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Information on EC 3.1.2.2 - palmitoyl-CoA hydrolase and Organism(s) Mus musculus and UniProt Accession P58137
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3.1.2.2 palmitoyl-CoA hydrolaseIUBMB Comments
Also hydrolyses CoA thioesters of other long-chain fatty acids.
Specify your search results
Word Map
- 3.1.2.2
- acyl-coas
- polyketide
- thioesters
-
nonribosomal
- acyltransferase
- synthetases
-
cyclization
- palmitate
- acyl-acps
-
macrocyclization
-
medium-chain
-
beta-oxidation
-
6-deoxyerythronolide
-
enoyl
-
beta-ketoacyl
-
macrolactone
-
nrpss
-
depalmitoylation
- malonyl-coa
- coash
- 4'-phosphopantetheine
-
tyrocidine
- orlistat
- palmitoyl-protein
- lipofuscinosis
- cuphea
-
transacylase
-
surfactin
-
ceroid
-
chain-length
-
uropygial
-
s-acylated
-
ketosynthase
-
chain-terminating
-
didomains
- 4-chlorobenzoate
- enterobactin
- saccharopolyspora
-
12-membered
- phosphopantetheine
- biotechnology
- n-acetylcysteamine
- ketoreductase
-
acyl-carrier
- myristoyl-coa
-
off-loading
- erythraea
- mallard
-
macrolactamization
-
offload
-
triketide
The taxonomic range for the selected organisms is: Mus musculus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
thioesterase, palmitoyl-coa hydrolase, acot7, thioesterase ii, acot1, type ii fas, acot2, thioesterase i, mte-i, cte-i, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ACH1
-
-
-
-
ACH2
-
-
-
-
Acot7
ACT
-
-
-
-
acyl CoA hydrolase
-
-
-
-
acyl coenzyme A hydrolase
-
-
-
-
acyl coenzyme A thioesterase
-
-
-
-
acyl-CoA thioesterase
acyl-CoA thioesterase 7
BACH
brain acyl-CoA hydrolase
CTE-I
fatty acyl thioesterase I
-
-
-
-
HIV-Nef associated acyl coA thioesterase
-
-
-
-
hydrolase, acyl coenzyme A
-
-
-
-
hydrolase, palmitoyl coenzyme A
-
-
-
-
LACH1
-
-
-
-
LACH2
-
-
-
-
long chain acyl-CoA hydrolase
-
-
-
-
long chain acyl-CoA thioesterase
-
-
-
-
long chain fatty-acyl-CoA hydrolase
-
-
-
-
long chain fatty-acyl-CoA thioesterase
-
-
-
-
long-chain acyl-CoA thioesterase
mitochondrial acyl-CoA thioesterase
-
-
-
-
MTE-I
palmitoyl coenzyme A hydrolase
-
-
-
-
palmitoyl thioesterase
-
-
-
-
palmitoyl-CoA deacylase
-
-
-
-
palmitoyl-CoA hydrolase
-
-
-
-
palmityl coenzyme A deacylase
-
-
-
-
palmityl thioesterase
-
-
-
-
palmityl thioesterase I
-
-
-
-
palmityl thioesterase II
-
-
-
-
PTE-Ia
PTE-Ib
TE
-
-
-
-
TE-II
-
-
-
-
thioesterase B
-
-
-
-
thioesterase II
-
-
-
-
very long chain acyl-CoA thioesterase
-
-
-
-
ZAP128
-
-
-
-
acyl-CoA thioesterase
-
-
-
-
brain acyl-CoA hydrolase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of thioester
hydrolysis of thioester
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
-
-, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
palmitoyl-CoA hydrolase
Also hydrolyses CoA thioesters of other long-chain fatty acids.
CAS REGISTRY NUMBER
COMMENTARY
37270-64-7
EC 3.1.2.2
9025-87-0
-
9025-87-0
EC 3.1.2.20
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3-hydroxy-3-methyl glutaryl-CoA + H2O
CoA + 3-hydroxy-3-methyl glutarate
-
-
-
?
3-hydroxy-3-methylglutaryl-CoA + H2O
CoA + 3-hydroxy-3-methylglutarate
-
-
?
trihydroxycoprostanoyl-CoA + H2O
CoA + trihydroxycoprostanoate
-
-
?
chenodeoxycholoyl-CoA + H2O
CoA + chenodeoxycholoate
activity is PPARalpha-inducible
-
-
?
chenodeoxycholoyl-CoA + H2O
CoA + chenodeoxycholoate
bile acid derivative substrate
-
-
?
acyl-CoA + H2O
CoA + a carboxylate
-
involved in fatty acid metabolism
-
?
arachidonoyl-CoA + H2O
arachidonic acid + CoA
-
enzyme is involved in steroidogenesis, overview
-
?
palmitoyl-CoA + H2O
CoA + palmitate
broad substrate specificity for long-chain acyl-CoA substrates
-
?
palmitoyl-CoA + H2O
CoA + palmitate
-
the enzyme affects specifically cellular systems and functions, but not all acyl-CoA-utilizing processes, overexpression leads to reduction of growth rate but not to phospholipid synthesis
-
?
additional information
?
-
enzyme might play an important role in prevention of CoA sequestration and in facilitating excretion of chain-shortened carboxylic acids, enzyme has a key regulatory function in peroxisomal lipid metabolism
-
?
additional information
?
-
-
enzyme might play an important role in prevention of CoA sequestration and in facilitating excretion of chain-shortened carboxylic acids, enzyme has a key regulatory function in peroxisomal lipid metabolism
-
?
additional information
?
-
-
isozyme CTE-I: diurnal regulation and regulation by fat content of the diet
-
?
additional information
?
-
the enzyme plays a role in spermatogenesis
-
-
?
additional information
?
-
role in eicosanoid synthesis and inflammation
-
-
?
additional information
?
-
-
role in eicosanoid synthesis and inflammation
-
-
?
additional information
?
-
-
PPT1-knockout mice, PPT1 deficiency causes persistent membrane anchorage of the palmitoylated synaptic vesicle proteins, which hinder the recycling of the vesicle components that normally fuse with the presynaptic plasma membrane during synaptic vesicle exocytosis
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
arachidonoyl-CoA + H2O
arachidonic acid + CoA
-
enzyme is involved in steroidogenesis, overview
-
?
palmitoyl-CoA + H2O
CoA + palmitate
-
the enzyme affects specifically cellular systems and functions, but not all acyl-CoA-utilizing processes, overexpression leads to reduction of growth rate but not to phospholipid synthesis
-
?
acyl-CoA + H2O
CoA + a carboxylate
-
involved in fatty acid metabolism
-
?
additional information
?
-
enzyme might play an important role in prevention of CoA sequestration and in facilitating excretion of chain-shortened carboxylic acids, enzyme has a key regulatory function in peroxisomal lipid metabolism
-
?
additional information
?
-
-
enzyme might play an important role in prevention of CoA sequestration and in facilitating excretion of chain-shortened carboxylic acids, enzyme has a key regulatory function in peroxisomal lipid metabolism
-
?
additional information
?
-
-
isozyme CTE-I: diurnal regulation and regulation by fat content of the diet
-
?
additional information
?
-
the enzyme plays a role in spermatogenesis
-
-
?
additional information
?
-
role in eicosanoid synthesis and inflammation
-
-
?
additional information
?
-
-
role in eicosanoid synthesis and inflammation
-
-
?
additional information
?
-
-
PPT1-knockout mice, PPT1 deficiency causes persistent membrane anchorage of the palmitoylated synaptic vesicle proteins, which hinder the recycling of the vesicle components that normally fuse with the presynaptic plasma membrane during synaptic vesicle exocytosis
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
acyl-CoA
substrate inhibition at concentrations higher than 0.005-0.01 mM of acyl-CoA longer than C10, BSA protects
nordihydroguaiaretic acid
-
inhibition of acyl-CoA thioesterase and mitochondrial arachidonic acid-related thioesterase
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
peroxisome proliferator WY-14,643
induction of enzyme expression, dependent on peroxisome proliferator-activated receptor alpha
peroxisome proliferator-activated receptor alpha
-
induction of the isozymes in the liver
-
PPARalpha
internal receptor protein essential for effect of stimulating compounds
-
Clofibrate
-
isozymes CTE-I and MTE-I are induced, induction is completely dependent on PPARalpha
Clofibrate
-
induction of all 4 isozymes, mediated through a strictly peroxisome proliferator-activated receptor alpha, PPARalpha, function in gene regulation
PPARalpha
-
internal receptor protein essential for effect of stimulating compounds
-
PPARalpha
-
gene expression inducing and regulatory role, mediates the stimulation by clofibrate
-
additional information
fasting induces enzyme expression, dependent on peroxisome proliferator-activated receptor alpha
-
additional information
-
fasting induces enzyme expression, dependent on peroxisome proliferator-activated receptor alpha
-
additional information
-
fat fasting rapidly induces all isozymes, rapidly reversible
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
diverse substrates, kinetics
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
strong expression of MTE-I, expression of CTE-I, PTE-Ib, and PTE-Ia
-
enzyme is induced during embryogenesis in association with neuronal differentiation
weak expression of MTE-I, expression of CTE-I, PTE-Ib, and PTE-Ia
up-regulated by lipopolysaccharide and that overexpression of Acot7 in a macrophage cell line alters the production of prostaglandins D2 and E2
-
in female mice, mRNA expression of Acot7 isoforms is highest in brain, lung, kidney, heart and ovary
additional information
-
major isozyme brain acyl-CoA hydrolase, enzyme expression level during pre- and post-natal brain development
major isozyme is CTE-I, poor expression of MTE-I, expression of PTE-Ia, no expression of PTE-Ib
-
expression in a neuron-specific manner. The level of the major 43000 Da isoform is low until embryonic day 12.5, elevates to a peak 7 days after birth. Thereafter, it declines somewhat and reaches a steady-state level in adulthood
-
Acot7 is expressed mainly in brain and testis of male mice. In female mice, mRNA expression of Acot7 isoforms is highest in brain, lung, kidney, heart and ovary
strong expression of MTE-I, expression of CTE-I, PTE-Ib, and PTE-Ia
strong expression of MTE-I, expression of CTE-I and PTE-Ia, no expression of PTE-Ib
-
moderate expression in male mice. In female mice, mRNA expression of Acot7 isoforms is highest in brain, lung, kidney, heart and ovary
major isozyme is CTE-I, strong expression of MTE-I, expression of PTE-Ia and PTE-Ib
major isozyme is CTE-I, only weak expression of PTE-Ia, expression of PTE-Ib, no expression of MTE-I
Acot1 mRNA levels are increased by 90fold in liver by treatment with Wy-14,643. Acot1 mRNA is also increased by 15fold in the liver of hepatocyte nuclear factor 4a (HNF4alpha) knockout animals. Acot1 is under regulation by an interplay between HNF4alpha and PPARalpha
major isozyme is CTE-I, strong expression of MTE-I, expression of PTE-Ia, no expression of PTE-Ib
-
moderate expression in male mice. In female mice, mRNA expression of Acot7 isoforms is highest in brain, lung, kidney, heart and ovary
strong expression of MTE-I, only weak expression of CTE-I, expression of PTE-Ia, no expression of PTE-Ib
strong expression of MTE-I, expression of CTE-I and PTE-Ia, no expression of PTE-Ib
major isozyme is CTE-I, poor expression of MTE-I, expression of PTE-Ia, no expression of PTE-Ib
before postnatal day 10 the enzyme is detected at very low levels, the enzyme content rapidly increases from postnatal day 14 and reaches maximal levels at postnatal day 21, remaining high until at least postnatal day 70
strong expression of MTE-I, expression of CTE-I, PTE-Ib, and PTE-Ia
-
ACS4 is rapidly induced by adrenocorticotropin and cAMP in Y1 adrenocortical cells
additional information
palmitoyl-CoA hydrolase activity is widespread in all tissues
additional information
-
palmitoyl-CoA hydrolase activity is widespread in all tissues
additional information
-
Acot7 gene is expressed as multiple isoforms in a tissue-specific manner. Expression in tissues other than brain and testis is likely to play important roles in fatty acid metabolism. Identification of five possible first exons in mouse Acot7 (Acot7ae). All five first exons are transcribed in a tissue-specific manner
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
isozyme PTE-2, major acyl-CoA thioesterase in peroxisomes
-
isozyme CTE-I, diurnal regulation and regulation by fat content of the diet
-
strongly decreased levels of ACOT7 activity and protein in cytosol in patients diagnosed with fatty acid oxidation defects
-
strongly decreased levels of ACOT7 activity and protein in mitochondria in patients diagnosed with fatty acid oxidation defects
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
the enzyme enhances fatty acid oxidation, possibly by mitigating the accumulation of fatty acid oxidation intermediates within the mitochondrial matrix. The enzyme increases proton leak in liver mitochondria
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). ACOT8_MOUSE
320
0
35827
Swiss-Prot
other Location (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
no glycoprotein
p48 is not N-glycosylated and does not enter the secretion pathway
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapor diffusion in 20% PEG 2000. Crystal structures of both the N- and C-terminal domains of the mouse enzyme. The quaternary arrangement in Acot7 features a trimer of hotdog fold dimers
vapour diffusion using PEG 2000 MME as precipitant at pH 7.0 and 17°C. Crystals have the symmetry of space group R32 (unit-cell parameters a = b = 136.83, c = 99.82 A, gamma = 120°). Two molecules are expected in the asymmetric unit. The crystals diffract to 2.4 A resolution using the laboratory X-ray source and are suitable for crystal structure determination
vapour diffusion using PEG 2000 MME as precipitant at pH 7.0 and 17°C. The crystals have the symmetry of space group R32 (unit-cell parameters a = b = 136.83, c = 99.82 A, gamma = 120°). Two molecules in the asymmetric unit. The crystals diffract to 2.4 A resolution
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E39D/T198N
mutant displays a 4fold increase in the catalytic activity compared with wild-type Acot7
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA sequence determination and analysis, expression in Escherichia coli BL21(DE3)
isozyme PTE-2, DNA sequence determination and analysis, expression as green-fluorescent-protein fusion protein in human skin fibroblasts
3 isozymes with differences in the 5'-end sequences, DNA and amino acid sequence determination and analysis, gene structure, functional expression in Escherichia coli BL21(DE3), expression in neuroblastoma cell line Neuro-2a
BACH, stable expression in C3H 10T1/2 fibroblastic cell line using an mifepristone (RU486)-inducible expression system as C-terminally MYC-tagged enzyme
-
from murine EST library, DNA and amino acid sequence determination and analysis, transient expression in HeLa cells, expression as inactive GST-fusion protein in bacteria
genes CTE-I, MTE-I, PTE-Ia and PTE-Ib, DNA and amino acid sequence determination and analysis, promotor cloning, genes possess targeting sequences for subcellular compartment localization, genes are organized in a narrow cluster on chromosome 12, expression of CTE-I in HepG2 cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Poupon, V.; Begue, B.; Gagnon, J.; Dautry-Varsat, A.; Cerf-Bensussan, N.; Benmerah, A.
Molecular cloning and characterization of MT-ACT48, a novel mitochondrial acyl-CoA thioesterase
J. Biol. Chem.
274
19188-19194
1999
Arabidopsis thaliana, Bacillus subtilis, Caenorhabditis elegans, Drosophila melanogaster, Escherichia coli, Haemophilus influenzae, Helicobacter pylori, Homo sapiens, Mus musculus (Q9R0X4), Mus musculus, Oryctolagus cuniculus, Rattus norvegicus
Hunt, M.C.; Lindquist, P.J.G.; Peters, J.M.; Gonzalez, F.J.; Diczfalusy, U.; Alexson, S.E.H.
Involvement of the peroxisome proliferator-activated receptor a in regulating long-chain acyl-CoA thioesterases
J. Lipid Res.
41
814-823
2000
Mus musculus
Hunt, M.C.; Solaas, K.; Kase, B.F.; Alexson, S.E.
Characterization of an acyl-coA thioesterase that functions as a major regulator of peroxisomal lipid metabolism
J. Biol. Chem.
277
1128-1138
2002
Homo sapiens (O14734), Mus musculus (P58137), Mus musculus
Hunt, M.; Lindquist, P.J.G.; Nousiainen, S.; Svensson, T.L.T.; Diczfalusy, U.; Alexson, S.E.H.
Cloning and regulation of peroxisome proliferator-induced acyl-CoA thioesterases from mouse liver
Adv. Exp. Med. Biol.
466
195-200
1999
Mus musculus
Lozano, R.C.; Maloberti, P.; Mendez, C.F.; Paz, C.; Podesta, E.J.
ACTH regulation of mitochondrial acyl-CoA thioesterase activity in Y1 adrenocortical tumour cells
Endocr. Res.
28
331-337
2002
Mus musculus
Hunt, M.C.; Nousiainen, S.E.; Huttunen, M.K.; Orii, K.E.; Svensson, L.T.; Alexson, S.E.
Peroxisome proliferator-induced long chain acyl-CoA thioesterases comprise a highly conserved novel multi-gene family involved in lipid metabolism
J. Biol. Chem.
274
34317-34326
1999
Mus musculus (O55137), Mus musculus
Kuramochi, Y.; Takagi-Sakuma, M.; Kitahara, M.; Emori, R.; Asaba, Y.; Sakaguchi, R.; Watanabe, T.; Kuroda, J.; Hiratsuka, K.; Nagae, Y.; Suga, T.; Yamada, J.
Characterization of mouse homolog of brain acyl-CoA hydrolase: molecular cloning and neuronal localization
Mol. Brain Res.
98
81-92
2002
Mus musculus (Q91V12), Mus musculus
Takagi, M.; Yamakawa, H.; Watanabe, T.; Suga, T.; Yamada, J.
Inducible expression of long-chain acyl-CoA hydrolase gene in cell cultures
Mol. Cell. Biochem.
252
379-385
2003
Mus musculus
Yamada, J.; Kuramochi, Y.; Takagi, M.; Suga, T.
Expression of acyl-CoA hydrolase in the developing mouse brain
Neurosci. Lett.
355
89-92
2004
Mus musculus
Serek, R.; Forwood, J.K.; Hume, D.A.; Martin, J.L.; Kobe, B.
Biochemical and molecular characterization of ACH2, an acyl-CoA thioesterase from Arabidopsis Thaliana
Acta Crystallogr. Sect. F
62
133-135
2006
Mus musculus, Mus musculus (Q91V12)
-
Takagi, M.; Kawabe, K.; Suga, T.; Yamada, J.
A 50-kDa isoform of mouse brain acyl-CoA hydrolase: expression and molecular properties
Arch. Biochem. Biophys.
429
100-105
2004
Mus musculus
Takagi, M.; Ohtomo, T.; Hiratsuka, K.; Kuramochi, Y.; Suga, T.; Yamada, J.
Localization of a long-chain acyl-CoA hydrolase in spermatogenic cells in mice
Arch. Biochem. Biophys.
446
161-166
2006
Mus musculus (Q91V12), Mus musculus
Maciel, F.C.; Maloberti, P.; Neuman, I.; Cano, F.; et al.
An arachidonic acid-preferring acyl-CoA synthetase is a hormone-dependent and obligatory protein in the sifnal transduction pathway of steroidogenic hormones
J. Mol. Endocrinol.
34
655-666
2005
Mus musculus
Hunt, M.C.; Greene, S.; Hultenby, K.; Svensson, L.T.; Engberg, S.; Alexson, S.E.
Alternative exon usage selectively determines both tissue distribution and subcellular localization of the acyl-CoA thioesterase 7 gene products
Cell. Mol. Life Sci.
64
1558-1570
2007
Mus musculus
Dongol, B.; Shah, Y.; Kim, I.; Gonzalez, F.J.; Hunt, M.C.
The acyl-CoA thioesterase I is regulated by PPARalpha and HNF4alpha via a distal response element in the promoter
J. Lipid Res.
48
1781-1791
2007
Mus musculus (O55137), Mus musculus
Forwood, J.K.; Thakur, A.S.; Guncar, G.; Marfori, M.; Mouradov, D.; Meng, W.; Robinson, J.; Huber, T.; Kellie, S.; Martin, J.L.; Hume, D.A.; Kobe, B.
Structural basis for recruitment of tandem hotdog domains in acyl-CoA thioesterase 7 and its role in inflammation
Proc. Natl. Acad. Sci. USA
104
10382-10387
2007
Mus musculus (Q91V12), Mus musculus
Kim, S.J.; Zhang, Z.; Sarkar, C.; Tsai, P.C.; Lee, Y.C.; Dye, L.; Mukherjee, A.B.
Palmitoyl protein thioesterase-1 deficiency impairs synaptic vesicle recycling at nerve terminals, contributing to neuropathology in humans and mice
J. Clin. Invest.
118
3075-3086
2008
Mus musculus, Homo sapiens (P50897)
EXTERNAL LINKS (specific for EC-Number 3.1.2.2)
Transporter Classification Database (TCDB): 4.C.3.1.1
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