|PCAT1_HUMAN » Lysophosphatidylcholine acyltransferase 1 » LysoPC acyltransferase 1; LPC acyltransferase 1; LPCAT-1; 1-alkylglycerophosphocholine O-acetyltransferase;Acetyl-CoA:lyso-platelet-activating factor acetyltransferase;Acetyl-CoA:lyso-PAF acetyltransferase; Lyso-PAF acetyltransferase; LysoPAFAT; 1-acylgly|
|Hydrophobic Thickness||30.8 ± 3.2 Å|
|Tilt Angle||30 ± 4°|
|Links to PCAT1_HUMAN||UniProtKB, Pfam, iHOP, STRING, PharmGKB, HGNC, Wikipedia, Interpro|
|Uniprot annotation for PCAT1_HUMAN » Lysophosphatidylcholine acyltransferase 1|
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. |
CATALYTIC ACTIVITY: Acyl-CoA + 1-acyl-sn-glycero-3-phosphocholine = CoA + 1,2-diacyl-sn-glycero-3-phosphocholine.
CATALYTIC ACTIVITY: Acetyl-CoA + 1-alkyl-sn-glycero-3- phosphocholine = CoA + 2-acetyl-1-alkyl-sn-glycero-3- phosphocholine.
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+) (By similarity).
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type II membrane protein (By similarity). Golgi apparatus membrane; Single-pass type II membrane protein (By similarity).
DOMAIN: The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphocholine (By similarity).
DOMAIN: The di-lysine motif confers endoplasmic reticulum localization for type I membrane proteins (By similarity).
-- Uniprot annotation--
|Uniprot features for PCAT1_HUMAN » Lysophosphatidylcholine acyltransferase 1|
CHAIN 1 534 Lysophosphatidylcholine acyltransferase 1. |
DOMAIN 379 414 EF-hand 1.
DOMAIN 451 486 EF-hand 2.
MOTIF 135 140 HXXXXD motif.
MOTIF 531 534 Di-lysine motif.