Reviewed, UniProtKB/Swiss-Prot Q05567 (SGPL_YEAST)

Names and origin

Protein names

Recommended name:
    Sphingosine-1-phosphate lyase
      Short name=SP-lyase
      Short name=ySPL
    EC=4.1.2.27
Alternative name(s):
    Sphingosine-1-phosphate aldolase
    Bestowed of sphingosine tolerance 1

Gene names

Name:	DPL1
Synonyms:	BST1
Ordered Locus Names:	YDR294C
ORF Names:	D9819.5

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	589 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Cleaves phosphorylated sphingoid bases (PSBs), such as sphingosine-1-phosphate, into fatty aldehydes and phosphoethanolamine. Ref.2
Catalytic activity	Sphinganine 1-phosphate = phosphoethanolamine + palmitaldehyde.
Cofactor	Pyridoxal phosphate By similarity.
Pathway	Lipid metabolism; sphingolipid metabolism.
Miscellaneous	Present with 13100 molecules/cell in log phase SD medium. Ref.3
Sequence similarities	Belongs to the group II decarboxylase family. Sphingosine-1-phosphate lyase subfamily.

Ontologies

Keywords
Ligand	Pyridoxal phosphate
Molecular function	Lyase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	calcium-mediated signaling Inferred from mutant phenotype. Source: SGD carboxylic acid metabolic process Inferred from electronic annotation. Source: InterPro cellular response to starvation Inferred from mutant phenotype. Source: SGD sphingolipid metabolic process Ref.2 Inferred from genetic interaction. Source: SGD
Cellular component	endoplasmic reticulum Inferred from direct assay. Source: SGD
Molecular function	carboxy-lyase activity Inferred from electronic annotation. Source: InterPro pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro sphinganine-1-phosphate aldolase activity Ref.2 Inferred from direct assay. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 589	589	Sphingosine-1-phosphate lyase		PRO_0000147018
Amino acid modifications
	Modified residue	380	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q05567-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 75FAF8182AF72266	FASTA	589	65,566
	10 20 30 40 50 60 MSGVSNKTVS INGWYGMPIH LLREEGDFAQ FMILTINELK IAIHGYLRNT PWYNMLKDYL 70 80 90 100 110 120 FVIFCYKLIS NFFYLLKVYG PVRLAVRTYE HSSRRLFRWL LDSPFLRGTV EKEVTKVKQS 130 140 150 160 170 180 IEDELIRSDS QLMNFPQLPS NGIPQDDVIE ELNKLNDLIP HTQWKEGKVS GAVYHGGDDL 190 200 210 220 230 240 IHLQTIAYEK YCVANQLHPD VFPAVRKMES EVVSMVLRMF NAPSDTGCGT TTSGGTESLL 250 260 270 280 290 300 LACLSAKMYA LHHRGITEPE IIAPVTAHAG FDKAAYYFGM KLRHVELDPT TYQVDLGKVK 310 320 330 340 350 360 KFINKNTILL VGSAPNFPHG IADDIEGLGK IAQKYKLPLH VDSCLGSFIV SFMEKAGYKN 370 380 390 400 410 420 LPLLDFRVPG VTSISCDTHK YGFAPKGSSV IMYRNSDLRM HQYYVNPAWT GGLYGSPTLA 430 440 450 460 470 480 GSRPGAIVVG CWATMVNMGE NGYIESCQEI VGAAMKFKKY IQENIPDLNI MGNPRYSVIS 490 500 510 520 530 540 FSSKTLNIHE LSDRLSKKGW HFNALQKPVA LHMAFTRLSA HVVDEICDIL RTTVQELKSE 550 560 570 580 SNSKPSPDGT SALYGVAGSV KTAGVADKLI VGFLDALYKL GPGEDTATK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 9169867] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[2]	"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: 9334171] [Abstract] Cited for: FUNCTION.
[3]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U51031 Genomic DNA. Translation: AAB64470.1.
PIR	S70123.
RefSeq	NP_010580.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	Q05567. 2 interactions.
Proteomic databases
PeptideAtlas	Q05567.
Genome annotation databases
Ensembl	YDR294C. Saccharomyces cerevisiae. [Contig view]
GeneID	851888.
GenomeReviews	Gene locus YDR294C in contig Z71256_GR.
KEGG	sce:YDR294C.
NMPDR	fig|4932.3.peg.1342.
Organism-specific databases
CYGD	YDR294c.
SGD	S000002702. DPL1.
Yeast-GFP	Search...
Phylogenomic databases
HOGENOM	Q05567.
OMA	Q05567. IIAACWA.
Enzyme and pathway databases
BRENDA	4.1.2.27. 250.
Gene expression databases
GermOnline	YDR294C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR002129. PyrdxlP-dep_de-COase. IPR015421. PyrdxlP-dep_Trfase_major_sub1. [Graphical view]
Gene3D	G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
PANTHER	PTHR11999. Pyridoxal_deC. 1 hit.
Pfam	PF00282. Pyridoxal_deC. 1 hit. [Graphical view]
PROSITE	PS00392. DDC_GAD_HDC_YDC. False negative. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	969868.

Entry information

Entry name

SGPL_YEAST

Accession

Primary (citable) accession number: Q05567

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 24, 2003
Last sequence update:	November 1, 1996
Last modified:	June 16, 2009
This is version 60 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)