Reviewed, UniProtKB/Swiss-Prot Q9V7Y2 (SGPL_DROME)

Names and origin

Protein names

Recommended name:
    Sphingosine-1-phosphate lyase
      Short name=SP-lyase
      Short name=SPL
    EC=4.1.2.27
Alternative name(s):
    Sphingosine-1-phosphate aldolase

Gene names

Name:	Sply
Synonyms:	Spl
ORF Names:	CG8946

Organism

Drosophila melanogaster (Fruit fly) [Complete proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	545 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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. Sphingolipid catabolism is required for normal development including viability, reproduction and muscle development. Ref.2
Catalytic activity	Sphinganine 1-phosphate = phosphoethanolamine + palmitaldehyde.
Cofactor	Pyridoxal phosphate By similarity.
Pathway	Lipid metabolism; sphingolipid metabolism.
Subcellular location	Endoplasmic reticulum membrane; Single-pass type III membrane protein By similarity.
Tissue specificity	Localized to the developing gut primordium during embryogenesis. Ref.2
Developmental stage	Expressed both maternally and zygotically. Expression is high in early and late embryos, and then again early in metamorphosis, followed by reduction to basal levels after eclosion of adult flies in both males and females. Ref.2
Sequence similarities	Belongs to the group II decarboxylase family. Sphingosine-1-phosphate lyase subfamily.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane
Domain	Signal-anchor Transmembrane
Ligand	Pyridoxal phosphate
Molecular function	Developmental protein Lyase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	carboxylic acid metabolic process Inferred from electronic annotation. Source: InterPro multicellular organismal development Inferred from electronic annotation. Source: UniProtKB-KW sphingolipid catabolic process Ref.2 Non-traceable author statement. Source: UniProtKB
Cellular component	integral to endoplasmic reticulum membrane Non-traceable author statement. Source: UniProtKB
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 Non-traceable author statement. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 545	545	Sphingosine-1-phosphate lyase		PRO_0000147016
Regions
	Topological domain	1 – 26	26	Lumenal Potential
	Transmembrane	27 – 47	21	Signal-anchor for type III membrane protein Potential
	Topological domain	48 – 545	498	Cytoplasmic Potential
Amino acid modifications
	Modified residue	342	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9V7Y2-1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 26000F4AE43F85FD	FASTA	545	60,305
	10 20 30 40 50 60 MRPFSGSDCL KPVTEGINRA FGAKEPWQVA TITATTVLGG VWLWTVICQD ENLYIRGKRQ 70 80 90 100 110 120 FFKFAKKIPA VRRQVETELA KAKNDFETEI KKSNAHLTYS ETLPEKGLSK EEILRLVDEH 130 140 150 160 170 180 LKTGHYNWRD GRVSGAVYGY KPDLVELVTE VYGKASYTNP LHADLFPGVC KMEAEVVRMA 190 200 210 220 230 240 CNLFHGNSAS CGTMTTGGTE SIVMAMKAYR DFAREYKGIT RPNIVVPKTV HAAFDKGGQY 250 260 270 280 290 300 FNIHVRSVDV DPETYEVDIK KFKRAINRNT ILLVGSAPNF PYGTIDDIEA IAALGVKYDI 310 320 330 340 350 360 PVHVDACLGS FVVALVRNAG YKLRPFDFEV KGVTSISADT HKYGFAPKGS SVILYSDKKY 370 380 390 400 410 420 KDHQFTVTTD WPGGVYGSPT VNGSRAGGII AACWATMMSF GYDGYLEATK RIVDTARYIE 430 440 450 460 470 480 RGVRDIDGIF IFGKPATSVI ALGSNVFDIF RLSDSLCKLG WNLNALQFPS GIHLCVTDMH 490 500 510 520 530 540 TQPGVADKFI ADVRSCTAEI MKDPGQPVVG KMALYGMAQS IPDRSVIGEV TRLFLHSMYY TPSQK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Functional expression of sphingosine-phosphate lyase from Arabidopsis and Drosophila." Van Veldhoven P.P. Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Sply regulation of sphingolipid signaling molecules is essential for Drosophila development." Herr D.R., Fyrst H., Phan V., Heinecke K., Georges R., Harris G.L., Saba J.D. Development 130:2443-2453(2003) [PubMed: 12702658] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE. Strain: Berkeley. Tissue: Embryo.
[3]	"The genome sequence of Drosophila melanogaster." Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C. Science 287:2185-2195(2000) [PubMed: 10731132] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[4]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract] Cited for: GENOME REANNOTATION.
[5]	"A Drosophila full-length cDNA resource." Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E. Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed: 12537569] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Embryo.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AJ297394 mRNA. Translation: CAC10531.1. AE013599 Genomic DNA. Translation: AAF57903.1. AY052075 mRNA. Translation: AAK93499.1.
RefSeq	NP_652032.1. NP_725652.1.
UniGene	Dm.3390
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9V7Y2. 1 interaction.
STRING	Q9V7Y2.
Proteomic databases
PRIDE	Q9V7Y2.
Genome annotation databases
Ensembl	FBtr0087008; FBpp0086159; FBgn0010591; Drosophila melanogaster. [Genome view]
GeneID	46059.
KEGG	dme:Dmel_CG8946.
Organism-specific databases
CTD	46059.
FlyBase	FBgn0010591. Sply.
Phylogenomic databases
HOGENOM	Q9V7Y2.
OMA	IIAACWA.
Enzyme and pathway databases
BioCyc	DMEL-XXX-02:DMEL-XXX-02-005096-MON. DMEL-XXX-02:DMEL-XXX-02-005097-MON.
BRENDA	4.1.2.27. 48.
Gene expression databases
ArrayExpress	Q9V7Y2.
GermOnline	CG8946. Drosophila melanogaster.
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	838670.

Entry information

Entry name

SGPL_DROME

Accession

Primary (citable) accession number: Q9V7Y2
Secondary accession number(s): Q0E946

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 24, 2003
Last sequence update:	May 1, 2000
Last modified:	November 3, 2009
This is version 62 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project