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Neuraminidase (EC 3.2.1.18)

 NRAM_I47A0              Reviewed;         469 AA.
Q8JSD9; Q9WMK7; Q9WMK8;
06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
01-OCT-2002, sequence version 1.
25-OCT-2017, entry version 78.
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/Fort Monmouth/1/1947 H1N1).
Viruses; ssRNA viruses; ssRNA negative-strand viruses;
Orthomyxoviridae; Influenzavirus A.
NCBI_TaxID=380282;
NCBI_TaxID=8782; Aves.
NCBI_TaxID=9606; Homo sapiens (Human).
NCBI_TaxID=9823; Sus scrofa (Pig).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=A/Fort Monmouth/1/1947-MA;
PubMed=10426210; DOI=10.1016/S0168-1702(99)00027-1;
Brown E.G., Bailly J.E.;
"Genetic analysis of mouse-adapted influenza A virus identifies roles
for the NA, PB1, and PB2 genes in virulence.";
Virus Res. 61:63-76(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=A/Fort Monmouth/1/1947-MA;
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).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=12136133; DOI=10.1073/pnas.162366899;
Kilbourne E.D., Smith C., Brett I., Pokorny B.A., Johansson B.,
Cox N.;
"The total influenza vaccine failure of 1947 revisited: major
intrasubtypic antigenic change can explain failure of vaccine in a
post-World War II epidemic.";
Proc. Natl. Acad. Sci. U.S.A. 99:10748-10752(2002).
[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).
-!- 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; AF494253; AAM76693.1; -; Genomic_RNA.
EMBL; Y14193; CAB40419.1; -; Genomic_RNA.
EMBL; Y14194; CAB40420.1; -; Genomic_RNA.
EMBL; AF250357; AAF77037.1; -; mRNA.
ProteinModelPortal; Q8JSD9; -.
SMR; Q8JSD9; -.
CAZy; GH34; Glycoside Hydrolase Family 34.
SABIO-RK; Q8JSD9; -.
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 1 469 Neuraminidase.
/FTId=PRO_0000280130.
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}.
METAL 298 298 Calcium; via carbonyl oxygen.
{ECO:0000255|HAMAP-Rule:MF_04071}.
METAL 324 324 Calcium. {ECO:0000255|HAMAP-
Rule:MF_04071}.
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 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 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}.
CARBOHYD 235 235 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04071}.
CARBOHYD 365 365 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 184 231 {ECO:0000255|HAMAP-Rule:MF_04071}.
DISULFID 233 238 {ECO:0000255|HAMAP-Rule:MF_04071}.
DISULFID 279 292 {ECO:0000255|HAMAP-Rule:MF_04071}.
DISULFID 281 290 {ECO:0000255|HAMAP-Rule:MF_04071}.
DISULFID 318 335 {ECO:0000255|HAMAP-Rule:MF_04071}.
DISULFID 421 446 {ECO:0000255|HAMAP-Rule:MF_04071}.
VARIANT 68 72 Missing (in strain: A/Fort Monmouth/1/
1947-MA).
VARIANT 130 130 K -> R (in strain: A/Fort Monmouth/1/
1947-MA).
VARIANT 339 339 N -> Y (in strain: A/Fort Monmouth/1/
1947-MA).
VARIANT 344 344 D -> N (in strain: A/Fort Monmouth/1/
1947-MA).
VARIANT 352 352 R -> K (in strain: A/Fort Monmouth/1/
1947-MA).
VARIANT 357 357 G -> V (in strain: A/Fort Monmouth/1/
1947-MA).
VARIANT 369 369 K -> Q (in strain: A/Fort Monmouth/1/
1947-MA).
VARIANT 382 383 DP -> ET (in strain: A/Fort Monmouth/1/
1947-MA).
VARIANT 388 389 LV -> FT (in strain: A/Fort Monmouth/1/
1947-MA).
VARIANT 393 393 I -> V (in strain: A/Fort Monmouth/1/
1947-MA).
VARIANT 396 396 M -> V (in strain: A/Fort Monmouth/1/
1947-MA).
VARIANT 460 460 D -> G (in strain: A/Fort Monmouth/1/
1947-MA).
VARIANT 465 466 LN -> FT (in strain: A/Fort Monmouth/1/
1947-MA).
CONFLICT 365 365 N -> I (in Ref. 1; CAB40420).
SEQUENCE 469 AA; 51499 MW; 74E0E3A8BB7F08BC CRC64;
MNPNQKIITI GSICMVVGII SLILQIGNIV SIWISHSIQT GNQNHTGTCD QSIITYKNST
WVNQTYVNIS NTNVVAGKDT TSVILAGNSS LCPIRGWAIY SKDNGVRIGS KGDVFVIREP
FISCSHLECK TFFLTQGALL NDKHSNGTVK DRSPYRALMS CPVGEAPSPY NSRFESVAWS
ASACHDGMGW LTIGISGPDD GAVAVLKYNG IITETIKSWR KEILRTQESE CVCVNGSCFT
IMTDGPSGGP ASYKIFKIEK GKVTKSIELD APNSHYEECS CYPDTSKVMC VCRDNWHGSN
RPWVSFDQNL DYQMGYICSG VFGDNPRPKD GKGSCGPVNV DGADGVKGFS YRYGNGGWIG
RTKSNSSRKG FEMIWDPNGW TDPDSNFLVK QDIVAMTDWS GYSGSFVQHP ELTGLDCMRP
CFWVELIRGR PKENTIWTSG SSISFCGVNS DTVDWSWPDD AELPLNIDK


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