ID J9QFE5_9INFA Unreviewed; 469 AA. AC J9QFE5; DT 28-NOV-2012, integrated into UniProtKB/TrEMBL. DT 28-NOV-2012, sequence version 1. DT 04-MAR-2015, entry version 13. DE RecName: Full=Neuraminidase {ECO:0000256|RuleBase:RU361252, ECO:0000256|SAAS:SAAS00062759}; DE EC=3.2.1.18 {ECO:0000256|RuleBase:RU361252, ECO:0000256|SAAS:SAAS00063188}; GN Name=NA {ECO:0000313|EMBL:AFO82967.1}; OS Influenza A virus (A/chicken/India/WB-NIV1057169/2010(H9N2)). OC Viruses; ssRNA negative-strand viruses; Orthomyxoviridae; OC Influenzavirus A. OX NCBI_TaxID=1210133 {ECO:0000313|EMBL:AFO82967.1}; RN [1] {ECO:0000313|EMBL:AFO82967.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=A/chicken/India/WB-NIV1057169/2010 RC {ECO:0000313|EMBL:AFO82967.1}; RX PubMed=22867041; RA Pawar S.D., Kale S.D., Rawankar A.S., Koratkar S.S., Raut C.G., RA Pande S.A., Mullick J., Mishra A.C.; RT "Avian influenza surveillance reveals presence of low pathogenic avian RT influenza viruses in poultry during 2009?2011 in the West Bengal RT State, India."; RL Virol. J. 9:151-151(2012). CC -!- FUNCTION: Catalyzes the removal of terminal sialic acid residues CC from viral and cellular glycoconjugates. CC {ECO:0000256|RuleBase:RU361252}. 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|RuleBase:RU361252, CC ECO:0000256|SAAS:SAAS00062942}. CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; CC Evidence={ECO:0000256|RuleBase:RU361252, CC ECO:0000256|SAAS:SAAS00170353}; CC Note=Binds 1 Ca(2+) ion per subunit. CC {ECO:0000256|RuleBase:RU361252, ECO:0000256|SAAS:SAAS00170353}; CC -!- SUBUNIT: Homotetramer. {ECO:0000256|RuleBase:RU361252, CC ECO:0000256|SAAS:SAAS00063168}. CC -!- SUBCELLULAR LOCATION: Virion membrane CC {ECO:0000256|RuleBase:RU361252, ECO:0000256|SAAS:SAAS00063102}. CC Host apical cell membrane {ECO:0000256|RuleBase:RU361252, CC ECO:0000256|SAAS:SAAS00063102}; Single-pass type II membrane CC protein {ECO:0000256|RuleBase:RU361252, CC ECO:0000256|SAAS:SAAS00063102}. 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; JX310068; AFO82967.1; -; 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:0052794; F:exo-alpha-(2->3)-sialidase activity; IEA:UniProtKB-EC. DR GO; GO:0052795; F:exo-alpha-(2->6)-sialidase activity; IEA:UniProtKB-EC. DR GO; GO:0052796; F:exo-alpha-(2->8)-sialidase activity; IEA:UniProtKB-EC. 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 3: Inferred from homology; KW Calcium {ECO:0000256|RuleBase:RU361252, KW ECO:0000256|SAAS:SAAS00062903}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00063019}; KW Glycoprotein {ECO:0000256|RuleBase:RU361252}; KW Glycosidase {ECO:0000256|RuleBase:RU361252, KW ECO:0000256|SAAS:SAAS00062426}; KW Host cell membrane {ECO:0000256|RuleBase:RU361252, KW ECO:0000256|SAAS:SAAS00062854}; KW Host membrane {ECO:0000256|RuleBase:RU361252, KW ECO:0000256|SAAS:SAAS00062524}; KW Hydrolase {ECO:0000256|RuleBase:RU361252, KW ECO:0000256|SAAS:SAAS00063156}; KW Membrane {ECO:0000256|SAAS:SAAS00114461}; KW Metal-binding {ECO:0000256|RuleBase:RU361252, KW ECO:0000256|SAAS:SAAS00062292}; KW Transmembrane {ECO:0000256|SAAS:SAAS00114524}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00114517}; KW Virion {ECO:0000256|RuleBase:RU361252, ECO:0000256|SAAS:SAAS00063088}. SQ SEQUENCE 469 AA; 51691 MW; 65FF63154E4F0739 CRC64; MSPNQKRIAL GSASLTIATI CLLIQIAILA TTMTLHFNQN DFTNSSKNQV VPCESIIIER NITEIVHLNG TITEKGSCPK AAEYKNWSKP QCQITGFVPF SKDNSIRLSA GGDIWVTREP YVSCGLRKCY QFALGQGTTL NNKHSNGTTH DRSPYRTLLM SELGVPFHLG TKQVCIAWSS SSCHDGRAWL HVCVTGDDRN ATASVIYDGM LTDSIRSWSG NILRTQESEC VCINGTCTVV MTDGSASGRA DTRILFIREG KIVHISPLSG SAQHVEECSC YPRYPEVRCV CRDNWKGSNR PVLYINVADY SIDSSYVCSG LVGDTPRNDD SSSSSNCRDP NNERGAPGVK GWAFDNGNDV WMGRTIKEDS RAGYETFRVV GGWTIANSKS QINRQVIVDS DNWSGYSGIF SVENKICINR CFYVELIRGR PQETIVWWTS NSIIVFCGTS GTYGTGSWPD GADINFMSI //