ID   F8R9M4_9INFA            Unreviewed;       469 AA.
AC   F8R9M4;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   26-NOV-2014, entry version 17.
DE   RecName: Full=Neuraminidase {ECO:0000256|SAAS:SAAS00062759};
DE            EC=3.2.1.18 {ECO:0000256|SAAS:SAAS00063188};
GN   Name=NA {ECO:0000313|EMBL:ADJ37640.1};
OS   Influenza A virus (A/England/347/2009(H1N1)).
OC   Viruses; ssRNA negative-strand viruses; Orthomyxoviridae;
OC   Influenzavirus A.
OX   NCBI_TaxID=856915 {ECO:0000313|EMBL:ADJ37640.1};
RN   [1] {ECO:0000313|EMBL:ADJ37640.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=A/England/347/2009 {ECO:0000313|EMBL:ADJ37640.1};
RX   PubMed=22013031; DOI=10.1128/JVI.05347-11;
RA   Baillie G.J., Galiano M., Agapow P.M., Myers R., Chiam R., Gall A.,
RA   Palser A.L., Watson S.J., Hedge J., Underwood A., Platt S., McLean E.,
RA   Pebody R.G., Rambaut A., Green J., Daniels R., Pybus O.G., Kellam P.,
RA   Zambon M.;
RT   "Evolutionary Dynamics of Local Pandemic H1N1/2009 Influenza Virus
RT   Lineages Revealed by Whole-Genome Analysis.";
RL   J. Virol. 86:11-18(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:
CC       Note=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}.
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DR   EMBL; HM567666; ADJ37640.1; -; 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   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:SAAS00151778};
KW   Metal-binding {ECO:0000256|SAAS:SAAS00062292};
KW   Transmembrane {ECO:0000256|SAAS:SAAS00151733};
KW   Transmembrane helix {ECO:0000256|SAAS:SAAS00151757};
KW   Virion {ECO:0000256|SAAS:SAAS00063088}.
SQ   SEQUENCE   469 AA;  51657 MW;  657D5A2A53B0E978 CRC64;
     MNPNQKIITI GSVCMTIGMA NLILQIGNII SIWISHSIQL GNQNQIETCN QSVITYENNT
     WVNQTYVNIS NTNFAAGQSV VSVKLAGNSS LCPVSGWAIY SKDNSVRIGS KGDVFVIREP
     FISCSPLECR TFFLTQGALL NDKHSNGTIK DRSPYRTLMS CPIGEVPSPY NSRFESVAWS
     ASACHDGINW LTIGISGPDN GAVAVLKYNG IITDTIKSWR NNILRTQESE CACVNGSCFT
     VMTDGPSNGQ ASYKIFRIEK GKIVKSVEMN APNYHYEECS CYPDSSEITC VCRDNWHGSN
     RPWVSFNQNL EYQIGYICSG IFGDNPRPND KTGSCGPVSF NGANGVKGFS FKYGNGVWIG
     RTKSISSRNG FEMIWDPNGW TGTDNNFSIK QDIVGINEWS GYSGSFVQHP ELTGLDCIRP
     CFWVELIRGR PKENTIWTSG SSISFCGVNS DTVGWSWPDG AELPFTIDK
//