ID A0A0L0BRT9_LUCCU Unreviewed; 634 AA. AC A0A0L0BRT9; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 27-MAR-2024, entry version 39. 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; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Oestroidea; OC 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., Murali S.C., RA Hughes D.S., Lee S.F., Perry T., Stroehlein A.J., Ansell B.R., RA Breugelmans B., Hofmann A., Qu J., Dugan S., Lee S.L., Chao H., Dinh H., RA Han Y., Doddapaneni H.V., Worley K.C., Muzny D.M., Ioannidis P., RA Waterhouse R.M., Zdobnov E.M., James P.J., Bagnall N.H., Kotze A.C., RA Gibbs R.A., Richards S., Batterham P., Gasser R.B.; RT "Lucilia cuprina genome unlocks parasitic fly biology to underpin future RT interventions."; RL Nat. Commun. 6:7344-7344(2015). CC -!- FUNCTION: Converts sphingomyelin to ceramide. CC {ECO:0000256|PIRNR:PIRNR000948}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a sphingomyelin + H2O = an N-acylsphing-4-enine + H(+) + CC phosphocholine; Xref=Rhea:RHEA:19253, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17636, ChEBI:CHEBI:52639, CC ChEBI:CHEBI:295975; EC=3.1.4.12; CC Evidence={ECO:0000256|ARBA:ARBA00023999}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19254; CC Evidence={ECO:0000256|ARBA:ARBA00023999}; 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. {ECO:0000256|PIRSR:PIRSR000948- CC 1}; CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}. CC -!- SIMILARITY: Belongs to the acid sphingomyelinase family. CC {ECO:0000256|ARBA:ARBA00008234, ECO:0000256|PIRNR:PIRNR000948}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {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 AlphaFoldDB; A0A0L0BRT9; -. DR STRING; 7375.A0A0L0BRT9; -. DR EnsemblMetazoa; KNC22713; KNC22713; FF38_05078. DR OMA; GCTFFRI; -. DR Proteomes; UP000037069; Unassembled WGS sequence. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. 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:0046513; P:ceramide biosynthetic process; IEA:UniProt. DR GO; GO:0006685; P:sphingomyelin catabolic process; IEA:UniProtKB-UniRule. DR CDD; cd00842; MPP_ASMase; 1. DR Gene3D; 3.60.21.10; -; 2. DR InterPro; IPR045473; ASM_C. DR InterPro; IPR041805; ASMase/PPN1_MPP. 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 PANTHER; PTHR10340; SPHINGOMYELIN PHOSPHODIESTERASE; 1. DR PANTHER; PTHR10340:SF29; SPHINGOMYELIN PHOSPHODIESTERASE; 1. DR Pfam; PF19272; ASMase_C; 1. DR Pfam; PF00149; Metallophos; 1. DR PIRSF; PIRSF000948; Sphingomy_PDE; 1. DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1. DR SUPFAM; SSF47862; Saposin; 1. DR PROSITE; PS50015; SAP_B; 1. PE 3: Inferred from homology; KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, KW ECO:0000256|PIRSR:PIRSR000948-2}; KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|PIRNR:PIRNR000948}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR000948}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|PIRSR:PIRSR000948-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000037069}; KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}; KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR000948-1}. FT SIGNAL 1..17 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 18..634 FT /note="Sphingomyelin phosphodiesterase" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5005535143" FT DOMAIN 91..182 FT /note="Saposin B-type" FT /evidence="ECO:0000259|PROSITE:PS50015" FT BINDING 220 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR000948-1" FT BINDING 222 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR000948-1" FT BINDING 293 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR000948-1" FT BINDING 293 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR000948-1" FT BINDING 333 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR000948-1" FT BINDING 441 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR000948-1" FT BINDING 475 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR000948-1" FT BINDING 477 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR000948-1" FT DISULFID 95..178 FT /evidence="ECO:0000256|PIRSR:PIRSR000948-2" FT DISULFID 98..170 FT /evidence="ECO:0000256|PIRSR:PIRSR000948-2" FT DISULFID 133..144 FT /evidence="ECO:0000256|PIRSR:PIRSR000948-2" FT DISULFID 235..240 FT /evidence="ECO:0000256|PIRSR:PIRSR000948-2" FT DISULFID 241..264 FT /evidence="ECO:0000256|PIRSR:PIRSR000948-2" FT DISULFID 400..449 FT /evidence="ECO:0000256|PIRSR:PIRSR000948-2" FT DISULFID 598..602 FT /evidence="ECO:0000256|PIRSR:PIRSR000948-2" FT DISULFID 608..621 FT /evidence="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 //