ID D7S0N3_9INFA Unreviewed; 469 AA. AC D7S0N3; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 29-OCT-2014, entry version 15. DE RecName: Full=Neuraminidase {ECO:0000256|SAAS:SAAS00062759}; DE EC=3.2.1.18 {ECO:0000256|SAAS:SAAS00063188}; GN Name=NA {ECO:0000313|EMBL:ADH83355.1}; OS Influenza A virus (A/swine/Guangdong/05/2009(H1N1)). OC Viruses; ssRNA negative-strand viruses; Orthomyxoviridae; OC Influenzavirus A. OX NCBI_TaxID=764142 {ECO:0000313|EMBL:ADH83355.1}; RN [1] {ECO:0000313|EMBL:ADH83355.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=A/swine/Guangdong/05/2009 {ECO:0000313|EMBL:ADH83355.1}; RX PubMed=21418598; RA Liu Y., Ji J., Xie Q., Wang J., Shang H., Chen C., Chen F., Xue C., RA Cao Y., Ma J., Bi Y.; RT "Isolation and complete genomic characterization of H1N1 subtype swine RT influenza viruses in southern China through the 2009 pandemic."; RL Virol. J. 8:129-129(2011). 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; HM215161; ADH83355.1; -; 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:SAAS00063156}; KW Membrane {ECO:0000256|SAAS:SAAS00151778}; KW Metal-binding {ECO:0000256|SAAS:SAAS00062292}; KW Transmembrane {ECO:0000256|SAAS:SAAS00151733}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00151757}; KW Virion {ECO:0000256|SAAS:SAAS00063088}. SQ SEQUENCE 469 AA; 51620 MW; A99854E3EAF04229 CRC64; MNTNQRIITI GTACLIIGIV SLLLRIGNIV SLWISHSIQT GEKNHSETCN RNTITYENST WVNQTYVNIS NINIAGGQGV ASIILAGNSS LCPVNGWAIY SKDNSIRIGS KGDIFVIREP FISCSHLECR TFFLTQGALL NDRHSNGTVK DRSPYRTLMS CPIGEAPSPY NSKFESVAWS ASACHDGMGW LTIGISGPDN GAVAVLKYNG IITDTIKSWR NRILRTQESE CVCINGSCFT IMTDGPSNGQ ASYKIFKMER GKIIKSVELD APNYHYEECS CYPDTGKVVC VCRDNWHASN RPWVSFDQNL DYQIGYICSG VFGDNPRSND GKGNCGPVLS NGANGVKGFS FRYGNGVWIG RTKSTNSRSG FEMIWDPNGW TETDSNFSMK QDIIALTDWS GYSGSFVQHP ELTGVNCIRP CFWVELIRGQ PKESTIWTSG SSISFCGVDS ETASWSWPDG ADLPFTIDK //