| 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. 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. The composition of the serine palmitoyltransferase (SPT) complex determines the substrate preference. 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. 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. Crucial for adipogenesis. |
| Protein Name | Serine Palmitoyltransferase 2Long Chain Base Biosynthesis Protein 2Lcb 2Long Chain Base Biosynthesis Protein 2aLcb2aSerine-Palmitoyl-Coa Transferase 2Spt 2 |
| Database Links | Reactome: R-HSA-1660661 |
| Cellular Localisation | Endoplasmic Reticulum MembraneSingle-Pass Membrane Protein |
| Alternative Protein Names | Serine Palmitoyltransferase 2 proteinLong Chain Base Biosynthesis Protein 2 proteinLcb 2 proteinLong Chain Base Biosynthesis Protein 2a proteinLcb2a proteinSerine-Palmitoyl-Coa Transferase 2 proteinSpt 2 proteinSPTLC2 proteinKIAA0526 proteinLCB2 protein |
Information sourced from Uniprot.org
