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Protein

Sphingosine-1-phosphate lyase 1

Gene

Sgpl1

Organism
Mus musculus (Mouse)
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. Elevates stress-induced ceramide production and apoptosis.1 Publication

Catalytic activityi

Sphinganine 1-phosphate = phosphoethanolamine + palmitaldehyde.1 Publication

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

  • androgen metabolic process Source: MGI
  • apoptotic signaling pathway Source: UniProtKB
  • ceramide metabolic process Source: UniProtKB
  • estrogen metabolic process Source: MGI
  • face morphogenesis Source: MGI
  • fatty acid metabolic process Source: UniProtKB
  • female gonad development Source: MGI
  • fibroblast migration Source: MGI
  • hemopoiesis Source: MGI
  • kidney development Source: MGI
  • Leydig cell differentiation Source: MGI
  • luteinization Source: MGI
  • nitrogen compound metabolic process Source: MGI
  • palate development Source: MGI
  • platelet-derived growth factor receptor signaling pathway Source: MGI
  • post-embryonic development Source: MGI
  • regulation of multicellular organism growth Source: MGI
  • skeletal system morphogenesis Source: MGI
  • spermatogenesis Source: MGI
  • sphingolipid catabolic process Source: UniProtKB
  • vasculogenesis Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Apoptosis, Lipid metabolism, Sphingolipid metabolism

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BRENDAi4.1.2.27. 3474.
ReactomeiR-MMU-1660661. Sphingolipid de novo biosynthesis.
UniPathwayiUPA00222.

Chemistry

SwissLipidsiSLP:000000935.

Names & Taxonomyi

Protein namesi
Recommended name:
Sphingosine-1-phosphate lyase 1 (EC:4.1.2.27)
Short name:
S1PL
Short name:
SP-lyase 1
Short name:
SPL 1
Short name:
mSPL
Alternative name(s):
Sphingosine-1-phosphate aldolase
Gene namesi
Name:Sgpl1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 10

Organism-specific databases

MGIiMGI:1261415. Sgpl1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 4040LumenalSequence analysisAdd
BLAST
Transmembranei41 – 6121Helical; Signal-anchor for type III membrane proteinSequence analysisAdd
BLAST
Topological domaini62 – 568507CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL5009.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 568568Sphingosine-1-phosphate lyase 1PRO_0000147013Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei353 – 3531N6-(pyridoxal phosphate)lysine; alternateBy similarity
Modified residuei353 – 3531N6-acetyllysine; alternateBy similarity
Modified residuei356 – 3561Nitrated tyrosineBy similarity
Modified residuei366 – 3661Nitrated tyrosineBy similarity
Modified residuei564 – 5641PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Nitration, Phosphoprotein

Proteomic databases

EPDiQ8R0X7.
MaxQBiQ8R0X7.
PaxDbiQ8R0X7.
PRIDEiQ8R0X7.

PTM databases

iPTMnetiQ8R0X7.
PhosphoSiteiQ8R0X7.
SwissPalmiQ8R0X7.

Expressioni

Tissue specificityi

Highest levels are found in liver, followed by kidney, lung, heart and brain.1 Publication

Gene expression databases

BgeeiQ8R0X7.
CleanExiMM_SGPL1.
ExpressionAtlasiQ8R0X7. baseline and differential.
GenevisibleiQ8R0X7. MM.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

BioGridi203199. 2 interactions.
IntActiQ8R0X7. 1 interaction.
MINTiMINT-4134482.
STRINGi10090.ENSMUSP00000090155.

Chemistry

BindingDBiQ8R0X7.

Structurei

3D structure databases

ProteinModelPortaliQ8R0X7.
SMRiQ8R0X7. Positions 110-553.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1383. Eukaryota.
COG0076. LUCA.
GeneTreeiENSGT00390000000046.
HOVERGENiHBG056982.
InParanoidiQ8R0X7.
KOiK01634.
OMAiCTLKEGM.
OrthoDBiEOG76T9QX.
TreeFamiTF300777.

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.

Q8R0X7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPGTDLLKLK DFEPYLEILE SYSTKAKNYV NGYCTKYEPW QLIAWSVLCT
60 70 80 90 100
LLIVWVYELI FQPESLWSRF KKKLFKLIRK MPFIGRKIEQ QVSKAKKDLV
110 120 130 140 150
KNMPFLKVDK DYVKTLPAQG MGTAEVLERL KEYSSMDGSW QEGKASGAVY
160 170 180 190 200
NGEPKLTELL VQAYGEFTWS NPLHPDIFPG LRKLEAEIVR MTCSLFNGGP
210 220 230 240 250
DSCGCVTSGG TESILMACKA YRDLALEKGI KTPEIVAPES AHAAFDKAAH
260 270 280 290 300
YFGMKIVRVA LKKNMEVDVQ AMKRAISRNT AMLVCSTPQF PHGVMDPVPE
310 320 330 340 350
VAKLAVRYKI PLHVDACLGG FLIVFMEKAG YPLEKPFDFR VKGVTSISAD
360 370 380 390 400
THKYGYAPKG SSVVMYSNEK YRTYQFFVGA DWQGGVYASP SIAGSRPGGI
410 420 430 440 450
IAACWAALMH FGENGYVEAT KQIIKTARFL KSELENIKNI FIFGDPQLSV
460 470 480 490 500
IALGSNDFDI YRLSNMMSAK GWNFNYLQFP RSIHFCITLV HTRKRVAIQF
510 520 530 540 550
LKDIRESVTQ IMKNPKAKTT GMGAIYGMAQ ATIDRKLVAE ISSVFLDCLY
560
TTDPVTQGNQ MNGSPKPR
Length:568
Mass (Da):63,677
Last modified:June 1, 2002 - v1
Checksum:iFA5D52E4E49DF09E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti305 – 3051A → T in AAC03768 (PubMed:9464245).Curated
Sequence conflicti473 – 4731N → K in BAC31437 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF036894 mRNA. Translation: AAC03768.1.
AK036747 mRNA. Translation: BAC29562.1.
AK037789 mRNA. Translation: BAC29872.1.
AK043024 mRNA. Translation: BAC31437.1.
AK049342 mRNA. Translation: BAC33695.1.
BC026135 mRNA. Translation: AAH26135.1.
CCDSiCCDS35914.1.
PIRiJC5923.
RefSeqiNP_001303602.1. NM_001316673.1.
NP_001303603.1. NM_001316674.1.
NP_033189.2. NM_009163.4.
UniGeneiMm.412319.
Mm.431862.

Genome annotation databases

EnsembliENSMUST00000092498; ENSMUSP00000090155; ENSMUSG00000020097.
ENSMUST00000122259; ENSMUSP00000112975; ENSMUSG00000020097.
GeneIDi20397.
KEGGimmu:20397.
UCSCiuc007ffk.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF036894 mRNA. Translation: AAC03768.1.
AK036747 mRNA. Translation: BAC29562.1.
AK037789 mRNA. Translation: BAC29872.1.
AK043024 mRNA. Translation: BAC31437.1.
AK049342 mRNA. Translation: BAC33695.1.
BC026135 mRNA. Translation: AAH26135.1.
CCDSiCCDS35914.1.
PIRiJC5923.
RefSeqiNP_001303602.1. NM_001316673.1.
NP_001303603.1. NM_001316674.1.
NP_033189.2. NM_009163.4.
UniGeneiMm.412319.
Mm.431862.

3D structure databases

ProteinModelPortaliQ8R0X7.
SMRiQ8R0X7. Positions 110-553.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi203199. 2 interactions.
IntActiQ8R0X7. 1 interaction.
MINTiMINT-4134482.
STRINGi10090.ENSMUSP00000090155.

Chemistry

BindingDBiQ8R0X7.
ChEMBLiCHEMBL5009.
SwissLipidsiSLP:000000935.

PTM databases

iPTMnetiQ8R0X7.
PhosphoSiteiQ8R0X7.
SwissPalmiQ8R0X7.

Proteomic databases

EPDiQ8R0X7.
MaxQBiQ8R0X7.
PaxDbiQ8R0X7.
PRIDEiQ8R0X7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000092498; ENSMUSP00000090155; ENSMUSG00000020097.
ENSMUST00000122259; ENSMUSP00000112975; ENSMUSG00000020097.
GeneIDi20397.
KEGGimmu:20397.
UCSCiuc007ffk.2. mouse.

Organism-specific databases

CTDi8879.
MGIiMGI:1261415. Sgpl1.

Phylogenomic databases

eggNOGiKOG1383. Eukaryota.
COG0076. LUCA.
GeneTreeiENSGT00390000000046.
HOVERGENiHBG056982.
InParanoidiQ8R0X7.
KOiK01634.
OMAiCTLKEGM.
OrthoDBiEOG76T9QX.
TreeFamiTF300777.

Enzyme and pathway databases

UniPathwayiUPA00222.
BRENDAi4.1.2.27. 3474.
ReactomeiR-MMU-1660661. Sphingolipid de novo biosynthesis.

Miscellaneous databases

ChiTaRSiSgpl1. mouse.
PROiQ8R0X7.
SOURCEiSearch...

Gene expression databases

BgeeiQ8R0X7.
CleanExiMM_SGPL1.
ExpressionAtlasiQ8R0X7. baseline and differential.
GenevisibleiQ8R0X7. MM.

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. "Identification of the first mammalian sphingosine phosphate lyase gene and its functional expression in yeast."
    Zhou J., Saba J.D.
    Biochem. Biophys. Res. Commun. 242:502-507(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY.
    Strain: C57BL/6J.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Bone and Thymus.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Liver.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiSGPL1_MOUSE
AccessioniPrimary (citable) accession number: Q8R0X7
Secondary accession number(s): O54955, Q8C942
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 24, 2003
Last sequence update: June 1, 2002
Last modified: June 8, 2016
This is version 123 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  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.