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Neuraminidase (EC 3.2.1.18)

 NRAM_I34A1              Reviewed;         454 AA.
P03468; A4GXH6; Q20N35; Q84043; Q8JUU4;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
06-MAR-2007, sequence version 2.
07-JUN-2017, entry version 128.
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/Puerto Rico/8/1934 H1N1).
Viruses; ssRNA viruses; ssRNA negative-strand viruses;
Orthomyxoviridae; Influenzavirus A.
NCBI_TaxID=211044;
NCBI_TaxID=8782; Aves.
NCBI_TaxID=9606; Homo sapiens (Human).
NCBI_TaxID=9823; Sus scrofa (Pig).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=7010182; DOI=10.1038/290213a0;
Fields S., Winter G., Brownlee G.G.;
"Structure of the neuraminidase gene in human influenza virus
A/PR/8/34.";
Nature 290:213-217(1981).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=11779399; DOI=10.1098/rstb.2001.0979;
Schickli J.H., Flandorfer A., Nakaya T., Martinez-Sobrido L.,
Garcia-Sastre A., Palese P.;
"Plasmid-only rescue of influenza A virus vaccine candidates.";
Philos. Trans. R. Soc. Lond., B, Biol. Sci. 356:1965-1973(2001).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC RNA], AND REVERSE GENETICS.
PubMed=15163504; DOI=10.1016/j.virusres.2004.02.028;
de Wit E., Spronken M.I.J., Bestebroer T.M., Rimmelzwaan G.F.,
Osterhaus A.D.M.E., Fouchier R.A.M.;
"Efficient generation and growth of influenza virus A/PR/8/34 from
eight cDNA fragments.";
Virus Res. 103:155-161(2004).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
Ghedin E., Spiro D., Miller N., Zaborsky J., Feldblyum T., Subbu V.,
Shumway M., Sparenborg J., Groveman L., Halpin R., Sitz J., Koo H.,
Salzberg S.L., Webster R.G., Hoffmann E., Krauss S., Naeve C., Bao Y.,
Bolotov P., Dernovoy D., Kiryutin B., Lipman D.J., Tatusova T.;
"The NIAID influenza genome sequencing project.";
Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
[5]
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).
[6]
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).
[7]
REVIEW.
PubMed=16192481; DOI=10.1056/NEJMra050740;
Moscona A.;
"Neuraminidase inhibitors for influenza.";
N. Engl. J. Med. 353:1363-1373(2005).
[8]
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: 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:
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}. 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}.
-!- 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; J02146; AAA43412.1; -; Genomic_RNA.
EMBL; AF389120; AAM75160.1; -; Genomic_RNA.
EMBL; EF467823; ABO21711.1; -; Genomic_RNA.
EMBL; CY009446; ABD77678.1; -; Genomic_RNA.
EMBL; K01031; AAA43415.1; -; Genomic_RNA.
RefSeq; NP_040981.1; NC_002018.1.
ProteinModelPortal; P03468; -.
SMR; P03468; -.
IntAct; P03468; 20.
BindingDB; P03468; -.
ChEMBL; CHEMBL2051; -.
CAZy; GH34; Glycoside Hydrolase Family 34.
GeneID; 956530; -.
KEGG; vg:956530; -.
KO; K19392; -.
OrthoDB; VOG0900006X; -.
Reactome; R-HSA-168255; Influenza Life Cycle.
Reactome; R-HSA-168275; Entry of Influenza Virion into Host Cell via Endocytosis.
Reactome; R-HSA-168277; Influenza Virus Induced Apoptosis.
Reactome; R-HSA-168288; Fusion of the Influenza Virion to the Host Cell Endosome.
Reactome; R-HSA-168298; Release.
Reactome; R-HSA-168302; Budding.
Reactome; R-HSA-168303; Packaging of Eight RNA Segments.
Reactome; R-HSA-168316; Assembly of Viral Components at the Budding Site.
Reactome; R-HSA-168336; Uncoating of the Influenza Virion.
Reactome; R-HSA-168874; Transport of HA trimer, NA tetramer and M2 tetramer from the endoplasmic reticulum to the Golgi Apparatus.
Reactome; R-HSA-192823; Viral mRNA Translation.
SABIO-RK; P03468; -.
PRO; PR:P03468; -.
Proteomes; UP000009255; Genome.
Proteomes; UP000109386; Genome.
Proteomes; UP000116373; Genome.
Proteomes; UP000170967; Genome.
GO; GO:0030666; C:endocytic vesicle membrane; TAS:Reactome.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0031904; C:endosome lumen; TAS:Reactome.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
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:0004308; F:exo-alpha-sialidase activity; TAS:Reactome.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0016504; F:peptidase activator activity; TAS:Reactome.
GO; GO:0046732; P:active induction of host immune response by virus; TAS:Reactome.
GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
GO; GO:0019064; P:fusion of virus membrane with host plasma membrane; TAS:Reactome.
GO; GO:0019060; P:intracellular transport of viral protein in host cell; TAS:Reactome.
GO; GO:0019065; P:receptor-mediated endocytosis of virus by host cell; TAS:Reactome.
GO; GO:0019061; P:uncoating of virus; TAS:Reactome.
GO; GO:0046761; P:viral budding from plasma membrane; IDA:UniProtKB.
GO; GO:0019072; P:viral genome packaging; TAS:Reactome.
GO; GO:0019076; P:viral release from host cell; TAS:Reactome.
GO; GO:0019083; P:viral transcription; TAS:Reactome.
GO; GO:0019068; P:virion assembly; TAS:Reactome.
GO; GO:0019062; P:virion attachment to host cell; TAS:Reactome.
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.
3: Inferred from homology;
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 1 454 Neuraminidase.
/FTId=PRO_0000078712.
TOPO_DOM 1 6 Intravirion. {ECO:0000255|HAMAP-
Rule:MF_04071}.
TRANSMEM 7 27 Helical. {ECO:0000255|HAMAP-
Rule:MF_04071}.
TOPO_DOM 28 454 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 75 Hypervariable stalk region.
{ECO:0000255|HAMAP-Rule:MF_04071}.
REGION 76 454 Head of neuraminidase.
{ECO:0000255|HAMAP-Rule:MF_04071}.
REGION 262 263 Substrate binding. {ECO:0000255|HAMAP-
Rule:MF_04071}.
ACT_SITE 136 136 Proton donor/acceptor.
{ECO:0000255|HAMAP-Rule:MF_04071}.
ACT_SITE 387 387 Nucleophile. {ECO:0000255|HAMAP-
Rule:MF_04071}.
METAL 279 279 Calcium; via carbonyl oxygen.
{ECO:0000255|HAMAP-Rule:MF_04071}.
METAL 283 283 Calcium; via carbonyl oxygen.
{ECO:0000255|HAMAP-Rule:MF_04071}.
METAL 309 309 Calcium. {ECO:0000255|HAMAP-
Rule:MF_04071}.
METAL 329 329 Calcium; via carbonyl oxygen.
{ECO:0000255|HAMAP-Rule:MF_04071}.
BINDING 103 103 Substrate. {ECO:0000255|HAMAP-
Rule:MF_04071}.
BINDING 137 137 Substrate. {ECO:0000255|HAMAP-
Rule:MF_04071}.
BINDING 278 278 Substrate. {ECO:0000255|HAMAP-
Rule:MF_04071}.
BINDING 353 353 Substrate. {ECO:0000255|HAMAP-
Rule:MF_04071}.
CARBOHYD 44 44 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 73 73 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04071}.
CARBOHYD 131 131 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04071}.
CARBOHYD 220 220 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04071}.
DISULFID 77 402 {ECO:0000255|HAMAP-Rule:MF_04071}.
DISULFID 109 114 {ECO:0000255|HAMAP-Rule:MF_04071}.
DISULFID 169 216 {ECO:0000255|HAMAP-Rule:MF_04071}.
DISULFID 218 223 {ECO:0000255|HAMAP-Rule:MF_04071}.
DISULFID 264 277 {ECO:0000255|HAMAP-Rule:MF_04071}.
DISULFID 266 275 {ECO:0000255|HAMAP-Rule:MF_04071}.
DISULFID 303 320 {ECO:0000255|HAMAP-Rule:MF_04071}.
DISULFID 406 431 {ECO:0000255|HAMAP-Rule:MF_04071}.
CONFLICT 8 8 I -> T (in Ref. 2; AAM75160).
CONFLICT 51 51 Q -> H (in Ref. 5; AAA43415).
CONFLICT 128 128 K -> R (in Ref. 1; AAA43412).
CONFLICT 131 131 N -> S (in Ref. 3; ABO21711 and 4;
ABD77678).
CONFLICT 314 314 E -> K (in Ref. 1; AAA43412).
CONFLICT 403 403 M -> I (in Ref. 1; AAA43412).
CONFLICT 451 451 S -> T (in Ref. 1; AAA43412).
SEQUENCE 454 AA; 50121 MW; 7C52E0A9FD93A98B CRC64;
MNPNQKIITI GSICLVVGLI SLILQIGNII SIWISHSIQT GSQNHTGICN QNIITYKNST
WVKDTTSVIL TGNSSLCPIR GWAIYSKDNS IRIGSKGDVF VIREPFISCS HLECRTFFLT
QGALLNDKHS NGTVKDRSPY RALMSCPVGE APSPYNSRFE SVAWSASACH DGMGWLTIGI
SGPDNGAVAV LKYNGIITET IKSWRKKILR TQESECACVN GSCFTIMTDG PSDGLASYKI
FKIEKGKVTK SIELNAPNSH YEECSCYPDT GKVMCVCRDN WHGSNRPWVS FDQNLDYQIG
YICSGVFGDN PRPEDGTGSC GPVYVDGANG VKGFSYRYGN GVWIGRTKSH SSRHGFEMIW
DPNGWTETDS KFSVRQDVVA MTDWSGYSGS FVQHPELTGL DCMRPCFWVE LIRGRPKEKT
IWTSASSISF CGVNSDTVDW SWPDGAELPF SIDK


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