ID   C6G5K0_9INFA            Unreviewed;       469 AA.
AC   C6G5K0;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   08-JUN-2016, entry version 33.
DE   RecName: Full=Neuraminidase {ECO:0000256|RuleBase:RU361252, ECO:0000256|SAAS:SAAS00062759};
DE            EC=3.2.1.18 {ECO:0000256|RuleBase:RU361252, ECO:0000256|SAAS:SAAS00063188};
GN   Name=NA {ECO:0000256|RuleBase:RU361252, ECO:0000313|EMBL:ACL11973.1};
OS   Influenza A virus (A/chicken/Chakwal/NARC-35/2001(H7N3)).
OC   Viruses; ssRNA viruses; ssRNA negative-strand viruses;
OC   Orthomyxoviridae; Influenzavirus A.
OX   NCBI_TaxID=585042 {ECO:0000313|EMBL:ACL11973.1};
RN   [1] {ECO:0000313|EMBL:ACL11973.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=A/chicken/Chakwal/NARC-35/2001 {ECO:0000313|EMBL:ACL11973.1};
RX   PubMed=20576101;
RA   Abbas M.A., Spackman E., Swayne D.E., Ahmed Z., Sarmento L.,
RA   Siddique N., Naeem K., Hameed A., Rehmani S.;
RT   "Sequence and phylogenetic analysis of H7N3 avian influenza viruses
RT   isolated from poultry in Pakistan 1995-2004.";
RL   Virol. J. 7:137-137(2010).
RN   [2] {ECO:0000313|EMBL:ADI34039.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=A/chicken/Chakwal/NARC-35/2001 {ECO:0000313|EMBL:ADI34039.1};
RA   Abbas M.A., Spackman E., Ahmed Z., Naeem K., Siddique N., Swayne D.,
RA   Sarmento L., Hameed A.;
RT   "Studies on Biological Characteristics & Evaluation of Antigenic Drift
RT   in the Field Isolates of Avian Influenza Viruses.";
RL   Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the removal of terminal sialic acid residues
CC       from viral and cellular glycoconjugates.
CC       {ECO:0000256|RuleBase:RU361252}.
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.
CC       {ECO:0000256|SAAS:SAAS00561304}.
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:SAAS00371510}.
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:SAAS00062942}.
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|RuleBase:RU361252};
CC       Note=Binds 1 Ca(2+) ion per subunit.
CC       {ECO:0000256|RuleBase:RU361252};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|RuleBase:RU361252,
CC       ECO:0000256|SAAS:SAAS00063168}.
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 {ECO:0000256|SAAS:SAAS00561056}.
CC   -!- SUBCELLULAR LOCATION: Virion membrane
CC       {ECO:0000256|SAAS:SAAS00561294}.
CC   -!- SUBCELLULAR LOCATION: Virion membrane
CC       {ECO:0000256|RuleBase:RU361252}. Host apical cell membrane
CC       {ECO:0000256|RuleBase:RU361252}; Single-pass type II membrane
CC       protein {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, ECO:0000256|SAAS:SAAS00561099}.
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DR   EMBL; FJ577520; ACL11973.1; -; Viral_cRNA.
DR   EMBL; HM346487; ADI34039.1; -; 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   3: Inferred from homology;
KW   Calcium {ECO:0000256|RuleBase:RU361252,
KW   ECO:0000256|SAAS:SAAS00448743};
KW   Disulfide bond {ECO:0000256|SAAS:SAAS00449120};
KW   Glycoprotein {ECO:0000256|RuleBase:RU361252};
KW   Glycosidase {ECO:0000256|RuleBase:RU361252,
KW   ECO:0000256|SAAS:SAAS00448849};
KW   Host cell membrane {ECO:0000256|RuleBase:RU361252,
KW   ECO:0000256|SAAS:SAAS00448685};
KW   Host membrane {ECO:0000256|RuleBase:RU361252,
KW   ECO:0000256|SAAS:SAAS00449348};
KW   Hydrolase {ECO:0000256|RuleBase:RU361252,
KW   ECO:0000256|SAAS:SAAS00448424};
KW   Membrane {ECO:0000256|SAAS:SAAS00448618, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|RuleBase:RU361252,
KW   ECO:0000256|SAAS:SAAS00448775};
KW   Transmembrane {ECO:0000256|SAAS:SAAS00449168,
KW   ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAAS:SAAS00448371,
KW   ECO:0000256|SAM:Phobius};
KW   Virion {ECO:0000256|RuleBase:RU361252, ECO:0000256|SAAS:SAAS00448515}.
FT   TRANSMEM      7     31       Helical. {ECO:0000256|SAM:Phobius}.
SQ   SEQUENCE   469 AA;  51877 MW;  6ECC8AAFFBC528A1 CRC64;
     MNPNQKIITI GVVNTTLSTI ALLIGIGNLV FNTVIHEKVG EQKTVAYPTV TSPVVPNCSD
     TIITYNSTVV NNITTTIVTE AERHFKSSLP LCPFRGFFPF HKDNAIRLGE NKDVIVTREP
     YVSCDYNDCW SFALAQGALL GTNHSNGTIK DRTPYRSLIR FPIGVAPVLG NYKEICVAWS
     SSSCFDGKEW MHVCMTGNDN DASAQIIYAG KMTDSIKSWR KDILRTQESE CQCIDGTCVV
     AVTDGPAANN ADHRIYWIRK GRVIKYENIP KTKIKHLEEC SCYVDIDVYC ICRDNWKGSN
     RPWMRINNET ILETGYVCSK FHSDTPRPDD PSTVSCDSPS NVNGGPGVKG FGFKTGNDVW
     LGRTVSNSGR SGFEIIKVTE GWINSPNHAK SVTQTLVSNN DWSGYSGSFI VESNGCFQPC
     FYIELIRGKP NKNDNVSWTS NSIVTFCGLD NEPGSGNWPD GSNIGFMPK
//