ID J9QFE5_9INFA Unreviewed; 469 AA. AC J9QFE5; DT 28-NOV-2012, integrated into UniProtKB/TrEMBL. DT 28-NOV-2012, sequence version 1. DT 31-JUL-2019, entry version 45. DE RecName: Full=Neuraminidase {ECO:0000256|HAMAP-Rule:MF_04071, ECO:0000256|RuleBase:RU361252, ECO:0000256|SAAS:SAAS00397549}; DE EC=3.2.1.18 {ECO:0000256|HAMAP-Rule:MF_04071, ECO:0000256|RuleBase:RU361252, ECO:0000256|SAAS:SAAS00397416}; 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; Negarnaviricota; Polyploviricotina; OC Insthoviricetes; Articulavirales; Orthomyxoviridae; OC 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., RA Pande S.A., 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 RT State, India."; RL Virol. J. 9:151-151(2012). 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. {ECO:0000256|HAMAP- CC Rule:MF_04071, ECO:0000256|SAAS:SAAS00844152}. 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 ECO:0000256|SAAS:SAAS01116071}; CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000256|HAMAP- CC Rule:MF_04071, ECO:0000256|RuleBase:RU361252, CC ECO:0000256|SAAS:SAAS00612833}; CC -!- ACTIVITY 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, ECO:0000256|SAAS:SAAS01070481}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_04071, CC ECO:0000256|RuleBase:RU361252, ECO:0000256|SAAS:SAAS00397177}. CC -!- SUBCELLULAR LOCATION: Host apical cell membrane CC {ECO:0000256|HAMAP-Rule:MF_04071, ECO:0000256|SAAS:SAAS00582107}; CC Single-pass type II membrane protein {ECO:0000256|HAMAP- CC Rule:MF_04071, ECO:0000256|SAAS:SAAS00582107}. Virion membrane CC {ECO:0000256|HAMAP-Rule:MF_04071}. Note=Preferentially accumulates CC at the apical plasma membrane in infected polarized epithelial CC cells, which is the virus assembly site. Uses lipid rafts for cell CC surface transport and apical sorting. In the virion, forms a CC mushroom-shaped spike on the surface of the membrane. CC {ECO:0000256|HAMAP-Rule:MF_04071}. 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 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 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; 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|HAMAP-Rule:MF_04071, KW ECO:0000256|RuleBase:RU361252, ECO:0000256|SAAS:SAAS00474703}; KW Disulfide bond {ECO:0000256|HAMAP-Rule:MF_04071, KW ECO:0000256|SAAS:SAAS00474860}; KW Glycoprotein {ECO:0000256|HAMAP-Rule:MF_04071, KW ECO:0000256|RuleBase:RU361252}; KW Glycosidase {ECO:0000256|HAMAP-Rule:MF_04071, KW ECO:0000256|RuleBase:RU361252, ECO:0000256|SAAS:SAAS00474810}; KW Host cell membrane {ECO:0000256|HAMAP-Rule:MF_04071, KW ECO:0000256|RuleBase:RU361252, ECO:0000256|SAAS:SAAS00474912}; KW Host membrane {ECO:0000256|HAMAP-Rule:MF_04071, KW ECO:0000256|RuleBase:RU361252, ECO:0000256|SAAS:SAAS00475059}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_04071, KW ECO:0000256|RuleBase:RU361252, ECO:0000256|SAAS:SAAS00475017}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_04071, KW ECO:0000256|SAAS:SAAS00474571}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_04071, KW ECO:0000256|RuleBase:RU361252, ECO:0000256|SAAS:SAAS00474602}; KW Signal-anchor {ECO:0000256|HAMAP-Rule:MF_04071}; KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_04071, KW ECO:0000256|SAAS:SAAS00474655}; KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_04071, KW ECO:0000256|SAAS:SAAS00475130}; KW Virion {ECO:0000256|HAMAP-Rule:MF_04071, KW ECO:0000256|RuleBase:RU361252, ECO:0000256|SAAS:SAAS00475258}. FT TRANSMEM 12 37 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 REGION 326 349 Disordered. {ECO:0000256|SAM:MobiDB- FT lite}. FT COMPBIAS 326 341 Polar. {ECO:0000256|SAM:MobiDB-lite}. 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; 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 //