| Comment type | Description |
|---|
| Alternative Products | Event=Alternative splicing; Named isoforms=3; Name=1; IsoId=Q3TFD2-1; Sequence=Displayed; Name=2; IsoId=Q3TFD2-2; Sequence=VSP_019914; Note=No experimental confirmation available.; Name=3; IsoId=Q3TFD2-3; Sequence=VSP_019913; Note=No experimental confirmation available.; |
| Biophysicochemical Properties | Kinetic parameters: KM=2.3 uM for 1-palmitoyl-LPC {ECO:0000269|PubMed:16704971, ECO:0000269|PubMed:18285344}; KM=3 uM for palmitoyl-CoA {ECO:0000269|PubMed:16704971, ECO:0000269|PubMed:18285344}; pH dependence: Optimum pH is 7.5. {ECO:0000269|PubMed:16704971, ECO:0000269|PubMed:18285344}; |
| Catalytic Activity | Acetyl-CoA + 1-alkyl-sn-glycero-3- phosphocholine = CoA + 2-acetyl-1-alkyl-sn-glycero-3- phosphocholine. {ECO:0000269|PubMed:16704971}. |
| Catalytic Activity | Acyl-CoA + 1-acyl-sn-glycero-3-phosphocholine = CoA + 1,2-diacyl-sn-glycero-3-phosphocholine. {ECO:0000269|PubMed:16704971}. |
| Developmental Stage | Expression increases steadily throughout embryogenesis and decreases slightly in the adult. {ECO:0000269|PubMed:16864775}. |
| Domain | The di-lysine motif confers endoplasmic reticulum localization for type I membrane proteins. {ECO:0000250}. |
| Domain | The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphocholine. {ECO:0000250}. |
| Enzyme Regulation | Not activated by inflammatory stimulation. Inhibited by Cu(2+) and Fe(2+). Activity is not affected by Co(2+), Mg(2+) or Mn(2+). {ECO:0000269|PubMed:18285344}. |
| Function | Possesses both acyltransferase and acetyltransferase activities. Activity is calcium-independent. Mediates the conversion of 1-acyl-sn-glycero-3-phosphocholine (LPC) into phosphatidylcholine (PC). Displays a clear preference for saturated fatty acyl-CoAs, and 1-myristoyl or 1-palmitoyl LPC as acyl donors and acceptors, respectively. May synthesize phosphatidylcholine in pulmonary surfactant, thereby playing a pivotal role in respiratory physiology. {ECO:0000269|PubMed:16704971, ECO:0000269|PubMed:18156367, ECO:0000269|PubMed:18285344}. |
| Induction | Constitutively expressed. Not induced by inflammatory stimulation. {ECO:0000269|PubMed:18285344}. |
| Pathway | Lipid metabolism; phospholipid metabolism. |
| Sequence Caution | Sequence=AAH05662.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305}; Sequence=BAC32594.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305}; Sequence=BAC32760.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305}; |
| Similarity | Belongs to the 1-acyl-sn-glycerol-3-phosphate acyltransferase family. {ECO:0000305}. |
| Similarity | Contains 2 EF-hand domains. {ECO:0000255|PROSITE- ProRule:PRU00448}. |
| Subcellular Location | Endoplasmic reticulum membrane; Single-pass type II membrane protein. Golgi apparatus membrane; Single-pass type II membrane protein. Lipid droplet {ECO:0000250}. Note=May adopt a monotopic topology when embedded in the lipid monolayer of the lipid droplet, with both termini exposed to the cytoplasm. {ECO:0000250}. |
| Tissue Specificity | Predominantly expressed in lung where it is enriched in alveolar type II cells. Expressed at lower levels in spleen and brain. Also detected in erythroleukemic cells and reticulocytes. Weakly or not expressed in other tissues. {ECO:0000269|PubMed:16704971, ECO:0000269|PubMed:16864775, ECO:0000269|PubMed:18156367}. |