ID A0A0U2L0R6_9INFA Unreviewed; 470 AA. AC A0A0U2L0R6; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 13-APR-2016, entry version 2. 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}; RA Xu Y., Wan X.-F.; RT "Lack of Antigenic Diversity in Contemporary H7 Avian-Origin Influenza RT A Viruses from North America."; RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases. 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 (By similarity). CC {ECO:0000256|SAAS:SAAS00234776}. 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: Virion membrane CC {ECO:0000256|RuleBase:RU361252}. Host apical cell membrane CC {ECO:0000256|RuleBase:RU361252}; Single-pass type II membrane CC protein {ECO:0000256|RuleBase:RU361252}. CC -!- PTM: N-glycosylated. {ECO:0000256|RuleBase:RU361252}. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 34 family. CC {ECO:0000256|RuleBase:RU361252}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; KU290296; ALT66974.1; -; Viral_cRNA. 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 //