Overview
| Uniprot ID | H0VLS0 |
| Protein Name | Lipid droplet-associated hydrolase |
| Gene Name | LDAH |
| Organism | Cavia porcellus |
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 326 |
KENLSKIKMLMKEKS |
| 330 |
SKIKMLMKEKSSHRQ |
Function
Probable serine lipid hydrolase associated with lipid droplets. Has low cholesterol esterase activity. Appears to lack triglyceride lipase activity. Involved in cholesterol and triglyceride homeostasis; stimulates cellular triglyceride accumulation and cellular cholesterol release. Acts antagonistically with PNPLA2/ATGL in regulation of cellular lipid stores. May regulate triglyceride accumulation indirectly through stimulation of PNPLA2/ATGL ubiquitination and proteasomal degradation. Promotes microtubule-dependent lipid droplet fusion. Highly expressed in macrophage-rich areas in atherosclerotic lesions, suggesting that it could promote cholesterol ester turnover in macrophages
Protein Sequence
10
MDSNTEEDIP
20
VREEFLLCGG
30
VETQVIKCGP
40
WTDLINDPNG
50
SRPKLLICVI
60
PGNPGFSAFY
70
VPFVKALYSL
80
TNRHFPIWII
90
AHAGHVLAPQ
100
NKKTDVTLED
110
PNAQEIEDIY
120
GLRGQIEHKI
130
SFLRTQVPKD
140
VKLILIGHSI
150
GSYMVLQILK
160
CVPELPVVHA
170
FLLFPTIERM
180
AESPNGKIAT
190
PLLCWFRYAL
200
YAISYLLLKP
210
CPDVVKSWLA
220
GLILQVVDIK
230
TEFPLTSMLQ
240
PSCLANAAYL
250
GAQEMRKVVQ
260
RDDDIIKQHL
270
SKITFYYGTV
280
DPWCPTEYYE
290
DMKKSFPEGD
300
IRLCNKNIPH
310
AFILRFSHDI
320
ADMIATWVKE
330
NLSKIKMLMK
340
EKSSHRQHLC
Q
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0005783 |
endoplasmic reticulum |
| Cellular Component |
GO:0005811 |
lipid droplet |
| Molecular Function |
GO:0004771 |
sterol ester esterase activity |
| Biological Process |
GO:0042632 |
cholesterol homeostasis |
| Biological Process |
GO:0035356 |
intracellular triglyceride homeostasis |
| Biological Process |
GO:0160077 |
lipid droplet fusion |
| Biological Process |
GO:0019915 |
lipid storage |
Reference
[1] Feng J, Chen X, Li R, Xie Y, Zhang X et al.. Lactylome analysis reveals potential target modified proteins in the retina of form-deprivation myopia.. iScience 27(9):110606. 2024 Sep 20. PMID: 39246443.