ID H2TS12_TAKRU Unreviewed; 582 AA.
AC H2TS12;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 3.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=Sphingomyelin phosphodiesterase {ECO:0000256|PIRNR:PIRNR000948};
DE EC=3.1.4.12 {ECO:0000256|PIRNR:PIRNR000948};
GN Name=smpd1 {ECO:0000313|Ensembl:ENSTRUP00000027470.3};
OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000027470.3, ECO:0000313|Proteomes:UP000005226};
RN [1] {ECO:0000313|Ensembl:ENSTRUP00000027470.3, ECO:0000313|Proteomes:UP000005226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21551351;
RA Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A., Hosoya S.,
RA Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.;
RT "Integration of the genetic map and genome assembly of fugu facilitates
RT insights into distinct features of genome evolution in teleosts and
RT mammals.";
RL Genome Biol. Evol. 3:424-442(2011).
RN [2] {ECO:0000313|Ensembl:ENSTRUP00000027470.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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 AlphaFoldDB; H2TS12; -.
DR STRING; 31033.ENSTRUP00000088389; -.
DR Ensembl; ENSTRUT00000027579.3; ENSTRUP00000027470.3; ENSTRUG00000010870.3.
DR eggNOG; KOG3770; Eukaryota.
DR GeneTree; ENSGT00950000183182; -.
DR HOGENOM; CLU_014743_3_1_1; -.
DR TreeFam; TF313674; -.
DR Proteomes; UP000005226; Chromosome 15.
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 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; PS51257; PROKAR_LIPOPROTEIN; 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:UP000005226};
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..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..582
FT /note="Sphingomyelin phosphodiesterase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5025462291"
FT DOMAIN 45..129
FT /note="Saposin B-type"
FT /evidence="ECO:0000259|PROSITE:PS50015"
FT BINDING 166
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000948-1"
FT BINDING 168
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000948-1"
FT BINDING 238
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000948-1"
FT BINDING 238
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000948-1"
FT BINDING 279
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000948-1"
FT BINDING 386
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000948-1"
FT BINDING 418
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000948-1"
FT BINDING 420
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000948-1"
FT DISULFID 49..125
FT /evidence="ECO:0000256|PIRSR:PIRSR000948-2"
FT DISULFID 52..117
FT /evidence="ECO:0000256|PIRSR:PIRSR000948-2"
FT DISULFID 80..91
FT /evidence="ECO:0000256|PIRSR:PIRSR000948-2"
FT DISULFID 181..186
FT /evidence="ECO:0000256|PIRSR:PIRSR000948-2"
FT DISULFID 187..210
FT /evidence="ECO:0000256|PIRSR:PIRSR000948-2"
FT DISULFID 346..392
FT /evidence="ECO:0000256|PIRSR:PIRSR000948-2"
FT DISULFID 550..554
FT /evidence="ECO:0000256|PIRSR:PIRSR000948-2"
SQ SEQUENCE 582 AA; 66341 MW; C8C9D58AF17C136D CRC64;
MRLPLAVLVS FSVVFGSCSP APGPEQNRLT FFEHLGHTGF KFSWRNLTCP TCKALFVILD
IALLTDTNEE HVARTAGEVC IRLHLAEERV CRSITELFRD DFIRALQRSL LLPREACALL
VGPSCGKYDI YAPWNVTLPG IPKPPVTPPS LPKPGSPQSR ILFLTDVHWD QEYTAGTTAD
CKEPLCCRKD SGFPSWRRRE AGYWGTYGKC DLPLRTVENL LENVAAAGAW DWVYWTGDIP
AHNIWSQTRT QQLSELTVIS RLIHKHLGPK VKVYPAVGNH ESTPVNSFPP PFIHGNRSSS
WLYNTMAEEW SPWLSEQAVK TLRYGGFYTM EIQPGLRVVS LNMNFCAAEN FWLLVNSTDP
ADQLQWLVHV LQESELKGEK VHIIGHIPPG LCLSSWSWNY YHIVNRYEST VTGQFFGHTH
MDEFEMFFDE ADKTRPFGVA FIAPSITTYV DLNPGYRVYY VDGNYKGSSR LVLDHETYIL
NLTEANHSPG SGKPVQDPKW ELLYRAREAY ALPSLFPADL DTLIQTFVKD DRFFQKFWYF
KHKGHVSEPC KDACKTTEIC LLRMNFSLFS HPLQCSNCVV LW
//
