Q54RV9 (SGPL_DICDI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Sphingosine-1-phosphate lyase
Short name=S1P lyase
Short name=S1PL
Short name=SP-lyase
Short name=SPL
EC=4.1.2.27

Alternative name(s):
Sphingosine-1-phosphate aldolase

Gene names

Name:	sglA
ORF Names:	DDB_G0282819

Organism

Dictyostelium discoideum (Slime mold)

Taxonomic identifier

44689 [NCBI]

Taxonomic lineage

Eukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium

Protein attributes

Sequence length	528 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Cleaves phosphorylated sphingoid bases (PSBs), such as sphingosine-1-phosphate, into fatty aldehydes and phosphoethanolamine By similarity. Sphingosine-1-phosphate (S1P) probably acts intracellularly as a second messenger perhaps by promoting cell proliferation; the absence of S1P lyase increases its concentration. This leads to increased lateral pseudopod formation as well as defects in the efficiency of chemotaxis (Ref.4). Overexpression of S1P lyase causes decreased growth rates, entry into stationary phase at lower cell density and increased sensitivity to the antitumor agents cisplatin and carboplatin; these effects are more pronounced in cells that express more enzyme (Ref.5). Ref.4
Catalytic activity	Sphinganine 1-phosphate = phosphoethanolamine + palmitaldehyde.
Cofactor	Pyridoxal phosphate By similarity.
Pathway	Lipid metabolism; sphingolipid metabolism.
Subcellular location	Endoplasmic reticulum membrane; Single-pass membrane protein Potential.
Developmental stage	Constitutively expressed during growth and development; not up-regulated by exposure to cisplatin. Ref.1
Disruption phenotype	Cells produce short fruiting bodies with a thick stalk and drastically reduced numbers of spores. Mutant cells grow exponentially at the same rate as wild-type and are 25-fold more resistant to the antitumor agent cisplatin than are wild-type (Ref.1). Mutant cells survive longer in stationary phase than wild-type cells, but are effected at multiple stages of development. Addition of 50 µM extracellular sphingosine-1-phosphate to wild-type cells mimics the developmental effect of the knockout (Ref.1), and leads to increased cisplatin resistance (Ref.5). Ref.1 Ref.3
Sequence similarities	Belongs to the group II decarboxylase family. Sphingosine-1-phosphate lyase subfamily.

Ontologies

Keywords
Biological process	Lipid metabolism Sphingolipid metabolism
Cellular component	Endoplasmic reticulum Membrane
Domain	Signal-anchor Transmembrane Transmembrane helix
Ligand	Pyridoxal phosphate
Molecular function	Lyase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	actin cytoskeleton organization Inferred from mutant phenotype Ref.1Ref.4. Source: dictyBase ameboidal cell migration Inferred from mutant phenotype Ref.4. Source: dictyBase carboxylic acid metabolic process Inferred from electronic annotation. Source: InterPro cell death Inferred from mutant phenotype Ref.1. Source: dictyBase cellular calcium ion homeostasis Inferred from sequence or structural similarity Ref.1. Source: dictyBase ceramide metabolic process Inferred from sequence or structural similarity Ref.3. Source: dictyBase chemotaxis Inferred from mutant phenotype Ref.4. Source: dictyBase negative regulation of aggregate size involved in sorocarp development Inferred from mutant phenotype Ref.1. Source: dictyBase negative regulation of lateral pseudopodium assembly Inferred from mutant phenotype Ref.4. Source: dictyBase positive phototaxis Inferred from mutant phenotype Ref.1. Source: dictyBase regulation of actin filament polymerization Inferred from sequence or structural similarity Ref.1. Source: dictyBase sorocarp development Inferred from mutant phenotype Ref.3Ref.1. Source: dictyBase sphingolipid catabolic process Inferred from sequence or structural similarity Ref.3. Source: dictyBase sporulation resulting in formation of a cellular spore Inferred from mutant phenotype Ref.1. Source: dictyBase
Cellular component	endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
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 Inferred from sequence or structural similarity Ref.3. Source: dictyBase
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 528	528	Sphingosine-1-phosphate lyase		PRO_0000328248
Regions
	Transmembrane	13 – 35	23	Helical; Potential
Amino acid modifications
	Modified residue	324	1	N6-(pyridoxal phosphate)lysine By similarity
Experimental info
	Sequence conflict	90	1	K → R in AAP37027. Ref.1
	Sequence conflict	233	1	D → G in AAP37027. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q54RV9 [UniParc]. Last modified May 24, 2005. Version 1. Checksum: 7C9411C9C73BBDA8	FASTA	528	58,239
	10 20 30 40 50 60 MDKANDYLKD YQPAKLVLAT AGITAASILA YQAITDRDFK DKLNKKIFRS IKSMPGVSDI 70 80 90 100 110 120 VKKERAKAKV ELKKMFKTDV RNAHYTLPLK GIKHEDLIEE MKALAKVDES HWVDSKVSGC 130 140 150 160 170 180 VYLGEKEHTK LLNEAYSLFS LSNPLHPSVF PSIRKFETES ISMVSNMLNA HSKVVGSLTS 190 200 210 220 230 240 GGTESIFMAV KAYRDFYKDR TDRPEIVVPV TIHAAFDKAC EYLKIRIVHI DVDPVSYKVD 250 260 270 280 290 300 MAAMKKAINK DTILVAGSAV NFPHGIIDPI DEIAKLAQQY DIGCHVDACL GGFILPFAEK 310 320 330 340 350 360 LDYDIPVFDF RIPGVTSMSV DTHKFGYAAK GTSVVLFGNK KLRRAMYFVA PNWPGGIYAS 370 380 390 400 410 420 PTLPGSRPGG LVAACWASLV SMGNDGFLEK AKGVMETTKK IIKGLQSING VKIIGDPKAM 430 440 450 460 470 480 VVAFTCDNIF YVNDYMSKKG WHLNALQRPN SLHVCVTAKM IGMESLFIED LKDSIKLVKD 490 500 510 520 NSGSLPKDGT APIYGSAHSV PDREMVGTIL SDFIDELITP DYKPSQST

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sphingosine-1-phosphate lyase has a central role in the development of Dictyostelium discoideum." Li G., Foote C., Alexander S., Alexander H. Development 128:3473-3483(2001) [PubMed: 11566853] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE. Strain: AX4.
[2]	"The genome of the social amoeba Dictyostelium discoideum." Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N. , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A. Nature 435:43-57(2005) [PubMed: 15875012] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AX4.
[3]	"Molecular basis for resistance to the anticancer drug cisplatin in Dictyostelium." Li G., Alexander H., Schneider N., Alexander S. Microbiology 146:2219-2227(2000) [PubMed: 10974109] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 232-270, GENE EXPRESSION, RESISTANCE TO CISPLATIN, DISRUPTION PHENOTYPE. Strain: AX4.
[4]	"Sphingosine-1-phosphate plays a role in the suppression of lateral pseudopod formation during Dictyostelium discoideum cell migration and chemotaxis." Kumar A., Wessels D., Daniels K.J., Alexander H., Alexander S., Soll D.R. Cell Motil. Cytoskeleton 59:227-241(2004) [PubMed: 15476260] [Abstract] Cited for: FUNCTIONS AS A NEGATIVE REGULATOR OF LATERAL PSEUDOPOD FORMATION. Strain: AX4.
[5]	"Overexpression of sphingosine-1-phosphate lyase or inhibition of sphingosine kinase in Dictyostelium discoideum results in a selective increase in sensitivity to platinum-based chemotherapy drugs." Min J., Stegner A.L., Alexander H., Alexander S. Eukaryot. Cell 3:795-805(2004) [PubMed: 15190000] [Abstract] Cited for: OVEREXPRESSING STRAINS ARE MORE SENSITIVE TO CISPLATIN, A MODEL OF CISPLATIN-RESISTANCE. Strain: AX3.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY283052 mRNA. Translation: AAP37027.1. AAFI02000047 Genomic DNA. Translation: EAL65989.1. AF233610 Genomic DNA. Translation: AAF97870.1.
RefSeq	XP_639378.1. XM_634286.1.
3D structure databases
ProteinModelPortal	Q54RV9.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblProtists	DDB0214888; DDB0214888; DDB_G0282819.
GeneID	8623817.
GenomeReviews	Gene locus sglA in contig CM000152_GR.
KEGG	ddi:DDB_G0282819.
Organism-specific databases
dictyBase	DDB_G0282819. sglA.
Phylogenomic databases
eggNOG	KOG1383.
GeneTree	EPrGT00050000004523.
HOGENOM	HBG657947.
OMA	IIAACWA.
PhylomeDB	Q54RV9.
Family and domain databases
InterPro	IPR002129. PyrdxlP-dep_de-COase. IPR015424. PyrdxlP-dep_Trfase_major_dom. IPR015421. PyrdxlP-dep_Trfase_major_sub1. [Graphical view]
Gene3D	G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
KO	K01634.
PANTHER	PTHR11999. Pyridoxal_deC. 1 hit.
Pfam	PF00282. Pyridoxal_deC. 1 hit. [Graphical view]
SUPFAM	SSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
ProtoNet	Search...

Entry information

Entry name

SGPL_DICDI

Accession

Primary (citable) accession number: Q54RV9
Secondary accession number(s): Q7Z271, Q9NC67

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 8, 2008
Last sequence update:	May 24, 2005
Last modified:	November 16, 2011
This is version 47 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)