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Details on Person UniProt:O15270 SPTLC2
| Class:Id | ReferenceGeneProduct:58443 |
|---|---|
| _chainChangeLog | chain:1-562 added on Fri February 6 2015 |
| _displayName | UniProt:O15270 SPTLC2 |
| _timestamp | 2025-02-21 18:52:05 |
| chain | chain:1-562 |
| checksum | 0C1AA1E233DE36F1 |
| comment | FUNCTION Component of the serine palmitoyltransferase multisubunit enzyme (SPT) that catalyzes the initial and rate-limiting step in sphingolipid biosynthesis by condensing L-serine and activated acyl-CoA (most commonly palmitoyl-CoA) to form long-chain bases (PubMed:19416851, PubMed:19648650, PubMed:20504773, PubMed:20920666). The SPT complex is composed of SPTLC1, SPTLC2 or SPTLC3 and SPTSSA or SPTSSB. Within this complex, the heterodimer consisting of SPTLC1 and SPTLC2/SPTLC3 forms the catalytic core (PubMed:19416851). The composition of the serine palmitoyltransferase (SPT) complex determines the substrate preference (PubMed:19416851). The SPTLC1-SPTLC2-SPTSSA complex shows a strong preference for C16-CoA substrate, while the SPTLC1-SPTLC3-SPTSSA isozyme uses both C14-CoA and C16-CoA as substrates, with a slight preference for C14-CoA (PubMed:19416851, PubMed:19648650). The SPTLC1-SPTLC2-SPTSSB complex shows a strong preference for C18-CoA substrate, while the SPTLC1-SPTLC3-SPTSSB isozyme displays an ability to use a broader range of acyl-CoAs, without apparent preference (PubMed:19416851, PubMed:19648650). Crucial for adipogenesis (By similarity).CATALYTIC ACTIVITY L-serine + hexadecanoyl-CoA + H(+) = 3-oxosphinganine + CO2 + CoACATALYTIC ACTIVITY octadecanoyl-CoA + L-serine + H(+) = 3-oxoeicosasphinganine + CO2 + CoACOFACTOR SPT complex catalytic activity is negatively regulated by ORMDL proteins, including ORMDL3, in the presence of ceramides (PubMed:37308477). This mechanism allows to maintain ceramide levels at sufficient concentrations for the production of complex sphingolipids, but which prevents the accumulation of ceramides to levels that trigger apoptosis (Probable).BIOPHYSICOCHEMICAL PROPERTIES Lipid metabolism; sphingolipid metabolism.SUBUNIT Component of the serine palmitoyltransferase (SPT) complex, which is composed of SPTLC1, SPTLC2 or SPTLC3 and SPTSSA or SPTSSB (PubMed:19416851). The heterodimer consisting of SPTLC1 and SPTLC2/SPTLC3 forms the catalytic core of the enzyme, while SPTSSA or SPTSSB subunits determine substrate specificity (PubMed:33558762, PubMed:37308477). SPT also interacts with ORMDL proteins, especially ORMDL3, which negatively regulate SPT activity in the presence of ceramides (PubMed:30700557, PubMed:33558762, PubMed:37308477). Forms dimers of heterodimers with SPTLC1 (PubMed:33558761, PubMed:33558762).INTERACTION Widely expressed.INDUCTION Expression at protein level is highly increased in brains of patients with Alzheimer disease. No changes are observed at mRNA level.DISEASE The disease is caused by variants affecting the gene represented in this entry. SPTLC2 disease mutations cause a shift in the substrate specificity of SPT resulting in the alternative use of L-alanine and L-glycine over its canonical substrate L-serine. This leads to the production of 1-deoxysphingolipids that cannot be correctly metabolized (PubMed:23658386).SIMILARITY Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family.SEQUENCE CAUTION Extended N-terminus. |
| description | recommendedName: fullName evidence="17"Serine palmitoyltransferase 2 ecNumber evidence="5"2.3.1.50 alternativeName: Long chain base biosynthesis protein 2 shortName: LCB 2 alternativeName: Long chain base biosynthesis protein 2a shortName evidence="16"LCB2a alternativeName: Serine-palmitoyl-CoA transferase 2 shortName: SPT 2 |
| geneName | SPTLC2 KIAA0526 LCB2 |
| identifier | O15270 |
| isSequenceChanged | FALSE |
| keyword | 3D-structure Acyltransferase Disease variant Endoplasmic reticulum Lipid metabolism Membrane Neurodegeneration Neuropathy Proteomics identification Pyridoxal phosphate Reference proteome Sphingolipid metabolism Transferase Transmembrane Transmembrane helix |
| modified | [InstanceEdit:9836292] Weiser, Joel, 2023-05-25 [InstanceEdit:9852000] Weiser, Joel, 2023-11-03 [InstanceEdit:9862192] Weiser, Joel, 2024-02-26 [InstanceEdit:9917590] Weiser, Joel, 2024-08-09 [InstanceEdit:9926675] Weiser, Joel, 2024-11-03 [InstanceEdit:9939033] Weiser, Joel, 2025-02-21 |
| name | SPTLC2 |
| referenceDatabase | [ReferenceDatabase:2] UniProt |
| referenceGene | [ReferenceDNASequence:8999776] ENSEMBL:ENSG00000100596 SPTLC2 [Homo sapiens] |
| secondaryIdentifier | SPTC2_HUMAN Q16685 |
| sequenceLength | 562 |
| species | [Species:48887] Homo sapiens |
| (referenceEntity) | [EntityWithAccessionedSequence:428146] PXLP-K379-SPTLC2 [endoplasmic reticulum membrane] [Homo sapiens] |
| (referenceSequence) | [ModifiedResidue:554223] N6-pyridoxal phosphate-L-lysine at 379 |
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No pathways have been reviewed or authored by UniProt:O15270 SPTLC2 (58443)
