ID A0A091DPL1_FUKDA Unreviewed; 618 AA.
AC A0A091DPL1;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE RecName: Full=Sphingomyelin phosphodiesterase {ECO:0000256|PIRNR:PIRNR000948};
DE EC=3.1.4.12 {ECO:0000256|PIRNR:PIRNR000948};
GN ORFNames=H920_13877 {ECO:0000313|EMBL:KFO24726.1};
OS Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Fukomys.
OX NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO24726.1, ECO:0000313|Proteomes:UP000028990};
RN [1] {ECO:0000313|EMBL:KFO24726.1, ECO:0000313|Proteomes:UP000028990}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Liver {ECO:0000313|EMBL:KFO24726.1};
RA Gladyshev V.N., Fang X.;
RT "The Damaraland mole rat (Fukomys damarensis) genome and evolution of
RT African mole rats.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; KN123504; KFO24726.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091DPL1; -.
DR STRING; 885580.ENSFDAP00000019591; -.
DR eggNOG; KOG3770; Eukaryota.
DR Proteomes; UP000028990; 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; -; 1.
DR Gene3D; 1.10.225.10; Saposin-like; 1.
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:SF34; SPHINGOMYELIN PHOSPHODIESTERASE; 1.
DR Pfam; PF19272; ASMase_C; 1.
DR Pfam; PF00149; Metallophos; 1.
DR PIRSF; PIRSF000948; Sphingomy_PDE; 1.
DR SMART; SM00741; SapB; 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:UP000028990};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR000948-1}.
FT DOMAIN 83..167
FT /note="Saposin B-type"
FT /evidence="ECO:0000259|PROSITE:PS50015"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 195
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000948-1"
FT BINDING 197
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000948-1"
FT BINDING 267
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000948-1"
FT BINDING 267
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000948-1"
FT BINDING 307
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000948-1"
FT BINDING 414
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000948-1"
FT BINDING 446
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000948-1"
FT BINDING 448
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000948-1"
FT DISULFID 87..163
FT /evidence="ECO:0000256|PIRSR:PIRSR000948-2"
FT DISULFID 90..155
FT /evidence="ECO:0000256|PIRSR:PIRSR000948-2"
FT DISULFID 118..129
FT /evidence="ECO:0000256|PIRSR:PIRSR000948-2"
FT DISULFID 210..215
FT /evidence="ECO:0000256|PIRSR:PIRSR000948-2"
FT DISULFID 216..239
FT /evidence="ECO:0000256|PIRSR:PIRSR000948-2"
FT DISULFID 374..420
FT /evidence="ECO:0000256|PIRSR:PIRSR000948-2"
FT DISULFID 573..577
FT /evidence="ECO:0000256|PIRSR:PIRSR000948-2"
FT DISULFID 583..596
FT /evidence="ECO:0000256|PIRSR:PIRSR000948-2"
SQ SEQUENCE 618 AA; 68889 MW; 822347559FEE4969 CRC64;
MPPHGASPSQ GHSSSGWEPG PERPTGAPRL GCLWLGLGLM VVLTLPDPKV LWAPARAHPL
PAQSYPGRFR GIMPQLQAAF GWWNLTCPVC KGLFTAIDFG LKKEPNVERV GSIATTLCKL
LKIAPPKVCQ SAVHLFEDDM IEVWTRSVLS PSEACGLLLG STCGNWDIFS SWNITLTAVP
KPPGAPVSRI LFLTDLHWDH DYLEGTDPNC VDPLCCRRGS GLPPPSKPGA GYWGEYSKCD
LPLRTLESML SGLGQAGPFD MVYWTGDIPA HDVWQQSRKD QLRALNTITD LVKKFLGPVP
VYPAVGNHES TPVNSFPPPF IKGNHSSNWL YEAMAKTWEP WLPAEALQTL RIGGFYALSP
RPGLRLISLN MNFCSRENFW LLINSTDPAG QLQWLIQELQ AAEDRGDKVH IIGHIPPGHC
LKSWSWNYYQ IVSRYENTLA GQFFGHTHVD EFEIFYDEET LSRPLSVAFL APSATTYIGL
NPGYRVYQID GNYSGSSHVV LDHETYILNL TQANAPGATP HWQRLYRARE TYGLPDALPA
AWHNLVYRMR DDARLFQTFW FLYHKGHPPP EPCGTPCRLT TLCAQLSARA DSPALCRHLV
PNESLLDVQR LSPRPLFC
//