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Neuraminidase (EC 3.2.1.18)

 NRAM_INBLE              Reviewed;         466 AA.
P03474;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
25-OCT-2017, entry version 129.
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 B virus (strain B/Lee/1940).
Viruses; ssRNA viruses; ssRNA negative-strand viruses;
Orthomyxoviridae; Influenzavirus B.
NCBI_TaxID=518987;
NCBI_TaxID=9606; Homo sapiens (Human).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=6294654; DOI=10.1073/pnas.79.22.6817;
Shaw M.W., Lamb R.A., Erickson B.W., Briedis D.J., Choppin P.W.;
"Complete nucleotide sequence of the neuraminidase gene of influenza B
virus.";
Proc. Natl. Acad. Sci. U.S.A. 79:6817-6821(1982).
[2]
MUTAGENESIS OF GLU-117; ASP-149; ARG-150; ARG-223; GLU-275; ARG-374
AND TYR-409.
PubMed=9874196; DOI=10.1046/j.1432-1327.1998.2580320.x;
Ghate A.A., Air G.M.;
"Site-directed mutagenesis of catalytic residues of influenza virus
neuraminidase as an aid to drug design.";
Eur. J. Biochem. 258:320-331(1998).
[3]
REVIEW.
PubMed=16192481; DOI=10.1056/NEJMra050740;
Moscona A.;
"Neuraminidase inhibitors for influenza.";
N. Engl. J. Med. 353:1363-1373(2005).
[4]
X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 77-466 IN COMPLEX WITH
SYNTHETIC INHIBITOR AND CALCIUM, SUBUNIT, COFACTOR, AND GLYCOSYLATION
AT ASN-284.
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).
[5]
X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 77-466 IN COMPLEX WITH
SYNTHETIC INHIBITOR AND CALCIUM, SUBUNIT, AND COFACTOR.
PubMed=10547289; DOI=10.1006/jmbi.1999.3180;
Finley J.B., Atigadda V.R., Duarte F., Zhao J.J., Brouillette W.J.,
Air G.M., Luo M.;
"Novel aromatic inhibitors of influenza virus neuraminidase make
selective interactions with conserved residues and water molecules in
the active site.";
J. Mol. Biol. 293:1107-1119(1999).
[6]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 78-466 IN COMPLEX WITH
SYNTHETIC INHIBITOR, SUBUNIT, AND COFACTOR.
PubMed=15159560; DOI=10.1107/S0907444904006225;
Lommer B.S., Ali S.M., Bajpai S.N., Brouillette W.J., Air G.M.,
Luo M.;
"A benzoic acid inhibitor induces a novel conformational change in the
active site of Influenza B virus neuraminidase.";
Acta Crystallogr. D 60:1017-1023(2004).
-!- 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:10547289,
ECO:0000269|PubMed:15159560, ECO:0000269|PubMed:7880809};
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
Evidence={ECO:0000255|HAMAP-Rule:MF_04071,
ECO:0000269|PubMed:10547289, ECO:0000269|PubMed:15159560,
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:10547289, ECO:0000269|PubMed:15159560,
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:7880809}.
-!- MISCELLANEOUS: The influenza B 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; J02095; AAA43749.1; -; Genomic_RNA.
PIR; A00886; NMIV4.
RefSeq; NP_056663.1; NC_002209.1.
PDB; 1B9S; X-ray; 2.50 A; A=77-466.
PDB; 1B9T; X-ray; 2.40 A; A=77-466.
PDB; 1B9V; X-ray; 2.35 A; A=77-466.
PDB; 1INF; X-ray; 2.40 A; A=77-466.
PDB; 1INV; X-ray; 2.40 A; A=77-466.
PDB; 1IVB; X-ray; 2.40 A; A=77-466.
PDB; 1VCJ; X-ray; 2.40 A; A=78-466.
PDBsum; 1B9S; -.
PDBsum; 1B9T; -.
PDBsum; 1B9V; -.
PDBsum; 1INF; -.
PDBsum; 1INV; -.
PDBsum; 1IVB; -.
PDBsum; 1VCJ; -.
ProteinModelPortal; P03474; -.
SMR; P03474; -.
BindingDB; P03474; -.
ChEMBL; CHEMBL3377; -.
DrugBank; DB03342; 4-(Acetylamino)-3-Guanidinobenzoic Acid.
DrugBank; DB08570; 4-(ACETYLAMINO)-3-HYDROXY-5-NITROBENZOIC ACID.
DrugBank; DB07762; 4-(N-ACETYLAMINO)-3-[N-(2-ETHYLBUTANOYLAMINO)]BENZOIC ACID.
CAZy; GH34; Glycoside Hydrolase Family 34.
GeneID; 26824004; -.
KEGG; vg:26824004; -.
OrthoDB; VOG0900006X; -.
SABIO-RK; P03474; -.
EvolutionaryTrace; P03474; -.
PRO; PR:P03474; -.
Proteomes; UP000008158; Genome.
Proteomes; UP000119685; 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; Reference proteome; Signal-anchor;
Transmembrane; Transmembrane helix; Virion.
CHAIN 1 466 Neuraminidase.
/FTId=PRO_0000078732.
TOPO_DOM 1 8 Intravirion. {ECO:0000255|HAMAP-
Rule:MF_04071}.
TRANSMEM 9 31 Helical. {ECO:0000255|HAMAP-
Rule:MF_04071}.
TOPO_DOM 32 466 Virion surface. {ECO:0000255|HAMAP-
Rule:MF_04071}.
REGION 13 35 Involved in apical transport and lipid
raft association. {ECO:0000255|HAMAP-
Rule:MF_04071}.
REGION 38 86 Hypervariable stalk region.
{ECO:0000255|HAMAP-Rule:MF_04071}.
REGION 89 466 Head of neuraminidase.
{ECO:0000255|HAMAP-Rule:MF_04071}.
REGION 275 276 Substrate binding. {ECO:0000255|HAMAP-
Rule:MF_04071}.
ACT_SITE 149 149 Proton donor/acceptor.
{ECO:0000255|HAMAP-Rule:MF_04071}.
ACT_SITE 409 409 Nucleophile. {ECO:0000255|HAMAP-
Rule:MF_04071}.
METAL 293 293 Calcium; via carbonyl oxygen.
{ECO:0000255|HAMAP-Rule:MF_04071,
ECO:0000269|PubMed:10547289,
ECO:0000269|PubMed:7880809}.
METAL 297 297 Calcium; via carbonyl oxygen.
{ECO:0000269|PubMed:10547289,
ECO:0000269|PubMed:7880809}.
METAL 324 324 Calcium. {ECO:0000255|HAMAP-
Rule:MF_04071,
ECO:0000269|PubMed:10547289,
ECO:0000269|PubMed:7880809}.
METAL 346 346 Calcium; via carbonyl oxygen.
{ECO:0000269|PubMed:10547289,
ECO:0000269|PubMed:7880809}.
BINDING 116 116 Substrate. {ECO:0000255|HAMAP-
Rule:MF_04071}.
BINDING 150 150 Substrate. {ECO:0000255|HAMAP-
Rule:MF_04071}.
BINDING 292 292 Substrate. {ECO:0000255|HAMAP-
Rule:MF_04071}.
BINDING 374 374 Substrate. {ECO:0000255|HAMAP-
Rule:MF_04071}.
CARBOHYD 56 56 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04071}.
CARBOHYD 64 64 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04071}.
CARBOHYD 144 144 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04071}.
CARBOHYD 284 284 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04071}.
DISULFID 87 420 {ECO:0000255|HAMAP-Rule:MF_04071}.
DISULFID 122 127 {ECO:0000255|HAMAP-Rule:MF_04071}.
DISULFID 182 229 {ECO:0000255|HAMAP-Rule:MF_04071}.
DISULFID 231 236 {ECO:0000255|HAMAP-Rule:MF_04071}.
DISULFID 277 291 {ECO:0000255|HAMAP-Rule:MF_04071}.
DISULFID 279 289 {ECO:0000255|HAMAP-Rule:MF_04071}.
DISULFID 318 337 {ECO:0000255|HAMAP-Rule:MF_04071}.
DISULFID 424 447 {ECO:0000255|HAMAP-Rule:MF_04071}.
MUTAGEN 117 117 E->G: Reduced substrate binding.
{ECO:0000269|PubMed:9874196}.
MUTAGEN 149 149 D->E: Almost complete loss of enzymatic
activity. {ECO:0000269|PubMed:9874196}.
MUTAGEN 150 150 R->K: Reduced substrate binding.
{ECO:0000269|PubMed:9874196}.
MUTAGEN 223 223 R->K: Reduced substrate binding.
{ECO:0000269|PubMed:9874196}.
MUTAGEN 275 275 E->D: Almost complete loss of enzymatic
activity. {ECO:0000269|PubMed:9874196}.
MUTAGEN 374 374 R->K: 80% loss of catalytic efficiency.
{ECO:0000269|PubMed:9874196}.
MUTAGEN 374 374 R->N: 94% loss of catalytic efficiency.
{ECO:0000269|PubMed:9874196}.
MUTAGEN 409 409 Y->F: Complete loss of enzymatic
activity. {ECO:0000269|PubMed:9874196}.
STRAND 88 90 {ECO:0000244|PDB:1INV}.
STRAND 92 98 {ECO:0000244|PDB:1B9V}.
HELIX 100 102 {ECO:0000244|PDB:1B9V}.
STRAND 106 108 {ECO:0000244|PDB:1B9T}.
STRAND 119 122 {ECO:0000244|PDB:1B9V}.
STRAND 127 133 {ECO:0000244|PDB:1B9V}.
STRAND 137 139 {ECO:0000244|PDB:1B9V}.
TURN 144 147 {ECO:0000244|PDB:1B9V}.
STRAND 155 160 {ECO:0000244|PDB:1B9V}.
TURN 167 169 {ECO:0000244|PDB:1B9V}.
STRAND 171 175 {ECO:0000244|PDB:1B9V}.
STRAND 177 183 {ECO:0000244|PDB:1B9V}.
STRAND 185 195 {ECO:0000244|PDB:1B9V}.
TURN 197 199 {ECO:0000244|PDB:1B9V}.
STRAND 201 206 {ECO:0000244|PDB:1B9V}.
STRAND 209 215 {ECO:0000244|PDB:1B9V}.
STRAND 217 220 {ECO:0000244|PDB:1B9V}.
STRAND 226 228 {ECO:0000244|PDB:1IVB}.
STRAND 230 232 {ECO:0000244|PDB:1B9V}.
STRAND 235 241 {ECO:0000244|PDB:1B9V}.
STRAND 245 247 {ECO:0000244|PDB:1B9T}.
STRAND 251 257 {ECO:0000244|PDB:1B9V}.
STRAND 260 265 {ECO:0000244|PDB:1B9V}.
STRAND 268 270 {ECO:0000244|PDB:1B9V}.
STRAND 275 292 {ECO:0000244|PDB:1B9V}.
STRAND 294 296 {ECO:0000244|PDB:1B9V}.
STRAND 301 306 {ECO:0000244|PDB:1B9V}.
TURN 307 310 {ECO:0000244|PDB:1B9V}.
STRAND 311 316 {ECO:0000244|PDB:1B9V}.
STRAND 324 326 {ECO:0000244|PDB:1B9V}.
STRAND 352 356 {ECO:0000244|PDB:1B9V}.
STRAND 361 367 {ECO:0000244|PDB:1B9V}.
STRAND 369 385 {ECO:0000244|PDB:1B9V}.
TURN 387 389 {ECO:0000244|PDB:1B9V}.
STRAND 395 406 {ECO:0000244|PDB:1B9V}.
STRAND 410 416 {ECO:0000244|PDB:1B9V}.
STRAND 418 432 {ECO:0000244|PDB:1B9V}.
STRAND 435 437 {ECO:0000244|PDB:1B9V}.
STRAND 439 448 {ECO:0000244|PDB:1B9V}.
STRAND 450 452 {ECO:0000244|PDB:1B9V}.
SEQUENCE 466 AA; 51442 MW; E6FF3E634F132263 CRC64;
MLPSTVQTLT LLLTSGGVLL SLYVSASLSY LLYSDVLLKF SSTKTTAPTM SLECTNASNA
QTVNHSATKE MTFPPPEPEW TYPRLSCQGS TFQKALLISP HRFGEIKGNS APLIIREPFV
ACGPKECRHF ALTHYAAQPG GYYNGTRKDR NKLRHLVSVK LGKIPTVENS IFHMAAWSGS
ACHDGREWTY IGVDGPDNDA LVKIKYGEAY TDTYHSYAHN ILRTQESACN CIGGDCYLMI
TDGSASGISK CRFLKIREGR IIKEILPTGR VEHTEECTCG FASNKTIECA CRDNSYTAKR
PFVKLNVETD TAEIRLMCTK TYLDTPRPDD GSIAGPCESN GDKWLGGIKG GFVHQRMASK
IGRWYSRTMS KTNRMGMELY VKYDGDPWTD SDALTLSGVM VSIEEPGWYS FGFEIKDKKC
DVPCIGIEMV HDGGKDTWHS AATAIYCLMG SGQLLWDTVT GVDMAL


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