ID K7PQX9_9INFA Unreviewed; 469 AA. AC K7PQX9; DT 06-FEB-2013, integrated into UniProtKB/TrEMBL. DT 06-FEB-2013, sequence version 1. DT 25-OCT-2017, entry version 31. 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: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 -!- 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:SAAS00612833}; CC -!- SUBUNIT: Homotetramer. {ECO:0000256|RuleBase:RU361252, CC ECO:0000256|SAAS:SAAS00114476}. CC -!- SUBCELLULAR LOCATION: Host apical cell membrane CC {ECO:0000256|SAAS:SAAS00582107}; Single-pass type II membrane CC protein {ECO:0000256|SAAS:SAAS00582107}. 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; 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-UniRule. DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-UniRule. 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 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, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|RuleBase:RU361252, KW ECO:0000256|SAAS:SAAS00114385}; KW Transmembrane {ECO:0000256|SAAS:SAAS00114524, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00114517, KW ECO:0000256|SAM:Phobius}; KW Virion {ECO:0000256|RuleBase:RU361252, ECO:0000256|SAAS:SAAS00114362}. 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 //