SGPL1

Sphingosine-1-phosphate lyase 1
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 4Q6R​
Identifiers
Symbols	SGPL1 ; S1PL; SPL
External IDs	OMIM: 603729 MGI: 1261415 HomoloGene: 2897 GeneCards: SGPL1 Gene
EC number	4.1.2.27
Gene ontology Molecular function • protein binding • sphinganine-1-phosphate aldolase activity • carboxy-lyase activity • pyridoxal phosphate binding Cellular component • endoplasmic reticulum • endoplasmic reticulum membrane • integral component of endoplasmic reticulum membrane Biological process • luteinization • vasculogenesis • kidney development • fatty acid metabolic process • sphingolipid metabolic process • ceramide metabolic process • spermatogenesis • androgen metabolic process • estrogen metabolic process • post-embryonic development • fibroblast migration • hemopoiesis • sphingolipid biosynthetic process • sphingolipid catabolic process • Leydig cell differentiation • regulation of multicellular organism growth • small molecule metabolic process • platelet-derived growth factor receptor signaling pathway • skeletal system morphogenesis • palate development • face morphogenesis • apoptotic signaling pathway Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	8879	20397
Ensembl	ENSG00000166224	ENSMUSG00000020097
UniProt	O95470	Q8R0X7
RefSeq (mRNA)	NM_003901	NM_009163
RefSeq (protein)	NP_003892	NP_033189
Location (UCSC)	Chr 10: 70.82 – 70.88 Mb	Chr 10: 61.1 – 61.15 Mb
PubMed search

Sphingosine-1-phosphate lyase 1 is an enzyme that in humans is encoded by the SGPL1 gene.^[1][2][3]

References

1. Zhou J, Saba JD (Mar 1998). "Identification of the first mammalian sphingosine phosphate lyase gene and its functional expression in yeast". Biochem Biophys Res Commun 242 (3): 502–7. doi:10.1006/bbrc.1997.7993. PMID 9464245.
2. Oskouian B, Sooriyakumaran P, Borowsky AD, Crans A, Dillard-Telm L, Tam YY, Bandhuvula P, Saba JD (Nov 2006). "Sphingosine-1-phosphate lyase potentiates apoptosis via p53- and p38-dependent pathways and is down-regulated in colon cancer". Proc Natl Acad Sci U S A 103 (46): 17384–9. doi:10.1073/pnas.0600050103. PMC 1859938. PMID 17090686.
3. "Entrez Gene: SGPL1 sphingosine-1-phosphate lyase 1".

Further reading

• Van Veldhoven PP, Mannaerts GP (1991). "Subcellular localization and membrane topology of sphingosine-1-phosphate lyase in rat liver.". J. Biol. Chem. 266 (19): 12502–7. PMID 2061324.
• Nagase T, Ishikawa K, Kikuno R, et al. (2000). "Prediction of the coding sequences of unidentified human genes. XV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro.". DNA Res. 6 (5): 337–45. doi:10.1093/dnares/6.5.337. PMID 10574462.
• Van Veldhoven PP, Gijsbers S, Mannaerts GP, et al. (2000). "Human sphingosine-1-phosphate lyase: cDNA cloning, functional expression studies and mapping to chromosome 10q22(1).". Biochim. Biophys. Acta 1487 (2-3): 128–34. doi:10.1016/s1388-1981(00)00079-2. PMID 11018465.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Reiss U, Oskouian B, Zhou J, et al. (2004). "Sphingosine-phosphate lyase enhances stress-induced ceramide generation and apoptosis.". J. Biol. Chem. 279 (2): 1281–90. doi:10.1074/jbc.M309646200. PMID 14570870.
• Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
• Zhan X, Desiderio DM (2006). "Nitroproteins from a human pituitary adenoma tissue discovered with a nitrotyrosine affinity column and tandem mass spectrometry.". Anal. Biochem. 354 (2): 279–89. doi:10.1016/j.ab.2006.05.024. PMID 16777052.