCY QFALGQGTTL DNKHSNDTVH DRIPHRTLLM NELGVPFHLG TRQVCIAWSS
SSCHDGKAWL HVCITGDDKN ATASFIYDGR LVDSIGSWSQ NILRTQESEC VCINGTCTVV
MTDGSASGRA DTRILFIEEG KIVHISPLAG SAQHVEECSC YPRYPGVRCI CRDNWKGSNR
PVVDINMEDY SIDSSYVCSG LVGDTPRNDD RSSNSNCRNP NNERGTQGVK GWAFDNGNDL
WMGRTISKDL RSGYETFKVI GGWSTPNSKS QINRQVIVDS DNRSGYSGIF SVEGKSCINR
CFYVELIRGR KQETRVWWTS NSIVVFCGTS GTYGTGSWPD GANINFMPI


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