Overview
| Uniprot ID | Q8N6M3 |
|---|
| Protein Name | Acyl-coenzyme A diphosphatase FITM2 |
|---|
| Gene Name | FITM2 |
|---|
| Organism | Homo sapiens |
|---|
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 52 |
PESYLSNKRNVLNVY |
Function
Fatty acyl-coenzyme A (CoA) diphosphatase that hydrolyzes fatty acyl-CoA to yield acyl-4'-phosphopantetheine and adenosine 3',5'-bisphosphate (By similarity) (PubMed:32915949). Preferentially hydrolyzes unsaturated long-chain acyl-CoA substrates such as oleoyl-CoA/(9Z)-octadecenoyl-CoA and arachidonoyl-CoA/(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA in the endoplasmic reticulum (ER) lumen (By similarity) (PubMed:32915949). This catalytic activity is required for maintaining ER structure and for lipid droplets (LDs) biogenesis, which are lipid storage organelles involved in maintaining lipid and energy homeostasis (By similarity) (PubMed:18160536, PubMed:32915949). Directly binds to diacylglycerol (DAGs) and triacylglycerol, which is also important for LD biogenesis (By similarity). May support directional budding of nacent LDs from the ER into the cytosol by reducing DAG levels at sites of LD formation (By similarity). Plays a role in the regulation of cell morphology and cytoskeletal organization (PubMed:21834987)
Protein Sequence
10
MEHLERCEWL
20
LRGTLVRAAV
30
RRYLPWALVA
40
SMLAGSLLKE
50
LSPLPESYLS
60
NKRNVLNVYF
70
VKVAWAWTFC
80
LLLPFIALTN
90
YHLTGKAGLV
100
LRRLSTLLVG
110
TAIWYICTSI
120
FSNIEHYTGS
130
CYQSPALEGV
140
RKEHQSKQQC
150
HQEGGFWHGF
160
DISGHSFLLT
170
FCALMIVEEM
180
SVLHEVKTDR
190
SHCLHTAITT
200
LVVALGILTF
210
IWVLMFLCTA
220
VYFHNLSQKV
230
FGTLFGLLSW
240
YGTYGFWYPK
250
AFSPGLPPQS
260
CSLNLKQDSY
KK
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0005789 |
endoplasmic reticulum membrane |
| Molecular Function |
GO:0010945 |
coenzyme A diphosphatase activity |
| Molecular Function |
GO:0019992 |
diacylglycerol binding |
| Molecular Function |
GO:0170007 |
endoplasmic reticulum-lipid droplet tether activity |
| Molecular Function |
GO:0017129 |
triglyceride binding |
| Biological Process |
GO:0045444 |
fat cell differentiation |
| Biological Process |
GO:0036115 |
fatty-acyl-CoA catabolic process |
| Biological Process |
GO:0035356 |
intracellular triglyceride homeostasis |
| Biological Process |
GO:0140042 |
lipid droplet formation |
| Biological Process |
GO:0034389 |
lipid droplet organization |
| Biological Process |
GO:0055088 |
lipid homeostasis |
| Biological Process |
GO:0019915 |
lipid storage |
| Biological Process |
GO:0008654 |
phospholipid biosynthetic process |
| Biological Process |
GO:0006641 |
triglyceride metabolic 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.