Search results for LPCAT1

Showing 11 results out of 11

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Protein (3 results from a total of 3)

Identifier: R-HSA-1498772
Species: Homo sapiens
Compartment: endoplasmic reticulum membrane
Primary external reference: UniProt: LPCAT1: Q8NF37
Identifier: R-HSA-6798758
Species: Homo sapiens
Compartment: azurophil granule membrane
Primary external reference: UniProt: LPCAT1: Q8NF37
Identifier: R-HSA-6806273
Species: Homo sapiens
Compartment: plasma membrane
Primary external reference: UniProt: LPCAT1: Q8NF37

Reaction (7 results from a total of 7)

Identifier: R-HSA-8873923
Species: Homo sapiens
Compartment: cytosol, endoplasmic reticulum membrane
The steroidogenic acute regulatory (StAR) protein-related lipid transfer (START) domain proteins constitute a family of evolutionarily conserved and widely expressed proteins that have been implicated in lipid transport, metabolism, and signaling. Human PCTP-like protein (STARD10) (Olayioye et al. 2005) is thought to be a dual specificity lipid transfer protein capable of shuttling phosphatidylcholine (PC) (and phosphatidylethanolamine (PE), not shown here) between intracellular membranes, especially to lamellar body membranes. Saturated PC is a major component of pulmonary surfactant, a mixture of proteins and phospholipids that plays an important role in facilitating gas exchange by maintaining alveolar stability. After synthesis in the endoplasmic reticulum, saturated PC is transported to lamellar bodies (LBs) for storage prior to secretion. Lysophosphatidylcholine acyltransferase 1 (LPCAT1) mediated reacylation is a final step in saturated PC synthesis prior to transport and LPCAT1 is proposed to form a complex with STARD10 at the ER membrane to facilitate the synthesis then transport of saturated PC to LBs (Lin et al. 2015).
Identifier: R-HSA-8873834
Species: Homo sapiens
Compartment: cytosol, endoplasmic reticulum membrane, lamellar body membrane
The steroidogenic acute regulatory (StAR) protein-related lipid transfer (START) domain proteins constitute a family of evolutionarily conserved and widely expressed proteins that have been implicated in lipid transport, metabolism, and signaling. Human PCTP-like protein (STARD10) (Olayioye et al. 2005) is thought to be a dual specificity lipid transfer protein capable of shuttling phosphatidylcholine (PC) (and phosphatidylethanolamine (PE), not shown here) between intracellular membranes, especially to lamellar body membranes. Saturated PC is a major component of pulmonary surfactant, a mixture of proteins and phospholipids that plays an important role in facilitating gas exchange by maintaining alveolar stability. After synthesis in the endoplasmic reticulum, saturated PC is transported to lamellar bodies (LBs) for storage prior to secretion. Lysophosphatidylcholine acyltransferase 1 (LPCAT1) mediated reacylation is a final step in saturated PC synthesis prior to transport and LPCAT1 is proposed to form a complex with STARD10 at the ER membrane to facilitate the synthesis then transport of saturated PC to LBs (Lin et al. 2015).
Identifier: R-HSA-1482539
Species: Homo sapiens
Compartment: endoplasmic reticulum membrane, cytosol
At the endoplasmic reticulum (ER) membrane, lysophospholipid acyltransferases acylate 1-acyl lysophosphatidylglycerol (LPG) to form phosphatidylglycerol (PG). The lysophospholipid acyltransferases involved are: lysophosphatidylcholine acyltransferase 1 (LPCAT1) (Nakanishi et al. 2006, Chen et al. 2006), lysophospholipid acyltransferase LPCAT4 (LPCAT4) aka LPEAT2 (Cao et al. 2008, Ye et al. 2005); or acyl-CoA:lysophosphatidylglycerol acyltransferase (LPGAT1) (Yang et al. 2004).
Identifier: R-HSA-1482635
Species: Homo sapiens
Compartment: endoplasmic reticulum membrane, cytosol
At the endoplasmic reticulum (ER) membrane, lysophospholipid acyltransferases acylate 2-acyl lysophosphatidylglycerol (LPG) to form phosphatidylglycerol (PG). The lysophospholipid acyltransferases involved are: lysophosphatidylcholine acyltransferase 1 (LPCAT1) (Nakanishi et al. 2006, Chen et al. 2006), lysophospholipid acyltransferase LPCAT4 (LPCAT4) aka LPEAT2 (Cao et al. 2008, Ye et al. 2005); or acyl-CoA:lysophosphatidylglycerol acyltransferase (LPGAT1) (Yang et al. 2004).
Identifier: R-HSA-1482533
Species: Homo sapiens
Compartment: endoplasmic reticulum membrane, cytosol
At the endoplasmic reticulum (ER) membrane, lysophospholipid acyltransferases acylate 2-acyl lysophosphatidylcholine (LPC) to form phosphatidylcholine (PC). The lysophospholipid acyltransferases involved are: lysophosphatidylcholine acyltransferase 1 (LPCAT1) (Nakanishi et al. 2006, Chen et al. 2006); lysophosphatidylcholine acyltransferase 2 (LPCAT2) (Shindou et al. 2006); lysophospholipid acyltransferase 5 (LPCAT3) (Hishikawa et al. 2008, Zhao et al. 2008, Gijon et al. 2008, Jain et al. 2009, Kazachkov et al. 2008); lysophospholipid acyltransferase LPCAT4 (LPCAT4) aka LPEAT2 (Cao et al. 2008, Ye et al. 2005); or lysophospholipid acyltransferase 2 (MBOAT2) aka LPCAT4 (Hishikawa et al. 2008, Gijon et al. 2008).
Identifier: R-HSA-1482547
Species: Homo sapiens
Compartment: endoplasmic reticulum membrane, cytosol
At the endoplasmic reticulum (ER) membrane, lysophospholipid acyltransferases acylate 1-acyl lysophosphatidylcholine (LPC) to form phosphatidylcholine (PC). The lysophospholipid acyltransferases involved are: lysophosphatidylcholine acyltransferase 1 (LPCAT1) (Nakanishi et al. 2006, Chen et al. 2006); lysophosphatidylcholine acyltransferase 2 (LPCAT2) (Shindou et al. 2006); lysophospholipid acyltransferase 5 (LPCAT3) (Hishikawa et al. 2008, Zhao et al. 2008, Gijon et al. 2008, Jain et al. 2009, Kazachkov et al. 2008); lysophospholipid acyltransferase LPCAT4 (LPCAT4) aka LPEAT2 (Cao et al. 2008, Ye et al. 2005); or lysophospholipid acyltransferase 2 (MBOAT2) aka LPCAT4 (Hishikawa et al. 2008, Gijon et al. 2008).
Identifier: R-HSA-75885
Species: Homo sapiens
Compartment: endoplasmic reticulum membrane, cytosol
At the endoplasmic reticulum (ER) membrane, 1-acyl-lysophosphatidic acid (LPA) is acylated to phosphatidic acid (PA) by the enzymes 1-acyl-sn-glycerol-3-phosphate acyltransferases (AGPAT1 through 11), and lysophosphatidylcholine acyltransferase (LPCAT1) (Aguado and Campbell 1998).

See recent review by Agarwal (2012, in press).

AGPAT1, 2, 3 and LPCAT1 have been characterized biochemically (AGPAT1, 2: Yamashita et al. 2007, West et al. 1997, Aguado and Campbell 1998, Gale et al. 2006; AGPAT3: Agarwal et al. 2006; LPCAT1: Nakanishi et al. 2006, Chen et al. 2006). Two additional proteins, AGPAT4 and AGPAT5, are inferred to have such activity based on studies of homologous mouse enzymes (Lu et al. 2005). These enzymes differ in their tissue specific patterns of expression in the body and in their preferences for specific acyl CoA molecules (Shindou and Shimizu 2009; Takeuchi and Reue 2009).

Complex (1 results from a total of 1)

Identifier: R-HSA-8873921
Species: Homo sapiens
Compartment: endoplasmic reticulum membrane
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