Overview
| Uniprot ID | A0A8D1SY88 |
| Protein Name | Serine palmitoyltransferase 1 |
| Gene Name | SPTLC1 |
| Organism | Sus scrofa |
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 115 |
LLDNPRVKAAALASL |
| 123 |
AAALASLKKYGVGTC |
| 194 |
AACFAIQKGLQASRS |
| 372 |
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
GIKAETSWFL
20
VGFVSTAPAY
30
HLILEGILIL
40
WIIRLLFSKT
50
YKLQERSDLT
60
VKEKEELIEE
70
WQPEPLVPPV
80
SKDHPALNYN
90
IVSGPPSHNI
100
VVNGKECINF
110
ASFNFLGLLD
120
NPRVKAAALA
130
SLKKYGVGTC
140
GPRGFYGTFD
150
VHLDLEDRLA
160
KFMKTEEAII
170
YSYGFATIAS
180
AIPAYSKRGD
190
IVFVDKAACF
200
AIQKGLQASR
210
SDIKLFEHND
220
MEDLERLLKE
230
QEIEDQKNPR
240
KARVTRRFIV
250
VEGLYMNTGT
260
ICPLPELVKL
270
KYKYKARIFL
280
EESLSFGVLG
290
EHGRGVTEHF
300
GINIDDIDLI
310
SANMENSLAS
320
IGGFCCGRSF
330
VIDHQRLSGQ
340
GYCFSASLPP
350
LLAAAAIEAL
360
NIMEENPGIF
370
AVLKEKCKRI
380
HKALQGISGL
390
KVAGESISPA
400
FHLQLEESTG
410
SRDKDVKLLQ
420
EIVTGCMDRG
430
IALTQARYLE
440
KEEKNLPPPS
450
IRVVVTVEQT
460
EEELDKAAST
470
INEVAQIVLL
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:0043604 |
amide biosynthetic process |
| Biological Process |
GO:0030148 |
sphingolipid biosynthetic 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.