Gene Ontology annotation through association of InterPro records with GO terms
Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
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
Combined Automated Annotation using Multiple IEA Methods
Enzymatic activity of naturally occurring 1-acylglycerol-3-phosphate-O-acyltransferase 2 mutants associated with congenital generalized lipodystrophy.
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Wild-type human AGPAT2 catalyzes LPA-to-PA conversion. Several CGL-associated variants strongly reduce activity, while A239V retains about 90% in this assay.
"However, the missense mutant, A239V, had 90% of the wild type activity."
The microsomal cardiolipin remodeling enzyme acyl-CoA lysocardiolipin acyltransferase is an acyltransferase of multiple anionic lysophospholipids.
Human 1-acylglycerol-3-phosphate O-acyltransferase isoforms 1 and 2: biochemical characterization and inability to rescue hepatic steatosis in Agpat2(-/-) gene lipodystrophic mice.
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Human AGPAT2 was biochemically characterized (LPA/acyl-CoA substrate specificity, kinetics) and co-localizes with AGPAT1 to the endoplasmic reticulum.
"When co-expressed, both isoforms co-localize to the endoplasmic reticulum."
Cloning and expression of two human lysophosphatidic acid acyltransferase cDNAs that enhance cytokine-induced signaling responses in cells.
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Cloned LPAAT-beta (AGPAT2); complements the E. coli plsC LPAAT mutant and shifts cellular lipid content from LPA to PA, demonstrating LPA-to-PA acyltransferase activity.
"complements its growth defect and shifts the equilibrium of cellular lipid content from LPA to PA and other lipids."
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The abstract reports enhanced TNF-alpha/IL-6 transcription and synthesis after LPAAT overexpression and IL-1beta stimulation; the full beta-versus-alpha experiments and controls remain inaccessible.
"suggesting LPAAT overexpression may amplify cellular signaling responses from cytokines."
Human lysophosphatidic acid acyltransferase. cDNA cloning, expression, and localization to chromosome 9q34.3.
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Cloned human LPAAT; recombinant protein has LPAAT activity preferring LPA as acceptor and arachidonyl-CoA as acyl donor.
"Recombinant protein produced in COS 7 cells exhibited LPAAT activity with a preference for LPA as the acceptor phosphoglycerol and arachidonyl coenzyme A as the acyl donor."
Characterization of a human lysophosphatidic acid acyltransferase that is encoded by a gene located in the class III region of the human major histocompatibility complex.
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The abstract describes the MHC-encoded alpha LPAAT paralog and the shared LPA-to-PA reaction. Exact beta-specific discussion in the full article was not recovered.
"LPAAT is the enzyme that in lipid metabolism converts lysophosphatidic acid (LPA) into phosphatidic acid (PA)."
Synthesis of PA
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In de novo PA synthesis, LPA is converted to PA by an LPA acyltransferase (AGPAT/LPAAT).
"LPA is converted to PA by a LPA acyltransferase (AGPAT, also known as LPAAT)."
Exocytosis of specific granule membrane proteins
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The event explicitly models AGPAT2 in a specific-granule membrane input set and plasma-membrane output set. The underlying AGPAT2-specific experimental localization requires further verification.
"Secondary (specific) granules are peroxidase-negative and rich in antimicrobial substances"
1-acyl LPA is acylated to PA by AGPAT (LPAAT)
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At the ER membrane, 1-acyl-LPA is acylated to PA by AGPAT enzymes; directly supports the core MF and ER-membrane location.
"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"
UniProtKB O15120: 1-acyl-sn-glycerol-3-phosphate acyltransferase beta (AGPAT2)
AGPAT2 is mutated in congenital generalized lipodystrophy linked to chromosome 9q34.
AGPAT2 interaction with CDP-diacylglycerol synthases promotes the flux of fatty acids through the CDP-diacylglycerol pathway.
Expression and regulation of 1-acyl-sn-glycerol- 3-phosphate acyltransferases in the epidermis.
Proteomic analysis of rat hippocampus exposed to the antidepressant paroxetine.
Proteome profiling of human neutrophil granule subsets, secretory vesicles, and cell membrane: correlation with transcriptome profiling of neutrophil precursors.
AGPAT2 acts at the crossroads of lipid biosynthesis and DRP1-mediated ER morphogenesis.