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Database: UniProt
Entry: A0A091DPL1_FUKDA
LinkDB: A0A091DPL1_FUKDA
Original site: A0A091DPL1_FUKDA 
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
//
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