ID A0A0B4UW68_9INFA Unreviewed; 470 AA.
AC A0A0B4UW68;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=Neuraminidase {ECO:0000256|HAMAP-Rule:MF_04071, ECO:0000256|RuleBase:RU361252};
DE EC=3.2.1.18 {ECO:0000256|HAMAP-Rule:MF_04071, ECO:0000256|RuleBase:RU361252};
GN Name=NA {ECO:0000256|HAMAP-Rule:MF_04071,
GN ECO:0000256|RuleBase:RU361252, ECO:0000313|EMBL:AJD13017.1};
OS Influenza A virus (A/duck/Jiangxi/5581/2013(mixed)).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Insthoviricetes; Articulavirales; Orthomyxoviridae; Alphainfluenzavirus;
OC Alphainfluenzavirus influenzae; Influenza A virus.
OX NCBI_TaxID=1587849 {ECO:0000313|EMBL:AJD13017.1, ECO:0000313|Proteomes:UP000174140};
RN [1] {ECO:0000313|EMBL:AJD13017.1, ECO:0000313|Proteomes:UP000174140}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A/duck/Jiangxi/5581/2013 {ECO:0000313|EMBL:AJD13017.1};
RX PubMed=25589662; DOI=10.1128/JVI.03167-14;
RA Ma C., Lam T.T.Y., Chai Y., Wang J., Fan X., Hong W., Zhang Y., Li L.,
RA Liu Y., Smith D.K., Webby R.J., Peiris J.S.M., Zhu H., Guan Y.;
RT "Emergence and evolution of h10 subtype influenza viruses in poultry in
RT china.";
RL J. Virol. 89:3534-3541(2015).
CC -!- FUNCTION: Catalyzes the removal of terminal sialic acid residues from
CC viral and cellular glycoconjugates. Cleaves off the terminal sialic
CC acids on the glycosylated HA during virus budding to facilitate virus
CC release. Additionally helps virus spread through the circulation by
CC further removing sialic acids from the cell surface. These cleavages
CC prevent self-aggregation and ensure the efficient spread of the progeny
CC virus from cell to cell. Otherwise, infection would be limited to one
CC round of replication. Described as a receptor-destroying enzyme because
CC it cleaves a terminal sialic acid from the cellular receptors. May
CC facilitate viral invasion of the upper airways by cleaving the sialic
CC acid moities on the mucin of the airway epithelial cells. Likely to
CC plays a role in the budding process through its association with lipid
CC rafts during intracellular transport. May additionally display a raft-
CC association independent effect on budding. Plays a role in the
CC determination of host range restriction on replication and virulence.
CC Sialidase activity in late endosome/lysosome traffic seems to enhance
CC virus replication. {ECO:0000256|HAMAP-Rule:MF_04071}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-
CC (2->8)- glycosidic linkages of terminal sialic acid residues in
CC oligosaccharides, glycoproteins, glycolipids, colominic acid and
CC synthetic substrates.; EC=3.2.1.18; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_04071, ECO:0000256|RuleBase:RU361252};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913,
CC ECO:0000256|HAMAP-Rule:MF_04071, ECO:0000256|RuleBase:RU361252};
CC -!- ACTIVITY REGULATION: Inhibited by the neuraminidase inhibitors
CC zanamivir (Relenza) and oseltamivir (Tamiflu). These drugs interfere
CC with the release of progeny virus from infected cells and are effective
CC against all influenza strains. Resistance to neuraminidase inhibitors
CC is quite rare. {ECO:0000256|HAMAP-Rule:MF_04071}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881,
CC ECO:0000256|HAMAP-Rule:MF_04071, ECO:0000256|RuleBase:RU361252}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-
CC pass type II membrane protein {ECO:0000256|ARBA:ARBA00004606}. Virion
CC membrane {ECO:0000256|HAMAP-Rule:MF_04071}. Host apical cell membrane
CC {ECO:0000256|HAMAP-Rule:MF_04071}; Single-pass type II membrane protein
CC {ECO:0000256|HAMAP-Rule:MF_04071}. Note=Preferentially accumulates at
CC the apical plasma membrane in infected polarized epithelial cells,
CC which is the virus assembly site. Uses lipid rafts for cell surface
CC transport and apical sorting. In the virion, forms a mushroom-shaped
CC spike on the surface of the membrane. {ECO:0000256|HAMAP-
CC Rule:MF_04071}.
CC -!- DOMAIN: Intact N-terminus is essential for virion morphogenesis.
CC Possess two apical sorting signals, one in the ectodomain, which is
CC likely to be a glycan, and the other in the transmembrane domain. The
CC transmembrane domain also plays a role in lipid raft association.
CC {ECO:0000256|HAMAP-Rule:MF_04071}.
CC -!- PTM: N-glycosylated. {ECO:0000256|HAMAP-Rule:MF_04071,
CC ECO:0000256|RuleBase:RU361252}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 34 family.
CC {ECO:0000256|HAMAP-Rule:MF_04071, ECO:0000256|RuleBase:RU361252}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_04071}.
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DR EMBL; KP287035; AJD13017.1; -; Viral_cRNA.
DR Proteomes; UP000174140; Genome.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0052794; F:exo-alpha-(2->3)-sialidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0052795; F:exo-alpha-(2->6)-sialidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0052796; F:exo-alpha-(2->8)-sialidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0046761; P:viral budding from plasma membrane; IEA:UniProtKB-UniRule.
DR Gene3D; 2.120.10.10; -; 1.
DR HAMAP; MF_04071; INFV_NRAM; 1.
DR InterPro; IPR001860; Glyco_hydro_34.
DR InterPro; IPR036278; Sialidase_sf.
DR Pfam; PF00064; Neur; 1.
DR SUPFAM; SSF50939; Sialidases; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|HAMAP-Rule:MF_04071};
KW Disulfide bond {ECO:0000256|HAMAP-Rule:MF_04071};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180, ECO:0000256|HAMAP-
KW Rule:MF_04071};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|HAMAP-
KW Rule:MF_04071};
KW Host cell membrane {ECO:0000256|ARBA:ARBA00022511, ECO:0000256|HAMAP-
KW Rule:MF_04071};
KW Host membrane {ECO:0000256|ARBA:ARBA00022870, ECO:0000256|HAMAP-
KW Rule:MF_04071};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_04071};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_04071};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_04071};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968, ECO:0000256|HAMAP-
KW Rule:MF_04071};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_04071};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_04071};
KW Virion {ECO:0000256|ARBA:ARBA00022844, ECO:0000256|HAMAP-Rule:MF_04071}.
FT TRANSMEM 12..35
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04071"
FT REGION 11..33
FT /note="Involved in apical transport and lipid raft
FT association"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04071"
FT REGION 91..470
FT /note="Head of neuraminidase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04071"
FT ACT_SITE 151
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04071"
FT ACT_SITE 406
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04071"
FT BINDING 118
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04071"
FT BINDING 152
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04071"
FT BINDING 277..278
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04071"
FT BINDING 293
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04071"
FT BINDING 294
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04071"
FT BINDING 298
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04071"
FT BINDING 325
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04071"
FT BINDING 372
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04071"
FT DISULFID 124..129
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04071"
FT DISULFID 184..231
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04071"
FT DISULFID 233..238
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04071"
FT DISULFID 279..292
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04071"
FT DISULFID 281..290
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04071"
SQ SEQUENCE 470 AA; 51809 MW; 308091134AC7BDA0 CRC64;
MNPNQKITCI SATGMTLSVV SLLIGVANLG LNIGLHYKVS DSSNINIPNM NETNPTTTII
NNNPQNNFTN ITNIIVNKDK EEMFLNLTKP LCEVNSWHIL SKDNAIRIGE DAHILVTREP
YLSCDPQGCK MFALSQGTTL RGRHANGTIH DRSPFRALIS WEMGQAPSPY NARVECIGWS
STSCHDGISR MSICISGPNN NASAVVWYGG RPVTEIPSWA GNILRTQESE CVCHKGICPV
VMTDGPANNR AATKIIYFKE GKIQKIEELK GNAQHIEECS CYGAAGMIKC ICRDNWRGAN
RPVITIDPEM MTHTSKYLCS KILTDTSRPS DPTSGNCDAP ITGGSPDPGV KGFAFLDGEN
SWLGRTISKD SRSGYEMLKV PNAETDTQSG PISYQMIVNN QNWSGYSGAF IDYWANKECF
NPVFYVELIR GRPKESSVLW TSNSIVALCG SRERLGSWSW HDGAEIIYFK
//
