ID A0A0N7APG9_9INFA Unreviewed; 465 AA. AC A0A0N7APG9; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 05-OCT-2016, entry version 9. 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:AJU15324.1}; OS Influenza A virus (A/chicken/Huai'an/041/2014(H7N9)). OC Viruses; ssRNA viruses; ssRNA negative-strand viruses; OC Orthomyxoviridae; Influenzavirus A. OX NCBI_TaxID=1621105 {ECO:0000313|EMBL:AJU15324.1}; RN [1] {ECO:0000313|EMBL:AJU15324.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=A/chicken/Huai'an/041/2014 {ECO:0000313|EMBL:AJU15324.1}; RA Yang P., Yan Q., Zhang M., Liu C., Shi Y., Yao H., He N.; RT "Genetic characterization of hemagglutinin and neuraminidase genes of RT avian influenza H7N9 virus isolated from both patients and live RT poultry market, Huai'an, China."; RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases. 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 -!- 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}. 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; KP864445; AJU15324.1; -; 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-KW. DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell. 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 GO; GO:0046761; P:viral budding from plasma membrane; IEA:InterPro. DR CDD; cd15483; Influenza_NA; 1. DR Gene3D; 2.120.10.10; -; 1. DR InterPro; IPR001860; Glyco_hydro_34. DR InterPro; IPR033654; Sialidase_Influenza_A/B. 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 465 AA; 51837 MW; C7F79B467E891604 CRC64; MNPNQKILCT SATAIIISAI AVLIGIANLG LNIGLHLKPG CNCSHSQPET TNTSQTIINN YYNETNITNI QMEERTSRNF NNLTKGLCTI NSWHIYGKDN AVRIGESSDV LVTREPYVSC DPDECRFYAL SQGTTIRGKH SNGTIHDRSQ YRALISWPLS SPPTVYNSRV ECIGWSSTSC HDGKSRMSIC ISGPNNNASA VVWYNRRPVA EINTWARNIL RTQESECVCH NGVCPVVFTD GSATGPADTR IYYFKEGKIL KWESLTGTAK HIEECSCYGE RTGITCTCRD NWQGSNRPVI QIDPVAMTHT SQYICSPVLT DTPRPNDPNI GKCNDPYPGN NNNGVKGFSY LDGANTWLGR TISTASRSGY EMLKVPNALT DDRSKPIQGQ TIVLNTDWSG YSGSFMDYWA EGDCYRACFY VELIRGRPKE DKVWWTSNSI VSMCSSTEFL GQWNWPDGAK IEYFL //