ID   C6G5K0_9INFA            Unreviewed;       469 AA.
AC   C6G5K0;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   04-FEB-2015, entry version 25.
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:ACL11973.1};
OS   Influenza A virus (A/chicken/Chakwal/NARC-35/2001(H7N3)).
OC   Viruses; ssRNA negative-strand viruses; Orthomyxoviridae;
OC   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   -!- 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   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|RuleBase:RU361252,
CC         ECO:0000256|SAAS:SAAS00175717};
CC       Note=Binds 1 Ca(2+) ion per subunit.
CC       {ECO:0000256|RuleBase:RU361252, ECO:0000256|SAAS:SAAS00175717};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|RuleBase:RU361252,
CC       ECO:0000256|SAAS:SAAS00114476}.
CC   -!- SUBCELLULAR LOCATION: Virion membrane
CC       {ECO:0000256|RuleBase:RU361252, ECO:0000256|SAAS:SAAS00114420}.
CC       Host apical cell membrane {ECO:0000256|RuleBase:RU361252,
CC       ECO:0000256|SAAS:SAAS00114420}; Single-pass type II membrane
CC       protein {ECO:0000256|RuleBase:RU361252,
CC       ECO:0000256|SAAS:SAAS00114420}.
CC   -!- PTM: N-glycosylated. {ECO:0000256|RuleBase:RU361252}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 34 family.
CC       {ECO:0000256|RuleBase:RU361252}.
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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:SAAS00114513};
KW   Disulfide bond {ECO:0000256|SAAS:SAAS00114594};
KW   Glycoprotein {ECO:0000256|RuleBase:RU361252};
KW   Glycosidase {ECO:0000256|RuleBase:RU361252,
KW   ECO:0000256|SAAS:SAAS00114535};
KW   Host cell membrane {ECO:0000256|RuleBase:RU361252,
KW   ECO:0000256|SAAS:SAAS00114522};
KW   Host membrane {ECO:0000256|RuleBase:RU361252,
KW   ECO:0000256|SAAS:SAAS00114565};
KW   Hydrolase {ECO:0000256|RuleBase:RU361252,
KW   ECO:0000256|SAAS:SAAS00114491};
KW   Membrane {ECO:0000256|SAAS:SAAS00114461};
KW   Metal-binding {ECO:0000256|RuleBase:RU361252,
KW   ECO:0000256|SAAS:SAAS00114385};
KW   Transmembrane {ECO:0000256|SAAS:SAAS00114524};
KW   Transmembrane helix {ECO:0000256|SAAS:SAAS00114517};
KW   Virion {ECO:0000256|RuleBase:RU361252, ECO:0000256|SAAS:SAAS00114362}.
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
//