ID A0A0U2L0R6_9INFA Unreviewed; 470 AA. AC A0A0U2L0R6; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 25-OCT-2017, entry version 12. DE RecName: Full=Neuraminidase {ECO:0000256|RuleBase:RU361252, ECO:0000256|SAAS:SAAS00114532}; DE EC=3.2.1.18 {ECO:0000256|RuleBase:RU361252, ECO:0000256|SAAS:SAAS00114514}; 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 -!- 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:SAAS00114528}. CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; CC Evidence={ECO:0000256|RuleBase:RU361252, CC ECO:0000256|SAAS:SAAS00612833}; CC -!- SUBUNIT: Homotetramer. {ECO:0000256|RuleBase:RU361252, CC ECO:0000256|SAAS:SAAS00114476}. CC -!- SUBCELLULAR LOCATION: Host apical cell membrane CC {ECO:0000256|SAAS:SAAS00582107}; Single-pass type II membrane CC protein {ECO:0000256|SAAS:SAAS00582107}. 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:SAAS00582269}. 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 GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-UniRule. DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-UniRule. 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-KW. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-UniRule. DR InterPro; IPR001860; Glyco_hydro_34. DR InterPro; IPR036278; Sialidase_sf. 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:SAAS00114513}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00114594}; KW Glycoprotein {ECO:0000256|RuleBase:RU361252}; KW Glycosidase {ECO:0000256|RuleBase:RU361252, KW ECO:0000256|SAAS:SAAS00114535}; KW Host cell membrane {ECO:0000256|RuleBase:RU361252, KW ECO:0000256|SAAS:SAAS00114522}; KW Host membrane {ECO:0000256|RuleBase:RU361252, KW ECO:0000256|SAAS:SAAS00114565}; KW Hydrolase {ECO:0000256|RuleBase:RU361252, KW ECO:0000256|SAAS:SAAS00114491}; KW Membrane {ECO:0000256|SAAS:SAAS00114461, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|RuleBase:RU361252, KW ECO:0000256|SAAS:SAAS00114385}; KW Transmembrane {ECO:0000256|SAAS:SAAS00114524, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00114517, KW ECO:0000256|SAM:Phobius}; KW Virion {ECO:0000256|RuleBase:RU361252, ECO:0000256|SAAS:SAAS00114362}. 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 //