ID M1GPD9_9INFA Unreviewed; 466 AA. AC M1GPD9; DT 01-MAY-2013, integrated into UniProtKB/TrEMBL. DT 01-MAY-2013, sequence version 1. DT 12-AUG-2020, entry version 38. DE RecName: Full=Neuraminidase {ECO:0000256|RuleBase:RU361252}; DE EC=3.2.1.18 {ECO:0000256|RuleBase:RU361252}; DE Flags: Fragment; GN Name=NA {ECO:0000256|RuleBase:RU361252, ECO:0000313|EMBL:AGE41328.1}; OS Influenza A virus (A/Japan/557/2008(H1N1)). OC Viruses; Riboviria; Negarnaviricota; Polyploviricotina; Insthoviricetes; OC Articulavirales; Orthomyxoviridae; Alphainfluenzavirus. 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 inhaled RT 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 from CC viral and cellular glycoconjugates. {ECO:0000256|RuleBase:RU361252}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha- CC (2->8)- glycosidic linkages of terminal sialic acid residues in CC oligosaccharides, glycoproteins, glycolipids, colominic acid and CC synthetic substrates.; EC=3.2.1.18; CC Evidence={ECO:0000256|RuleBase:RU361252}; CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; CC Evidence={ECO:0000256|ARBA:ARBA00001913, CC ECO:0000256|RuleBase:RU361252}; CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881, CC ECO:0000256|RuleBase:RU361252}. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004606}; Single- CC pass type II membrane protein {ECO:0000256|ARBA:ARBA00004606}. Virion CC membrane {ECO:0000256|RuleBase:RU361252}. Host apical cell membrane CC {ECO:0000256|RuleBase:RU361252}; Single-pass type II membrane protein CC {ECO:0000256|RuleBase:RU361252}. 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-UniRule. DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell. DR GO; GO:0052794; F:exo-alpha-(2->3)-sialidase activity; IEA:UniProtKB-UniRule. DR GO; GO:0052795; F:exo-alpha-(2->6)-sialidase activity; IEA:UniProtKB-UniRule. DR GO; GO:0052796; F:exo-alpha-(2->8)-sialidase activity; IEA:UniProtKB-UniRule. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-UniRule. DR GO; GO:0046761; P:viral budding from plasma membrane; IEA:InterPro. DR CDD; cd15483; Influenza_NA; 1. DR HAMAP; MF_04071; INFV_NRAM; 1. DR InterPro; IPR001860; Glyco_hydro_34. DR InterPro; IPR033654; Sialidase_Influenza_A/B. DR InterPro; IPR036278; Sialidase_sf. DR Pfam; PF00064; Neur; 1. DR SUPFAM; SSF50939; SSF50939; 1. PE 3: Inferred from homology; KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|RuleBase:RU361252}; KW Glycoprotein {ECO:0000256|RuleBase:RU361252}; KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361252}; KW Host cell membrane {ECO:0000256|ARBA:ARBA00022511, KW ECO:0000256|RuleBase:RU361252}; KW Host membrane {ECO:0000256|RuleBase:RU361252}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361252}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|RuleBase:RU361252}; KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|SAM:Phobius}; Virion {ECO:0000256|RuleBase:RU361252}. FT TRANSMEM 12..32 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:AGE41328.1" FT NON_TER 466 FT /evidence="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 //