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Reviewed, UniProtKB/Swiss-Prot Q8R0X7 (SGPL1_MOUSE)

Last modified June 16, 2009. Version 60. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Sphingosine-1-phosphate lyase 1
      Short name=SP-lyase
      Short name=mSPL
    EC=4.1.2.27
Alternative name(s):
    Sphingosine-1-phosphate aldolase
Gene names
Name: Sgpl1
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

Protein attributes

Sequence length568 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

Cleaves phosphorylated sphingoid bases (PSBs), such as sphingosine-1-phosphate, into fatty aldehydes and phosphoethanolamine. Elevates stress-induced ceramide production and apoptosis.

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

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

Sequence similarities

Belongs to the group II decarboxylase family. Sphingosine-1-phosphate lyase subfamily.

Ontologies

Keywords
   Biological processApoptosis
Lipid metabolism
   Cellular componentEndoplasmic reticulum
Membrane
   DomainSignal-anchor
Transmembrane
   LigandPyridoxal phosphate
   Molecular functionLyase
Gene Ontology (GO)
   Biological processapoptosis

Inferred from sequence or structural similarity. Source: UniProtKB

carboxylic acid metabolic process

Inferred from electronic annotation. Source: InterPro

ceramide metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

face morphogenesis

Inferred from mutant phenotype. Source: MGI

fibroblast migration

Inferred from mutant phenotype. Source: MGI

hemopoiesis

Inferred from mutant phenotype. Source: MGI

kidney development

Inferred from mutant phenotype. Source: MGI

nitrogen compound metabolic process

Inferred from mutant phenotype. Source: MGI

palate development

Inferred from mutant phenotype. Source: MGI

platelet-derived growth factor receptor signaling pathway

Inferred from mutant phenotype. Source: MGI

post-embryonic development

Inferred from mutant phenotype. Source: MGI

regulation of multicellular organism growth

Inferred from mutant phenotype. Source: MGI

skeletal system morphogenesis

Inferred from mutant phenotype. Source: MGI

vasculogenesis

Inferred from mutant phenotype. Source: MGI

   Cellular componentendoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functioncarboxy-lyase activity

Inferred from electronic annotation. Source: InterPro

pyridoxal phosphate binding

Inferred from electronic annotation. Source: InterPro

sphinganine-1-phosphate aldolase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 568568Sphingosine-1-phosphate lyase 1
PRO_0000147013

Regions

Topological domain1 – 4040Lumenal Potential
Transmembrane41 – 6121Signal-anchor for type III membrane protein Potential
Topological domain62 – 568507Cytoplasmic Potential

Amino acid modifications

Modified residue3531N6-(pyridoxal phosphate)lysine By similarity

Experimental info

Sequence conflict3051A → T in AAC03768. Ref.1
Sequence conflict4731N → K in BAC31437. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q8R0X7-1 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: FA5D52E4E49DF09E

FASTA56863,677
        10         20         30         40         50         60 
MPGTDLLKLK DFEPYLEILE SYSTKAKNYV NGYCTKYEPW QLIAWSVLCT LLIVWVYELI 

        70         80         90        100        110        120 
FQPESLWSRF KKKLFKLIRK MPFIGRKIEQ QVSKAKKDLV KNMPFLKVDK DYVKTLPAQG 

       130        140        150        160        170        180 
MGTAEVLERL KEYSSMDGSW QEGKASGAVY NGEPKLTELL VQAYGEFTWS NPLHPDIFPG 

       190        200        210        220        230        240 
LRKLEAEIVR MTCSLFNGGP DSCGCVTSGG TESILMACKA YRDLALEKGI KTPEIVAPES 

       250        260        270        280        290        300 
AHAAFDKAAH YFGMKIVRVA LKKNMEVDVQ AMKRAISRNT AMLVCSTPQF PHGVMDPVPE 

       310        320        330        340        350        360 
VAKLAVRYKI PLHVDACLGG FLIVFMEKAG YPLEKPFDFR VKGVTSISAD THKYGYAPKG 

       370        380        390        400        410        420 
SSVVMYSNEK YRTYQFFVGA DWQGGVYASP SIAGSRPGGI IAACWAALMH FGENGYVEAT 

       430        440        450        460        470        480 
KQIIKTARFL KSELENIKNI FIFGDPQLSV IALGSNDFDI YRLSNMMSAK GWNFNYLQFP 

       490        500        510        520        530        540 
RSIHFCITLV HTRKRVAIQF LKDIRESVTQ IMKNPKAKTT GMGAIYGMAQ ATIDRKLVAE 

       550        560 
ISSVFLDCLY TTDPVTQGNQ MNGSPKPR 

« Hide

References

« Hide 'large scale' references
[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: 9464245] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
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. expand/collapse author list , 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: 16141072] [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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

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.
IPIIPI00320480.
PIRJC5923.
RefSeqNP_033189.2.
UniGeneMm.412319

3D structure databases

ModBaseSearch...

Proteomic databases

PRIDEQ8R0X7.

Genome annotation databases

EnsemblENSMUSG00000020097. Mus musculus. [Contig view]
GeneID20397.
KEGGmmu:20397.

Organism-specific databases

MGIMGI:1261415. Sgpl1.

Phylogenomic databases

HOVERGENQ8R0X7.
OMAQ8R0X7. IIAACWA.

Enzyme and pathway databases

BRENDA4.1.2.27. 244.

Gene expression databases

ArrayExpressQ8R0X7.
BgeeQ8R0X7.
CleanExMM_SGPL1.
GermOnlineENSMUSG00000020097. Mus musculus.

Family and domain databases

InterProIPR002129. PyrdxlP-dep_de-COase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
[Graphical view]
Gene3DG3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
PANTHERPTHR11999. Pyridoxal_deC. 1 hit.
PfamPF00282. Pyridoxal_deC. 1 hit.
[Graphical view]
PROSITEPS00392. DDC_GAD_HDC_YDC. False negative.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio298346.
SOURCESearch...

Entry information

Entry nameSGPL1_MOUSE
AccessionPrimary (citable) accession number: Q8R0X7
Secondary accession number(s): O54955, Q8C942
Entry history
Integrated into UniProtKB/Swiss-Prot: October 24, 2003
Last sequence update: June 1, 2002
Last modified: June 16, 2009
This is version 60 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

MGD cross-references

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents