ID M1GPD9_9INFA Unreviewed; 466 AA. AC M1GPD9; DT 01-MAY-2013, integrated into UniProtKB/TrEMBL. DT 01-MAY-2013, sequence version 1. DT 07-JAN-2015, entry version 11. DE RecName: Full=Neuraminidase {ECO:0000256|RuleBase:RU361252, ECO:0000256|SAAS:SAAS00114532}; DE EC=3.2.1.18 {ECO:0000256|RuleBase:RU361252, ECO:0000256|SAAS:SAAS00114514}; DE Flags: Fragment; GN Name=NA {ECO:0000313|EMBL:AGE41328.1}; OS Influenza A virus (A/Japan/557/2008(H1N1)). OC Viruses; ssRNA negative-strand viruses; Orthomyxoviridae; OC Influenzavirus A. OX NCBI_TaxID=1279777 {ECO:0000313|EMBL:AGE41328.1}; RN [1] {ECO:0000313|EMBL:AGE41328.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=A/Japan/557/2008 {ECO:0000313|EMBL:AGE41328.1}; RX PubMed=23335741; RA Yates P.J., Mehta N., Horton J., Tisdale M.; RT "Virus susceptibility analyses from a phase IV clinical trial of RT inhaled zanamivir treatment in children infected with influenza."; RL Antimicrob. Agents Chemother. 0:0-0(2013). 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:SAAS00114528}. CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; CC Evidence={ECO:0000256|RuleBase:RU361252, CC ECO:0000256|SAAS:SAAS00175717}; CC Note=Binds 1 Ca(2+) ion per subunit. CC {ECO:0000256|RuleBase:RU361252, ECO:0000256|SAAS:SAAS00175717}; CC -!- SUBUNIT: Homotetramer. {ECO:0000256|RuleBase:RU361252, CC ECO:0000256|SAAS:SAAS00114476}. CC -!- SUBCELLULAR LOCATION: Virion membrane CC {ECO:0000256|RuleBase:RU361252, ECO:0000256|SAAS:SAAS00114420}. CC Host apical cell membrane {ECO:0000256|RuleBase:RU361252, CC ECO:0000256|SAAS:SAAS00114420}; Single-pass type II membrane CC protein {ECO:0000256|RuleBase:RU361252, CC ECO:0000256|SAAS:SAAS00114420}. 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; KC457875; AGE41328.1; -; 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 3: Inferred from homology; KW Calcium {ECO:0000256|RuleBase:RU361252, KW ECO:0000256|SAAS:SAAS00114513}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00114594}; KW Glycoprotein {ECO:0000256|RuleBase:RU361252}; KW Glycosidase {ECO:0000256|RuleBase:RU361252, KW ECO:0000256|SAAS:SAAS00114535}; KW Host cell membrane {ECO:0000256|RuleBase:RU361252, KW ECO:0000256|SAAS:SAAS00114522}; KW Host membrane {ECO:0000256|RuleBase:RU361252, KW ECO:0000256|SAAS:SAAS00114565}; KW Hydrolase {ECO:0000256|RuleBase:RU361252, KW ECO:0000256|SAAS:SAAS00114491}; KW Membrane {ECO:0000256|SAAS:SAAS00114461}; KW Metal-binding {ECO:0000256|RuleBase:RU361252, KW ECO:0000256|SAAS:SAAS00114385}; KW Transmembrane {ECO:0000256|SAAS:SAAS00114524}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00114517}; KW Virion {ECO:0000256|RuleBase:RU361252, ECO:0000256|SAAS:SAAS00114362}. FT NON_TER 1 1 {ECO:0000313|EMBL:AGE41328.1}. FT NON_TER 466 466 {ECO:0000313|EMBL:AGE41328.1}. SQ SEQUENCE 466 AA; 51220 MW; 49D7E26BF72954E3 CRC64; PNQKIITIGS ISIAIGIISL MLQIGNIISI WASHSIQTGS QNNTGICNQR IITYENSTWV NHTYVNINNT NVVAGEDKTS VTLAGNSSLC SISGWAIYTK DNSIRIGSKG DVFVIREPFI SCSHLECRTF FLTQGALLND KHSNGTVKDR SPYRALMSCP LGEAPSPYNS KFESVAWSAS ACHDGMGWLT IGISGPDNGA VAVLKYNGII TGTIKSWKKQ ILRTQESECV CMNGSCFTIM TDGPSNKAAS YKIFKIEKGK VTKSIELNAP NFHYEECSCY PDTGIVMCVC RDNWHGSNRP WVSFNQNLDY QIGYICSGVF GDNPRPEDGE GSCNPVTVDG ANGVKGFSYK YDNGVWIGRT KSNRLRKGFE MIWDPNGWTN TDSDFSVKQD VVAITDWSGY SGSFVQHPEL TGLDCIRPCF WVELVRGLPR ENTTIWTSGS SISFCGVNSD TANWSWPDGA ELPFTM //