Overview
| Uniprot ID | Q9NWW9 |
|---|
| Protein Name | Phospholipase A and acyltransferase 2 |
|---|
| Gene Name | PLAAT2 |
|---|
| Organism | Homo sapiens |
|---|
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 62 |
TNKAIVKKELLSVVA |
Function
Exhibits both phospholipase A1/2 and acyltransferase activities (PubMed:19615464, PubMed:22605381, PubMed:22825852, PubMed:26503625). Shows phospholipase A1 (PLA1) and A2 (PLA2) activity, catalyzing the calcium-independent release of fatty acids from the sn-1 or sn-2 position of glycerophospholipids (PubMed:19615464, PubMed:22605381, PubMed:22825852). For most substrates, PLA1 activity is much higher than PLA2 activity (PubMed:19615464). Shows O-acyltransferase activity, catalyzing the transfer of a fatty acyl group from glycerophospholipid to the hydroxyl group of lysophospholipid (PubMed:19615464). Shows N-acyltransferase activity, catalyzing the calcium-independent transfer of a fatty acyl group at the sn-1 position of phosphatidylcholine (PC) and other glycerophospholipids to the primary amine of phosphatidylethanolamine (PE), forming N-acylphosphatidylethanolamine (NAPE), which serves as precursor for N-acylethanolamines (NAEs) (PubMed:19615464, PubMed:22605381, PubMed:22825852). Catalyzes N-acylation of PE using both sn-1 and sn-2 palmitoyl groups of PC as acyl donor (PubMed:22605381). Exhibits high phospholipase A1/2 activity and low N-acyltransferase activity (PubMed:22825852)
Protein Sequence
10
MALARPRPRL
20
GDLIEISRFG
30
YAHWAIYVGD
40
GYVVHLAPAS
50
EIAGAGAASV
60
LSALTNKAIV
70
KKELLSVVAG
80
GDNYRVNNKH
90
DDRYTPLPSN
100
KIVKRAEELV
110
GQELPYSLTS
120
DNCEHFVNHL
130
RYGVSRSDQV
140
TGAVTTVGVA
150
AGLLAAASLV
160
GILLARSKRE
RQ
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0005737 |
cytoplasm |
| Cellular Component |
GO:0005829 |
cytosol |
| Cellular Component |
GO:0016020 |
membrane |
| Molecular Function |
GO:0004623 |
A2-type glycerophospholipase activity |
| Molecular Function |
GO:0016746 |
acyltransferase activity |
| Molecular Function |
GO:0008970 |
glycerophospholipid phospholipase A1 activity |
| Molecular Function |
GO:0016410 |
N-acyltransferase activity |
| Biological Process |
GO:0016042 |
lipid catabolic process |
| Biological Process |
GO:0070292 |
N-acylphosphatidylethanolamine metabolic process |
| Biological Process |
GO:0036152 |
phosphatidylethanolamine acyl-chain remodeling |
Reference
[1] Guo X, Ren X, Yan C, Huang H. Quantitative Proteomics Reveals the Role of Lysine Lactylation in Lenalidomide-Resistance in Multiple Myeloma Cells.. ACS Chem Biol 20(7):1728-1738. 2025 Jul 18. PMID: 40590393.