ID K7PQX9_9INFA Unreviewed; 469 AA. AC K7PQX9; DT 06-FEB-2013, integrated into UniProtKB/TrEMBL. DT 06-FEB-2013, sequence version 1. DT 28-MAR-2018, entry version 35. DE RecName: Full=Neuraminidase {ECO:0000256|HAMAP-Rule:MF_04071, ECO:0000256|RuleBase:RU361252, ECO:0000256|SAAS:SAAS00114532}; DE EC=3.2.1.18 {ECO:0000256|HAMAP-Rule:MF_04071, ECO:0000256|RuleBase:RU361252, ECO:0000256|SAAS:SAAS00114514}; GN Name=NA {ECO:0000256|HAMAP-Rule:MF_04071, GN 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|HAMAP-Rule:MF_04071, CC ECO:0000256|RuleBase:RU361252, ECO:0000256|SAAS:SAAS00114528}. CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000256|HAMAP- CC Rule:MF_04071, ECO:0000256|RuleBase:RU361252, CC ECO:0000256|SAAS:SAAS00612833}; CC -!- ENZYME 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. {ECO:0000256|HAMAP- CC Rule:MF_04071}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_04071, CC ECO:0000256|RuleBase:RU361252, 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 -!- DOMAIN: Intact N-terminus is essential for virion morphogenesis. CC Possess two apical sorting signals, one in the ectodomain, which CC is likely to be a glycan, and the other in the transmembrane CC domain. The transmembrane domain also plays a role in lipid raft CC association. {ECO:0000256|HAMAP-Rule:MF_04071}. CC -!- PTM: N-glycosylated. {ECO:0000256|HAMAP-Rule:MF_04071, CC ECO:0000256|RuleBase:RU361252}. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 34 family. CC {ECO:0000256|HAMAP-Rule:MF_04071, ECO:0000256|RuleBase:RU361252, CC ECO:0000256|SAAS:SAAS00582269}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|HAMAP-Rule:MF_04071}. 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-UniRule. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-UniRule. DR GO; GO:0046761; P:viral budding from plasma membrane; IEA:UniProtKB-UniRule. 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|HAMAP-Rule:MF_04071, KW ECO:0000256|RuleBase:RU361252, ECO:0000256|SAAS:SAAS00114513}; KW Disulfide bond {ECO:0000256|HAMAP-Rule:MF_04071, KW ECO:0000256|SAAS:SAAS00114594}; KW Glycoprotein {ECO:0000256|HAMAP-Rule:MF_04071, KW ECO:0000256|RuleBase:RU361252}; KW Glycosidase {ECO:0000256|HAMAP-Rule:MF_04071, KW ECO:0000256|RuleBase:RU361252, ECO:0000256|SAAS:SAAS00114535}; KW Host cell membrane {ECO:0000256|HAMAP-Rule:MF_04071, KW ECO:0000256|RuleBase:RU361252, ECO:0000256|SAAS:SAAS00114522}; KW Host membrane {ECO:0000256|HAMAP-Rule:MF_04071, KW ECO:0000256|RuleBase:RU361252, ECO:0000256|SAAS:SAAS00114565}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_04071, KW ECO:0000256|RuleBase:RU361252, ECO:0000256|SAAS:SAAS00114491}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_04071, KW ECO:0000256|SAAS:SAAS00114461}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_04071, KW ECO:0000256|RuleBase:RU361252, ECO:0000256|SAAS:SAAS00114385}; KW Signal-anchor {ECO:0000256|HAMAP-Rule:MF_04071}; KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_04071, KW ECO:0000256|SAAS:SAAS00114524}; KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_04071, KW ECO:0000256|SAAS:SAAS00114517}; KW Virion {ECO:0000256|HAMAP-Rule:MF_04071, KW ECO:0000256|RuleBase:RU361252, ECO:0000256|SAAS:SAAS00114362}. FT TRANSMEM 7 34 Helical. {ECO:0000256|HAMAP-Rule: FT MF_04071}. FT REGION 11 33 Involved in apical transport and lipid FT raft association. {ECO:0000256|HAMAP- FT Rule:MF_04071}. FT REGION 91 469 Head of neuraminidase. FT {ECO:0000256|HAMAP-Rule:MF_04071}. FT REGION 277 278 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_04071}. FT ACT_SITE 151 151 Proton donor/acceptor. FT {ECO:0000256|HAMAP-Rule:MF_04071}. FT ACT_SITE 402 402 Nucleophile. {ECO:0000256|HAMAP-Rule: FT MF_04071}. FT METAL 294 294 Calcium; via carbonyl oxygen. FT {ECO:0000256|HAMAP-Rule:MF_04071}. FT METAL 298 298 Calcium; via carbonyl oxygen. FT {ECO:0000256|HAMAP-Rule:MF_04071}. FT METAL 324 324 Calcium. {ECO:0000256|HAMAP-Rule: FT MF_04071}. FT METAL 344 344 Calcium; via carbonyl oxygen. FT {ECO:0000256|HAMAP-Rule:MF_04071}. FT BINDING 118 118 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_04071}. FT BINDING 152 152 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_04071}. FT BINDING 293 293 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_04071}. FT BINDING 368 368 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_04071}. FT DISULFID 92 417 {ECO:0000256|HAMAP-Rule:MF_04071}. FT DISULFID 124 129 {ECO:0000256|HAMAP-Rule:MF_04071}. FT DISULFID 184 231 {ECO:0000256|HAMAP-Rule:MF_04071}. FT DISULFID 233 238 {ECO:0000256|HAMAP-Rule:MF_04071}. FT DISULFID 279 292 {ECO:0000256|HAMAP-Rule:MF_04071}. FT DISULFID 281 290 {ECO:0000256|HAMAP-Rule:MF_04071}. FT DISULFID 318 335 {ECO:0000256|HAMAP-Rule:MF_04071}. FT DISULFID 421 446 {ECO:0000256|HAMAP-Rule:MF_04071}. 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 //