SGPL_CAEEL
ID SGPL_CAEEL Reviewed; 552 AA.
AC Q9Y194;
DT 24-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Sphingosine-1-phosphate lyase;
DE Short=S1PL;
DE Short=SP-lyase;
DE Short=SPL {ECO:0000303|PubMed:12682045};
DE EC=4.1.2.27 {ECO:0000269|PubMed:12682045};
DE AltName: Full=Sphingosine-1-phosphate aldolase;
GN Name=spl-1; ORFNames=Y66H1B.4;
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 [MRNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=12682045; DOI=10.1074/jbc.m302857200;
RA Mendel J., Heinecke K., Fyrst H., Saba J.D.;
RT "Sphingosine phosphate lyase expression is essential for normal development
RT in Caenorhabditis elegans.";
RL J. Biol. Chem. 278:22341-22349(2003).
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: Cleaves phosphorylated sphingoid bases (PSBs or S1Ps) at the
CC C2-3 carbon bond to yield a fatty aldehyde and phosphoethanolamine.
CC These bioactive sphingolipid metabolites are essential for normal
CC development, intestinal integrity, growth and reproduction.
CC {ECO:0000269|PubMed:12682045}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=sphinganine 1-phosphate = hexadecanal + phosphoethanolamine;
CC Xref=Rhea:RHEA:18593, ChEBI:CHEBI:17600, ChEBI:CHEBI:57939,
CC ChEBI:CHEBI:58190; EC=4.1.2.27;
CC Evidence={ECO:0000269|PubMed:12682045};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18594;
CC Evidence={ECO:0000269|PubMed:12682045};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=15-methylhexadecasphing-4-enine 1-phosphate = (2E)-13-
CC methyltetradecenal + phosphoethanolamine; Xref=Rhea:RHEA:34719,
CC ChEBI:CHEBI:58190, ChEBI:CHEBI:70991, ChEBI:CHEBI:70995;
CC Evidence={ECO:0000305|PubMed:12682045};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:34720;
CC Evidence={ECO:0000305|PubMed:12682045};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=15-methylhexadecasphinganine 1-phosphate = 13-
CC methyltetradecanal + phosphoethanolamine; Xref=Rhea:RHEA:34743,
CC ChEBI:CHEBI:58190, ChEBI:CHEBI:71030, ChEBI:CHEBI:71034;
CC Evidence={ECO:0000305|PubMed:12682045};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:34744;
CC Evidence={ECO:0000305|PubMed:12682045};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
CC {ECO:0000269|PubMed:12682045}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Single-pass type III membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: High expression found in the intestinal cells and
CC faint expression in the head. {ECO:0000269|PubMed:12682045}.
CC -!- DEVELOPMENTAL STAGE: Found in the majority of L1 larvae and in all L2,
CC L3 and L4 larvae and adults showing medium to high expression. Highest
CC levels found in older adults. {ECO:0000269|PubMed:12682045}.
CC -!- DISRUPTION PHENOTYPE: Without spl-1 expression, animals become bloated,
CC pale, congested with eggs and hatched larvae, and demonstrate shrunken
CC gut and gonadal structures. {ECO:0000269|PubMed:12682045}.
CC -!- SIMILARITY: Belongs to the group II decarboxylase family. Sphingosine-
CC 1-phosphate lyase subfamily. {ECO:0000305}.
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DR EMBL; AF144639; AAD44756.1; -; mRNA.
DR EMBL; FO081175; CCD69676.1; -; Genomic_DNA.
DR PIR; T33760; T33760.
DR RefSeq; NP_499913.1; NM_067512.5.
DR AlphaFoldDB; Q9Y194; -.
DR SMR; Q9Y194; -.
DR BioGRID; 42019; 5.
DR IntAct; Q9Y194; 1.
DR STRING; 6239.Y66H1B.4; -.
DR SwissLipids; SLP:000000008; -.
DR EPD; Q9Y194; -.
DR PaxDb; Q9Y194; -.
DR PeptideAtlas; Q9Y194; -.
DR EnsemblMetazoa; Y66H1B.4.1; Y66H1B.4.1; WBGene00004981.
DR GeneID; 176857; -.
DR KEGG; cel:CELE_Y66H1B.4; -.
DR UCSC; Y66H1B.4; c. elegans.
DR CTD; 176857; -.
DR WormBase; Y66H1B.4; CE20348; WBGene00004981; spl-1.
DR eggNOG; KOG1383; Eukaryota.
DR HOGENOM; CLU_028929_1_0_1; -.
DR InParanoid; Q9Y194; -.
DR OMA; AFWQLRG; -.
DR OrthoDB; 517323at2759; -.
DR PhylomeDB; Q9Y194; -.
DR Reactome; R-CEL-1660661; Sphingolipid de novo biosynthesis.
DR UniPathway; UPA00222; -.
DR PRO; PR:Q9Y194; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00004981; Expressed in adult organism and 4 other tissues.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008117; F:sphinganine-1-phosphate aldolase activity; IBA:GO_Central.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR GO; GO:0030149; P:sphingolipid catabolic process; IBA:GO_Central.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR Pfam; PF00282; Pyridoxal_deC; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Lipid metabolism; Lyase; Membrane;
KW Pyridoxal phosphate; Reference proteome; Signal-anchor;
KW Sphingolipid metabolism; Transmembrane; Transmembrane helix.
FT CHAIN 1..552
FT /note="Sphingosine-1-phosphate lyase"
FT /id="PRO_0000147015"
FT TOPO_DOM 1..31
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 32..52
FT /note="Helical; Signal-anchor for type III membrane
FT protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 53..552
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 347
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 552 AA; 61097 MW; D12FFE7EBE9D3CFC CRC64;
MDSVKHTTEI IVDLTKMHYH MINDRLSRYD PVVLVLAAFG GTLVYTKVVH LYRKSEDPIL
KRMGAYVFSL LRKLPAVRDK IEKELAAEKP KLIESIHKDD KDKQFISTLP IAPLSQDSIM
ELAKKYEDYN TFNIDGGRVS GAVYTDRHAE HINLLGKIYE KYAFSNPLHP DVFPGARKME
AELIRMVLNL YNGPEDSSGS VTSGGTESII MACFSYRNRA HSLGIEHPVI LACKTAHAAF
DKAAHLCGMR LRHVPVDSDN RVDLKEMERL IDSNVCMLVG SAPNFPSGTI DPIPEIAKLG
KKYGIPVHVD ACLGGFMIPF MNDAGYLIPV FDFRNPGVTS ISCDTHKYGC TPKGSSIVMY
RSKELHHFQY FSVADWCGGI YATPTIAGSR AGANTAVAWA TLLSFGRDEY VRRCAQIVKH
TRMLAEKIEK IKWIKPYGKS DVSLVAFSGN GVNIYEVSDK MMKLGWNLNT LQNPAAIHIC
LTINQANEEV VNAFAVDLEK ICEELAAKGE QKADSGMAAM YGMAAQVPKS VVDEVIALYI
DATYSAPPST SN
