ID   A0A0U2L0R6_9INFA        Unreviewed;       470 AA.
AC   A0A0U2L0R6;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   11-MAY-2016, entry version 3.
DE   RecName: Full=Neuraminidase {ECO:0000256|RuleBase:RU361252, ECO:0000256|SAAS:SAAS00062759};
DE            EC=3.2.1.18 {ECO:0000256|RuleBase:RU361252, ECO:0000256|SAAS:SAAS00063188};
GN   Name=NA {ECO:0000256|RuleBase:RU361252, ECO:0000313|EMBL:ALT66974.1};
OS   Influenza A virus (A/northern shoveler/Utah/A00468715/2009(H7N6)).
OC   Viruses; ssRNA viruses; ssRNA negative-strand viruses;
OC   Orthomyxoviridae; Influenzavirus A.
OX   NCBI_TaxID=1769703 {ECO:0000313|EMBL:ALT66974.1};
RN   [1] {ECO:0000313|EMBL:ALT66974.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=A/northern shoveler/Utah/A00468715/2009
RC   {ECO:0000313|EMBL:ALT66974.1};
RX   PubMed=26858078; DOI=10.1038/srep20688;
RA   Xu Y., Bailey E., Spackman E., Li T., Wang H., Long L.P., Baroch J.A.,
RA   Cunningham F.L., Lin X., Jarman R.G., DeLiberto T.J., Wan X.F.;
RT   "Limited Antigenic Diversity in Contemporary H7 Avian-Origin Influenza
RT   A Viruses from North America.";
RL   Sci. Rep. 6:20688-20688(2016).
CC   -!- FUNCTION: Catalyzes the removal of terminal sialic acid residues
CC       from viral and cellular glycoconjugates. Cleaves off the terminal
CC       sialic acids on the glycosylated HA during virus budding to
CC       facilitate virus release. Additionally helps virus spread through
CC       the circulation by further removing sialic acids from the cell
CC       surface. These cleavages prevent self-aggregation and ensure the
CC       efficient spread of the progeny virus from cell to cell.
CC       Otherwise, infection would be limited to one round of replication.
CC       Described as a receptor-destroying enzyme because it cleaves a
CC       terminal sialic acid from the cellular receptors. May facilitate
CC       viral invasion of the upper airways by cleaving the sialic acid
CC       moities on the mucin of the airway epithelial cells. Likely to
CC       plays a role in the budding process through its association with
CC       lipid rafts during intracellular transport. May additionally
CC       display a raft-association independent effect on budding. Plays a
CC       role in the determination of host range restriction on replication
CC       and virulence. Sialidase activity in late endosome/lysosome
CC       traffic seems to enhance virus replication.
CC       {ECO:0000256|SAAS:SAAS00371510}.
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of alpha-(2->3)-, alpha-(2->6)-,
CC       alpha-(2->8)- glycosidic linkages of terminal sialic acid residues
CC       in oligosaccharides, glycoproteins, glycolipids, colominic acid
CC       and synthetic substrates. {ECO:0000256|RuleBase:RU361252,
CC       ECO:0000256|SAAS:SAAS00062942}.
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|RuleBase:RU361252};
CC       Note=Binds 1 Ca(2+) ion per subunit.
CC       {ECO:0000256|RuleBase:RU361252};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|RuleBase:RU361252,
CC       ECO:0000256|SAAS:SAAS00063168}.
CC   -!- SUBCELLULAR LOCATION: Host apical cell membrane
CC       {ECO:0000256|SAAS:SAAS00561320}; Single-pass type II membrane
CC       protein {ECO:0000256|SAAS:SAAS00561320}.
CC   -!- SUBCELLULAR LOCATION: Virion membrane
CC       {ECO:0000256|SAAS:SAAS00561294}.
CC   -!- PTM: N-glycosylated. {ECO:0000256|RuleBase:RU361252}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 34 family.
CC       {ECO:0000256|RuleBase:RU361252, ECO:0000256|SAAS:SAAS00561099}.
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DR   EMBL; KU290296; ALT66974.1; -; Viral_cRNA.
DR   GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0055036; C:virion membrane; IEA:InterPro.
DR   GO; GO:0052794; F:exo-alpha-(2->3)-sialidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0052795; F:exo-alpha-(2->6)-sialidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0052796; F:exo-alpha-(2->8)-sialidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 2.120.10.10; -; 1.
DR   InterPro; IPR001860; Glyco_hydro_34.
DR   InterPro; IPR011040; Sialidases.
DR   Pfam; PF00064; Neur; 1.
DR   SUPFAM; SSF50939; SSF50939; 1.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|RuleBase:RU361252,
KW   ECO:0000256|SAAS:SAAS00448743};
KW   Disulfide bond {ECO:0000256|SAAS:SAAS00449120};
KW   Glycoprotein {ECO:0000256|RuleBase:RU361252};
KW   Glycosidase {ECO:0000256|RuleBase:RU361252,
KW   ECO:0000256|SAAS:SAAS00448849};
KW   Host cell membrane {ECO:0000256|RuleBase:RU361252,
KW   ECO:0000256|SAAS:SAAS00448685};
KW   Host membrane {ECO:0000256|RuleBase:RU361252,
KW   ECO:0000256|SAAS:SAAS00449348};
KW   Hydrolase {ECO:0000256|RuleBase:RU361252,
KW   ECO:0000256|SAAS:SAAS00448424};
KW   Membrane {ECO:0000256|SAAS:SAAS00448618, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|RuleBase:RU361252,
KW   ECO:0000256|SAAS:SAAS00448775};
KW   Transmembrane {ECO:0000256|SAAS:SAAS00449168,
KW   ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAAS:SAAS00448371,
KW   ECO:0000256|SAM:Phobius};
KW   Virion {ECO:0000256|RuleBase:RU361252, ECO:0000256|SAAS:SAAS00448515}.
FT   TRANSMEM      7     31       Helical. {ECO:0000256|SAM:Phobius}.
SQ   SEQUENCE   470 AA;  51741 MW;  1204528C0CB23896 CRC64;
     MNPNQKIICI SATGMTLSVV SLLIGLANLG LNIGLHFKVG DTPETEPPST NETNSTTTII
     NYNTQNNFTN VTNIVLIKEE NKMFTNLSKP LCEVNSWHIL SKDNAIRIGE NAHILVTREP
     YLSCGPHECR MFALSQGTTL RGRHANGTIH DRSPFRALIS WEMGQAPSPY NVRVECVGWS
     STSCHDGISR MSICMSGPNN NASAVVWYNG RPVTEIASWA GNILRTQESE CVCHNGICPV
     VMTDGPANNR AETKIIYFKE GKIQKIEELT GSAQHIEECS CYGAEEVIKC ICRDNWKGAN
     RPVITINPTT MTHTSKYLCS KILTDTSRPN DPGSGNCDAP ITGGSPDPGV KGFAFLDGGN
     SWLGRTISKD SRSGYEMLKV PNAETDNQSG PVAHQVIVNN QNWSGYSGAF IDYWADRECF
     NPCFYVELIR GRPKESSVLW TSNSIVALCG SRERLGSWSW HDGAEIIYFK
//