Overview
| Uniprot ID | D4A2H2 |
|---|
| Protein Name | Serine palmitoyltransferase 1 |
|---|
| Gene Name | Sptlc1 |
|---|
| Organism | Rattus norvegicus |
|---|
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 230 |
EQEIEDQKNPRKARV |
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 (By similarity). Required for adipocyte cell viability and metabolic homeostasis (By similarity)
Protein Sequence
10
MATVAEQWVL
20
VEMVQALYEA
30
PAYHLILEGI
40
LILWIIRLVF
50
SKTYKLQERS
60
DLTAKEKEEL
70
IEEWQPEPLV
80
PPVSRNHPAL
90
NYNIVSGPPT
100
HNIVVNGKEC
110
VNFASFNFLG
120
LLANPRVKAA
130
AFASLKKYGV
140
GTCGPRGFYG
150
TFDVHLDLEE
160
RLAKFMKTEE
170
AIIYSYGFST
180
IASAIPAYSK
190
RGDIVFVDSA
200
ACFAIQKGLQ
210
ASRSDIKLFK
220
HNDVADLERL
230
LKEQEIEDQK
240
NPRKARVTRR
250
FIVAEGLYMN
260
TGTICPLPEL
270
VRLKYKYKAR
280
IFLEESLSFG
290
VLGEHGRGVT
300
EHYGISIDDI
310
DLISANMENA
320
LASVGGFCCG
330
RSFVVDHQRL
340
SGQGYCFSAS
350
LPPLLAAAAI
360
EALNIMEENP
370
GIFAVLKKKC
380
QTIHKSLQGV
390
SGLKVVGESL
400
CPALHLQLEE
410
STGSRERDMK
420
LLQEIVEQCM
430
NKGIALTQAR
440
YLDKEEKCLP
450
PPSIRVVVTV
460
EQTDEELQRA
470
AATIREAAQA
VLL
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0098554 |
cytoplasmic side of endoplasmic reticulum membrane |
| Cellular Component |
GO:0005783 |
endoplasmic reticulum |
| Cellular Component |
GO:0005789 |
endoplasmic reticulum membrane |
| Cellular Component |
GO:0017059 |
serine palmitoyltransferase complex |
| Molecular Function |
GO:0030170 |
pyridoxal phosphate binding |
| Molecular Function |
GO:0004758 |
serine C-palmitoyltransferase activity |
| Biological Process |
GO:0046513 |
ceramide biosynthetic process |
| Biological Process |
GO:0006688 |
glycosphingolipid biosynthetic process |
| Biological Process |
GO:1904504 |
positive regulation of lipophagy |
| Biological Process |
GO:1904649 |
regulation of fat cell apoptotic process |
| Biological Process |
GO:0046511 |
sphinganine biosynthetic process |
| Biological Process |
GO:0030148 |
sphingolipid biosynthetic process |
| Biological Process |
GO:0006665 |
sphingolipid metabolic process |
| Biological Process |
GO:0006686 |
sphingomyelin biosynthetic process |
| Biological Process |
GO:0046512 |
sphingosine biosynthetic process |
Reference
[1] Sheng L, Xu H, Wang Y, Ni J, Xiang T et al.. Systematic analysis of lysine lactylation in nucleus pulposus cells.. iScience 27(11):111157. 2024 Nov 15. PMID: 39524337.