ID C5MVT9_9INFA Unreviewed; 274 AA. AC C5MVT9; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 13-SEP-2023, entry version 53. DE RecName: Full=Neuraminidase {ECO:0000256|RuleBase:RU361252}; DE EC=3.2.1.18 {ECO:0000256|RuleBase:RU361252}; DE Flags: Fragment; GN Name=NA {ECO:0000256|RuleBase:RU361252, ECO:0000313|EMBL:ACS45192.1}; OS Influenza A virus (A/Dublin/04/2009(H1N1)). OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina; OC Insthoviricetes; Articulavirales; Orthomyxoviridae; Alphainfluenzavirus. OX NCBI_TaxID=653735 {ECO:0000313|EMBL:ACS45192.1}; RN [1] {ECO:0000313|EMBL:ACS45192.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=A/Dublin/04/2009 {ECO:0000313|EMBL:ACS45192.1}; RA Carr M.J., Duffy M., Tuite G., Hall W.W.; RT "Human infection with novel swine-lineage H1N1 influenza virus in RT Ireland."; RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the removal of terminal sialic acid residues from CC viral and cellular glycoconjugates. {ECO:0000256|RuleBase:RU361252}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha- CC (2->8)- glycosidic linkages of terminal sialic acid residues in CC oligosaccharides, glycoproteins, glycolipids, colominic acid and CC synthetic substrates.; EC=3.2.1.18; CC Evidence={ECO:0000256|RuleBase:RU361252}; CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; CC Evidence={ECO:0000256|ARBA:ARBA00001913, CC ECO:0000256|RuleBase:RU361252}; CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881, CC ECO:0000256|RuleBase:RU361252}. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004606}; Single- CC pass type II membrane protein {ECO:0000256|ARBA:ARBA00004606}. Virion CC membrane {ECO:0000256|RuleBase:RU361252}. Host apical cell membrane CC {ECO:0000256|RuleBase:RU361252}; Single-pass type II membrane protein CC {ECO:0000256|RuleBase:RU361252}. CC -!- PTM: N-glycosylated. {ECO:0000256|RuleBase:RU361252}. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 34 family. CC {ECO:0000256|RuleBase:RU361252}. 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; GQ281078; ACS45192.1; -; Viral_cRNA. DR CAZy; GH34; Glycoside Hydrolase Family 34. DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell. 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 Gene3D; 2.120.10.10; -; 1. DR InterPro; IPR001860; Glyco_hydro_34. DR InterPro; IPR036278; Sialidase_sf. DR Pfam; PF00064; Neur; 1. DR SUPFAM; SSF50939; Sialidases; 1. PE 3: Inferred from homology; KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|RuleBase:RU361252}; KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180, KW ECO:0000256|RuleBase:RU361252}; KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361252}; KW Host cell membrane {ECO:0000256|ARBA:ARBA00022511, KW ECO:0000256|RuleBase:RU361252}; KW Host membrane {ECO:0000256|ARBA:ARBA00022870, KW ECO:0000256|RuleBase:RU361252}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361252}; KW Membrane {ECO:0000256|ARBA:ARBA00023136}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|RuleBase:RU361252}; KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}; KW Virion {ECO:0000256|ARBA:ARBA00022844, ECO:0000256|RuleBase:RU361252}. FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:ACS45192.1" FT NON_TER 274 FT /evidence="ECO:0000313|EMBL:ACS45192.1" SQ SEQUENCE 274 AA; 30229 MW; AA32410CFA84501C CRC64; NSIRIGSKGD VFVIREPFIS CSPLECRTFF LTQGALLNDK HSNGTIKDRS PYRTLMSCPI GEVPSPYNSR FESVAWSASA CHDGINWLTI GISGPDNGAV AVLKYNGIIT DTIKSWRNNI LRTQESECAC VNGSCFTVMT DGPSDGQASY KIFRIEKGKI VKSVEMNAPN YHYEECSCYP DSSEITCVCR DNWHGSNRPW VSFNQNLEYQ IGYICSGIFG DNPRPNDKTG SCGPVSSNGA NGVKGFSFKY GNGVWIGRTK SISSRNGFEM IWDP //