ID J9QFE5_9INFA Unreviewed; 469 AA. AC J9QFE5; DT 28-NOV-2012, integrated into UniProtKB/TrEMBL. DT 28-NOV-2012, sequence version 1. DT 12-APR-2017, entry version 27. 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:AFO82967.1}; OS Influenza A virus (A/chicken/India/WB-NIV1057169/2010(H9N2)). OC Viruses; ssRNA viruses; ssRNA negative-strand viruses; OC Orthomyxoviridae; Influenzavirus A. 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. CC {ECO:0000256|SAAS:SAAS00234081}. 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 -!- SUBUNIT: Homotetramer. {ECO:0000256|RuleBase:RU361252, CC ECO:0000256|SAAS:SAAS00114476}. 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; 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-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:SAAS00062903}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00063019}; KW Glycoprotein {ECO:0000256|RuleBase:RU361252}; KW Glycosidase {ECO:0000256|RuleBase:RU361252, KW ECO:0000256|SAAS:SAAS00062426}; KW Host cell membrane {ECO:0000256|RuleBase:RU361252, KW ECO:0000256|SAAS:SAAS00062854}; KW Host membrane {ECO:0000256|RuleBase:RU361252, KW ECO:0000256|SAAS:SAAS00062524}; 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:SAAS00062292}; 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:SAAS00063088}. FT TRANSMEM 12 37 Helical. {ECO:0000256|SAM:Phobius}. 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 //