2.3.1.51: 1-acylglycerol-3-phosphate O-acyltransferase
This is an abbreviated version!
For detailed information about 1-acylglycerol-3-phosphate O-acyltransferase, go to the full flat file.
Word Map on EC 2.3.1.51
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2.3.1.51
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adipose
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triacylglycerols
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triglyceride
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lipodystrophy
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phospholipid
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acyl-coas
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lipase
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diacylglycerol
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droplet
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adipocytes
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berardinelli-seip
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lipolysis
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glycerolipids
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agpats
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glycerophospholipids
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chanarin-dorfman
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hypertriglyceridemia
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lysophospholipids
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seipin
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ichthyosis
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perilipins
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acanthosis
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ichthyosiform
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nigricans
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erythroderma
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identification-58
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kennedy
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acyl-acyl
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endophilins
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lipoatrophy
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acyl-coa-dependent
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medicine
- 2.3.1.51
- adipose
- triacylglycerols
- triglyceride
- lipodystrophy
- phospholipid
- acyl-coas
- lipase
- diacylglycerol
- droplet
- adipocytes
-
berardinelli-seip
-
lipolysis
- glycerolipids
- agpats
- glycerophospholipids
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chanarin-dorfman
- hypertriglyceridemia
- lysophospholipids
-
seipin
- ichthyosis
-
perilipins
-
acanthosis
-
ichthyosiform
-
nigricans
- erythroderma
-
identification-58
-
kennedy
-
acyl-acyl
-
endophilins
-
lipoatrophy
-
acyl-coa-dependent
- medicine
Reaction
Synonyms
1-acyl-sn-glycero-3-phosphate acyltransferase, 1-acyl-sn-glycero-3-phosphate acyltransferase 1, 1-acyl-sn-glycero-3-phosphate acyltransferase 9, 1-acyl-sn-glycerol 3-phosphate acyltransferase, 1-acyl-sn-glycerol-3-phosphate acyltransferas, 1-acyl-sn-glycerol-3-phosphate acyltransferase, 1-acyl-sn-glycerol-3-phosphate O-acyltransferase, 1-acylglycero-3-phosphate acyltransferase, 1-acylglycerol 3-phosphate O-acyltransferase, 1-acylglycerol-3-phosphate acyltransferase, 1-acylglycerol-3-phosphate-O-acyltransferase, 1-acylglycerol-3-phosphate-O-acyltransferase 2, 1-acylglycerol-3-phosphate-O-acyltransferase isoform10/glycerol-3-phosphate acyltransferase isoform 3, 1-acylglycerol-3-phosphate-O-acyltransferase-1, 1-acylglycerolphosphate acyltransferase, 1-acylglycerophosphate acyltransferase, 1-Agpat2, ABHD5, acyl-CoA: sn-1-acyl-glycerol-3-phosphate acyltransferase, acyl-CoA:1-acylglycerol-sn-3-phosphate acyltransferase, acyl-CoA:lysophosphatidic acid acyltransferase, acyl-CoA:lysophospholipid acyltransferase, acyl-coenzyme A-dependent lysophosphatidic acid acyltransferase, acylglycerophosphate acyltransferase 4, acyltransferase, 1-acylglycerol phosphate, AGPAT, AGPAT/PlsC, AGPAT1, AGPAT10/GPAT3, AGPAT11, AGPAT2, AGPAT3, AGPAT4, AGPAT5, AGPAT6/GPAT4, AGPAT9, ALE1, At4g24160, AtLPAAt2, CGFI-58, cgi-58 protein, CGI-58/ABHD5, CHLREDRAFT_174358, coenzyme A-dependent lysophosphatidic acid, CrLPAAT1, CT775, CT_775, endoplasmic reticulum-located LPAT, ER-located LPAT, glycerol-3-phosphate acyltransferase-1, GPAT-1, ICT1 protein, LOA1, LPA acyltransferase, LPAAT, LPAAT-beta, LPAAT1, LPAAT2, LPAAT3, LPAAT4, LPAATbeta, LPAATdelta, LPAT, LPCAT1, LPCAT2, lysophosphatidic acid acyl transferase, lysophosphatidic acid acyltansferase, lysophosphatidic acid acyltransferase, lysophosphatidic acid acyltransferase 3, lysophosphatidic acid acyltransferase beta, lysophosphatidic acid ayltransferase, lysophosphatidic acid-acyltransferase, lysophosphatidic acid–specific acyltransferase, lysophosphatidyl acyltransferase, lysophosphatidyl acyltransferase 4, lysophosphatidylcholine acyltransferase 1, lysophospholipid acyltransferase, lysophospholipid:acyl-CoA acyltransferase, mAGPAT1, mAGPAT2, mAGPAT3, mAGPAT4, mAGPAT5, More, oleoyl-CoA lysophosphatidic acid acyltransferase, PCC8801_1274, plastidial LPAAT, plastidial lysophosphatidic acid acyltransferase, PlsC, PlsC4, PrLPAAT1, Scl1, ScLPAAT, SLC1, Slc1p, Slc4p, SlPlsC1, SMc00714 protein, SnGlycerol 3-P acyltransferase, TmPlsC, TM_1693, YPR139c
ECTree
2.3.1.51 1-acylglycerol-3-phosphate O-acyltransferaseAdvanced search results
results (
results (Localization
Localization on EC 2.3.1.51 - 1-acylglycerol-3-phosphate O-acyltransferase
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LOCALIZATION 
ORGANISM
UNIPROT
COMMENTARY 
GeneOntology No.
LITERATURE
SOURCE
isoform AGPAT1 localizes to cytoskeletal components, particularly to areas of actin polymerization in myoblasts
additional information
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mature protein of 32000 Da processed from the precursor protein of 38000 Da
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white adipose tissue of mice, precise role of cgi-58 protein in the cytoplasm unknown
LPAT2, co-localizes with calreticulin in the endoplasmic reticulum
enzyme contains the conserved His residue close to a short stretch of hydrophilic amino acids, which is intercalated between two potential transmembrane helices. The active site histidine resides in the lumen of the endoplasmic reticulum
the most conserved motif containing the presumed active site histidine of isoform Slc1 is oriented in the the membrane towards the lumen, whereas other conserved motifs are cytosolic.embrane to the endereas other conserved motifs are cytosolic
CrLPAAT1 is an integral membrane protein with two potential transmembrane domains (TM), namely TM1 (residues 94-116) and TM2 (residues 188-205), along with a chloroplast transit peptide (cTP) of 46 amino acid residues at the N-terminus. The segment between cTP and TM1 is enriched with serine (Ser) and proline (Pro) residues, the Ser/Pro-rich domain together with a transmembrane alpha-helix might be a sorting/insertion signal for the post-import sorting pathway
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more than 60% of total activity associated with membranes in white adipose tissue
the N-terminal two-helix motif associates with the membrane. Full-length TmPlsC is membrane-bound and not removed by a 0.5 M NaCl wash
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the N-terminal two-helix motif associates with the membrane. Full-length TmPlsC is membrane-bound and not removed by a 0.5 M NaCl wash
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the N-terminal two-helix motif associates with the membrane. Full-length TmPlsC is membrane-bound and not removed by a 0.5 M NaCl wash
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the N-terminal two-helix motif associates with the membrane. Full-length TmPlsC is membrane-bound and not removed by a 0.5 M NaCl wash
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LPAAT is located in the cytoplasmic endomembrane compartment, two microsomal LPAAT isozymes are identified. Diversity of LPAAT microsomal isozymes in rapeseed, overview
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the presence of the enzyme in the mitochondrial fraction cannot be explained by the contamination of microsomes in this fraction
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the presence of the enzyme in the mitochondrial fraction cannot be explained by the contamination of microsomes in this fraction
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KX256279
a transmembrane enzyme, it exhibits an overlap between the transmembrane and LPLAT_AGPAT-like domains
additional information
putative topology models of CrLPAAT1, overview
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additional information
isozyme AGPAT3 is predominantly in the endoplasmic reticulum but has been detected in the nuclear envelope. Lipid synthesis occurs on the inner nuclear membrane (INM) and nuclear lipid droplets
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additional information
isozyme AGPAT3 is predominantly in the endoplasmic reticulum but has been detected in the nuclear envelope. Lipid synthesis occurs on the inner nuclear membrane (INM) and nuclear lipid droplets
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additional information
isozyme AGPAT3 is predominantly in the endoplasmic reticulum but has been detected in the nuclear envelope. Lipid synthesis occurs on the inner nuclear membrane (INM) and nuclear lipid droplets
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additional information
isozyme AGPAT3 is predominantly in the endoplasmic reticulum but has been detected in the nuclear envelope. Lipid synthesis occurs on the inner nuclear membrane (INM) and nuclear lipid droplets
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additional information
isozyme AGPAT3 is predominantly in the endoplasmic reticulum but has been detected in the nuclear envelope. Lipid synthesis occurs on the inner nuclear membrane (INM) and nuclear lipid droplets
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additional information
isozyme AGPAT5 is predominantly in the endoplasmic reticulum but has been detected in the nuclear envelope and mitochondria. Lipid synthesis occurs on the inner nuclear membrane (INM) and nuclear lipid droplets
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additional information
isozyme AGPAT5 is predominantly in the endoplasmic reticulum but has been detected in the nuclear envelope and mitochondria. Lipid synthesis occurs on the inner nuclear membrane (INM) and nuclear lipid droplets
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additional information
isozyme AGPAT5 is predominantly in the endoplasmic reticulum but has been detected in the nuclear envelope and mitochondria. Lipid synthesis occurs on the inner nuclear membrane (INM) and nuclear lipid droplets
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additional information
isozyme AGPAT5 is predominantly in the endoplasmic reticulum but has been detected in the nuclear envelope and mitochondria. Lipid synthesis occurs on the inner nuclear membrane (INM) and nuclear lipid droplets
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additional information
isozyme AGPAT5 is predominantly in the endoplasmic reticulum but has been detected in the nuclear envelope and mitochondria. Lipid synthesis occurs on the inner nuclear membrane (INM) and nuclear lipid droplets
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additional information
seipin is colocalized with AGPAT2 and LIPIN-1 in the endoplasmic reticulum. A seipin-AGPAT2-LIPIN-1 complex may compartmentalize phosphatidic acid and diglyceride to enhance triglyceride synthesis
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additional information
seipin is colocalized with AGPAT2 and LIPIN-1 in the endoplasmic reticulum. A seipin-AGPAT2-LIPIN-1 complex may compartmentalize phosphatidic acid and diglyceride to enhance triglyceride synthesis
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additional information
seipin is colocalized with AGPAT2 and LIPIN-1 in the endoplasmic reticulum. A seipin-AGPAT2-LIPIN-1 complex may compartmentalize phosphatidic acid and diglyceride to enhance triglyceride synthesis
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additional information
seipin is colocalized with AGPAT2 and LIPIN-1 in the endoplasmic reticulum. A seipin-AGPAT2-LIPIN-1 complex may compartmentalize phosphatidic acid and diglyceride to enhance triglyceride synthesis
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additional information
seipin is colocalized with AGPAT2 and LIPIN-1 in the endoplasmic reticulum. A seipin-AGPAT2-LIPIN-1 complex may compartmentalize phosphatidic acid and diglyceride to enhance triglyceride synthesis
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additional information
KX256278
subcelluar localization study in transgenic Nicotiana tabacum leaves
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additional information
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subcelluar localization study in transgenic Nicotiana tabacum leaves
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