ID L0CRQ8_9INFA Unreviewed; 469 AA. AC L0CRQ8; DT 06-MAR-2013, integrated into UniProtKB/TrEMBL. DT 06-MAR-2013, sequence version 1. DT 29-OCT-2014, entry version 10. DE SubName: Full=Neuraminidase {ECO:0000313|EMBL:AGA18963.1}; GN Name=NA {ECO:0000313|EMBL:AGA18963.1}; OS Influenza A virus (A/swine/Colombo/48/2004(H3N2)). OC Viruses; ssRNA negative-strand viruses; Orthomyxoviridae; OC Influenzavirus A. OX NCBI_TaxID=1262600 {ECO:0000313|EMBL:AGA18963.1}; RN [1] {ECO:0000313|EMBL:AGA18963.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=A/swine/Colombo/48/2004 {ECO:0000313|EMBL:AGA18963.1}; RX PubMed=23621918; DOI=10.3201/eid1903.120945; RA Perera H.K.K., Wickramasinghe G., Cheung C.L., Nishiura H., RA Smith D.K., Poon L.L.M., Perera A.K.C., Ma S.K., Sunil-Chandra N.P., RA Guan Y., Peiris J.S.M.; RT "Swine influenza in sri lanka."; RL Emerg. Infect. Dis. 19:481-484(2013). 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|SAAS:SAAS00062942}. CC -!- COFACTOR: Binds 1 calcium ion per subunit. CC {ECO:0000256|SAAS:SAAS00063080}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|SAAS:SAAS00063168}. CC -!- SUBCELLULAR LOCATION: Virion membrane CC {ECO:0000256|SAAS:SAAS00063102}. Host apical cell membrane CC {ECO:0000256|SAAS:SAAS00063102}; Single-pass type II membrane CC protein {ECO:0000256|SAAS:SAAS00063102}. 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; KC197816; AGA18963.1; -; 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:0004308; F:exo-alpha-sialidase activity; IEA:InterPro. 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 4: Predicted; KW Calcium {ECO:0000256|SAAS:SAAS00062903}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00063019}; KW Glycosidase {ECO:0000256|SAAS:SAAS00062426}; KW Host cell membrane {ECO:0000256|SAAS:SAAS00062854}; KW Host membrane {ECO:0000256|SAAS:SAAS00062524}; KW Hydrolase {ECO:0000256|SAAS:SAAS00063156}; KW Membrane {ECO:0000256|SAAS:SAAS00062477}; KW Metal-binding {ECO:0000256|SAAS:SAAS00062292}; KW Transmembrane {ECO:0000256|SAAS:SAAS00063177}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00063095}; KW Virion {ECO:0000256|SAAS:SAAS00063088}. SQ SEQUENCE 469 AA; 52107 MW; 8ADFA5823F7737DD CRC64; MNPNQKIITI GSVSLTISTI CFFMQIAILI TTVTLHFKQY EFNSPPNNQV MLCEPTIIER NITEIVYLTN TTIEKEICPK LAEYRNWSKP QCDITGFAPF SKDNSIRLSA GGDIWVTREP YVSCDPDKCY QFALGQGTTL NNVHSNDTVH DRTPYRTLLM NELGVPFHLG TKQVCIAWSS SSCHDGKAWL HVCVTGDDKN ATASFIYNGR LVDSIVSWSK KILRTQESEC VCINGTCTVV MTDGNVSGKA DTKILFIEEG KIVHTSTLSG SAQHVEECSC YPRYPGVRCV CRDNWKGSNR PIVDINIKDY SIVSSYVCSG LVGDTPRKND SSSSSHCLDP NNEEGGHGVK GWAFDDGNDV WMGRTISEKL RSGYETFKVI EGWSNPNSKL QINRQVIVDR GNRSGYSGIF SVEGKSCINR CFYVELIRGR KEETEVLWTS NSIVVFCGTS GTYGTGSWPD GADINLMPI //