SGPL_DROME
ID SGPL_DROME Reviewed; 545 AA.
AC Q9V7Y2; Q0E946;
DT 24-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Sphingosine-1-phosphate lyase {ECO:0000305};
DE Short=S1PL;
DE Short=SP-lyase;
DE Short=SPL;
DE EC=4.1.2.27 {ECO:0000269|PubMed:12702658};
DE AltName: Full=Sphingosine-1-phosphate aldolase;
GN Name=Sply {ECO:0000312|FlyBase:FBgn0010591}; Synonyms=Spl; ORFNames=CG8946;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Van Veldhoven P.P.;
RT "Functional expression of sphingosine-phosphate lyase from Arabidopsis and
RT Drosophila.";
RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12702658; DOI=10.1242/dev.00456;
RA Herr D.R., Fyrst H., Phan V., Heinecke K., Georges R., Harris G.L.,
RA Saba J.D.;
RT "Sply regulation of sphingolipid signaling molecules is essential for
RT Drosophila development.";
RL Development 130:2443-2453(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [6]
RP FUNCTION, PATHWAY, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF GLU-119;
RP ARG-210 AND SER-335.
RX PubMed=28165339; DOI=10.1172/jci89626;
RA Lovric S., Goncalves S., Gee H.Y., Oskouian B., Srinivas H., Choi W.I.,
RA Shril S., Ashraf S., Tan W., Rao J., Airik M., Schapiro D., Braun D.A.,
RA Sadowski C.E., Widmeier E., Jobst-Schwan T., Schmidt J.M., Girik V.,
RA Capitani G., Suh J.H., Lachaussee N., Arrondel C., Patat J., Gribouval O.,
RA Furlano M., Boyer O., Schmitt A., Vuiblet V., Hashmi S., Wilcken R.,
RA Bernier F.P., Innes A.M., Parboosingh J.S., Lamont R.E., Midgley J.P.,
RA Wright N., Majewski J., Zenker M., Schaefer F., Kuss N., Greil J.,
RA Giese T., Schwarz K., Catheline V., Schanze D., Franke I., Sznajer Y.,
RA Truant A.S., Adams B., Desir J., Biemann R., Pei Y., Ars E., Lloberas N.,
RA Madrid A., Dharnidharka V.R., Connolly A.M., Willing M.C., Cooper M.A.,
RA Lifton R.P., Simons M., Riezman H., Antignac C., Saba J.D., Hildebrandt F.;
RT "Mutations in sphingosine-1-phosphate lyase cause nephrosis with ichthyosis
RT and adrenal insufficiency.";
RL J. Clin. Invest. 127:912-928(2017).
CC -!- FUNCTION: Cleaves phosphorylated sphingoid bases (PSBs), such as
CC sphingosine-1-phosphate, into fatty aldehydes and phosphoethanolamine.
CC Sphingolipid catabolism is required for normal development including
CC viability, reproduction and muscle development.
CC {ECO:0000269|PubMed:12702658, ECO:0000269|PubMed:28165339}.
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:12702658};
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:12702658, ECO:0000269|PubMed:28165339}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:O95470}; Single-pass type III membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Localized to the developing gut primordium during
CC embryogenesis. {ECO:0000269|PubMed:12702658}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC Expression is high in early and late embryos, and then again early in
CC metamorphosis, followed by reduction to basal levels after eclosion of
CC adult flies in both males and females. {ECO:0000269|PubMed:12702658}.
CC -!- DISRUPTION PHENOTYPE: Flies lacking Sply display decreased viability
CC associated with altered nephrocytes morphology. Altered lipid
CC metabolism with accumulation of sphingosine-1-phosphate upstream
CC intermediates is observed. {ECO:0000269|PubMed:28165339}.
CC -!- SIMILARITY: Belongs to the group II decarboxylase family. Sphingosine-
CC 1-phosphate lyase subfamily. {ECO:0000305}.
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DR EMBL; AJ297394; CAC10531.1; -; mRNA.
DR EMBL; AE013599; AAF57903.1; -; Genomic_DNA.
DR EMBL; AY052075; AAK93499.1; -; mRNA.
DR RefSeq; NP_652032.1; NM_143775.3.
DR RefSeq; NP_725652.1; NM_166215.2.
DR AlphaFoldDB; Q9V7Y2; -.
DR SMR; Q9V7Y2; -.
DR BioGRID; 70079; 3.
DR IntAct; Q9V7Y2; 2.
DR MINT; Q9V7Y2; -.
DR STRING; 7227.FBpp0086158; -.
DR PaxDb; Q9V7Y2; -.
DR PRIDE; Q9V7Y2; -.
DR DNASU; 46059; -.
DR EnsemblMetazoa; FBtr0087007; FBpp0086158; FBgn0010591.
DR EnsemblMetazoa; FBtr0087008; FBpp0086159; FBgn0010591.
DR GeneID; 46059; -.
DR KEGG; dme:Dmel_CG8946; -.
DR CTD; 46059; -.
DR FlyBase; FBgn0010591; Sply.
DR VEuPathDB; VectorBase:FBgn0010591; -.
DR eggNOG; KOG1383; Eukaryota.
DR GeneTree; ENSGT00390000000046; -.
DR HOGENOM; CLU_028929_1_0_1; -.
DR InParanoid; Q9V7Y2; -.
DR OMA; FKDHQFT; -.
DR OrthoDB; 517323at2759; -.
DR PhylomeDB; Q9V7Y2; -.
DR Reactome; R-DME-1660661; Sphingolipid de novo biosynthesis.
DR SignaLink; Q9V7Y2; -.
DR UniPathway; UPA00222; -.
DR BioGRID-ORCS; 46059; 0 hits in 1 CRISPR screen.
DR ChiTaRS; Sply; fly.
DR GenomeRNAi; 46059; -.
DR PRO; PR:Q9V7Y2; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0010591; Expressed in embryonic/larval hemocyte (Drosophila) and 40 other tissues.
DR Genevisible; Q9V7Y2; DM.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; ISM:FlyBase.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008117; F:sphinganine-1-phosphate aldolase activity; IDA:FlyBase.
DR GO; GO:0007527; P:adult somatic muscle development; IMP:FlyBase.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR GO; GO:0030149; P:sphingolipid catabolic process; IMP:UniProtKB.
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 Developmental protein; Endoplasmic reticulum; Lipid metabolism; Lyase;
KW Membrane; Pyridoxal phosphate; Reference proteome; Signal-anchor;
KW Sphingolipid metabolism; Transmembrane; Transmembrane helix.
FT CHAIN 1..545
FT /note="Sphingosine-1-phosphate lyase"
FT /id="PRO_0000147016"
FT TOPO_DOM 1..26
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 27..47
FT /note="Helical; Signal-anchor for type III membrane
FT protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 48..545
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 342
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT MUTAGEN 119
FT /note="E->G: No effect on function in sphingolipid
FT catabolic process."
FT /evidence="ECO:0000269|PubMed:28165339"
FT MUTAGEN 210
FT /note="R->Q: Decreased function in sphingolipid catabolic
FT process."
FT /evidence="ECO:0000269|PubMed:28165339"
FT MUTAGEN 335
FT /note="S->I: Loss of function in sphingolipid catabolic
FT process."
FT /evidence="ECO:0000269|PubMed:28165339"
SQ SEQUENCE 545 AA; 60305 MW; 26000F4AE43F85FD CRC64;
MRPFSGSDCL KPVTEGINRA FGAKEPWQVA TITATTVLGG VWLWTVICQD ENLYIRGKRQ
FFKFAKKIPA VRRQVETELA KAKNDFETEI KKSNAHLTYS ETLPEKGLSK EEILRLVDEH
LKTGHYNWRD GRVSGAVYGY KPDLVELVTE VYGKASYTNP LHADLFPGVC KMEAEVVRMA
CNLFHGNSAS CGTMTTGGTE SIVMAMKAYR DFAREYKGIT RPNIVVPKTV HAAFDKGGQY
FNIHVRSVDV DPETYEVDIK KFKRAINRNT ILLVGSAPNF PYGTIDDIEA IAALGVKYDI
PVHVDACLGS FVVALVRNAG YKLRPFDFEV KGVTSISADT HKYGFAPKGS SVILYSDKKY
KDHQFTVTTD WPGGVYGSPT VNGSRAGGII AACWATMMSF GYDGYLEATK RIVDTARYIE
RGVRDIDGIF IFGKPATSVI ALGSNVFDIF RLSDSLCKLG WNLNALQFPS GIHLCVTDMH
TQPGVADKFI ADVRSCTAEI MKDPGQPVVG KMALYGMAQS IPDRSVIGEV TRLFLHSMYY
TPSQK
