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Protein

Sphingosine-1-phosphate lyase

Gene

DPL1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
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.2 Publications

Catalytic activityi

Sphinganine 1-phosphate = phosphoethanolamine + palmitaldehyde.1 Publication

Cofactori

pyridoxal 5'-phosphate1 Publication

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

  • calcium-mediated signaling Source: SGD
  • carboxylic acid metabolic process Source: InterPro
  • cellular response to starvation Source: SGD
  • sphingolipid metabolic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Lipid metabolism, Sphingolipid metabolism

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciMetaCyc:YDR294C-MONOMER.
YEAST:YDR294C-MONOMER.
BRENDAi4.1.2.27. 984.
ReactomeiR-SCE-1660661. Sphingolipid de novo biosynthesis.
UniPathwayiUPA00222.

Chemistry

SwissLipidsiSLP:000000071.
SLP:000000196.

Names & Taxonomyi

Protein namesi
Recommended name:
Sphingosine-1-phosphate lyase (EC:4.1.2.27)
Short name:
S1PL
Short name:
SP-lyase
Short name:
ySPL
Alternative name(s):
Bestowed of sphingosine tolerance 1
Sphingosine-1-phosphate aldolase
Gene namesi
Name:DPL1
Synonyms:BST1
Ordered Locus Names:YDR294C
ORF Names:D9819.5
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDR294C.
SGDiS000002702. DPL1.

Subcellular locationi

GO - Cellular componenti

  • cortical endoplasmic reticulum Source: SGD
  • perinuclear endoplasmic reticulum Source: SGD
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi172 – 1721A → P: Loss of enzyme activity. 1 Publication
Mutagenesisi174 – 1741Y → F: Mildly decreased enzyme activity. 1 Publication
Mutagenesisi198 – 1981H → A: Decreased enzyme activity. 1 Publication
Mutagenesisi380 – 3801K → A: Loss of enzyme activity. 1 Publication
Mutagenesisi386 – 3861K → A: Loss of enzyme activity. 1 Publication
Mutagenesisi554 – 5541Y → F: Decreased enzyme activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 589589Sphingosine-1-phosphate lyasePRO_0000147018Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei380 – 3801N6-(pyridoxal phosphate)lysine

Proteomic databases

MaxQBiQ05567.
PeptideAtlasiQ05567.
PRIDEiQ05567.

PTM databases

iPTMnetiQ05567.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

BioGridi32346. 47 interactions.
DIPiDIP-49371N.
IntActiQ05567. 2 interactions.
MINTiMINT-4481843.

Structurei

Secondary structure

1
589
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi145 – 15713Combined sources
Helixi164 – 1663Combined sources
Beta strandi169 – 1724Combined sources
Helixi178 – 19013Combined sources
Turni199 – 2013Combined sources
Helixi203 – 21917Combined sources
Turni224 – 2263Combined sources
Beta strandi229 – 2346Combined sources
Helixi235 – 25319Combined sources
Beta strandi260 – 2645Combined sources
Helixi269 – 2779Combined sources
Beta strandi281 – 2855Combined sources
Turni289 – 2913Combined sources
Turni296 – 2994Combined sources
Helixi300 – 3023Combined sources
Beta strandi305 – 3139Combined sources
Turni317 – 3193Combined sources
Turni326 – 3305Combined sources
Helixi331 – 3344Combined sources
Beta strandi339 – 3424Combined sources
Turni343 – 3464Combined sources
Helixi347 – 3504Combined sources
Helixi351 – 3533Combined sources
Turni354 – 3574Combined sources
Beta strandi373 – 3775Combined sources
Turni378 – 3825Combined sources
Beta strandi389 – 3924Combined sources
Helixi396 – 3994Combined sources
Turni400 – 4023Combined sources
Beta strandi417 – 4193Combined sources
Helixi425 – 46339Combined sources
Beta strandi476 – 4827Combined sources
Turni484 – 4874Combined sources
Helixi488 – 4969Combined sources
Turni497 – 4993Combined sources
Beta strandi511 – 5144Combined sources
Turni517 – 5204Combined sources
Helixi523 – 53715Combined sources
Helixi567 – 5759Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3MC6X-ray3.15A/C103-589[»]
ProteinModelPortaliQ05567.
SMRiQ05567. Positions 101-579.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ05567.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

GeneTreeiENSGT00390000000046.
HOGENOMiHOG000190693.
InParanoidiQ05567.
KOiK01634.
OMAiCTLKEGM.
OrthoDBiEOG722JJC.

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.

Q05567-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGVSNKTVS INGWYGMPIH LLREEGDFAQ FMILTINELK IAIHGYLRNT
60 70 80 90 100
PWYNMLKDYL FVIFCYKLIS NFFYLLKVYG PVRLAVRTYE HSSRRLFRWL
110 120 130 140 150
LDSPFLRGTV EKEVTKVKQS IEDELIRSDS QLMNFPQLPS NGIPQDDVIE
160 170 180 190 200
ELNKLNDLIP HTQWKEGKVS GAVYHGGDDL IHLQTIAYEK YCVANQLHPD
210 220 230 240 250
VFPAVRKMES EVVSMVLRMF NAPSDTGCGT TTSGGTESLL LACLSAKMYA
260 270 280 290 300
LHHRGITEPE IIAPVTAHAG FDKAAYYFGM KLRHVELDPT TYQVDLGKVK
310 320 330 340 350
KFINKNTILL VGSAPNFPHG IADDIEGLGK IAQKYKLPLH VDSCLGSFIV
360 370 380 390 400
SFMEKAGYKN LPLLDFRVPG VTSISCDTHK YGFAPKGSSV IMYRNSDLRM
410 420 430 440 450
HQYYVNPAWT GGLYGSPTLA GSRPGAIVVG CWATMVNMGE NGYIESCQEI
460 470 480 490 500
VGAAMKFKKY IQENIPDLNI MGNPRYSVIS FSSKTLNIHE LSDRLSKKGW
510 520 530 540 550
HFNALQKPVA LHMAFTRLSA HVVDEICDIL RTTVQELKSE SNSKPSPDGT
560 570 580
SALYGVAGSV KTAGVADKLI VGFLDALYKL GPGEDTATK
Length:589
Mass (Da):65,566
Last modified:November 1, 1996 - v1
Checksum:i75FAF8182AF72266
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U51031 Genomic DNA. Translation: AAB64470.1.
BK006938 Genomic DNA. Translation: DAA12133.1.
PIRiS70123.
RefSeqiNP_010580.1. NM_001180602.1.

Genome annotation databases

EnsemblFungiiYDR294C; YDR294C; YDR294C.
GeneIDi851888.
KEGGisce:YDR294C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U51031 Genomic DNA. Translation: AAB64470.1.
BK006938 Genomic DNA. Translation: DAA12133.1.
PIRiS70123.
RefSeqiNP_010580.1. NM_001180602.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3MC6X-ray3.15A/C103-589[»]
ProteinModelPortaliQ05567.
SMRiQ05567. Positions 101-579.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32346. 47 interactions.
DIPiDIP-49371N.
IntActiQ05567. 2 interactions.
MINTiMINT-4481843.

Chemistry

SwissLipidsiSLP:000000071.
SLP:000000196.

PTM databases

iPTMnetiQ05567.

Proteomic databases

MaxQBiQ05567.
PeptideAtlasiQ05567.
PRIDEiQ05567.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDR294C; YDR294C; YDR294C.
GeneIDi851888.
KEGGisce:YDR294C.

Organism-specific databases

EuPathDBiFungiDB:YDR294C.
SGDiS000002702. DPL1.

Phylogenomic databases

GeneTreeiENSGT00390000000046.
HOGENOMiHOG000190693.
InParanoidiQ05567.
KOiK01634.
OMAiCTLKEGM.
OrthoDBiEOG722JJC.

Enzyme and pathway databases

UniPathwayiUPA00222.
BioCyciMetaCyc:YDR294C-MONOMER.
YEAST:YDR294C-MONOMER.
BRENDAi4.1.2.27. 984.
ReactomeiR-SCE-1660661. Sphingolipid de novo biosynthesis.

Miscellaneous databases

EvolutionaryTraceiQ05567.
NextBioi969868.
PROiQ05567.

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. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
    Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
    , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
    Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. "The BST1 gene of Saccharomyces cerevisiae is the sphingosine-1-phosphate lyase."
    Saba J.D., Nara F., Bielawska A., Garrett S., Hannun Y.A.
    J. Biol. Chem. 272:26087-26090(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  4. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  5. "Structure and function of sphingosine-1-phosphate lyase, a key enzyme of sphingolipid metabolism."
    Bourquin F., Riezman H., Capitani G., Grutter M.G.
    Structure 18:1054-1065(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.15 ANGSTROMS) OF 103-589 IN COMPLEX WITH PYRIDOXAL PHOSPHATE, CATALYTIC ACTIVITY, FUNCTION, COFACTOR, SUBUNIT, MUTAGENESIS OF ALA-172; TYR-174; HIS-198; LYS-380; LYS-386 AND TYR-554.

Entry informationi

Entry nameiSGPL_YEAST
AccessioniPrimary (citable) accession number: Q05567
Secondary accession number(s): D6VSS3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 24, 2003
Last sequence update: November 1, 1996
Last modified: May 11, 2016
This is version 121 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 13100 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  5. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

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.