Overview
| Uniprot ID | Q92604 |
| Protein Name | Acyl-CoA:lysophosphatidylglycerol acyltransferase 1 |
| Gene Name | LPGAT1 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 276 |
TWILGYRKPTVTHVH |
Function
Lysophospholipid acyltransferase involved in fatty acyl chain remodeling of glycerophospholipids in the endoplasmic reticulum membrane (By similarity). Selectively catalyzes the transfer and esterification of saturated long-chain fatty acids from acyl-CoA to the sn-1 position of 1-lyso-2-acyl phosphatidylethanolamines (1-lyso-PE, LPE), with a preference for stearoyl CoA over palmitoyl CoA as acyl donor (PubMed:36049524). Acts in concert with an unknown phospholipase A1 to convert palmitate phosphatidylethanolamine (PE) species into stearate ones. Provides substrates to the PE methylation pathway, controlling stearate/palmitate composition of PE and phosphatidylcholine (PC) species with an overall impact on de novo hepatic lipid synthesis, body fat content and life span (By similarity). Can acylate lysophosphatidylglycerols (LPG) using various saturated fatty acyl-CoAs as acyl donors (PubMed:15485873). Can also acylate monoacylglycerols with a preference for 2-monoacylglycerols over 1-monoacylglycerols (By similarity). Has no activity toward lysophosphatidic acids (LPA) (By similarity)
Protein Sequence
10
MAITLEEAPW
20
LGWLLVKALM
30
RFAFMVVNNL
40
VAIPSYICYV
50
IILQPLRVLD
60
SKRFWYIEGI
70
MYKWLLGMVA
80
SWGWYAGYTV
90
MEWGEDIKAV
100
SKDEAVMLVN
110
HQATGDVCTL
120
MMCLQDKGLV
130
VAQMMWLMDH
140
IFKYTNFGIV
150
SLVHGDFFIR
160
QGRSYRDQQL
170
LLLKKHLENN
180
YRSRDRKWIV
190
LFPEGGFLRK
200
RRETSQAFAK
210
KNNLPFLTNV
220
TLPRSGATKI
230
ILNALVAQQK
240
NGSPAGGDAK
250
ELDSKSKGLQ
260
WIIDTTIAYP
270
KAEPIDIQTW
280
ILGYRKPTVT
290
HVHYRIFPIK
300
DVPLETDDLT
310
TWLYQRFVEK
320
EDLLSHFYET
330
GAFPPSKGHK
340
EAVSREMTLS
350
NLWIFLIQSF
360
AFLSGYMWYN
370
IIQYFYHCLF
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0005737 |
cytoplasm |
| Cellular Component |
GO:0012505 |
endomembrane system |
| Cellular Component |
GO:0005783 |
endoplasmic reticulum |
| Cellular Component |
GO:0005789 |
endoplasmic reticulum membrane |
| Cellular Component |
GO:0016020 |
membrane |
| Molecular Function |
GO:0003841 |
1-acylglycerol-3-phosphate O-acyltransferase activity |
| Molecular Function |
GO:0003846 |
2-acylglycerol O-acyltransferase activity |
| Molecular Function |
GO:0047144 |
2-acylglycerol-3-phosphate O-acyltransferase activity |
| Molecular Function |
GO:0047190 |
2-acylglycerophosphocholine O-acyltransferase activity |
| Molecular Function |
GO:0016746 |
acyltransferase activity |
| Molecular Function |
GO:0071618 |
lysophosphatidylethanolamine acyltransferase activity |
| Molecular Function |
GO:0071617 |
lysophospholipid acyltransferase activity |
| Biological Process |
GO:0036152 |
phosphatidylethanolamine acyl-chain remodeling |
| Biological Process |
GO:0036148 |
phosphatidylglycerol acyl-chain remodeling |
| Biological Process |
GO:0036149 |
phosphatidylinositol acyl-chain remodeling |
| Biological Process |
GO:0008654 |
phospholipid biosynthetic process |
| Biological Process |
GO:0045723 |
positive regulation of fatty acid biosynthetic process |
| Biological Process |
GO:0019432 |
triglyceride biosynthetic process |
Reference
[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.