Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniPathway vocabulary mapping
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
Automatic Gene Ontology annotation based on Rhea mapping
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
Molecular identification of a novel mammalian brain isoform of acyl-CoA:lysophospholipid acyltransferase with prominent ethanolamine lysophospholipid acylating activity, LPEAT2.
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Heterologous expression of LPEAT2/LPCAT4 strongly increased LPEAT activity.
"Ectopic expression of LPEAT2 in mammalian HEK293T cells led to a dramatic increase (up to 9-fold) in LPEAT activity"
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The enzyme accepts several lysophospholipid headgroups but not glycerol-3-phosphate, LPA, LPI, or DAG in the reported assays.
"LPEAT2 also exhibited significant acyl-CoA-dependent acyltransferase activity toward 1-O-alkenyl-lysophosphatidylethanolamine, lysophosphatidylglycerol, 1-O-alkyl-lysophosphatidylcholine, lysophosphatidylserine, and lysophosphatidylcholine but lacked appreciable acylating activity toward glycerol 3-phosphate, lysophosphatidic acid, lysophosphatidylinositol, and diacylglycerol"
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LPCAT4/LPEAT2 uses a broad range of medium- and long-chain acyl-CoAs.
"LPEAT2 recognizes a broad range of medium and long chain fatty acyl-CoA"
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Overexpressed LPEAT2 localized to the endoplasmic reticulum.
"When overexpressed in mammalian cells, LPEAT2 is localized to the endoplasmic reticulum."
Defining the membrane proteome of NK cells.
LPLAT10/LPEAT2 produces atypical phospholipids with an unsaturated FA at the sn-1 position.
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LPLAT10/LPEAT2/LPCAT4 generates phospholipids bearing unsaturated fatty acids at sn-1.
"Here, we report that LPLAT10 (also known as LPEAT2 or LPCAT4) is a lysophospholipid acyltransferase responsible for generating PLs with an unsaturated FA at the sn-1 position."
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It acylates LPC, LPE, and LPS selectively at sn-1 using saturated or unsaturated acyl-CoAs.
"In vitro, LPLAT10 incorporated both saturated and unsaturated FAs into lysophosphatidylcholine, lysophosphatidylethanolamine, and lysophosphatidylserine, selectively at the sn-1 position."
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LPLAT10 has relatively higher affinity for unsaturated fatty acyl-CoAs.
"LPLAT10 appeared to have a relatively higher affinity for unsaturated FA-CoAs."
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Position-resolved assays found no LPCAT4 activity toward 2-acyl LPG with a free sn-1 position.
"LPLAT10 did not act on sn-2 dominant LPI, LPG, and LPA"
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Loss of Lplat10 selectively depleted brain phospholipids with unsaturated sn-1 chains in mice.
"Consistently, only PLs with unsaturated FAs such as oleic acid (C18:1), linoleic acid (C18:2), arachidonic acid (C20:4), and DHA (C22:6) at the sn-1 position decreased in the brain from Lplat10-deficient mice."
Cloning and characterization a novel human 1-acyl-sn-glycerol-3-phosphate acyltransferase gene AGPAT7.
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The cloned human LPCAT4/AGPAT7 product is 524 amino acids and contains a predicted acyltransferase domain.
"The AGPAT7 cDNA is 1898 bp in length, encoding a putative protein with 524 amino acid residues, which contains an acyltransferase domain in 123-234 aa."
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The overexpressed protein localized mainly to the ER in HeLa cells.
"AGPAT7 protein was mainly localized to the endoplasmic reticulum (ER) in Hela cells."
Overexpression of lysophospholipid acyltransferase, LPLAT10/LPCAT4/LPEAT2, in the mouse liver increases glucose-stimulated insulin secretion.
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Liver-specific LPLAT10 overexpression in mice increased hepatic and serum PC 40:7 containing C18:1 and C22:6.
"Hepatic and serum levels of phosphatidylcholine 40:7, containing C18:1 and C22:6, were increased in Ad-LPLAT10-treated mice."
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This mouse gain-of-function intervention increased glucose-stimulated insulin secretion and suppressed postprandial hyperglycemia.
"Postprandial hyperglycemia was suppressed by the induction of glucose-stimulated insulin secretion in Ad-LPLAT10-treated mice compared with that in control Ad vector-treated mice."
Pan-cancer analysis identifies LPCATs family as a prognostic biomarker and validation of LPCAT4/WNT/β-catenin/c-JUN/ACSL3 in hepatocellular carcinoma.
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In hepatocellular carcinoma models, LPCAT4 promoted cell growth and cholesterol biosynthesis through increased ACSL3 expression.
"LPCAT4 enhanced cell growth and cholesterol biosynthesis by up-regulating ACSL3 in hepatocellular carcinoma (HCC)."
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The reported LPCAT4-to-ACSL3 regulation was mediated by WNT/β-catenin/c-JUN signaling in the studied HCC context.
"WNT/β-catenin/c-JUN signaling pathway mediated LPCAT4's regulation on ACSL3."
2-acyl LPC is acylated to PC by LPCAT
1-acyl LPG is acylated to PG by LPGAT
1-acyl LPC is acylated to PC by LPCAT
2-acyl LPG is acylated to PG by LPGAT
1-acyl LPS is acylated to PS by LPSAT
2-acyl LPE is acylated to PE by LPEAT
1-acyl LPE is acylated to PE by LPEAT
2-acyl LPS is acylated to PS by LPSAT
Acyl chain remodelling of PC
Acyl chain remodelling of PS
Acyl chain remodelling of PE
Acyl chain remodelling of PG
1-acyl LPA is acylated to PA by AGPAT (LPAAT)