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Neuraminidase (EC 3.2.1.18)

 NRAM_I33A0              Reviewed;         453 AA.
P03470; Q67215; Q67216; Q67217;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
20-DEC-2005, sequence version 2.
25-APR-2018, entry version 119.
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/Wilson-Smith/1933 H1N1) (Influenza A virus
(strain A/WS/1933 H1N1)).
Viruses; ssRNA viruses; ssRNA negative-strand viruses;
Orthomyxoviridae; Alphainfluenzavirus.
NCBI_TaxID=381518;
NCBI_TaxID=8782; Aves.
NCBI_TaxID=9606; Homo sapiens (Human).
NCBI_TaxID=9823; Sus scrofa (Pig).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=A/WSN/33;
PubMed=7077751;
Hiti A.L., Nayak D.P.;
"Complete nucleotide sequence of the neuraminidase gene of human
influenza virus A/WSN/33.";
J. Virol. 41:730-734(1982).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=A/NWS/33, A/WS/33, and A/WSN/33;
PubMed=8560787; DOI=10.1007/BF01701815;
Ward A.C.;
"Changes in the neuraminidase of neurovirulent influenza virus
strains.";
Virus Genes 10:253-260(1995).
[3]
SUBCELLULAR LOCATION.
PubMed=10864667; DOI=10.1128/JVI.74.14.6538-6545.2000;
Barman S., Nayak D.P.;
"Analysis of the transmembrane domain of influenza virus
neuraminidase, a type II transmembrane glycoprotein, for apical
sorting and raft association.";
J. Virol. 74:6538-6545(2000).
[4]
FUNCTION.
STRAIN=A/WSN/33;
PubMed=16140748; DOI=10.1128/JVI.79.18.11705-11715.2005;
Suzuki T., Takahashi T., Guo C.T., Hidari K.I., Miyamoto D., Goto H.,
Kawaoka Y., Suzuki Y.;
"Sialidase activity of influenza A virus in an endocytic pathway
enhances viral replication.";
J. Virol. 79:11705-11715(2005).
[5]
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).
[6]
REVIEW.
PubMed=16192481; DOI=10.1056/NEJMra050740;
Moscona A.;
"Neuraminidase inhibitors for influenza.";
N. Engl. J. Med. 353:1363-1373(2005).
[7]
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).
-!- FUNCTION: Unlike other strains, A/WSN/33 neuraminidase binds and
activates plasminogen into plasmin in the vicinity of HA so that
activated plasmin cleaves HA rendering the virus infectious.
{ECO:0000269|PubMed:16140748}.
-!- 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, ECO:0000269|PubMed:16140748}.
-!- 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:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
Evidence={ECO:0000255|HAMAP-Rule:MF_04071};
-!- 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}.
-!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-
Rule:MF_04071, ECO:0000269|PubMed:10864667}. Host apical cell
membrane {ECO:0000255|HAMAP-Rule:MF_04071,
ECO:0000269|PubMed:10864667}; Single-pass type II membrane protein
{ECO:0000255|HAMAP-Rule:MF_04071, ECO:0000269|PubMed:10864667}.
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}.
-!- 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; J02177; AAA43397.1; ALT_SEQ; Genomic_RNA.
EMBL; L25815; AAA91326.1; -; mRNA.
EMBL; L25816; AAA91327.1; -; mRNA.
EMBL; L25817; AAA91328.1; -; mRNA.
ProteinModelPortal; P03470; -.
SMR; P03470; -.
BindingDB; P03470; -.
ChEMBL; CHEMBL1287610; -.
CAZy; GH34; Glycoside Hydrolase Family 34.
OrthoDB; VOG0900006X; -.
PRO; PR:P03470; -.
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.
2: Evidence at transcript level;
Calcium; Disulfide bond; Glycoprotein; Glycosidase;
Host cell membrane; Host membrane; Hydrolase; Membrane; Metal-binding;
Signal-anchor; Transmembrane; Transmembrane helix; Virion.
CHAIN 1 453 Neuraminidase.
/FTId=PRO_0000078726.
TOPO_DOM 1 6 Intravirion. {ECO:0000255|HAMAP-
Rule:MF_04071}.
TRANSMEM 7 27 Helical. {ECO:0000255|HAMAP-
Rule:MF_04071}.
TOPO_DOM 28 453 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 74 Hypervariable stalk region.
{ECO:0000255|HAMAP-Rule:MF_04071}.
REGION 75 453 Head of neuraminidase.
{ECO:0000255|HAMAP-Rule:MF_04071}.
REGION 261 262 Substrate binding. {ECO:0000255|HAMAP-
Rule:MF_04071}.
ACT_SITE 135 135 Proton donor/acceptor.
{ECO:0000255|HAMAP-Rule:MF_04071}.
ACT_SITE 386 386 Nucleophile. {ECO:0000255|HAMAP-
Rule:MF_04071}.
METAL 278 278 Calcium; via carbonyl oxygen.
{ECO:0000255|HAMAP-Rule:MF_04071}.
METAL 282 282 Calcium; via carbonyl oxygen.
{ECO:0000255|HAMAP-Rule:MF_04071}.
METAL 308 308 Calcium. {ECO:0000255|HAMAP-
Rule:MF_04071}.
METAL 328 328 Calcium; via carbonyl oxygen.
{ECO:0000255|HAMAP-Rule:MF_04071}.
BINDING 102 102 Substrate. {ECO:0000255|HAMAP-
Rule:MF_04071}.
BINDING 136 136 Substrate. {ECO:0000255|HAMAP-
Rule:MF_04071}.
BINDING 277 277 Substrate. {ECO:0000255|HAMAP-
Rule:MF_04071}.
BINDING 352 352 Substrate. {ECO:0000255|HAMAP-
Rule:MF_04071}.
CARBOHYD 44 44 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04071}.
CARBOHYD 72 72 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04071}.
CARBOHYD 130 130 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04071}.
CARBOHYD 219 219 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04071}.
DISULFID 76 401 {ECO:0000255|HAMAP-Rule:MF_04071}.
DISULFID 108 113 {ECO:0000255|HAMAP-Rule:MF_04071}.
DISULFID 168 215 {ECO:0000255|HAMAP-Rule:MF_04071}.
DISULFID 217 222 {ECO:0000255|HAMAP-Rule:MF_04071}.
DISULFID 263 276 {ECO:0000255|HAMAP-Rule:MF_04071}.
DISULFID 265 274 {ECO:0000255|HAMAP-Rule:MF_04071}.
DISULFID 302 319 {ECO:0000255|HAMAP-Rule:MF_04071}.
DISULFID 405 430 {ECO:0000255|HAMAP-Rule:MF_04071}.
VARIANT 53 53 I -> S (in strain: A/WSN/33).
VARIANT 56 57 YN -> HK (in strain: A/NWS/33).
VARIANT 57 57 N -> K (in strain: A/WSN/33).
VARIANT 130 130 N -> R (in strain: A/WSN/33).
VARIANT 130 130 N -> Y (in strain: A/NWS/33).
VARIANT 133 133 V -> F (in strain: A/WSN/33).
VARIANT 133 133 V -> S (in strain: A/NWS/33).
VARIANT 184 184 N -> D (in strain: A/WSN/33).
VARIANT 206 206 K -> N (in strain: A/WSN/33).
VARIANT 232 232 N -> D (in strain: A/WSN/33 and A/NWS/
33).
VARIANT 297 297 Q -> K (in strain: A/WSN/33).
VARIANT 316 316 P -> T (in strain: A/WSN/33 and A/NWS/
33).
VARIANT 336 336 R -> K (in strain: A/WSN/33).
VARIANT 373 373 V -> M (in strain: A/WSN/33).
VARIANT 414 414 R -> L (in strain: A/WSN/33).
VARIANT 414 414 R -> Q (in strain: A/NWS/33).
VARIANT 418 419 ET -> DA (in strain: A/WSN/33).
VARIANT 434 434 S -> G (in strain: A/WSN/33).
CONFLICT 172 172 M -> V (in Ref. 1; AAA43397).
CONFLICT 380 382 MTD -> ITN (in Ref. 1; AAA43397).
SEQUENCE 453 AA; 49687 MW; 76E63E3A97D1EFEC CRC64;
MNPNQKIITI GSICMVVGII SLILQIGNII SIWISHSIQT GNQNHTGICN QGIITYNVVA
GQDSTSVILT GNSSLCPIRG WAIHSKDNGI RIGSKGDVFV IREPFISCSH LECRTFFLTQ
GALLNDKHSN GTVKDRSPYR ALMSCPVGEA PSPYNSRFES VAWSASACHD GMGWLTIGIS
GPDNGAVAVL KYNGIITETI KSWRKKILRT QESECTCVNG SCFTIMTDGP SNGLASYKIF
KIEKGKVTKS IELNAPNSHY EECSCYPDTG KVMCVCRDNW HGSNRPWVSF DQNLDYQIGY
ICSGVFGDNP RPKDGPGSCG PVSADGANGV KGFSYRYGNG VWIGRTKSDS SRHGFEMIWD
PNGWTETDSR FSVRQDVVAM TDRSGYSGSF VQHPELTGLD CMRPCFWVEL IRGRPEEETI
WTSGSIISFC GVNSDTVDWS WPDGAELPFT IDK


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