ID C5MVT9_9INFA Unreviewed; 274 AA. AC C5MVT9; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 11-DEC-2019, entry version 44. DE RecName: Full=Neuraminidase {ECO:0000256|RuleBase:RU361252, ECO:0000256|SAAS:SAAS00397549}; DE EC=3.2.1.18 {ECO:0000256|RuleBase:RU361252, ECO:0000256|SAAS:SAAS00397416}; 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; Negarnaviricota; Polyploviricotina; Insthoviricetes; OC 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 ECO:0000256|SAAS:SAAS01126145}; CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; CC Evidence={ECO:0000256|RuleBase:RU361252, CC ECO:0000256|SAAS:SAAS00612833}; CC -!- ACTIVITY REGULATION: Inhibited by the neuraminidase inhibitors CC zanamivir (Relenza) and oseltamivir (Tamiflu). These drugs interfere CC with the release of progeny virus from infected cells and are effective CC against all influenza strains. Resistance to neuraminidase inhibitors CC is quite rare. {ECO:0000256|SAAS:SAAS01070481}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|RuleBase:RU361252, CC ECO:0000256|SAAS:SAAS00397177}. CC -!- SUBCELLULAR LOCATION: Host apical cell membrane CC {ECO:0000256|RuleBase:RU361252, ECO:0000256|SAAS:SAAS00582107}; Single- CC pass type II membrane protein {ECO:0000256|RuleBase:RU361252, CC ECO:0000256|SAAS:SAAS00582107}. Virion membrane 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, 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; 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:0016021; C:integral component of membrane; IEA:UniProtKB-UniRule. 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 InterPro; IPR001860; Glyco_hydro_34. 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, ECO:0000256|SAAS:SAAS00474703}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00474860}; KW Glycoprotein {ECO:0000256|RuleBase:RU361252}; KW Glycosidase {ECO:0000256|RuleBase:RU361252, ECO:0000256|SAAS:SAAS00474810}; KW Host cell membrane {ECO:0000256|RuleBase:RU361252, KW ECO:0000256|SAAS:SAAS00474912}; KW Host membrane {ECO:0000256|RuleBase:RU361252, KW ECO:0000256|SAAS:SAAS00475059}; KW Hydrolase {ECO:0000256|RuleBase:RU361252, ECO:0000256|SAAS:SAAS00475017}; KW Membrane {ECO:0000256|SAAS:SAAS00474571}; KW Metal-binding {ECO:0000256|RuleBase:RU361252, KW ECO:0000256|SAAS:SAAS00474602}; KW Transmembrane {ECO:0000256|SAAS:SAAS00474655}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00475130}; KW Virion {ECO:0000256|RuleBase:RU361252, ECO:0000256|SAAS:SAAS00475258}. 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 //