ID   A0A0G2QS34_9INFA        Unreviewed;       469 AA.
AC   A0A0G2QS34;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   28-MAR-2018, entry version 22.
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:AHA57002.1};
OS   Influenza A virus (A/duck/Guangxi/NN/2006(H9N2)).
OC   Viruses; ssRNA viruses; ssRNA negative-strand viruses;
OC   Orthomyxoviridae; Influenzavirus A.
OX   NCBI_TaxID=1413198 {ECO:0000313|EMBL:AHA57002.1, ECO:0000313|Proteomes:UP000128397};
RN   [1] {ECO:0000313|EMBL:AHA57002.1, ECO:0000313|Proteomes:UP000128397}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A/duck/Guangxi/NN/2006 {ECO:0000313|EMBL:AHA57002.1};
RA   Peng Y., Xie Z., Liu J., Pang Y., Xie Z., Xie L., Luo S., Fan Q.;
RT   "Genetic analysis of H9 subtype avian influenza viruses in Guangxi,
RT   Southern China during 2005 to 2010.";
RL   Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
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; KF768219; AHA57002.1; -; Viral_cRNA.
DR   Proteomes; UP000128397; Genome.
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-UniRule.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0046761; P:viral budding from plasma membrane; IEA:UniProtKB-UniRule.
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|HAMAP-Rule:MF_04071,
KW   ECO:0000256|RuleBase:RU361252, ECO:0000256|SAAS:SAAS00114513};
KW   Complete proteome {ECO:0000313|Proteomes:UP000128397};
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     29       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    469       Head of neuraminidase.
FT                                {ECO:0000256|HAMAP-Rule:MF_04071}.
FT   REGION      276    277       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       293    293       Calcium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_04071}.
FT   METAL       297    297       Calcium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_04071}.
FT   METAL       324    324       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     292    292       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_04071}.
FT   BINDING     371    371       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_04071}.
FT   DISULFID     92    417       {ECO:0000256|HAMAP-Rule:MF_04071}.
FT   DISULFID    124    129       {ECO:0000256|HAMAP-Rule:MF_04071}.
FT   DISULFID    183    230       {ECO:0000256|HAMAP-Rule:MF_04071}.
FT   DISULFID    232    237       {ECO:0000256|HAMAP-Rule:MF_04071}.
FT   DISULFID    278    291       {ECO:0000256|HAMAP-Rule:MF_04071}.
FT   DISULFID    280    289       {ECO:0000256|HAMAP-Rule:MF_04071}.
SQ   SEQUENCE   469 AA;  51840 MW;  0971EC63BED3B234 CRC64;
     MNPNQKIIAI GSVSLTIATI CFLMQIAILT TTMTLHFRQN ECSSPSNNQV VPCEPIIIER
     NTTEIVHLNS TTIEKEICPK VAEYKNWSKP QCQITGFAPF SKDNSIRLSA GGDIWVTREP
     YVSCSLGKCY QFALGQGTTL KNKHSNGTTH DRIPHRTLLM NELGVPFHLG TKQVCIAWSS
     SSCHDGRAWV HICVTGDDKN ATASIIYDGM LVDSIGSWSK NILRTQESEC VCINGTCAVV
     MTDGSASGKA DTRILFIREG KIINISPLSG SAQHVEECSC YPRYPEVRCV CRDNWKGSNR
     PVLYINMADY SIESSYVCSG LVGDTPRNDD SSSSSNCRDP NNERGAPGVK GWAFDDGNDV
     WMGRTIKDNS RSGYETFRVV NGWTTANSKS QINRQVIVDI DNWSGYSGIF SVEGKNCINR
     CFYVELIRGR PQESRVWWTS NSIIVFCGTS GTYGTGSWPD GANINFMPI
//