ASM1_CAEEL
ID ASM1_CAEEL Reviewed; 564 AA.
AC Q10916;
DT 19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Sphingomyelin phosphodiesterase 1;
DE EC=3.1.4.12 {ECO:0000269|PubMed:9603947};
DE AltName: Full=Acid sphingomyelinase 1;
DE Short=ASM-1 {ECO:0000303|PubMed:9603947};
DE Flags: Precursor;
GN Name=asm-1; ORFNames=B0252.2;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY,
RP SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=9603947; DOI=10.1074/jbc.273.23.14374;
RA Lin X., Hengartner M.O., Kolesnick R.;
RT "Caenorhabditis elegans contains two distinct acid sphingomyelinases.";
RL J. Biol. Chem. 273:14374-14379(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- FUNCTION: Sphingomyelin phosphodiesterase (sphingomyelinase) that
CC converts sphingomyelin to ceramide (N-acyl-sphingoid base) and
CC phosphocholine at acidic pH. Displays its enzymatic activity when
CC secreted. May play distinct roles in signaling.
CC {ECO:0000269|PubMed:9603947}.
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:0000269|PubMed:9603947};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19254;
CC Evidence={ECO:0000269|PubMed:9603947};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-acyl-15-methylhexadecasphing-4-enine-1-phosphocholine
CC = H(+) + N-acyl-15-methylhexadecasphing-4-enine + phosphocholine;
CC Xref=Rhea:RHEA:34739, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:70775, ChEBI:CHEBI:70846, ChEBI:CHEBI:295975;
CC Evidence={ECO:0000305|PubMed:9603947};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:34740;
CC Evidence={ECO:0000305|PubMed:9603947};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q92484};
CC Note=Binds 2 Zn(2+) per subunit. {ECO:0000250|UniProtKB:Q92484};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=92 uM for sphingomyelin (at pH 5.0) {ECO:0000269|PubMed:9603947};
CC Vmax=2.9 mmol/h/mg enzyme with sphingomyelin as substrate (at pH 5.0)
CC {ECO:0000269|PubMed:9603947};
CC -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
CC {ECO:0000269|PubMed:9603947}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9603947}.
CC -!- DEVELOPMENTAL STAGE: Preferentially expressed in embryos, lower
CC expression in later development. {ECO:0000269|PubMed:9603947}.
CC -!- MISCELLANEOUS: There are two types of sphingomyelinases: asm (acid),
CC and nsm (neutral). Only acid sphingomyelinases have been found in
CC worms. {ECO:0000250|UniProtKB:P17405, ECO:0000269|PubMed:9603947}.
CC -!- MISCELLANEOUS: Does not require zinc ions as a cofactor.
CC {ECO:0000269|PubMed:9603947}.
CC -!- SIMILARITY: Belongs to the acid sphingomyelinase family. {ECO:0000305}.
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DR EMBL; FO080139; CCD61537.1; -; Genomic_DNA.
DR PIR; T15291; T15291.
DR RefSeq; NP_495415.2; NM_063014.6.
DR AlphaFoldDB; Q10916; -.
DR SMR; Q10916; -.
DR STRING; 6239.B0252.2; -.
DR SwissLipids; SLP:000000009; -.
DR EPD; Q10916; -.
DR PaxDb; Q10916; -.
DR PeptideAtlas; Q10916; -.
DR EnsemblMetazoa; B0252.2.1; B0252.2.1; WBGene00000211.
DR GeneID; 174131; -.
DR KEGG; cel:CELE_B0252.2; -.
DR UCSC; B0252.2; c. elegans.
DR CTD; 174131; -.
DR WormBase; B0252.2; CE30230; WBGene00000211; asm-1.
DR eggNOG; KOG3770; Eukaryota.
DR GeneTree; ENSGT00950000183182; -.
DR HOGENOM; CLU_014743_3_0_1; -.
DR InParanoid; Q10916; -.
DR OMA; YSIEEHL; -.
DR OrthoDB; 1142100at2759; -.
DR PhylomeDB; Q10916; -.
DR UniPathway; UPA00222; -.
DR PRO; PR:Q10916; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00000211; Expressed in embryo and 3 other tissues.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005764; C:lysosome; IDA:WormBase.
DR GO; GO:0061750; F:acid sphingomyelin phosphodiesterase activity; IBA:GO_Central.
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:0008081; F:phosphoric diester hydrolase activity; IBA:GO_Central.
DR GO; GO:0004767; F:sphingomyelin phosphodiesterase activity; IDA:UniProtKB.
DR GO; GO:0046513; P:ceramide biosynthetic process; IDA:UniProtKB.
DR GO; GO:0006685; P:sphingomyelin catabolic process; IDA:UniProtKB.
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 Pfam; PF19272; ASMase_C; 1.
DR Pfam; PF00149; Metallophos; 1.
DR PIRSF; PIRSF000948; Sphingomy_PDE; 1.
DR SMART; SM00741; SapB; 1.
DR SUPFAM; SSF47862; SSF47862; 1.
DR SUPFAM; SSF56300; SSF56300; 1.
DR PROSITE; PS50015; SAP_B; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Glycosidase; Hydrolase; Lipid metabolism;
KW Metal-binding; Reference proteome; Secreted; Signal;
KW Sphingolipid metabolism; Zinc.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..564
FT /note="Sphingomyelin phosphodiesterase 1"
FT /id="PRO_0000002325"
FT DOMAIN 37..121
FT /note="Saposin B-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT BINDING 165
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P17405"
FT BINDING 167
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P17405"
FT BINDING 234
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P17405"
FT BINDING 234
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P17405"
FT BINDING 274
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P17405"
FT BINDING 381
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P17405"
FT BINDING 415
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P17405"
FT BINDING 417
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P17405"
FT CARBOHYD 151
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT CARBOHYD 221
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT CARBOHYD 351
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT CARBOHYD 430
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT CARBOHYD 556
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 41..117
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 44..110
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 72..83
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 180..185
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 186..206
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 341..389
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 538..542
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 548..561
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
SQ SEQUENCE 564 AA; 65201 MW; EE3C424B5D905159 CRC64;
MRIIYLISTV LLIYTNATVL RTKESIQNKV TYDKYGFQPL CISCTGLISV ASFFLKFDVS
EPVILEFATI VCKLFAKQPW AVCDGISSQF RDEFFYVFRR LANESPSQIC GIILPDCADP
TDPSESGWMV ALPPKPKRTR ISKKKVQKKP NMSMSQNLNV LQLTDLHVDF EYKYPSEANC
DDPVCCRVSV SEPKKAAGYW GSVGKCDIPF WTVENMLSHI NKTHMIDMVI MTGDYINHVD
WEYSIEEHLS VLRKLHRLVQ NTFPSTPIYW ALGNHEGVPV NSFAPHSVDE RFWPTWLYKE
FQTMSGPWLS EGAKDSLLKR GSYSTQVMDG LKLITLNTGF CEVTNFFLYL NQSDPDSSMS
WFVKELFESE KKGEQVYVLA HIPPGDSECL EGWAFNYYRV IQRFSSTIAA QFFGHDHLDY
FTVFYEDMHN VSSKPISVGY ASPSVTTFEY QNPAYRIYEI DPYNKFKIVD FTTYYADLEK
ATEDKKPVWE KLYSARQAHG MDDLSPLSWN KVIQKLFTSE KKREKFYQYA FRNFSPQCDS
TCQMQLMCNL RMGHHNSTLY CPTF
