ID Q9IP55_9INFA Unreviewed; 450 AA. AC Q9IP55; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-SEP-2007, entry version 29. DE Neuraminidase (EC 3.2.1.18). OS Influenza A virus (A/Hong Kong/485/97(H5N1)). OC Viruses; ssRNA negative-strand viruses; Orthomyxoviridae; OC Influenzavirus A. OX NCBI_TaxID=132612; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=A/Hong Kong/485/97; RX MEDLINE=20231940; PubMed=10769072; RA Hiromoto Y., Yamazaki Y., Fukushima T., Saito T., Lindstrom S.E., RA Omoe K., Nerome R., Lim W., Sugita S., Nerome K.; RT "Evolutionary characterization of the six internal genes of H5N1 human RT influenza A virus."; RL J. Gen. Virol. 81:1293-1303(2000). 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 residues in CC oligosaccharides, glycoproteins, glycolipids, colominic acid and CC 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; AF084274; AAF74324.1; -; Genomic_RNA. DR HSSP; P03472; 1F8E. DR GO; GO:0016021; C:integral to membrane; 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 3: Inferred from homology; KW Glycosidase; Hydrolase; Membrane; Transmembrane; Virion. SQ SEQUENCE 450 AA; 49535 MW; E9CA5A0D59E7C8F3 CRC64; MNPNQKIITI GSICMVVGII SLMLQIGNII SVWVSHIIQT WHPNQPEPCN QSINFYTEQA AASVTLAGNS SLCPISGWAI YSKDNSIRIG SKGDVFVIRE PFISCSHLEC RTFFLTQGAL LNDKHSNGTV KDRSPYRTLM SCPVGEAPSP YNSRFESVAW SASACHDGIS WLTIGISGPD NGAVAVLKYN GIITDTIKSW RNNILRTQES ECACVNGSCF TVMTDGPSNE QASYKIFKIE KGRVVKSVEL NAPNYHYEEC SCYPDAGEIT CVCRDNWHGS NRPWVSFNQN LEYQIGYICS GVFGDSPRPN DGTGSCGPVS LNGAYGVKGF SFKYGNGVWI GRTKSTSSRS GFEMIWDPNG WTETDSSFSL KQDIIAITDW SGYSGSFIQH PELTGLNCMR PCFWVELIRG RPKEKTIWTS GSSVSFCGVN SDTMGWSWPD GAELPFTIDK //