ID B5LBD0_9INFA Unreviewed; 443 AA. AC B5LBD0; DT 14-OCT-2008, integrated into UniProtKB/TrEMBL. DT 14-OCT-2008, sequence version 1. DT 08-JUN-2016, entry version 37. 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}; DE Flags: Fragment; GN Name=NA {ECO:0000256|RuleBase:RU361252, ECO:0000313|EMBL:ACF40959.1}; OS Influenza A virus (A/turkey/England/N28/1973(H5N2)). OC Viruses; ssRNA viruses; ssRNA negative-strand viruses; OC Orthomyxoviridae; Influenzavirus A. OX NCBI_TaxID=511839 {ECO:0000313|EMBL:ACF40959.1}; RN [1] {ECO:0000313|EMBL:ACF40959.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=A/turkey/England/N28/73 {ECO:0000313|EMBL:ACF40959.1}; RX PubMed=18753228; DOI=10.1099/vir.0.2008/001875-0; RA Zhao Z.M., Shortridge K.F., Garcia M., Guan Y., Wan X.F.; RT "Genotypic diversity of H5N1 highly pathogenic avian influenza RT viruses."; RL J. Gen. Virol. 89:2182-2193(2008). RN [2] {ECO:0000313|EMBL:ACF40959.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=A/turkey/England/N28/73 {ECO:0000313|EMBL:ACF40959.1}; RA Zhao Z., Garcia M., Guan Y., Shortridge K.F., Wan X.-F.; RL Submitted (APR-2008) 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 -!- 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}. 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; EU636686; ACF40959.1; -; 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:SAAS00475017}; KW Membrane {ECO:0000256|SAAS:SAAS00474571}; KW Metal-binding {ECO:0000256|RuleBase:RU361252, KW ECO:0000256|SAAS:SAAS00448775}; KW Transmembrane {ECO:0000256|SAAS:SAAS00474655}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00475130}; KW Virion {ECO:0000256|RuleBase:RU361252, ECO:0000256|SAAS:SAAS00448515}. FT NON_TER 1 1 {ECO:0000313|EMBL:ACF40959.1}. FT NON_TER 443 443 {ECO:0000313|EMBL:ACF40959.1}. SQ SEQUENCE 443 AA; 49079 MW; C196569260DDD8A4 CRC64; FLMQIAILAT TVTLHFKQHE CNPPAINQVT PCEPIIVERN ITEIVYLNST SIEREICPEA VEYRNWSKPQ CQITGFAPFS KDNSIRLSAG GDIWVTREPY VSCDPGKCYQ FALGQGTTLD NKHSNGTIHD RIPHRTLLMN ELGVPFHLGT KQVCIAWSSS SCHDGRAWLH ICVTGDDRNA TASFIYDGRL VDSIGSWSQN ILRTQESECV CINGTCTVVM TDGSASGRAD TRILFIKEGK IVHISPLSGS AQHIEECSCY PRYPDVRCIC RDNWKGSNRP VIDINMADYS IDSSYVCSGL VGDTPRNDDS SSSSNCRDPN NERGNPGVKG WAFDNGDDVW MGRTISKDSR SGYETFKVIG GWSTPNSKSQ VNRQVIVDNN NRSGYSGIFS VEGKSCINRC FYVELIRGRP QETRVWWTSN SIVVFCGTSG TYGTGSWPDG ANI //