ID   Y8017_DICDI             Reviewed;         458 AA.
AC   Q1ZXD9;
DT   24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Sphingomyelinase DDB_G0288017;
DE            EC=3.1.4.12;
GN   ORFNames=DDB_G0288017;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
CC   -!- FUNCTION: Catalyzes the hydrolysis of sphingomyelin to form ceramide
CC       and phosphocholine. {ECO:0000250}.
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
CC   -!- SIMILARITY: Belongs to the neutral sphingomyelinase family.
CC       {ECO:0000305}.
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; AAFI02000107; EAS66844.1; -; Genomic_DNA.
DR   RefSeq; XP_001134527.1; XM_001134527.1.
DR   AlphaFoldDB; Q1ZXD9; -.
DR   SMR; Q1ZXD9; -.
DR   PaxDb; Q1ZXD9; -.
DR   PRIDE; Q1ZXD9; -.
DR   EnsemblProtists; EAS66844; EAS66844; DDB_G0288017.
DR   GeneID; 8626414; -.
DR   KEGG; ddi:DDB_G0288017; -.
DR   dictyBase; DDB_G0288017; -.
DR   eggNOG; ENOG502S367; Eukaryota.
DR   HOGENOM; CLU_053972_0_0_1; -.
DR   InParanoid; Q1ZXD9; -.
DR   OMA; FIRPPGI; -.
DR   PhylomeDB; Q1ZXD9; -.
DR   UniPathway; UPA00222; -.
DR   PRO; PR:Q1ZXD9; -.
DR   Proteomes; UP000002195; Chromosome 5.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004620; F:phospholipase activity; IBA:GO_Central.
DR   GO; GO:0004767; F:sphingomyelin phosphodiesterase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006665; P:sphingolipid metabolic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd09078; nSMase; 1.
DR   Gene3D; 3.60.10.10; -; 1.
DR   InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR   InterPro; IPR005135; Endo/exonuclease/phosphatase.
DR   InterPro; IPR017766; Sphingomyelinase/PLipase_C.
DR   Pfam; PF03372; Exo_endo_phos; 1.
DR   SUPFAM; SSF56219; SSF56219; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Lipid metabolism; Magnesium; Metal-binding; Reference proteome;
KW   Sphingolipid metabolism.
FT   CHAIN           1..458
FT                   /note="Sphingomyelinase DDB_G0288017"
FT                   /id="PRO_0000389554"
FT   REGION          91..111
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        447
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         135
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   SITE            296
FT                   /note="Important for substrate recognition"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   458 AA;  51899 MW;  192EE444306C1404 CRC64;
     MTKTIKLLTY NVFIRPPGIK NNENDWKDER IECLISDSLS PHINYNKGSK SAQGIPNAVY
     SVDKTSFPYI PYFSPWKYPV YGKLMEVTGM NKKAKSPPPP SSLKQQNLHN NSSDYQSIAP
     SKSILAQYDI ICLQELFSAF SYRQRRFIEK AEQQGFQYYA TSPSPPYLRS TFLVDGGLTV
     ISKYPIVASD FFLYEQGVDS DMLSSKGVLY TKIKVVPTGS SNDDENFIHL FTTHMQASYA
     PKSDGSKTVK ASATQDQASN YKNDNIRLIQ LNQLREFIFE KTFKDKSIII LAGDLNVNGR
     VSKDDPKDGD SYLQMLELLS NSDQRDLPTG KKIFTIQDLL RDDFNGEHPP TVGDIKFLKD
     KKQEIPLETV LTNPNDFGCM KRLDYILLFN REFETSIDGV ELNFKVPSPT QPSKHSQQHN
     SISPLKGSTK VDPFFIQGFP FTQLSDHYGV STILQINK