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Neuraminidase (EC 3.2.1.18)

 NRAM_I18A0              Reviewed;         469 AA.
Q9IGQ6; O10421;
13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
25-OCT-2017, entry version 92.
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/Brevig Mission/1/1918 H1N1) (Influenza A
virus (strain A/South Carolina/1/1918 H1N1)).
Viruses; ssRNA viruses; ssRNA negative-strand viruses;
Orthomyxoviridae; Influenzavirus A.
NCBI_TaxID=88776;
NCBI_TaxID=8782; Aves.
NCBI_TaxID=9606; Homo sapiens (Human).
NCBI_TaxID=9823; Sus scrofa (Pig).
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=10823895; DOI=10.1073/pnas.100140097;
Reid A.H., Fanning T.G., Janczewski T.A., Taubenberger J.K.;
"Characterization of the 1918 'Spanish' influenza virus neuraminidase
gene.";
Proc. Natl. Acad. Sci. U.S.A. 97:6785-6790(2000).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 12-23.
STRAIN=A/South Carolina/1/18;
PubMed=9065404; DOI=10.1126/science.275.5307.1793;
Taubenberger J.K., Reid A.H., Krafft A.E., Bijwaard K.E.,
Fanning T.G.;
"Initial genetic characterization of the 1918 'Spanish' influenza
virus.";
Science 275:1793-1796(1997).
[3]
X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 83-467 IN COMPLEX WITH
CALCIUM AND INHIBITOR ZANAMIVIR, COFACTOR, SUBUNIT, GLYCOSYLATION AT
ASN-146, AND DISULFIDE BOND.
PubMed=18715929; DOI=10.1128/JVI.00959-08;
Xu X., Zhu X., Dwek R.A., Stevens J., Wilson I.A.;
"Structural characterization of the 1918 influenza virus H1N1
neuraminidase.";
J. Virol. 82:10493-10501(2008).
-!- 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:18715929};
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
Evidence={ECO:0000255|HAMAP-Rule:MF_04071,
ECO:0000269|PubMed:18715929};
-!- 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:18715929}.
-!- 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:18715929}.
-!- 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.
-!- MISCELLANEOUS: South Carolina isolate has been sequenced from
formalid fixed-lung tissues of a 21-year-old male which died in
1918 at Ft. Jackson, SC. Brevig Mission isolate has been sequenced
from lung tissues of an Inuit woman buried in the permafrost in a
gravesite near Brevig Mission, Alaska. This sample was recovered
by John Hultin, retired pathologist.
-!- SIMILARITY: Belongs to the glycosyl hydrolase 34 family.
{ECO:0000255|HAMAP-Rule:MF_04071}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; AF250356; AAF77036.1; -; mRNA.
EMBL; U94893; AAC57065.1; -; Genomic_DNA.
PDB; 3B7E; X-ray; 1.45 A; A/B=83-467.
PDB; 3BEQ; X-ray; 1.64 A; A/B=83-467.
PDB; 3CYE; X-ray; 1.65 A; A/B=83-469.
PDBsum; 3B7E; -.
PDBsum; 3BEQ; -.
PDBsum; 3CYE; -.
ProteinModelPortal; Q9IGQ6; -.
SMR; Q9IGQ6; -.
BindingDB; Q9IGQ6; -.
ChEMBL; CHEMBL1795169; -.
CAZy; GH34; Glycoside Hydrolase Family 34.
iPTMnet; Q9IGQ6; -.
PRIDE; Q9IGQ6; -.
OrthoDB; VOG0900006X; -.
BRENDA; 3.2.1.18; 7479.
SABIO-RK; Q9IGQ6; -.
EvolutionaryTrace; Q9IGQ6; -.
PRO; PR:Q9IGQ6; -.
Proteomes; UP000008430; 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.
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; 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 1 469 Neuraminidase.
/FTId=PRO_0000310569.
TOPO_DOM 1 6 Intravirion. {ECO:0000255|HAMAP-
Rule:MF_04071}.
TRANSMEM 7 27 Helical. {ECO:0000255|HAMAP-
Rule:MF_04071}.
TOPO_DOM 28 469 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 90 Hypervariable stalk region.
{ECO:0000255|HAMAP-Rule:MF_04071}.
REGION 91 469 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 402 402 Nucleophile. {ECO:0000255|HAMAP-
Rule:MF_04071}.
METAL 294 294 Calcium; via carbonyl oxygen.
{ECO:0000255|HAMAP-Rule:MF_04071,
ECO:0000269|PubMed:18715929}.
METAL 298 298 Calcium; via carbonyl oxygen.
{ECO:0000255|HAMAP-Rule:MF_04071,
ECO:0000269|PubMed:18715929}.
METAL 324 324 Calcium. {ECO:0000255|HAMAP-
Rule:MF_04071,
ECO:0000269|PubMed:18715929}.
METAL 344 344 Calcium; via carbonyl oxygen.
{ECO:0000255|HAMAP-Rule:MF_04071,
ECO:0000269|PubMed:18715929}.
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 368 368 Substrate. {ECO:0000255|HAMAP-
Rule:MF_04071}.
CARBOHYD 50 50 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04071}.
CARBOHYD 58 58 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04071}.
CARBOHYD 63 63 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04071}.
CARBOHYD 68 68 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04071}.
CARBOHYD 88 88 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04071}.
CARBOHYD 146 146 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04071,
ECO:0000269|PubMed:18715929}.
CARBOHYD 235 235 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04071}.
DISULFID 92 417 {ECO:0000255|HAMAP-Rule:MF_04071,
ECO:0000269|PubMed:18715929}.
DISULFID 124 129 {ECO:0000255|HAMAP-Rule:MF_04071,
ECO:0000269|PubMed:18715929}.
DISULFID 184 231 {ECO:0000255|HAMAP-Rule:MF_04071,
ECO:0000269|PubMed:18715929}.
DISULFID 233 238 {ECO:0000255|HAMAP-Rule:MF_04071,
ECO:0000269|PubMed:18715929}.
DISULFID 279 292 {ECO:0000255|HAMAP-Rule:MF_04071,
ECO:0000269|PubMed:18715929}.
DISULFID 281 290 {ECO:0000255|HAMAP-Rule:MF_04071,
ECO:0000269|PubMed:18715929}.
DISULFID 318 335 {ECO:0000255|HAMAP-Rule:MF_04071,
ECO:0000269|PubMed:18715929}.
DISULFID 421 446 {ECO:0000255|HAMAP-Rule:MF_04071,
ECO:0000269|PubMed:18715929}.
STRAND 95 102 {ECO:0000244|PDB:3B7E}.
HELIX 105 109 {ECO:0000244|PDB:3B7E}.
STRAND 115 124 {ECO:0000244|PDB:3B7E}.
STRAND 129 142 {ECO:0000244|PDB:3B7E}.
HELIX 143 145 {ECO:0000244|PDB:3B7E}.
TURN 146 149 {ECO:0000244|PDB:3B7E}.
STRAND 157 162 {ECO:0000244|PDB:3B7E}.
TURN 169 171 {ECO:0000244|PDB:3B7E}.
STRAND 173 177 {ECO:0000244|PDB:3B7E}.
STRAND 179 185 {ECO:0000244|PDB:3B7E}.
STRAND 190 197 {ECO:0000244|PDB:3B7E}.
STRAND 203 208 {ECO:0000244|PDB:3B7E}.
STRAND 211 217 {ECO:0000244|PDB:3B7E}.
STRAND 219 222 {ECO:0000244|PDB:3B7E}.
STRAND 228 230 {ECO:0000244|PDB:3B7E}.
STRAND 232 234 {ECO:0000244|PDB:3B7E}.
STRAND 237 245 {ECO:0000244|PDB:3B7E}.
STRAND 247 249 {ECO:0000244|PDB:3B7E}.
STRAND 252 259 {ECO:0000244|PDB:3B7E}.
STRAND 262 268 {ECO:0000244|PDB:3B7E}.
STRAND 277 284 {ECO:0000244|PDB:3B7E}.
STRAND 287 293 {ECO:0000244|PDB:3B7E}.
STRAND 302 306 {ECO:0000244|PDB:3B7E}.
STRAND 312 316 {ECO:0000244|PDB:3B7E}.
STRAND 324 326 {ECO:0000244|PDB:3B7E}.
STRAND 350 353 {ECO:0000244|PDB:3B7E}.
STRAND 356 361 {ECO:0000244|PDB:3B7E}.
STRAND 365 376 {ECO:0000244|PDB:3B7E}.
TURN 377 381 {ECO:0000244|PDB:3B7E}.
STRAND 388 399 {ECO:0000244|PDB:3B7E}.
STRAND 403 408 {ECO:0000244|PDB:3B7E}.
HELIX 410 413 {ECO:0000244|PDB:3B7E}.
STRAND 416 429 {ECO:0000244|PDB:3B7E}.
TURN 430 432 {ECO:0000244|PDB:3B7E}.
STRAND 433 436 {ECO:0000244|PDB:3B7E}.
STRAND 438 450 {ECO:0000244|PDB:3B7E}.
SEQUENCE 469 AA; 51406 MW; 28888692D4394159 CRC64;
MNPNQKIITI GSICMVVGII SLILQIGNII SIWVSHSIQT GNQNHPETCN QSIITYENNT
WVNQTYVNIS NTNVVAGQDA TSVILTGNSS LCPISGWAIY SKDNGIRIGS KGDVFVIREP
FISCSHLECR TFFLTQGALL NDKHSNGTVK DRSPYRTLMS CPVGEAPSPY NSRFESVAWS
ASACHDGMGW LTIGISGPDN GAVAVLKYNG IITDTIKSWR NNILRTQESE CACVNGSCFT
IMTDGPSNGQ ASYKILKIEK GKVTKSIELN APNYHYEECS CYPDTGKVMC VCRDNWHGSN
RPWVSFDQNL DYQIGYICSG VFGDNPRPND GTGSCGPVSS NGANGIKGFS FRYDNGVWIG
RTKSTSSRSG FEMIWDPNGW TETDSSFSVR QDIVAITDWS GYSGSFVQHP ELTGLDCMRP
CFWVELIRGQ PKENTIWTSG SSISFCGVNS DTVGWSWPDG AELPFSIDK


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