ID A0A0L0BRT9_LUCCU Unreviewed; 634 AA. AC A0A0L0BRT9; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 30-AUG-2017, entry version 13. DE RecName: Full=Sphingomyelin phosphodiesterase {ECO:0000256|PIRNR:PIRNR000948}; DE EC=3.1.4.12 {ECO:0000256|PIRNR:PIRNR000948}; GN ORFNames=FF38_05078 {ECO:0000313|EMBL:KNC22713.1}; OS Lucilia cuprina (Green bottle fly) (Australian sheep blowfly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha; OC Oestroidea; Calliphoridae; Luciliinae; Lucilia. OX NCBI_TaxID=7375 {ECO:0000313|EMBL:KNC22713.1, ECO:0000313|Proteomes:UP000037069}; RN [1] {ECO:0000313|EMBL:KNC22713.1, ECO:0000313|Proteomes:UP000037069} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LS {ECO:0000313|EMBL:KNC22713.1, RC ECO:0000313|Proteomes:UP000037069}; RC TISSUE=Full body {ECO:0000313|EMBL:KNC22713.1}; RX PubMed=26108605; DOI=10.1038/ncomms8344; RA Anstead C.A., Korhonen P.K., Young N.D., Hall R.S., Jex A.R., RA Murali S.C., Hughes D.S., Lee S.F., Perry T., Stroehlein A.J., RA Ansell B.R., Breugelmans B., Hofmann A., Qu J., Dugan S., Lee S.L., RA Chao H., Dinh H., Han Y., Doddapaneni H.V., Worley K.C., Muzny D.M., RA Ioannidis P., Waterhouse R.M., Zdobnov E.M., James P.J., Bagnall N.H., RA Kotze A.C., Gibbs R.A., Richards S., Batterham P., Gasser R.B.; RT "Lucilia cuprina genome unlocks parasitic fly biology to underpin RT future interventions."; RL Nat. Commun. 6:7344-7344(2015). CC -!- FUNCTION: Converts sphingomyelin to ceramide. CC {ECO:0000256|PIRNR:PIRNR000948}. CC -!- CATALYTIC ACTIVITY: Sphingomyelin + H(2)O = N-acylsphingosine + CC phosphocholine. {ECO:0000256|PIRNR:PIRNR000948}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000948-1}; CC Note=Binds 2 Zn(2+) ions per subunit. CC {ECO:0000256|PIRSR:PIRSR000948-1}; CC -!- SIMILARITY: Belongs to the acid sphingomyelinase family. CC {ECO:0000256|PIRNR:PIRNR000948}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KNC22713.1}. 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; JRES01001458; KNC22713.1; -; Genomic_DNA. DR EnsemblMetazoa; KNC22713; KNC22713; FF38_05078. DR OMA; TWTREYN; -. DR Proteomes; UP000037069; Unassembled WGS sequence. DR GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004767; F:sphingomyelin phosphodiesterase activity; IEA:UniProtKB-UniRule. DR GO; GO:0006685; P:sphingomyelin catabolic process; IEA:UniProtKB-UniRule. DR Gene3D; 3.60.21.10; -; 1. DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH. DR InterPro; IPR029052; Metallo-depent_PP-like. DR InterPro; IPR011001; Saposin-like. DR InterPro; IPR008139; SaposinB_dom. DR InterPro; IPR011160; Sphingomy_PDE. DR Pfam; PF00149; Metallophos; 1. DR PIRSF; PIRSF000948; Sphingomy_PDE; 1. DR SUPFAM; SSF47862; SSF47862; 1. DR SUPFAM; SSF56300; SSF56300; 1. DR PROSITE; PS50015; SAP_B; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000037069}; KW Disulfide bond {ECO:0000256|PIRSR:PIRSR000948-2}; KW Glycosidase {ECO:0000256|PIRNR:PIRNR000948}; KW Hydrolase {ECO:0000256|PIRNR:PIRNR000948}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000948-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000037069}; KW Signal {ECO:0000256|SAM:SignalP}; KW Zinc {ECO:0000256|PIRSR:PIRSR000948-1}. FT SIGNAL 1 17 {ECO:0000256|SAM:SignalP}. FT CHAIN 18 634 Sphingomyelin phosphodiesterase. FT {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5005535143. FT DOMAIN 91 182 Saposin B-type. {ECO:0000259|PROSITE: FT PS50015}. FT METAL 220 220 Zinc 1. {ECO:0000256|PIRSR:PIRSR000948- FT 1}. FT METAL 222 222 Zinc 1; via tele nitrogen. FT {ECO:0000256|PIRSR:PIRSR000948-1}. FT METAL 293 293 Zinc 1. {ECO:0000256|PIRSR:PIRSR000948- FT 1}. FT METAL 293 293 Zinc 2. {ECO:0000256|PIRSR:PIRSR000948- FT 1}. FT METAL 333 333 Zinc 2. {ECO:0000256|PIRSR:PIRSR000948- FT 1}. FT METAL 441 441 Zinc 2; via tele nitrogen. FT {ECO:0000256|PIRSR:PIRSR000948-1}. FT METAL 475 475 Zinc 2; via pros nitrogen. FT {ECO:0000256|PIRSR:PIRSR000948-1}. FT METAL 477 477 Zinc 1; via tele nitrogen. FT {ECO:0000256|PIRSR:PIRSR000948-1}. FT DISULFID 95 178 {ECO:0000256|PIRSR:PIRSR000948-2}. FT DISULFID 98 170 {ECO:0000256|PIRSR:PIRSR000948-2}. FT DISULFID 133 144 {ECO:0000256|PIRSR:PIRSR000948-2}. FT DISULFID 235 240 {ECO:0000256|PIRSR:PIRSR000948-2}. FT DISULFID 241 264 {ECO:0000256|PIRSR:PIRSR000948-2}. FT DISULFID 400 449 {ECO:0000256|PIRSR:PIRSR000948-2}. FT DISULFID 598 602 {ECO:0000256|PIRSR:PIRSR000948-2}. FT DISULFID 608 621 {ECO:0000256|PIRSR:PIRSR000948-2}. SQ SEQUENCE 634 AA; 72121 MW; BC8C7F4A6A6CE09B CRC64; MLSKLILLAL LAVAVRGLNL PGVPVDFEQD DETLSAISQD IANKFSEEYV KFLETGVESS ILKQISTQLA KSHTKKDMFT KSIAELHSAD QFVMCTTCRS VANVIVETFR AEDGELNGPN AESTTKKMVL ELCNRFHIQT PEVCSGLVDL NWPILHYIIM NSLADTRSLC GMLPIRFCKV KQNNFNWSVK VDKGKGLLTA PKSDVPQKTE NDLNIVQITD IHFDPDYKVG ASAECEEPLC CRLNPLGGVS ESAKAGYWSD YRYCDAPLHM VENAFDHIKE THKKIDYIYQ TGDIVPHNVW TTSKEGNKAM LTQINDLMIE KFPDVQIFPS VGNHEPHPTN IFGNEDVPAE LSMNWLYEHL WSIWQRWLPD EAKETVLKGG YYTVSPKPGF RIISLNNNDC YIYNWWIYLD GSATSQPQLD WLQKTLLAAE KAGEYVHILA HIPSGESDCW TVWAREYNRI IERYSHIIGG IFGGHTHKDE MNLHYSQNGH AMAIYWNGGS LTSYSFKNPN YRTYDIEPVT YQVVDHHTWI FNVTEANELG ANGTPRWFKE YQFTEFTNDL SPAGIDALFE KMAAEPDVLL QFWKYKMTSA DPLVDAGCNE RCLLSTICHL VRTVYDEPGR CNELKAKLKE SLNY //