ID B1MR93_9INFA Unreviewed; 449 AA. AC B1MR93; DT 29-APR-2008, integrated into UniProtKB/TrEMBL. DT 29-APR-2008, sequence version 1. DT 16-DEC-2008, entry version 7. DE RecName: Full=Neuraminidase; DE EC=3.2.1.18; GN Name=NA; OS Influenza A virus (A/chicken/Yunnan/1083/2003(H5N1)). OC Viruses; ssRNA negative-strand viruses; Orthomyxoviridae; OC Influenzavirus A. OX NCBI_TaxID=496744; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=A/chicken/Yunnan/1083/2003; RX PubMed=18216109; DOI=10.1128/JVI.02468-07; RA Wang J., Vijaykrishna D., Duan L., Bahl J., Zhang J.X., Webster R.G., RA Peiris J.S., Chen H., Smith G.J., Guan Y.; RT "Identification of the progenitors of Indonesian and Vietnamese avian RT influenza A (H5N1) viruses from southern China."; RL J. Virol. 82:3405-3414(2008). 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 (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; CY029379; ACA48002.1; -; Viral_cRNA. 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: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 3: Inferred from homology; SQ SEQUENCE 449 AA; 48984 MW; 7D7EFE877FDE9CCD CRC64; MNPNQKIITI GSICMVTGIV SLMLQIGNMI SIWVSHSIHT GNQHQAEPIS NTNFLTEKAV ASVTLAGNSS LCPISGWAVH SKDNSIRIGS KGDVFVIREP FISCSHLECR TFFLTQGALL NDKHSNGTVK DRSPHRTLMS CPVGEAPSPY NSKFESVAWS ASACHDGTSW LTIGISGPDN GAVAVLKYNG IITDTIKSWR NNILRTQESE CACVNGSCFT VMTDGPSNGQ ASYKIFKMEK GKVVKSVELD APNYHYEECS CYPDAGEITC VCRDNWHGSN RPWVSFNQNL EYQIGYICSG VFGDNPRPND GTGSCGPVSS NGAYGVKGFS FKYGNGVWIG RTKSTNSRSG FEMIWDPNGW TETDSSFSVK QDIVAITDWS GYSGSFVQHP ELTGLDCIRP CFWVELIRGR PKESTIWTSG SSISFCGVNS DTVGWSWPDG AELPFTIDK //