Overview
| Uniprot ID | A0A5G2R287 |
| Protein Name | Serine palmitoyltransferase 1 |
| Gene Name | SPTLC1 |
| Organism | Sus scrofa |
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 118 |
LLDNPRVKAAALASL |
| 126 |
AAALASLKKYGVGTC |
| 197 |
AACFAIQKGLQASRS |
| 343 |
EKCKRIHKALQGISG |
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 also composed of SPTLC2 or SPTLC3 and SPTSSA or SPTSSB. Within this complex, the heterodimer with SPTLC2 or 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. Required for adipocyte cell viability and metabolic homeostasis
Protein Sequence
10
MAAVAEQWVL
20
VEMVQALYEA
30
PAYHLILEGI
40
LILWIIRLLF
50
SKTYKLQERS
60
DLTVKEKEEL
70
IEEWQPEPLV
80
PPVSKDHPAL
90
NYNIVSGPPS
100
HNIVVNGKEC
110
INFASFNFLG
120
LLDNPRVKAA
130
ALASLKKYGV
140
GTCGPRGFYG
150
TFDVHLDLED
160
RLAKFMKTEE
170
AIIYSYGFAT
180
IASAIPAYSK
190
RGDIVFVDKA
200
ACFAIQKGLQ
210
ASRSDIKLFE
220
HNDMEDLERL
230
LKEQEIEDQK
240
NPRKARVTRR
250
FIVVEGLYMN
260
TGTICPLPEL
270
VKLKYKYKAR
280
IFLEESLSFG
290
VLGEHGRGVT
300
EHFGINRLSG
310
QGYCFSASLP
320
PLLAAAAIEA
330
LNIMEENPGI
340
FAVLKEKCKR
350
IHKALQGISG
360
LKVAGESISP
370
AFHLQLEEST
380
GSRDKDVKLL
390
QEIVTGCMDR
400
GIALTQARYL
410
EKEEKNLPPP
420
SIRVVVTVEQ
430
TEEELDKAAS
440
TINEVAQIVL
L
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0016020 |
membrane |
| Molecular Function |
GO:0030170 |
pyridoxal phosphate binding |
| Molecular Function |
GO:0004758 |
serine C-palmitoyltransferase activity |
| Biological Process |
GO:0006665 |
sphingolipid metabolic process |
Reference
[1] Fan S, Zhou R, Wen H, Ye H, Ma S et al.. Global profiling of protein lactylome in porcine granulosa cells.. J Ovarian Res 18(1):177. 2025 Aug 8. PMID: 40781717.