ID J9QFE5_9INFA Unreviewed; 469 AA. AC J9QFE5; DT 28-NOV-2012, integrated into UniProtKB/TrEMBL. DT 28-NOV-2012, sequence version 1. DT 02-DEC-2020, entry version 50. DE RecName: Full=Neuraminidase {ECO:0000256|HAMAP-Rule:MF_04071, ECO:0000256|RuleBase:RU361252}; DE EC=3.2.1.18 {ECO:0000256|HAMAP-Rule:MF_04071, ECO:0000256|RuleBase:RU361252}; GN Name=NA {ECO:0000256|HAMAP-Rule:MF_04071, GN ECO:0000256|RuleBase:RU361252, ECO:0000313|EMBL:AFO82967.1}; OS Influenza A virus (A/chicken/India/WB-NIV1057169/2010(H9N2)). OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina; OC Insthoviricetes; Articulavirales; Orthomyxoviridae; Alphainfluenzavirus. OX NCBI_TaxID=1210133 {ECO:0000313|EMBL:AFO82967.1}; RN [1] {ECO:0000313|EMBL:AFO82967.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=A/chicken/India/WB-NIV1057169/2010 RC {ECO:0000313|EMBL:AFO82967.1}; RX PubMed=22867041; RA Pawar S.D., Kale S.D., Rawankar A.S., Koratkar S.S., Raut C.G., Pande S.A., RA Mullick J., Mishra A.C.; RT "Avian influenza surveillance reveals presence of low pathogenic avian RT influenza viruses in poultry during 2009?2011 in the West Bengal State, RT India."; RL Virol. J. 9:151-151(2012). CC -!- FUNCTION: Catalyzes the removal of terminal sialic acid residues from CC viral and cellular glycoconjugates. Cleaves off the terminal sialic CC acids on the glycosylated HA during virus budding to facilitate virus CC release. Additionally helps virus spread through the circulation by CC further removing sialic acids from the cell surface. These cleavages CC prevent self-aggregation and ensure the efficient spread of the progeny CC virus from cell to cell. Otherwise, infection would be limited to one CC round of replication. Described as a receptor-destroying enzyme because CC it cleaves a terminal sialic acid from the cellular receptors. May CC facilitate viral invasion of the upper airways by cleaving the sialic CC acid moities on the mucin of the airway epithelial cells. Likely to CC plays a role in the budding process through its association with lipid CC rafts during intracellular transport. May additionally display a raft- CC association independent effect on budding. Plays a role in the CC determination of host range restriction on replication and virulence. CC Sialidase activity in late endosome/lysosome traffic seems to enhance CC virus replication. {ECO:0000256|HAMAP-Rule:MF_04071}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha- CC (2->8)- glycosidic linkages of terminal sialic acid residues in CC oligosaccharides, glycoproteins, glycolipids, colominic acid and CC synthetic substrates.; EC=3.2.1.18; Evidence={ECO:0000256|HAMAP- CC Rule:MF_04071, ECO:0000256|RuleBase:RU361252}; CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; CC Evidence={ECO:0000256|ARBA:ARBA00001913, CC ECO:0000256|HAMAP-Rule:MF_04071, ECO:0000256|RuleBase:RU361252}; CC -!- ACTIVITY REGULATION: Inhibited by the neuraminidase inhibitors CC zanamivir (Relenza) and oseltamivir (Tamiflu). These drugs interfere CC with the release of progeny virus from infected cells and are effective CC against all influenza strains. Resistance to neuraminidase inhibitors CC is quite rare. {ECO:0000256|HAMAP-Rule:MF_04071}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881, CC ECO:0000256|HAMAP-Rule:MF_04071, ECO:0000256|RuleBase:RU361252}. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004606}; Single- CC pass type II membrane protein {ECO:0000256|ARBA:ARBA00004606}. Virion CC membrane {ECO:0000256|HAMAP-Rule:MF_04071}. Host apical cell membrane CC {ECO:0000256|HAMAP-Rule:MF_04071}; Single-pass type II membrane protein CC {ECO:0000256|HAMAP-Rule:MF_04071}. Note=Preferentially accumulates at CC the apical plasma membrane in infected polarized epithelial cells, CC which is the virus assembly site. Uses lipid rafts for cell surface CC transport and apical sorting. In the virion, forms a mushroom-shaped CC spike on the surface of the membrane. {ECO:0000256|HAMAP- CC Rule:MF_04071}. CC -!- DOMAIN: Intact N-terminus is essential for virion morphogenesis. CC Possess two apical sorting signals, one in the ectodomain, which is CC likely to be a glycan, and the other in the transmembrane domain. The CC transmembrane domain also plays a role in lipid raft association. CC {ECO:0000256|HAMAP-Rule:MF_04071}. CC -!- PTM: N-glycosylated. {ECO:0000256|HAMAP-Rule:MF_04071, CC ECO:0000256|RuleBase:RU361252}. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 34 family. CC {ECO:0000256|HAMAP-Rule:MF_04071, ECO:0000256|RuleBase:RU361252}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC 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; JX310068; AFO82967.1; -; 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-SubCell. 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|ARBA:ARBA00022837, ECO:0000256|HAMAP-Rule:MF_04071, KW ECO:0000256|RuleBase:RU361252}; KW Disulfide bond {ECO:0000256|HAMAP-Rule:MF_04071}; KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180, ECO:0000256|HAMAP- KW Rule:MF_04071, ECO:0000256|RuleBase:RU361252}; KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|HAMAP- KW Rule:MF_04071, ECO:0000256|RuleBase:RU361252}; KW Host cell membrane {ECO:0000256|ARBA:ARBA00022511, ECO:0000256|HAMAP- KW Rule:MF_04071, ECO:0000256|RuleBase:RU361252}; KW Host membrane {ECO:0000256|ARBA:ARBA00022870, ECO:0000256|HAMAP- KW Rule:MF_04071, ECO:0000256|RuleBase:RU361252}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_04071, KW ECO:0000256|RuleBase:RU361252}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_04071}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_04071, ECO:0000256|RuleBase:RU361252}; KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968, ECO:0000256|HAMAP- KW Rule:MF_04071}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP- KW Rule:MF_04071}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP- KW Rule:MF_04071}; KW Virion {ECO:0000256|ARBA:ARBA00022844, ECO:0000256|HAMAP-Rule:MF_04071, KW ECO:0000256|RuleBase:RU361252}. FT TRANSMEM 12..37 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04071" FT REGION 11..33 FT /note="Involved in apical transport and lipid raft FT association" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04071" FT REGION 91..469 FT /note="Head of neuraminidase" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04071" FT REGION 276..277 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04071" FT REGION 326..349 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 326..341 FT /note="Polar" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 151 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04071" FT ACT_SITE 406 FT /note="Nucleophile" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04071" FT METAL 293 FT /note="Calcium; via carbonyl oxygen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04071" FT METAL 297 FT /note="Calcium; via carbonyl oxygen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04071" FT METAL 324 FT /note="Calcium" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04071" FT BINDING 118 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04071" FT BINDING 152 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04071" FT BINDING 292 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04071" FT BINDING 371 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04071" FT DISULFID 92..417 FT /evidence="ECO:0000256|HAMAP-Rule:MF_04071" FT DISULFID 124..129 FT /evidence="ECO:0000256|HAMAP-Rule:MF_04071" FT DISULFID 183..230 FT /evidence="ECO:0000256|HAMAP-Rule:MF_04071" FT DISULFID 232..237 FT /evidence="ECO:0000256|HAMAP-Rule:MF_04071" FT DISULFID 278..291 FT /evidence="ECO:0000256|HAMAP-Rule:MF_04071" FT DISULFID 280..289 FT /evidence="ECO:0000256|HAMAP-Rule:MF_04071" SQ SEQUENCE 469 AA; 51691 MW; 65FF63154E4F0739 CRC64; MSPNQKRIAL GSASLTIATI CLLIQIAILA TTMTLHFNQN DFTNSSKNQV VPCESIIIER NITEIVHLNG TITEKGSCPK AAEYKNWSKP QCQITGFVPF SKDNSIRLSA GGDIWVTREP YVSCGLRKCY QFALGQGTTL NNKHSNGTTH DRSPYRTLLM SELGVPFHLG TKQVCIAWSS SSCHDGRAWL HVCVTGDDRN ATASVIYDGM LTDSIRSWSG NILRTQESEC VCINGTCTVV MTDGSASGRA DTRILFIREG KIVHISPLSG SAQHVEECSC YPRYPEVRCV CRDNWKGSNR PVLYINVADY SIDSSYVCSG LVGDTPRNDD SSSSSNCRDP NNERGAPGVK GWAFDNGNDV WMGRTIKEDS RAGYETFRVV GGWTIANSKS QINRQVIVDS DNWSGYSGIF SVENKICINR CFYVELIRGR PQETIVWWTS NSIIVFCGTS GTYGTGSWPD GADINFMSI //