ASM3_CAEEL
ID ASM3_CAEEL Reviewed; 589 AA.
AC Q9UAY4;
DT 19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Putative sphingomyelin phosphodiesterase asm-3;
DE EC=3.1.4.12;
DE Flags: Precursor;
GN Name=asm-3; ORFNames=W03G1.7;
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 [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: Converts sphingomyelin to ceramide.
CC {ECO:0000250|UniProtKB:Q10916}.
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=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 -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q10916}.
CC -!- MISCELLANEOUS: There are two types of sphingomyelinases: asm (acid),
CC and nsm (neutral). Only acid sphingomyelinase has been found in worms.
CC {ECO:0000250|UniProtKB:P17405, ECO:0000250|UniProtKB:Q10916}.
CC -!- SIMILARITY: Belongs to the acid sphingomyelinase family. {ECO:0000305}.
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DR EMBL; FO081096; CCD69084.1; -; Genomic_DNA.
DR PIR; T34001; T34001.
DR RefSeq; NP_001040996.1; NM_001047531.1.
DR AlphaFoldDB; Q9UAY4; -.
DR SMR; Q9UAY4; -.
DR STRING; 6239.W03G1.7a; -.
DR EPD; Q9UAY4; -.
DR PaxDb; Q9UAY4; -.
DR PeptideAtlas; Q9UAY4; -.
DR EnsemblMetazoa; W03G1.7a.1; W03G1.7a.1; WBGene00000213.
DR GeneID; 176879; -.
DR KEGG; cel:CELE_W03G1.7; -.
DR UCSC; W03G1.7b; c. elegans.
DR CTD; 176879; -.
DR WormBase; W03G1.7a; CE31626; WBGene00000213; asm-3.
DR eggNOG; KOG3770; Eukaryota.
DR GeneTree; ENSGT00950000183182; -.
DR HOGENOM; CLU_014743_3_0_1; -.
DR InParanoid; Q9UAY4; -.
DR OMA; VIDYEEW; -.
DR OrthoDB; 1142100at2759; -.
DR PhylomeDB; Q9UAY4; -.
DR UniPathway; UPA00222; -.
DR PRO; PR:Q9UAY4; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00000213; Expressed in adult organism and 1 other tissue.
DR ExpressionAtlas; Q9UAY4; baseline and differential.
DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005764; C:lysosome; IBA:GO_Central.
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; ISS:UniProtKB.
DR GO; GO:0046513; P:ceramide biosynthetic process; ISS:UniProtKB.
DR GO; GO:1905691; P:lipid droplet disassembly; IMP:UniProtKB.
DR GO; GO:0006685; P:sphingomyelin catabolic process; ISS:UniProtKB.
DR CDD; cd00842; MPP_ASMase; 1.
DR Gene3D; 3.60.21.10; -; 1.
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; 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 3: Inferred from homology;
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..589
FT /note="Putative sphingomyelin phosphodiesterase asm-3"
FT /id="PRO_0000002327"
FT DOMAIN 18..101
FT /note="Saposin B-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT REGION 562..589
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 139
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P17405"
FT BINDING 141
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P17405"
FT BINDING 217
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P17405"
FT BINDING 217
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P17405"
FT BINDING 257
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P17405"
FT BINDING 364
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P17405"
FT BINDING 398
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P17405"
FT BINDING 400
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P17405"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT CARBOHYD 237
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT CARBOHYD 334
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT CARBOHYD 463
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 21..97
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 24..89
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 52..63
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 154..159
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 160..188
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 530..535
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 541..553
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
SQ SEQUENCE 589 AA; 67451 MW; 7B23383D13062880 CRC64;
MLLGLLVLSL AFQGTLAVTE CEECKSIVDL LQFEWGEKKT EECVMEIAVF ICETFHIEDN
DVCNFIISDF SDEFMYVIKQ ILVTPHQLCG LLMKNDCGDF VDPLATIWNM TIPGNQPPFV
PKQVVPPGNP TLRALHLTDL HVDMFYTVGL EADCGTPQCC RPQDMNVEIV ENGDVKQPAG
PWGSVGSCDT PYWLLTNMLQ NIASTAGKLD YIMVSGDLVS HTVWAYTPET HSFMVKNLSD
TIRSYFPKTP VYFAVGNHEG VPVDNIAPHF TPKKYHMDWL YKAMSNAWQG WIPADQEKSL
EYNGCYMKKI YDGLRMISLN NVYGDRINFW LYINQTDPDG TLQWLINQLQ DAENVGDKVH
IVAHIPGSDG EALEGYALNY YKIINRYANT VVGQFFGHTH SEKFYMMYAN PDDYKSTPTN
VVYSAPSVTP YSDYFPAYRI YTIDGVHKGS TYQVIDYEEW FFNLTSNNAN PTNVKWEVLY
QSANMEYGLK GQIPTEYNQM IERMKTDDSL FNKYYENHNR RSIYDGRAPC NDQQCRNGYL
CDARQFHQTQ QLCTDLEGGI QKPEPKKNKY SARFATSNER RRGKEECKI
