ID B1A803_9INFA Unreviewed; 468 AA. AC B1A803; DT 08-APR-2008, integrated into UniProtKB/TrEMBL. DT 08-APR-2008, sequence version 1. DT 23-SEP-2008, entry version 6. DE RecName: Full=Neuraminidase; DE EC=3.2.1.18; GN Name=NA; OS Influenza A virus (A/duck/Eastern China/488/2003(H10N3)). OC Viruses; ssRNA negative-strand viruses; Orthomyxoviridae; OC Influenzavirus A. OX NCBI_TaxID=503313; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=A/duck/Eastern China/488/2003; 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 neuraminidase-subtyping of avian RT influenza viruses."; RL Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases. 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 (By CC similarity). 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. CC -!- SUBUNIT: Homotetramer. CC -!- SUBUNIT: Homotetramer (By similarity). CC -!- SUBCELLULAR LOCATION: Virion membrane. Apical cell membrane; CC Single-pass type II membrane protein (By similarity). CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 34 family. 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 GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW. DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-KW. DR GO; GO:0004308; F:exo-alpha-sialidase activity; IEA:InterPro. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR InterPro; IPR001860; Glyco_hydro_34. DR Pfam; PF00064; Neur; 1. DR ProDom; PD000431; Glyco_hydro_34; 1. PE 2: Evidence at transcript level; KW Cell membrane; Glycosidase; Hydrolase; Membrane; Transmembrane; KW Virion. 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 //