ID E1TZ58_9INFA Unreviewed; 466 AA. AC E1TZ58; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 29-APR-2015, entry version 18. 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:0000256|RuleBase:RU361252, ECO:0000313|EMBL:ADO21050.1}; OS Influenza A virus (A/swine/Guangxi/10/2007(H9N2)). OC Viruses; ssRNA negative-strand viruses; Orthomyxoviridae; OC Influenzavirus A. OX NCBI_TaxID=892007 {ECO:0000313|EMBL:ADO21050.1}; RN [1] {ECO:0000313|EMBL:ADO21050.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=A/swine/Guangxi/10/2007 {ECO:0000313|EMBL:ADO21050.1}; RA Yu H., Zhou Y.-J., Li G.-X., Tong G.-Z.; RT "Genetic diversity of H9N2 influenza viruses from pigs in China: a RT potential threat to human health?"; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. 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; CY075056; ADO21050.1; -; 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 466 AA; 51242 MW; CFAF80D50130FC21 CRC64; MNPNQKIIAI GSVSLTIATI CFLMQIAILA TTMTLHFKQN ECSNPSNNQV VPCEPTIIER NIVHLNSTTI EKEICPKVAE YKNWSKPQCQ ITGSAPFSKG NSIRLSAGGD IWVTREPYVS CSLGKCYQFA LGQGTTLKNK HSNGTTHDRG PHRTLLMSEL GVPFHLGTKQ VCIAWSSSSC HDGKAWLHVC VTGDDKNATA SIIYDGMLVD SIGSWSKNIL RTQESECVCI NGTCTVVMTD GSASGKADTR ILFIREGKIV HISPLSGSAQ HVEECSCYPR YPEVRCVCRD NWKGSNRPVL YINMADYSIE SSYVCSGLVG DTPRNDDSYS SSNCRDPNNE SGAPGVKGWA FDNGNDIWMG RTIKEDSRSG YETFRVVGGW TTANSKSQIN RQVIVDSDNW SGYSGIFSVE GKNCINRCFY VELIRGRPQE TRVWWTSNSI IVFCGTSGTY GTGSWPDGAN INFMPI //