SPTLC1

Serine palmitoyltransferase, long chain base subunit 1

Identifiers

SPTLC1 ; HSAN1; HSN1; LBC1; LCB1; SPT1; SPTI

External IDs

OMIM: 605712 MGI: 1099431 HomoloGene: 4681 IUPHAR: 2509 ChEMBL: 1250343 GeneCards: SPTLC1 Gene

2.3.1.50

Gene ontology
Molecular function	• serine C-palmitoyltransferase activity • protein binding • pyridoxal phosphate binding
Cellular component	• endoplasmic reticulum membrane • integral component of membrane • serine C-palmitoyltransferase complex • SPOTS complex
Biological process	• sphingolipid metabolic process • sphingomyelin biosynthetic process • sphingolipid biosynthetic process • small molecule metabolic process • sphinganine biosynthetic process • sphingosine biosynthetic process • ceramide biosynthetic process
Sources: Amigo / QuickGO

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 9:
92.03 – 92.12 Mb

Chr 13:
53.33 – 53.38 Mb

PubMed search

Serine palmitoyltransferase, long chain base subunit 1, also known as SPTLC1, is a protein which in humans is encoded by the SPTLC1 gene.^[1]^[2]

Serine palmitoyltransferase, which consists of two different subunits, is the initial enzyme in sphingolipid biosynthesis. It converts L-serine and palmitoyl CoA to 3-oxosphinganine with pyridoxal 5'-phosphate as a cofactor. The product of this gene is the long chain base subunit 1 of serine palmitoyltransferase. Mutations in this gene were identified in patients with hereditary sensory neuropathy type 1. Alternatively spliced variants encoding different isoforms have been identified.^[1]

References

1 2 "Entrez Gene: SPTLC1 serine palmitoyltransferase, long chain base subunit 1".
↑ Weiss B, Stoffel W (October 1997). "Human and murine serine-palmitoyl-CoA transferase--cloning, expression and characterization of the key enzyme in sphingolipid synthesis". Eur. J. Biochem. 249 (1): 239–47. doi:10.1111/j.1432-1033.1997.00239.x. PMID 9363775.

Weiss B, Stoffel W (1997). "Human and murine serine-palmitoyl-CoA transferase--cloning, expression and characterization of the key enzyme in sphingolipid synthesis.". Eur. J. Biochem. 249 (1): 239–47. doi:10.1111/j.1432-1033.1997.00239.x. PMID 9363775.
Gable K, Slife H, Bacikova D, et al. (2000). "Tsc3p is an 80-amino acid protein associated with serine palmitoyltransferase and required for optimal enzyme activity.". J. Biol. Chem. 275 (11): 7597–603. doi:10.1074/jbc.275.11.7597. PMID 10713067.
Hanada K, Hara T, Nishijima M (2000). "Purification of the serine palmitoyltransferase complex responsible for sphingoid base synthesis by using affinity peptide chromatography techniques.". J. Biol. Chem. 275 (12): 8409–15. doi:10.1074/jbc.275.12.8409. PMID 10722674.
Perry DK, Carton J, Shah AK, et al. (2000). "Serine palmitoyltransferase regulates de novo ceramide generation during etoposide-induced apoptosis.". J. Biol. Chem. 275 (12): 9078–84. doi:10.1074/jbc.275.12.9078. PMID 10722759.
Bejaoui K, Wu C, Scheffler MD, et al. (2001). "SPTLC1 is mutated in hereditary sensory neuropathy, type 1.". Nat. Genet. 27 (3): 261–2. doi:10.1038/85817. PMID 11242106.
Dawkins JL, Hulme DJ, Brahmbhatt SB, et al. (2001). "Mutations in SPTLC1, encoding serine palmitoyltransferase, long chain base subunit-1, cause hereditary sensory neuropathy type I.". Nat. Genet. 27 (3): 309–12. doi:10.1038/85879. PMID 11242114.
Nicholson GA, Dawkins JL, Blair IP, et al. (2001). "Hereditary sensory neuropathy type I: haplotype analysis shows founders in southern England and Europe.". Am. J. Hum. Genet. 69 (3): 655–9. doi:10.1086/323252. PMC 1235494. PMID 11479835.
Stachowitz S, Alessandrini F, Abeck D, et al. (2003). "Permeability barrier disruption increases the level of serine palmitoyltransferase in human epidermis.". J. Invest. Dermatol. 119 (5): 1048–52. doi:10.1046/j.1523-1747.2002.19524.x. PMID 12445191.
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.
CAMPBELL AM, HOFFMAN HL (1996). "SENSORY RADICULAR NEUROPATHY ASSOCIATED WITH MUSCLE WASTING IN TWO CASES.". Brain 87: 67–74. doi:10.1093/brain/87.1.67. PMID 14152213.
Verhoeven K, Coen K, De Vriendt E, et al. (2004). "SPTLC1 mutation in twin sisters with hereditary sensory neuropathy type I.". Neurology 62 (6): 1001–2. doi:10.1212/01.wnl.0000115388.10828.5c. PMID 15037712.
Humphray SJ, Oliver K, Hunt AR, et al. (2004). "DNA sequence and analysis of human chromosome 9.". Nature 429 (6990): 369–74. doi:10.1038/nature02465. PMC 2734081. PMID 15164053.
Dedov VN, Dedova IV, Nicholson GA (2006). "Hypoxia causes aggregation of serine palmitoyltransferase followed by non-apoptotic death of human lymphocytes.". Cell Cycle 3 (10): 1271–7. doi:10.4161/cc.3.10.1163. PMID 15467453.
Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network.". Nature 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
McCampbell A, Truong D, Broom DC, et al. (2006). "Mutant SPTLC1 dominantly inhibits serine palmitoyltransferase activity in vivo and confers an age-dependent neuropathy.". Hum. Mol. Genet. 14 (22): 3507–21. doi:10.1093/hmg/ddi380. PMID 16210380.
Chen M, Han G, Dietrich CR, et al. (2007). "The essential nature of sphingolipids in plants as revealed by the functional identification and characterization of the Arabidopsis LCB1 subunit of serine palmitoyltransferase.". Plant Cell 18 (12): 3576–93. doi:10.1105/tpc.105.040774. PMC 1785403. PMID 17194770.
Hornemann T, Wei Y, von Eckardstein A (2007). "Is the mammalian serine palmitoyltransferase a high-molecular-mass complex?". Biochem. J. 405 (1): 157–64. doi:10.1042/BJ20070025. PMC 1925250. PMID 17331073.
Ewing RM, Chu P, Elisma F, et al. (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry.". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.

External links

GeneReviews/NIH/NCBI/UW entry on Hereditary Sensory Neuropathy Type I

Transferases: acyltransferases (EC 2.3)

2.3.1: other than amino-acyl groups	acetyltransferases: Acetyl-Coenzyme A acetyltransferase N-Acetylglutamate synthase Choline acetyltransferase Dihydrolipoyl transacetylase Acetyl-CoA C-acyltransferase Beta-galactoside transacetylase Chloramphenicol acetyltransferase N-acetyltransferase Serotonin N-acetyl transferase HGSNAT ARD1A Histone acetyltransferase P300/CBP NAT2 palmitoyltransferases: Carnitine O-palmitoyltransferase CPT1 CPT2 Serine C-palmitoyltransferase SPTLC1 SPTLC2 other: Acyltransferase like 2 Aminolevulinic acid synthase Beta-ketoacyl-ACP synthase Glyceronephosphate O-acyltransferase Lecithin—cholesterol acyltransferase Glycerol-3-phosphate O-acyltransferase 1-acylglycerol-3-phosphate O-acyltransferase 2-acylglycerol-3-phosphate O-acyltransferase ABHD5

2.3.2: Aminoacyltransferases	Gamma-glutamyl transpeptidase Peptidyl transferase Transglutaminase Tissue transglutaminase Keratinocyte transglutaminase Factor XIII

2.3.3: converted into alkyl on transfer	Citrate synthase ATP citrate lyase HMG-CoA synthase Malate synthase

Metabolism, lipid metabolism, glycolipid enzymes

Sphingolipid

To glycosphingolipid	Glycosyltransferase Sulfotransferase

To ceramide	From ganglioside Beta-galactosidase Hexosaminidase A Neuraminidase Glucocerebrosidase From globoside Hexosaminidase B Alpha-galactosidase Beta-galactosidase Glucocerebrosidase From sphingomyelin Sphingomyelin phosphodiesterase Sphingomyelin phosphodiesterase 1 From sulfatide Arylsulfatase A Galactosylceramidase

To sphingosine	Ceramidase ACER1 ACER2 ACER3 ASAH1 ASAH2 ASAH2B ASAH2C

Other	Sphingosine kinase

NCL

Ceramide synthesis

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SPTLC1

References

Further reading

External links