ID K7PQX9_9INFA Unreviewed; 469 AA. AC K7PQX9; DT 06-FEB-2013, integrated into UniProtKB/TrEMBL. DT 06-FEB-2013, sequence version 1. DT 05-OCT-2016, entry version 24. 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:AFP36186.1}; OS Influenza A virus (A/swine/Hungary/362/2011(H1N1)). OC Viruses; ssRNA viruses; ssRNA negative-strand viruses; OC Orthomyxoviridae; Influenzavirus A. OX NCBI_TaxID=1211898 {ECO:0000313|EMBL:AFP36186.1}; RN [1] {ECO:0000313|EMBL:AFP36186.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=A/swine/Hungary/362/2011 {ECO:0000313|EMBL:AFP36186.1}; RX PubMed=23118459; DOI=10.1128/JVI.02503-12; RA Banyai K., Kovacs E., Toth A.G., Biksi I., Szentpali-Gavaller K., RA Balint A., Dencso L., Dan A.; RT "Genome Sequence of a Monoreassortant H1N1 Swine Influenza Virus RT Isolated from a Pig in Hungary."; RL J. Virol. 86:13133-13133(2012). 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 -!- 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 membrane CC {ECO:0000256|SAAS:SAAS00561294}. 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; JX398001; AFP36186.1; -; 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 GO; GO:0046761; P:viral budding from plasma membrane; IEA:InterPro. DR CDD; cd15483; Influenza_NA; 1. DR Gene3D; 2.120.10.10; -; 1. DR InterPro; IPR001860; Glyco_hydro_34. DR InterPro; IPR033654; Sialidase_Influenza_A/B. 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 34 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 469 AA; 51628 MW; 86E2F63175D04F3A CRC64; MNPNQKIIII SSICMTNGIA SLILQIGSMI SIWISHSIQI GNQNQIETCN QSVIIYENKT WVNQTYVNIS NNNFVAEQTV VSVKLAGSSS LCPVSGWAIY SKDNSVRIGS KGDVFVIREP FISCSHLECR TFFLTQGALL NDKHSNGTVK DRSPYRTLMS CPIGEVPSPY NSKFESVAWS ASACHDGTSW LTIGISGPDN GAVAVLKYND IITDTIKSWK NNILRTQESE CACLNGSCFT VMTDGPSNGQ ASYKIFKIEK GKVVKSVELN APNYHYEECS CYPDSGEIIC VCRDNWHGSN RPWVSFNQNL EYQIGYICSG VLGDNPRPND RTGSCGPVSS HGANGVKGFS FKYGNGIWIG RTKSISSRSG FEMIWDPNGW TGTDNNYSVK QDIVGITDWS GYSGSFVQHP ELTGLDCIRP CFWVELIRGR PKENTIWTSG SSISFCGVNS DTVGWSWPDG AELPFIIDK //