ID C6G5K0_9INFA Unreviewed; 469 AA. AC C6G5K0; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 27-MAY-2015, entry version 27. 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 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: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: 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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:SAAS00062903}; 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}; KW Metal-binding {ECO:0000256|RuleBase:RU361252, KW ECO:0000256|SAAS:SAAS00062292}; KW Transmembrane {ECO:0000256|SAAS:SAAS00114524}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00114517}; KW Virion {ECO:0000256|RuleBase:RU361252, ECO:0000256|SAAS:SAAS00063088}. 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 //