ID B5LBD0_9INFA Unreviewed; 443 AA. AC B5LBD0; DT 14-OCT-2008, integrated into UniProtKB/TrEMBL. DT 14-OCT-2008, sequence version 1. DT 10-APR-2019, entry version 52. 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}; 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 Negarnaviricota; Polyploviricotina; Insthoviricetes; Articulavirales; OC Orthomyxoviridae; Alphainfluenzavirus. 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 -!- CATALYTIC ACTIVITY: CC Reaction=Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha- CC (2->8)- glycosidic linkages of terminal sialic acid residues in CC oligosaccharides, glycoproteins, glycolipids, colominic acid and CC synthetic substrates.; EC=3.2.1.18; CC Evidence={ECO:0000256|RuleBase:RU361252, CC ECO:0000256|SAAS:SAAS01126145}; CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; CC Evidence={ECO:0000256|RuleBase:RU361252, CC ECO:0000256|SAAS:SAAS00612833}; CC -!- ACTIVITY REGULATION: Inhibited by the neuraminidase inhibitors CC zanamivir (Relenza) and oseltamivir (Tamiflu). These drugs CC interfere with the release of progeny virus from infected cells CC and are effective against all influenza strains. Resistance to CC neuraminidase inhibitors is quite rare. CC {ECO:0000256|SAAS:SAAS01070481}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|RuleBase:RU361252, CC ECO:0000256|SAAS:SAAS00114476}. CC -!- SUBCELLULAR LOCATION: Host apical cell membrane CC {ECO:0000256|RuleBase:RU361252, ECO:0000256|SAAS:SAAS00582107}; CC Single-pass type II membrane protein CC {ECO:0000256|RuleBase:RU361252, ECO:0000256|SAAS:SAAS00582107}. CC Virion membrane {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:SAAS00582269}. 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-UniRule. DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell. DR GO; GO:0052794; F:exo-alpha-(2->3)-sialidase activity; IEA:UniProtKB-UniRule. DR GO; GO:0052795; F:exo-alpha-(2->6)-sialidase activity; IEA:UniProtKB-UniRule. DR GO; GO:0052796; F:exo-alpha-(2->8)-sialidase activity; IEA:UniProtKB-UniRule. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-UniRule. DR GO; GO:0046761; P:viral budding from plasma membrane; IEA:InterPro. DR CDD; cd15483; Influenza_NA; 1. DR HAMAP; MF_04071; INFV_NRAM; 1. DR InterPro; IPR001860; Glyco_hydro_34. DR InterPro; IPR033654; Sialidase_Influenza_A/B. DR InterPro; IPR036278; Sialidase_sf. 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}. 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 //