SGPL_ARATH
ID SGPL_ARATH Reviewed; 544 AA.
AC Q9C509; Q549V9; Q8LEF9;
DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Sphingosine-1-phosphate lyase;
DE Short=AtSPL1;
DE Short=S1PL;
DE Short=SP-lyase;
DE Short=SPL;
DE EC=4.1.2.27;
DE AltName: Full=Dihydrosphingosine phosphate lyase 1;
DE Short=AtDPL1;
DE AltName: Full=Sphingosine-1-phosphate aldolase;
GN Name=DPL1; OrderedLocusNames=At1g27980; ORFNames=F13K9.8;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=18849574; DOI=10.1093/pcp/pcn149;
RA Nishikawa M., Hosokawa K., Ishiguro M., Minamioka H., Tamura K.,
RA Hara-Nishimura I., Takahashi Y., Shimazaki K., Imai H.;
RT "Degradation of sphingoid long-chain base 1-phosphates (LCB-1Ps):
RT functional characterization and expression of AtDPL1 encoding LCB-1P lyase
RT involved in the dehydration stress response in Arabidopsis.";
RL Plant Cell Physiol. 49:1758-1763(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 412-544.
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=17635905; DOI=10.1074/jbc.m705074200;
RA Tsegaye Y., Richardson C.G., Bravo J.E., Mulcahy B.J., Lynch D.V.,
RA Markham J.E., Jaworski J.G., Chen M., Cahoon E.B., Dunn T.M.;
RT "Arabidopsis mutants lacking long chain base phosphate lyase are fumonisin-
RT sensitive and accumulate trihydroxy-18:1 long chain base phosphate.";
RL J. Biol. Chem. 282:28195-28206(2007).
CC -!- FUNCTION: Cleaves phosphorylated sphingoid bases (PSBs), such as
CC sphingosine-1-phosphate, into fatty aldehydes and phosphoethanolamine.
CC May play a minor role in maintenance of sphingolipid metabolism during
CC normal plant development and growth, but be required for maintaining
CC sphingoid long chain bases (LCB) and their phosphorylated derivatives
CC (LCB-P) levels when sphingolipid metabolism is perturbed. May play a
CC role in dehydration stress. {ECO:0000269|PubMed:17635905,
CC ECO:0000269|PubMed:18849574}.
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:17635905, ECO:0000269|PubMed:18849574};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000305|PubMed:17635905, ECO:0000305|PubMed:18849574}; Single-pass
CC type III membrane protein {ECO:0000305|PubMed:17635905,
CC ECO:0000305|PubMed:18849574}.
CC -!- TISSUE SPECIFICITY: Expressed in the peripheral parts of leaves and the
CC bases of trichomes. {ECO:0000269|PubMed:18849574}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions. {ECO:0000269|PubMed:18849574}.
CC -!- SIMILARITY: Belongs to the group II decarboxylase family. Sphingosine-
CC 1-phosphate lyase subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM62669.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB175035; BAD13416.1; -; mRNA.
DR EMBL; AC069471; AAG51494.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30898.1; -; Genomic_DNA.
DR EMBL; AF360166; AAK25876.1; -; mRNA.
DR EMBL; AY113914; AAM44962.1; -; mRNA.
DR EMBL; AY085442; AAM62669.1; ALT_INIT; mRNA.
DR PIR; C86405; C86405.
DR RefSeq; NP_174119.1; NM_102563.4.
DR AlphaFoldDB; Q9C509; -.
DR SMR; Q9C509; -.
DR STRING; 3702.AT1G27980.1; -.
DR PaxDb; Q9C509; -.
DR PRIDE; Q9C509; -.
DR ProteomicsDB; 234544; -.
DR EnsemblPlants; AT1G27980.1; AT1G27980.1; AT1G27980.
DR GeneID; 839691; -.
DR Gramene; AT1G27980.1; AT1G27980.1; AT1G27980.
DR KEGG; ath:AT1G27980; -.
DR Araport; AT1G27980; -.
DR TAIR; locus:2010524; AT1G27980.
DR eggNOG; KOG1383; Eukaryota.
DR HOGENOM; CLU_028929_1_1_1; -.
DR InParanoid; Q9C509; -.
DR OMA; FKDHQFT; -.
DR OrthoDB; 517323at2759; -.
DR PhylomeDB; Q9C509; -.
DR BioCyc; ARA:AT1G27980-MON; -.
DR BioCyc; MetaCyc:AT1G27980-MON; -.
DR BRENDA; 4.1.2.27; 399.
DR UniPathway; UPA00222; -.
DR PRO; PR:Q9C509; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C509; baseline and differential.
DR Genevisible; Q9C509; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
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; IGI:TAIR.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR GO; GO:0030149; P:sphingolipid catabolic process; IMP:TAIR.
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; Stress response; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..544
FT /note="Sphingosine-1-phosphate lyase"
FT /id="PRO_0000147017"
FT TOPO_DOM 1..29
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 30..50
FT /note="Helical; Signal-anchor for type III membrane
FT protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 51..544
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 349
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 544 AA; 59478 MW; CC5C9952C2317248 CRC64;
MDSFSYSSMK SMLIQARGSL NSRLSEFEPL VLLLVPLVSL FLAQIIGSVF GVVHEKGLKA
CLIGFIMGLL KMIPGVQNYI DAEKQKVVDQ LQSGSSSKKK NKTEVLPVKG LGVEVLEKME
NEKRNDAIWQ GKCSGTVYIG GAESEGHFSL INQACSMFAH TNPLHIDVFQ SVVRFESEVV
AMTAALLGSK ETASGGQICG NMTSGGTESI VLAVKSSRDY MKYKKGITRP EMIIPESGHS
AYDKAAQYFK IKLWRVPVDK DFRADVKATR RHINRNTIMI VGSAPGFPHG IIDPIEELGQ
LALSYGICFH VDLCLGGFVL PFARKLGYQI PPFDFSVQGV TSISVDVHKY GLAPKGTSTV
LYRNHEIRKH QFVAVTEWSG GLYVSPTIAG SRPGSLVAGA WAAMMSLGEE GYLQNTSKIM
EASKRLEEGV REIHELFVIG KPDMTIVAFG SKALDIFEVN DIMSSKGWHL NALQRPNSIH
ICITLQHVPV VDDFLRDLRE AVETVKANPG PITGGLAPIY GAAGKMPDRG MVNELLVSFM
DSQY
