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Protein

Sphingosine-1-phosphate lyase

Gene

Sply

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

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.1 Publication

Catalytic activityi

Sphinganine 1-phosphate = phosphoethanolamine + palmitaldehyde.

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

  • adult somatic muscle development Source: FlyBase
  • carboxylic acid metabolic process Source: InterPro
  • lateral inhibition Source: FlyBase
  • multicellular organism development Source: UniProtKB-KW
  • sphingolipid catabolic process Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Lyase

Keywords - Biological processi

Lipid metabolism, Sphingolipid metabolism

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

ReactomeiR-DME-1660661. Sphingolipid de novo biosynthesis.
UniPathwayiUPA00222.

Names & Taxonomyi

Protein namesi
Recommended name:
Sphingosine-1-phosphate lyase (EC:4.1.2.27)
Short name:
S1PL
Short name:
SP-lyase
Short name:
SPL
Alternative name(s):
Sphingosine-1-phosphate aldolase
Gene namesi
Name:Sply
Synonyms:Spl
ORF Names:CG8946
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0010591. Sply.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 2626LumenalSequence analysisAdd
BLAST
Transmembranei27 – 4721Helical; Signal-anchor for type III membrane proteinSequence analysisAdd
BLAST
Topological domaini48 – 545498CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 545545Sphingosine-1-phosphate lyasePRO_0000147016Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei342 – 3421N6-(pyridoxal phosphate)lysineBy similarity

Proteomic databases

PaxDbiQ9V7Y2.
PRIDEiQ9V7Y2.

Expressioni

Tissue specificityi

Localized to the developing gut primordium during embryogenesis.1 Publication

Developmental stagei

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.1 Publication

Gene expression databases

BgeeiQ9V7Y2.
GenevisibleiQ9V7Y2. DM.

Interactioni

Protein-protein interaction databases

BioGridi70079. 1 interaction.
IntActiQ9V7Y2. 2 interactions.
STRINGi7227.FBpp0086158.

Structurei

3D structure databases

ProteinModelPortaliQ9V7Y2.
SMRiQ9V7Y2. Positions 71-541.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1383. Eukaryota.
COG0076. LUCA.
GeneTreeiENSGT00390000000046.
InParanoidiQ9V7Y2.
KOiK01634.
OMAiCTLKEGM.
OrthoDBiEOG76T9QX.
PhylomeDBiQ9V7Y2.

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.

Q9V7Y2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRPFSGSDCL KPVTEGINRA FGAKEPWQVA TITATTVLGG VWLWTVICQD
60 70 80 90 100
ENLYIRGKRQ FFKFAKKIPA VRRQVETELA KAKNDFETEI KKSNAHLTYS
110 120 130 140 150
ETLPEKGLSK EEILRLVDEH LKTGHYNWRD GRVSGAVYGY KPDLVELVTE
160 170 180 190 200
VYGKASYTNP LHADLFPGVC KMEAEVVRMA CNLFHGNSAS CGTMTTGGTE
210 220 230 240 250
SIVMAMKAYR DFAREYKGIT RPNIVVPKTV HAAFDKGGQY FNIHVRSVDV
260 270 280 290 300
DPETYEVDIK KFKRAINRNT ILLVGSAPNF PYGTIDDIEA IAALGVKYDI
310 320 330 340 350
PVHVDACLGS FVVALVRNAG YKLRPFDFEV KGVTSISADT HKYGFAPKGS
360 370 380 390 400
SVILYSDKKY KDHQFTVTTD WPGGVYGSPT VNGSRAGGII AACWATMMSF
410 420 430 440 450
GYDGYLEATK RIVDTARYIE RGVRDIDGIF IFGKPATSVI ALGSNVFDIF
460 470 480 490 500
RLSDSLCKLG WNLNALQFPS GIHLCVTDMH TQPGVADKFI ADVRSCTAEI
510 520 530 540
MKDPGQPVVG KMALYGMAQS IPDRSVIGEV TRLFLHSMYY TPSQK
Length:545
Mass (Da):60,305
Last modified:May 1, 2000 - v1
Checksum:i26000F4AE43F85FD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ297394 mRNA. Translation: CAC10531.1.
AE013599 Genomic DNA. Translation: AAF57903.1.
AY052075 mRNA. Translation: AAK93499.1.
RefSeqiNP_652032.1. NM_143775.3.
NP_725652.1. NM_166215.2.
UniGeneiDm.3390.

Genome annotation databases

EnsemblMetazoaiFBtr0087007; FBpp0086158; FBgn0010591.
FBtr0087008; FBpp0086159; FBgn0010591.
GeneIDi46059.
KEGGidme:Dmel_CG8946.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ297394 mRNA. Translation: CAC10531.1.
AE013599 Genomic DNA. Translation: AAF57903.1.
AY052075 mRNA. Translation: AAK93499.1.
RefSeqiNP_652032.1. NM_143775.3.
NP_725652.1. NM_166215.2.
UniGeneiDm.3390.

3D structure databases

ProteinModelPortaliQ9V7Y2.
SMRiQ9V7Y2. Positions 71-541.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi70079. 1 interaction.
IntActiQ9V7Y2. 2 interactions.
STRINGi7227.FBpp0086158.

Proteomic databases

PaxDbiQ9V7Y2.
PRIDEiQ9V7Y2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0087007; FBpp0086158; FBgn0010591.
FBtr0087008; FBpp0086159; FBgn0010591.
GeneIDi46059.
KEGGidme:Dmel_CG8946.

Organism-specific databases

CTDi46059.
FlyBaseiFBgn0010591. Sply.

Phylogenomic databases

eggNOGiKOG1383. Eukaryota.
COG0076. LUCA.
GeneTreeiENSGT00390000000046.
InParanoidiQ9V7Y2.
KOiK01634.
OMAiCTLKEGM.
OrthoDBiEOG76T9QX.
PhylomeDBiQ9V7Y2.

Enzyme and pathway databases

UniPathwayiUPA00222.
ReactomeiR-DME-1660661. Sphingolipid de novo biosynthesis.

Miscellaneous databases

ChiTaRSiSply. fly.
GenomeRNAii46059.
PROiQ9V7Y2.

Gene expression databases

BgeeiQ9V7Y2.
GenevisibleiQ9V7Y2. DM.

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. "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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  4. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Embryo.

Entry informationi

Entry nameiSGPL_DROME
AccessioniPrimary (citable) accession number: Q9V7Y2
Secondary accession number(s): Q0E946
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 24, 2003
Last sequence update: May 1, 2000
Last modified: July 6, 2016
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  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.