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Protein

Sphingosine-1-phosphate lyase

Gene

DPL1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Cleaves phosphorylated sphingoid bases (PSBs), such as sphingosine-1-phosphate, into fatty aldehydes and phosphoethanolamine. May play a minor role in maintenance of sphingolipid metabolism during normal plant development and growth, but be required for maintaining sphingoid long chain bases (LCB) and their phosphorylated derivatives (LCB-P) levels when sphingolipid metabolism is perturbed. May play a role in dehydration stress.2 Publications

Catalytic activityi

Sphinganine 1-phosphate = phosphoethanolamine + palmitaldehyde.2 Publications

Cofactori

Pathwayi: sphingolipid metabolism

This protein is involved in the pathway sphingolipid metabolism, which is part of Lipid metabolism.
View all proteins of this organism that are known to be involved in the pathway sphingolipid metabolism and in Lipid metabolism.

GO - Molecular functioni

GO - Biological processi

  • carboxylic acid metabolic process Source: InterPro
  • sphingolipid catabolic process Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Lipid metabolism, Sphingolipid metabolism, Stress response

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciARA:AT1G27980-MONOMER.
MetaCyc:AT1G27980-MONOMER.
BRENDAi4.1.2.27. 399.
ReactomeiR-ATH-1660661. Sphingolipid de novo biosynthesis.
UniPathwayiUPA00222.

Names & Taxonomyi

Protein namesi
Recommended name:
Sphingosine-1-phosphate lyase (EC:4.1.2.27)
Short name:
AtSPL1
Short name:
S1PL
Short name:
SP-lyase
Short name:
SPL
Alternative name(s):
Dihydrosphingosine phosphate lyase 1
Short name:
AtDPL1
Sphingosine-1-phosphate aldolase
Gene namesi
Name:DPL1
Ordered Locus Names:At1g27980
ORF Names:F13K9.8
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 1

Organism-specific databases

TAIRiAT1G27980.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 2929LumenalSequence analysisAdd
BLAST
Transmembranei30 – 5021Helical; Signal-anchor for type III membrane proteinSequence analysisAdd
BLAST
Topological domaini51 – 544494CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • endoplasmic reticulum Source: TAIR
  • endoplasmic reticulum membrane Source: UniProtKB-SubCell
  • integral component of membrane Source: UniProtKB-KW
  • membrane Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Disruption phenotypei

No visible phenotype under normal growth conditions.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 544544Sphingosine-1-phosphate lyasePRO_0000147017Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei349 – 3491N6-(pyridoxal phosphate)lysineBy similarity

Proteomic databases

PaxDbiQ9C509.
PRIDEiQ9C509.

Expressioni

Tissue specificityi

Expressed in the peripheral parts of leaves and the bases of trichomes.1 Publication

Gene expression databases

GenevisibleiQ9C509. AT.

Interactioni

Protein-protein interaction databases

STRINGi3702.AT1G27980.1.

Structurei

3D structure databases

ProteinModelPortaliQ9C509.
SMRiQ9C509. Positions 106-544.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1383. Eukaryota.
COG0076. LUCA.
HOGENOMiHOG000190693.
InParanoidiQ9C509.
KOiK01634.
OMAiCTLKEGM.
PhylomeDBiQ9C509.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
InterProiIPR002129. PyrdxlP-dep_de-COase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
[Graphical view]
PfamiPF00282. Pyridoxal_deC. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9C509-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDSFSYSSMK SMLIQARGSL NSRLSEFEPL VLLLVPLVSL FLAQIIGSVF
60 70 80 90 100
GVVHEKGLKA CLIGFIMGLL KMIPGVQNYI DAEKQKVVDQ LQSGSSSKKK
110 120 130 140 150
NKTEVLPVKG LGVEVLEKME NEKRNDAIWQ GKCSGTVYIG GAESEGHFSL
160 170 180 190 200
INQACSMFAH TNPLHIDVFQ SVVRFESEVV AMTAALLGSK ETASGGQICG
210 220 230 240 250
NMTSGGTESI VLAVKSSRDY MKYKKGITRP EMIIPESGHS AYDKAAQYFK
260 270 280 290 300
IKLWRVPVDK DFRADVKATR RHINRNTIMI VGSAPGFPHG IIDPIEELGQ
310 320 330 340 350
LALSYGICFH VDLCLGGFVL PFARKLGYQI PPFDFSVQGV TSISVDVHKY
360 370 380 390 400
GLAPKGTSTV LYRNHEIRKH QFVAVTEWSG GLYVSPTIAG SRPGSLVAGA
410 420 430 440 450
WAAMMSLGEE GYLQNTSKIM EASKRLEEGV REIHELFVIG KPDMTIVAFG
460 470 480 490 500
SKALDIFEVN DIMSSKGWHL NALQRPNSIH ICITLQHVPV VDDFLRDLRE
510 520 530 540
AVETVKANPG PITGGLAPIY GAAGKMPDRG MVNELLVSFM DSQY
Length:544
Mass (Da):59,478
Last modified:June 1, 2001 - v1
Checksum:iCC5C9952C2317248
GO

Sequence cautioni

The sequence AAM62669.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB175035 mRNA. Translation: BAD13416.1.
AC069471 Genomic DNA. Translation: AAG51494.1.
CP002684 Genomic DNA. Translation: AEE30898.1.
AF360166 mRNA. Translation: AAK25876.1.
AY113914 mRNA. Translation: AAM44962.1.
AY085442 mRNA. Translation: AAM62669.1. Different initiation.
PIRiC86405.
RefSeqiNP_174119.1. NM_102563.3.
UniGeneiAt.17690.
At.66881.

Genome annotation databases

EnsemblPlantsiAT1G27980.1; AT1G27980.1; AT1G27980.
GeneIDi839691.
GrameneiAT1G27980.1; AT1G27980.1; AT1G27980.
KEGGiath:AT1G27980.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB175035 mRNA. Translation: BAD13416.1.
AC069471 Genomic DNA. Translation: AAG51494.1.
CP002684 Genomic DNA. Translation: AEE30898.1.
AF360166 mRNA. Translation: AAK25876.1.
AY113914 mRNA. Translation: AAM44962.1.
AY085442 mRNA. Translation: AAM62669.1. Different initiation.
PIRiC86405.
RefSeqiNP_174119.1. NM_102563.3.
UniGeneiAt.17690.
At.66881.

3D structure databases

ProteinModelPortaliQ9C509.
SMRiQ9C509. Positions 106-544.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3702.AT1G27980.1.

Proteomic databases

PaxDbiQ9C509.
PRIDEiQ9C509.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT1G27980.1; AT1G27980.1; AT1G27980.
GeneIDi839691.
GrameneiAT1G27980.1; AT1G27980.1; AT1G27980.
KEGGiath:AT1G27980.

Organism-specific databases

TAIRiAT1G27980.

Phylogenomic databases

eggNOGiKOG1383. Eukaryota.
COG0076. LUCA.
HOGENOMiHOG000190693.
InParanoidiQ9C509.
KOiK01634.
OMAiCTLKEGM.
PhylomeDBiQ9C509.

Enzyme and pathway databases

UniPathwayiUPA00222.
BioCyciARA:AT1G27980-MONOMER.
MetaCyc:AT1G27980-MONOMER.
BRENDAi4.1.2.27. 399.
ReactomeiR-ATH-1660661. Sphingolipid de novo biosynthesis.

Miscellaneous databases

PROiQ9C509.

Gene expression databases

GenevisibleiQ9C509. AT.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
InterProiIPR002129. PyrdxlP-dep_de-COase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
[Graphical view]
PfamiPF00282. Pyridoxal_deC. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Degradation of sphingoid long-chain base 1-phosphates (LCB-1Ps): functional characterization and expression of AtDPL1 encoding LCB-1P lyase involved in the dehydration stress response in Arabidopsis."
    Nishikawa M., Hosokawa K., Ishiguro M., Minamioka H., Tamura K., Hara-Nishimura I., Takahashi Y., Shimazaki K., Imai H.
    Plant Cell Physiol. 49:1758-1763(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
  2. "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
    Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K.
    , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
    Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  4. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  5. "Full-length cDNA from Arabidopsis thaliana."
    Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
    Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 412-544.
  6. "Arabidopsis mutants lacking long chain base phosphate lyase are fumonisin-sensitive and accumulate trihydroxy-18:1 long chain base phosphate."
    Tsegaye Y., Richardson C.G., Bravo J.E., Mulcahy B.J., Lynch D.V., Markham J.E., Jaworski J.G., Chen M., Cahoon E.B., Dunn T.M.
    J. Biol. Chem. 282:28195-28206(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiSGPL_ARATH
AccessioniPrimary (citable) accession number: Q9C509
Secondary accession number(s): Q549V9, Q8LEF9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 21, 2003
Last sequence update: June 1, 2001
Last modified: February 17, 2016
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.