ID C5MVT9_9INFA Unreviewed; 274 AA. AC C5MVT9; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 29-OCT-2014, entry version 22. DE SubName: Full=Neuraminidase {ECO:0000313|EMBL:ACS45192.1}; DE Flags: Fragment; GN Name=NA {ECO:0000313|EMBL:ACS45192.1}; OS Influenza A virus (A/Dublin/04/2009(H1N1)). OC Viruses; ssRNA negative-strand viruses; Orthomyxoviridae; OC Influenzavirus A. 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 -!- 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|SAAS:SAAS00062942}. CC -!- COFACTOR: Binds 1 calcium ion per subunit. CC {ECO:0000256|SAAS:SAAS00063080}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|SAAS:SAAS00063168}. CC -!- SUBCELLULAR LOCATION: Virion membrane CC {ECO:0000256|SAAS:SAAS00063102}. Host apical cell membrane CC {ECO:0000256|SAAS:SAAS00063102}; Single-pass type II membrane CC protein {ECO:0000256|SAAS:SAAS00063102}. 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 GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of 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:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR Gene3D; 2.120.10.10; -; 1. DR InterPro; IPR001860; Glyco_hydro_34. DR InterPro; IPR011040; Sialidases. DR Pfam; PF00064; Neur; 1. DR SUPFAM; SSF50939; SSF50939; 1. PE 4: Predicted; KW Calcium {ECO:0000256|SAAS:SAAS00062903}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00063019}; KW Glycosidase {ECO:0000256|SAAS:SAAS00062426}; KW Host cell membrane {ECO:0000256|SAAS:SAAS00062854}; KW Host membrane {ECO:0000256|SAAS:SAAS00062524}; KW Hydrolase {ECO:0000256|SAAS:SAAS00114491}; KW Membrane {ECO:0000256|SAAS:SAAS00114461}; KW Metal-binding {ECO:0000256|SAAS:SAAS00062292}; KW Transmembrane {ECO:0000256|SAAS:SAAS00114524}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00114517}; KW Virion {ECO:0000256|SAAS:SAAS00063088}. FT NON_TER 1 1 {ECO:0000313|EMBL:ACS45192.1}. FT NON_TER 274 274 {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 //