ID B1A803_9INFA Unreviewed; 468 AA. AC B1A803; DT 08-APR-2008, integrated into UniProtKB/TrEMBL. DT 08-APR-2008, sequence version 1. DT 10-MAY-2017, entry version 49. 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:ACA04654.1}; OS Influenza A virus (A/duck/Eastern China/488/2003(H10N3)). OC Viruses; ssRNA viruses; ssRNA negative-strand viruses; OC Orthomyxoviridae; Influenzavirus A. OX NCBI_TaxID=503313 {ECO:0000313|EMBL:ACA04654.1}; RN [1] {ECO:0000313|EMBL:ACA04654.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=A/duck/Eastern China/488/2003 {ECO:0000313|EMBL:ACA04654.1}; RA Qiu B.-F., Liu W.-J., Peng D.-X., Hu S.-L., Tang Y.-H., Liu X.-F.; RL Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ACA04654.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=A/duck/Eastern China/488/2003 {ECO:0000313|EMBL:ACA04654.1}; RX PubMed=18984006; DOI=10.1016/j.jviromet.2008.10.001; RA Qiu B.F., Liu W.J., Peng D.X., Hu S.L., Tang Y.H., Liu X.F.; RT "A reverse transcription-PCR for subtyping of the neuraminidase of RT avian influenza viruses."; RL J. Virol. Methods 155:193-198(2009). 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 -!- 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; EU429712; ACA04654.1; -; mRNA. DR CAZy; GH34; Glycoside Hydrolase Family 34. 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-KW. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-UniRule. DR InterPro; IPR001860; Glyco_hydro_34. DR InterPro; IPR011040; Sialidases. DR Pfam; PF00064; Neur; 1. DR SUPFAM; SSF50939; SSF50939; 1. PE 2: Evidence at transcript level; 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:SAAS00114565}; 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:SAAS00114362}. FT TRANSMEM 7 31 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 468 AA; 51631 MW; DA1216C047E89C94 CRC64; MNPNQKITTI GVVSTTLSTI ALLIGIGNLI FNTVIHEKIG DHQTVVYPTI TAPVVPNCSD TIITYNNTVV NNITTIITKA ETHFKSSLPL CPFRGFFPFH KDNAIRLGEN KNVIATREPY VSCDNDDCWS FALAQGALLG TKHSNGTIKD RTPYRSLIRF PIGTAPVLGN YKEICVAWSS SSCFDGKEWM HVCMTGNDND ASGQIMYAGK MTDSIKSWRK DILRTQESEC QCIDGTCVVA VTDGPAASSA DHRIYWIREG KVLKYENIPK TKIQHLEECS CYVDIDVYCI CRDNWKGSNR PWMRINNETI LETGYVCSKF HSDTPRPADP STVSCDSPSN VNGGPGVKGF GFKTGNDVWL GRTVSTSGRS GFEIIKVTEG WINSPNHAKS VTQTLVSNND WSGYSGSFIV ENNGCFQPCF YIELIRGRPN KNDDVSWTSN SIVTFCGLDN EPGSGNWPDG SNIGFMPK //