ID   A0A0U2L0R6_9INFA        Unreviewed;       470 AA.
AC   A0A0U2L0R6;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   20-DEC-2017, entry version 13.
DE   RecName: Full=Neuraminidase {ECO:0000256|HAMAP-Rule:MF_04071, ECO:0000256|RuleBase:RU361252, ECO:0000256|SAAS:SAAS00114532};
DE            EC=3.2.1.18 {ECO:0000256|HAMAP-Rule:MF_04071, ECO:0000256|RuleBase:RU361252, ECO:0000256|SAAS:SAAS00114514};
GN   Name=NA {ECO:0000256|HAMAP-Rule:MF_04071,
GN   ECO:0000256|RuleBase:RU361252, ECO:0000313|EMBL:ALT66974.1};
OS   Influenza A virus (A/northern shoveler/Utah/A00468715/2009(H7N6)).
OC   Viruses; ssRNA viruses; ssRNA negative-strand viruses;
OC   Orthomyxoviridae; Influenzavirus A.
OX   NCBI_TaxID=1769703 {ECO:0000313|EMBL:ALT66974.1};
RN   [1] {ECO:0000313|EMBL:ALT66974.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=A/northern shoveler/Utah/A00468715/2009
RC   {ECO:0000313|EMBL:ALT66974.1};
RX   PubMed=26858078; DOI=10.1038/srep20688;
RA   Xu Y., Bailey E., Spackman E., Li T., Wang H., Long L.P., Baroch J.A.,
RA   Cunningham F.L., Lin X., Jarman R.G., DeLiberto T.J., Wan X.F.;
RT   "Limited Antigenic Diversity in Contemporary H7 Avian-Origin Influenza
RT   A Viruses from North America.";
RL   Sci. Rep. 6:20688-20688(2016).
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|HAMAP-Rule:MF_04071,
CC       ECO:0000256|RuleBase:RU361252, ECO:0000256|SAAS:SAAS00114528}.
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_04071, ECO:0000256|RuleBase:RU361252,
CC         ECO:0000256|SAAS:SAAS00612833};
CC   -!- ENZYME REGULATION: Inhibited by the neuraminidase inhibitors
CC       zanamivir (Relenza) and oseltamivir (Tamiflu). These drugs
CC       interfere with the release of progeny virus from infected cells
CC       and are effective against all influenza strains. Resistance to
CC       neuraminidase inhibitors is quite rare. {ECO:0000256|HAMAP-
CC       Rule:MF_04071}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_04071,
CC       ECO:0000256|RuleBase:RU361252, ECO:0000256|SAAS:SAAS00114476}.
CC   -!- SUBCELLULAR LOCATION: Host apical cell membrane
CC       {ECO:0000256|SAAS:SAAS00582107}; Single-pass type II membrane
CC       protein {ECO:0000256|SAAS:SAAS00582107}.
CC   -!- DOMAIN: Intact N-terminus is essential for virion morphogenesis.
CC       Possess two apical sorting signals, one in the ectodomain, which
CC       is likely to be a glycan, and the other in the transmembrane
CC       domain. The transmembrane domain also plays a role in lipid raft
CC       association. {ECO:0000256|HAMAP-Rule:MF_04071}.
CC   -!- PTM: N-glycosylated. {ECO:0000256|HAMAP-Rule:MF_04071,
CC       ECO:0000256|RuleBase:RU361252}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 34 family.
CC       {ECO:0000256|HAMAP-Rule:MF_04071, ECO:0000256|RuleBase:RU361252,
CC       ECO:0000256|SAAS:SAAS00582269}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_04071}.
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DR   EMBL; KU290296; ALT66974.1; -; 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-UniRule.
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   HAMAP; MF_04071; INFV_NRAM; 1.
DR   InterPro; IPR001860; Glyco_hydro_34.
DR   InterPro; IPR036278; Sialidase_sf.
DR   Pfam; PF00064; Neur; 1.
DR   SUPFAM; SSF50939; SSF50939; 1.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|HAMAP-Rule:MF_04071,
KW   ECO:0000256|RuleBase:RU361252, ECO:0000256|SAAS:SAAS00114513};
KW   Disulfide bond {ECO:0000256|HAMAP-Rule:MF_04071,
KW   ECO:0000256|SAAS:SAAS00114594};
KW   Glycoprotein {ECO:0000256|HAMAP-Rule:MF_04071,
KW   ECO:0000256|RuleBase:RU361252};
KW   Glycosidase {ECO:0000256|HAMAP-Rule:MF_04071,
KW   ECO:0000256|RuleBase:RU361252, ECO:0000256|SAAS:SAAS00114535};
KW   Host cell membrane {ECO:0000256|HAMAP-Rule:MF_04071,
KW   ECO:0000256|RuleBase:RU361252, ECO:0000256|SAAS:SAAS00114522};
KW   Host membrane {ECO:0000256|HAMAP-Rule:MF_04071,
KW   ECO:0000256|RuleBase:RU361252, ECO:0000256|SAAS:SAAS00114565};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_04071,
KW   ECO:0000256|RuleBase:RU361252, ECO:0000256|SAAS:SAAS00114491};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_04071,
KW   ECO:0000256|SAAS:SAAS00114461};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_04071,
KW   ECO:0000256|RuleBase:RU361252, ECO:0000256|SAAS:SAAS00114385};
KW   Signal-anchor {ECO:0000256|HAMAP-Rule:MF_04071};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_04071,
KW   ECO:0000256|SAAS:SAAS00114524};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_04071,
KW   ECO:0000256|SAAS:SAAS00114517};
KW   Virion {ECO:0000256|HAMAP-Rule:MF_04071,
KW   ECO:0000256|RuleBase:RU361252, ECO:0000256|SAAS:SAAS00114362}.
FT   TRANSMEM      7     31       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_04071}.
FT   REGION       11     33       Involved in apical transport and lipid
FT                                raft association. {ECO:0000256|HAMAP-
FT                                Rule:MF_04071}.
FT   REGION       91    470       Head of neuraminidase.
FT                                {ECO:0000256|HAMAP-Rule:MF_04071}.
FT   REGION      277    278       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_04071}.
FT   ACT_SITE    151    151       Proton donor/acceptor.
FT                                {ECO:0000256|HAMAP-Rule:MF_04071}.
FT   ACT_SITE    406    406       Nucleophile. {ECO:0000256|HAMAP-Rule:
FT                                MF_04071}.
FT   METAL       294    294       Calcium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_04071}.
FT   METAL       298    298       Calcium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_04071}.
FT   METAL       325    325       Calcium. {ECO:0000256|HAMAP-Rule:
FT                                MF_04071}.
FT   BINDING     118    118       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_04071}.
FT   BINDING     152    152       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_04071}.
FT   BINDING     293    293       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_04071}.
FT   BINDING     372    372       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_04071}.
FT   DISULFID    124    129       {ECO:0000256|HAMAP-Rule:MF_04071}.
FT   DISULFID    184    231       {ECO:0000256|HAMAP-Rule:MF_04071}.
FT   DISULFID    233    238       {ECO:0000256|HAMAP-Rule:MF_04071}.
FT   DISULFID    279    292       {ECO:0000256|HAMAP-Rule:MF_04071}.
FT   DISULFID    281    290       {ECO:0000256|HAMAP-Rule:MF_04071}.
SQ   SEQUENCE   470 AA;  51741 MW;  1204528C0CB23896 CRC64;
     MNPNQKIICI SATGMTLSVV SLLIGLANLG LNIGLHFKVG DTPETEPPST NETNSTTTII
     NYNTQNNFTN VTNIVLIKEE NKMFTNLSKP LCEVNSWHIL SKDNAIRIGE NAHILVTREP
     YLSCGPHECR MFALSQGTTL RGRHANGTIH DRSPFRALIS WEMGQAPSPY NVRVECVGWS
     STSCHDGISR MSICMSGPNN NASAVVWYNG RPVTEIASWA GNILRTQESE CVCHNGICPV
     VMTDGPANNR AETKIIYFKE GKIQKIEELT GSAQHIEECS CYGAEEVIKC ICRDNWKGAN
     RPVITINPTT MTHTSKYLCS KILTDTSRPN DPGSGNCDAP ITGGSPDPGV KGFAFLDGGN
     SWLGRTISKD SRSGYEMLKV PNAETDNQSG PVAHQVIVNN QNWSGYSGAF IDYWADRECF
     NPCFYVELIR GRPKESSVLW TSNSIVALCG SRERLGSWSW HDGAEIIYFK
//