ID A0A0G2QS48_9INFA Unreviewed; 469 AA. AC A0A0G2QS48; DT 16-SEP-2015, integrated into UniProtKB/TrEMBL. DT 16-SEP-2015, sequence version 1. DT 28-FEB-2018, entry version 21. DE RecName: Full=Neuraminidase {ECO:0000256|HAMAP-Rule:MF_04071, ECO:0000256|SAAS:SAAS00114532}; DE EC=3.2.1.18 {ECO:0000256|HAMAP-Rule:MF_04071, ECO:0000256|SAAS:SAAS00114514}; GN Name=NA {ECO:0000256|HAMAP-Rule:MF_04071, GN ECO:0000313|EMBL:AHA57022.1}; OS Influenza A virus (A/Chinese francolin/Guangxi/B7/2010(H9N2)). OC Viruses; ssRNA viruses; ssRNA negative-strand viruses; OC Orthomyxoviridae; Influenzavirus A. OX NCBI_TaxID=1413193 {ECO:0000313|EMBL:AHA57022.1, ECO:0000313|Proteomes:UP000110745}; RN [1] {ECO:0000313|EMBL:AHA57022.1, ECO:0000313|Proteomes:UP000110745} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=A/Chinese francolin/Guangxi/B7/2010 RC {ECO:0000313|EMBL:AHA57022.1}; RA Peng Y., Xie Z., Liu J., Pang Y., Xie Z., Xie L., Luo S., Fan Q.; RT "Genetic analysis of H9 subtype avian influenza viruses in Guangxi, RT Southern China during 2005 to 2010."; RL Submitted (OCT-2013) 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|HAMAP-Rule:MF_04071, CC ECO:0000256|SAAS:SAAS00114528}. CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000256|HAMAP- CC Rule:MF_04071, ECO:0000256|SAAS:SAAS00612833}; CC -!- ENZYME REGULATION: Inhibited by the neuraminidase inhibitors CC zanamivir (Relenza) and oseltamivir (Tamiflu). These drugs CC interfere with the release of progeny virus from infected cells CC and are effective against all influenza strains. Resistance to CC neuraminidase inhibitors is quite rare. {ECO:0000256|HAMAP- CC Rule:MF_04071}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_04071, 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 -!- DOMAIN: Intact N-terminus is essential for virion morphogenesis. CC Possess two apical sorting signals, one in the ectodomain, which CC is likely to be a glycan, and the other in the transmembrane CC domain. The transmembrane domain also plays a role in lipid raft CC association. {ECO:0000256|HAMAP-Rule:MF_04071}. CC -!- PTM: N-glycosylated. {ECO:0000256|HAMAP-Rule:MF_04071}. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 34 family. CC {ECO:0000256|HAMAP-Rule:MF_04071, ECO:0000256|SAAS:SAAS00582269}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|HAMAP-Rule:MF_04071}. 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; KF768204; AHA57022.1; -; Viral_cRNA. DR Proteomes; UP000110745; Genome. 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-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 CDD; cd15483; Influenza_NA; 1. DR HAMAP; MF_04071; INFV_NRAM; 1. DR InterPro; IPR001860; Glyco_hydro_34. DR InterPro; IPR033654; Sialidase_Influenza_A/B. DR InterPro; IPR036278; Sialidase_sf. DR Pfam; PF00064; Neur; 1. DR SUPFAM; SSF50939; SSF50939; 1. PE 3: Inferred from homology; KW Calcium {ECO:0000256|HAMAP-Rule:MF_04071, KW ECO:0000256|SAAS:SAAS00114513}; KW Complete proteome {ECO:0000313|Proteomes:UP000110745}; KW Disulfide bond {ECO:0000256|HAMAP-Rule:MF_04071, KW ECO:0000256|SAAS:SAAS00114594}; KW Glycoprotein {ECO:0000256|HAMAP-Rule:MF_04071}; KW Glycosidase {ECO:0000256|HAMAP-Rule:MF_04071, KW ECO:0000256|SAAS:SAAS00114535}; KW Host cell membrane {ECO:0000256|HAMAP-Rule:MF_04071, KW ECO:0000256|SAAS:SAAS00114522}; KW Host membrane {ECO:0000256|HAMAP-Rule:MF_04071, KW ECO:0000256|SAAS:SAAS00114565}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_04071, KW ECO:0000256|SAAS:SAAS00114491}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_04071, KW ECO:0000256|SAAS:SAAS00114461}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_04071, KW ECO:0000256|SAAS:SAAS00114385}; KW Signal-anchor {ECO:0000256|HAMAP-Rule:MF_04071}; KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_04071, KW ECO:0000256|SAAS:SAAS00114524}; KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_04071, KW ECO:0000256|SAAS:SAAS00114517}; KW Virion {ECO:0000256|HAMAP-Rule:MF_04071, KW ECO:0000256|SAAS:SAAS00114362}. FT TRANSMEM 7 30 Helical. {ECO:0000256|HAMAP-Rule: FT MF_04071}. FT REGION 11 33 Involved in apical transport and lipid FT raft association. {ECO:0000256|HAMAP- FT Rule:MF_04071}. FT REGION 91 469 Head of neuraminidase. FT {ECO:0000256|HAMAP-Rule:MF_04071}. FT REGION 276 277 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_04071}. FT ACT_SITE 151 151 Proton donor/acceptor. FT {ECO:0000256|HAMAP-Rule:MF_04071}. FT ACT_SITE 406 406 Nucleophile. {ECO:0000256|HAMAP-Rule: FT MF_04071}. FT METAL 293 293 Calcium; via carbonyl oxygen. FT {ECO:0000256|HAMAP-Rule:MF_04071}. FT METAL 297 297 Calcium; via carbonyl oxygen. FT {ECO:0000256|HAMAP-Rule:MF_04071}. FT METAL 324 324 Calcium. {ECO:0000256|HAMAP-Rule: FT MF_04071}. FT BINDING 118 118 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_04071}. FT BINDING 152 152 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_04071}. FT BINDING 292 292 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_04071}. FT BINDING 371 371 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_04071}. FT DISULFID 92 417 {ECO:0000256|HAMAP-Rule:MF_04071}. FT DISULFID 124 129 {ECO:0000256|HAMAP-Rule:MF_04071}. FT DISULFID 183 230 {ECO:0000256|HAMAP-Rule:MF_04071}. FT DISULFID 232 237 {ECO:0000256|HAMAP-Rule:MF_04071}. FT DISULFID 278 291 {ECO:0000256|HAMAP-Rule:MF_04071}. FT DISULFID 280 289 {ECO:0000256|HAMAP-Rule:MF_04071}. SQ SEQUENCE 469 AA; 51404 MW; 2CB026A3DAC928F0 CRC64; MNPNQKIVAI GSASLTIATM CLLLQIALFA TTMTLHFKQT GCTNSSDNQA VPCGPIIIER NTTEIVHLNS TTLEKETCPK SAGYRNWSKP QCQITGFAPF SKDNSIRLAA AGDIWVTREP YVSCGLGKCY QFALGQGTTL DNKHSNGTTH DRTPHRTLLM NELGVPFHLA TKQVCIAWSS SSCHDGKAWL HVCVTGDDKN ATASIIYDGI LVDSIASWSK NILRTQESEC VCINGTCTVV MTDGSASGRA DTRILFIREG KIVHISPLSG SAQHVEECSC YPRYPEVRCV CRDNWKGSNR PVLFINMADY SIDSSYVCSG LVGDTPRNDD RSSSSNCRDP NNERGAPGVK GWAFDSGNDI WMGRTIEKDS RSGYETFRVI GGWSTANSKS QINRQVIVDR DNSSGYSGIF SVEGKSCINR CFYVELIRGR PKENRVWWTS NSIIVFCGTS GTYGTGSWPD GANINLMPI //