ID   A0A0G2QS34_9INFA        Unreviewed;       469 AA.
AC   A0A0G2QS34;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   18-JAN-2017, entry version 12.
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};
GN   Name=NA {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   -!- FUNCTION: Catalyzes the removal of terminal sialic acid residues
CC       from viral and cellular glycoconjugates. Cleaves off the terminal
CC       sialic acids on the glycosylated HA during virus budding to
CC       facilitate virus release. Additionally helps virus spread through
CC       the circulation by further removing sialic acids from the cell
CC       surface. These cleavages prevent self-aggregation and ensure the
CC       efficient spread of the progeny virus from cell to cell.
CC       Otherwise, infection would be limited to one round of replication.
CC       Described as a receptor-destroying enzyme because it cleaves a
CC       terminal sialic acid from the cellular receptors. May facilitate
CC       viral invasion of the upper airways by cleaving the sialic acid
CC       moities on the mucin of the airway epithelial cells. Likely to
CC       plays a role in the budding process through its association with
CC       lipid rafts during intracellular transport. May additionally
CC       display a raft-association independent effect on budding. Plays a
CC       role in the determination of host range restriction on replication
CC       and virulence. Sialidase activity in late endosome/lysosome
CC       traffic seems to enhance virus replication.
CC       {ECO:0000256|SAAS:SAAS00234081}.
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   -!- SUBUNIT: Homotetramer. {ECO:0000256|RuleBase:RU361252,
CC       ECO:0000256|SAAS:SAAS00114476}.
CC   -!- SUBCELLULAR LOCATION: Host apical cell membrane
CC       {ECO:0000256|SAAS:SAAS00561320}; Single-pass type II membrane
CC       protein {ECO:0000256|SAAS:SAAS00561320}.
CC   -!- SUBCELLULAR LOCATION: Virion membrane
CC       {ECO:0000256|SAAS:SAAS00561294}.
CC   -!- PTM: N-glycosylated. {ECO:0000256|RuleBase:RU361252}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 34 family.
CC       {ECO:0000256|RuleBase:RU361252, ECO:0000256|SAAS:SAAS00561099}.
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DR   EMBL; KF768219; AHA57002.1; -; Viral_cRNA.
DR   Proteomes; UP000128397; Segment 6 neuraminidase (na) gene.
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   GO; GO:0046761; P:viral budding from plasma membrane; IEA:InterPro.
DR   CDD; cd15483; Influenza_NA; 1.
DR   Gene3D; 2.120.10.10; -; 1.
DR   InterPro; IPR001860; Glyco_hydro_34.
DR   InterPro; IPR033654; Sialidase_Influenza_A/B.
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:SAAS00062903};
KW   Complete proteome {ECO:0000313|Proteomes:UP000128397};
KW   Disulfide bond {ECO:0000256|SAAS:SAAS00063019};
KW   Glycoprotein {ECO:0000256|RuleBase:RU361252};
KW   Glycosidase {ECO:0000256|RuleBase:RU361252,
KW   ECO:0000256|SAAS:SAAS00062426};
KW   Host cell membrane {ECO:0000256|RuleBase:RU361252,
KW   ECO:0000256|SAAS:SAAS00062854};
KW   Host membrane {ECO:0000256|RuleBase:RU361252,
KW   ECO:0000256|SAAS:SAAS00062524};
KW   Hydrolase {ECO:0000256|RuleBase:RU361252,
KW   ECO:0000256|SAAS:SAAS00063156};
KW   Membrane {ECO:0000256|SAAS:SAAS00114461, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|RuleBase:RU361252,
KW   ECO:0000256|SAAS:SAAS00062292};
KW   Transmembrane {ECO:0000256|SAAS:SAAS00114524,
KW   ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAAS:SAAS00114517,
KW   ECO:0000256|SAM:Phobius};
KW   Virion {ECO:0000256|RuleBase:RU361252, ECO:0000256|SAAS:SAAS00063088}.
FT   TRANSMEM      7     29       Helical. {ECO:0000256|SAM:Phobius}.
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
//