ID Q9IP55_9INFA Unreviewed; 450 AA. AC Q9IP55; D1LN60; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 25-OCT-2017, entry version 89. 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:ACZ45122.1}; OS Influenza A virus (A/Hong Kong/485/1997(H5N1)). OC Viruses; ssRNA viruses; ssRNA negative-strand viruses; OC Orthomyxoviridae; Influenzavirus A. OX NCBI_TaxID=680692 {ECO:0000313|EMBL:AAF74324.1}; RN [1] {ECO:0000313|EMBL:AAF74324.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=A/Hong Kong/485/97 {ECO:0000313|EMBL:AAF74324.1}; RX 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). RN [2] {ECO:0000313|EMBL:ACZ45122.1, ECO:0000313|Proteomes:UP000120622} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=A/Hong Kong/485/1997 {ECO:0000313|EMBL:ACZ45122.1}; RA Kim L.M., Scott M.A., Suarez D.L., Spackman E., Swayne D.E., RA Afonso C.L.; RT "USDA Agriculture Research Service Avian Influenza Virus Sequencing RT Project."; RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases. 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 -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; CC Evidence={ECO:0000256|RuleBase:RU361252, CC ECO:0000256|SAAS:SAAS00612833}; CC -!- SUBUNIT: Homotetramer. {ECO:0000256|RuleBase:RU361252, CC ECO:0000256|SAAS:SAAS00114476}. CC -!- SUBCELLULAR LOCATION: Host apical cell membrane CC {ECO:0000256|SAAS:SAAS00582107}; Single-pass type II membrane CC protein {ECO:0000256|SAAS:SAAS00582107}. 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:SAAS00582269}. 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 EMBL; GU052144; ACZ45122.1; -; Viral_cRNA. DR ProteinModelPortal; Q9IP55; -. DR CAZy; GH34; Glycoside Hydrolase Family 34. DR Proteomes; UP000120622; Genome. 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-UniRule. 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 GO; GO:0046761; P:viral budding from plasma membrane; IEA:InterPro. DR CDD; cd15483; Influenza_NA; 1. DR InterPro; IPR001860; Glyco_hydro_34. DR InterPro; IPR033654; Sialidase_Influenza_A/B. DR InterPro; IPR036278; Sialidase_sf. 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:SAAS00114513}; KW Complete proteome {ECO:0000313|Proteomes:UP000120622}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00114594}; KW Glycoprotein {ECO:0000256|RuleBase:RU361252}; KW Glycosidase {ECO:0000256|RuleBase:RU361252, KW ECO:0000256|SAAS:SAAS00114535}; KW Host cell membrane {ECO:0000256|RuleBase:RU361252, KW ECO:0000256|SAAS:SAAS00114522}; 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:SAAS00114385}; 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 34 Helical. {ECO:0000256|SAM:Phobius}. 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 //