ID I7H095_9INFA Unreviewed; 469 AA. AC I7H095; DT 03-OCT-2012, integrated into UniProtKB/TrEMBL. DT 03-OCT-2012, sequence version 1. DT 29-OCT-2014, entry version 11. DE SubName: Full=Neuraminidase {ECO:0000313|EMBL:BAM34381.1}; GN Name=NA {ECO:0000313|EMBL:BAM34381.1}; OS Influenza A virus (A/Yamaguchi/217/2009(H1N1)). OC Viruses; ssRNA negative-strand viruses; Orthomyxoviridae; OC Influenzavirus A. OX NCBI_TaxID=1166457 {ECO:0000313|EMBL:BAM34381.1}; RN [1] {ECO:0000313|EMBL:BAM34381.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=A/Yamaguchi/217/2009 {ECO:0000313|EMBL:BAM34381.1}; RA Obuchi M., Toda S., Tsukagoshi H., Oogane T., Abiko C., Funatogawa K., RA Mizuta K., Shirabe K., Kozawa K., Noda M., Kimura H., Tashiro M.; RT "Molecular Analysis of Genome of the Pandemic Influenza A(H1N1) 2009 RT Virus Associated with Fatal Infections in Gunma, Tochigi, Yamagata, RT and Yamaguchi Prefectures in Japan during the First Pandemic Wave."; RL Jpn. J. Infect. Dis. 65:363-367(2012). 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; AB704512; BAM34381.1; -; 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:SAAS00062477}; KW Metal-binding {ECO:0000256|SAAS:SAAS00062292}; KW Transmembrane {ECO:0000256|SAAS:SAAS00063177}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00063095}; KW Virion {ECO:0000256|SAAS:SAAS00063088}. SQ SEQUENCE 469 AA; 51612 MW; 425AF951B81CF409 CRC64; MNPNQKIITI GSVCMTIGMA NLILQIGNII SIWISHSIQL GNQNQIETCN QSVITYENNT WVNQTYVNIS NTNFAAGQSV VSVKLAGNSS LCPVSGWAIY SKDNSIRIGS KGDVFVIREP FISCSPLECR TFFLTQGALL NDKHSNGTIK DRSPYRTLMS CPIGEVPSPY NSRFESVAWS ASACHDGINW LTIGISGPDN GAVAVLKYNG IITDTIKSWR NNILRTQESE CACVNGSCFT VMTDGPSDGQ ASYKIFRIEK GKIVKSVEMN APNYHYEECS CYPDSSEITC VCRDNWHGSN RPWVSFNQNL EYQIGYICSG IFGDNPRPND KTGSCGPVSS NGANGVKGFS FKYGNGVWIG RTKSISSRNG FEMIWDPNGW TGTDNNFSIK QDIVGINEWS GYSGSFVQHP ELTGLDCIRP CFWVELIRGR PKENTIWTSG SSISFCGVNS DTVGWSWPDG AELPFTIDK //