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Information on EC 2.3.1.176 - propanoyl-CoA C-acyltransferase
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2.3.1.176 propanoyl-CoA C-acyltransferaseIUBMB Comments
Also acts on dihydroxy-5beta-cholestanoyl-CoA and other branched chain acyl-CoA derivatives. The enzyme catalyses the penultimate step in the formation of bile acids. The bile acid moiety is transferred from the acyl-CoA thioester (RCO-SCoA) to either glycine or taurine (NH2R') by EC 2.3.1.65, bile acid-CoA:amino acid N-acyltransferase .
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Word Map
- 2.3.1.176
- allergen
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lipid-transfer
- peach
-
l-cells
-
ige-binding
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l-fabp
- aegypti
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lipid-binding
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phytanic
- profilin
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immunocap
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nbd-cholesterol
- 3-ketoacyl-coa
- 3-oxoacyl-coas
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larvicidal
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pristanic
- phytol
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thiolytic
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d-bifunctional
- dehydroergosterol
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3hcholesterol
- zellweger
- drug development
- medicine
- agriculture
- pharmacology
- nutrition
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
Synonyms
scp-2, nsltp, sterol carrier protein-2, non-specific lipid transfer protein, scp-x, sterol carrier protein x, sterol carrier protein-x, scp-2/thiolase, tgscp2, hascp-2, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
3-oxopristanoyl-CoA hydrolase
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3-oxopristanoyl-CoA thiolase
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EC 2.3.1.154
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formerly
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oxopristanoyl-CoA thiolase
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peroxisomal 3-oxoacyl coenzyme A thiolase
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peroxisomal thiolase 2
peroxisome sterol carrier protein thiolase
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PTE-2
SCP-2
Scp2
SCPc
sterol carrier protein x
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sterol carrier protein-2
sterol carrier protein-c
sterol carrier protein-x
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
3alpha,7alpha,12alpha-trihydroxy-5beta-cholanoyl-CoA + propanoyl-CoA = CoA + 3alpha,7alpha,12alpha-trihydroxy-24-oxo-5beta-cholestanoyl-CoA
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acyl group transfer
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
3alpha,7alpha,12alpha-trihydroxy-5beta-cholanoyl-CoA:propanoyl-CoA C-acyltransferase
Also acts on dihydroxy-5beta-cholestanoyl-CoA and other branched chain acyl-CoA derivatives. The enzyme catalyses the penultimate step in the formation of bile acids. The bile acid moiety is transferred from the acyl-CoA thioester (RCO-SCoA) to either glycine or taurine (NH2R') by EC 2.3.1.65, bile acid-CoA:amino acid N-acyltransferase [3].
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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
3alpha,7alpha,12alpha-trihydroxy-5beta-cholanoyl-CoA + propanoyl-CoA
CoA + 3alpha,7alpha,12alpha-trihydroxy-24-oxo-5beta-cholestanoyl-CoA
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?
additional information
?
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SCP-2, significantly enhances disruption of the dihydroergosterol microcrystalline structure when in the presence of excess cholesterol. In experiments with model membranes containing 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine, cholesterol, and 1,2-dioleoylsn-glycero-3-[phospho-L-serine], SCP-2 enhances exchange of sterol between microcrystals and large unilamellar vesicles nearly 92fold more in the initial rate than the spontaneous exchange
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additional information
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recombinant MsSCP-2 binds to NBD-cholesterol with high affinity, which is suppressed by sterol carrier protein-2 inhibitors
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?
additional information
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recombinant MsSCP-2 binds to NBD-cholesterol with high affinity, which is suppressed by sterol carrier protein-2 inhibitors
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?
additional information
?
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recombinant MsSCP-2 binds to NBD-cholesterol with high affinity, which is suppressed by sterol carrier protein-2 inhibitors
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?
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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
3alpha,7alpha,12alpha-trihydroxy-5beta-cholanoyl-CoA + propanoyl-CoA
CoA + 3alpha,7alpha,12alpha-trihydroxy-24-oxo-5beta-cholestanoyl-CoA
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?
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2,2'-diphenyl-4H,4'H-[6,6'-bibenzo[d][1,3]oxazine]-4,4'-dione
sterol carrier protein-2 is a validated target for development of novel insecticides due to its divergent protein structure and function from the vertebrate SCP-2. HaSCP-2 is important for normal development and fertility in Helicoverpa armigera. H1 (N2,N7-di(1-naphthyl)-9H-2,7-fluorenedisulfonamide) and H14 (2,2'-diphenyl-4H,4'H-[6,6'-bibenzo[d][1,3]oxazine]-4,4'-dione) have inhibitory effect on the growth of Helicoverpa armigera larvae
alpha-mangostin
SCPI-1 or mangostin-treatment cause most death on day-3 and day-4 after the treatment started when larvae in control groups were all alive and molting from 1st to 2nd instars
N-(4-{[4-(3,4-dichlorophenyl)-1,3-thiazol-2-yl]amino}phenyl)acetamide
i.e. SCPI-1, SCPI-1 or mangostin-treatment cause most death on day-3 and day-4 after the treatment started when larvae in control groups were all alive and molting from 1st to 2nd instars
N2,N7-di(1-naphthyl)-9H-2,7-fluorenedisulfonamide
sterol carrier protein-2 is a validated target for development of novel insecticides due to its divergent protein structure and function from the vertebrate SCP-2. HaSCP-2 is important for normal development and fertility in Helicoverpa armigera. H1 (N2,N7-di(1-naphthyl)-9H-2,7-fluorenedisulfonamide) and H14 (2,2'-diphenyl-4H,4'H-[6,6'-bibenzo[d][1,3]oxazine]-4,4'-dione) have inhibitory effect on the growth of Helicoverpa armigera larvae
SCPI-1
i.e. N-(4-[[4-(3,4-dichlorophenyl)-1,3-thiazol-2-yl]amino]phenyl)acetamide hydrobromide
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Adrenoleukodystrophy
Identification of the peroxisomal beta-oxidation enzymes involved in the biosynthesis of docosahexaenoic acid.
Adrenoleukodystrophy
Identification of the peroxisomal beta-oxidation enzymes involved in the degradation of long-chain dicarboxylic acids.
Anaphylaxis
2S albumins and nsLTP are involved in anaphylaxis to pizza sauce: IgE recognition before and after allergen processing.
Anaphylaxis
Different co-sensitizations could determine different risk assessment in peach allergy? Evaluation of an anaphylactic biomarker in Pru p 3 positive patients.
Atherosclerosis
Sterol carrier protein-2 deficiency attenuates diet-induced dyslipidemia and atherosclerosis in mice.
Carcinoma, Hepatocellular
Biosynthesis of nonspecific lipid transfer protein (sterol carrier protein 2) on free polyribosomes as a larger precursor in rat liver.
Carcinoma, Hepatocellular
Elevated cholesterol and decreased sterol carrier protein-2 in peroxisomes from AS-30D hepatoma compared to normal rat liver.
Carcinoma, Hepatocellular
Intracellular dissemination of peroxidative stress. Internalization, transport, and lethal targeting of a cholesterol hydroperoxide species by sterol carrier protein-2-overexpressing hepatoma cells.
Carcinoma, Hepatocellular
Pro-sterol carrier protein-2: role of the N-terminal presequence in structure, function, and peroxisomal targeting.
Carcinoma, Hepatocellular
Secretion of a nonspecific lipid transfer protein by hepatoma cells in culture.
Carcinoma, Hepatocellular
Sterol carrier protein-2 directly interacts with caveolin-1 in vitro and in vivo.
Carcinoma, Hepatocellular
Sterol carrier protein-2 functions in phosphatidylinositol transfer and signaling.
Carcinoma, Hepatocellular
Sterol carrier protein-2 overexpression enhances sterol cycling and inhibits cholesterol ester synthesis and high density lipoprotein cholesterol secretion.
Chondrodysplasia Punctata, Rhizomelic
Identification of the peroxisomal beta-oxidation enzymes involved in the biosynthesis of docosahexaenoic acid.
Chondrodysplasia Punctata, Rhizomelic
Identification of the peroxisomal beta-oxidation enzymes involved in the degradation of long-chain dicarboxylic acids.
Chondrodysplasia Punctata, Rhizomelic
Subcellular localisation and processing of non-specific lipid transfer protein are not aberrant in Rhizomelic Chondrodysplasia Punctata fibroblasts.
Cowpox
Structural Conservation and Functional Diversity of the Poxvirus Immune Evasion (PIE) Domain Superfamily.
Dwarfism
A lipid transfer protein variant with a mutant eight-cysteine motif causes photoperiod- and thermo-sensitive dwarfism in rice.
Dyslipidemias
Sterol carrier protein-2 deficiency attenuates diet-induced dyslipidemia and atherosclerosis in mice.
Dystonia
Mutations in the gene encoding peroxisomal sterol carrier protein X (SCPx) cause leukencephalopathy with dystonia and motor neuropathy.
Food Hypersensitivity
Characteristics of pollen-related food allergy based on individual pollen allergy profiles in the Chinese population.
Food Hypersensitivity
Comparison of IgE-Binding Capacity, Cross-Reactivity and Biological Potency of Allergenic Non-Specific Lipid Transfer Proteins from Peach, Cherry and Hazelnut.
Food Hypersensitivity
Different co-sensitizations could determine different risk assessment in peach allergy? Evaluation of an anaphylactic biomarker in Pru p 3 positive patients.
Food Hypersensitivity
Interaction of Non-Specific Lipid-Transfer Proteins With Plant-Derived Lipids and Its Impact on Allergic Sensitization.
Food Hypersensitivity
Pru p 7 sensitization is a predominant cause of severe, cypress pollen-associated peach allergy.
Gallstones
Overexpression of sterol carrier protein-2 mRNA in patients with cholesterol gallstones.
Hypercholesterolemia
Elevated cholesterol and decreased sterol carrier protein-2 in peroxisomes from AS-30D hepatoma compared to normal rat liver.
Hypercholesterolemia
Reduced hepatic sterol carrier protein-2 expression in the streptozotocin treated diabetic rat.
Hyperglycemia
Physicochemical properties of polysaccharides separated from Camellia oleifera Abel seed cake and its hypoglycemic activity on streptozotocin-induced diabetic mice.
Hypersensitivity
Characteristics of pollen-related food allergy based on individual pollen allergy profiles in the Chinese population.
Hypersensitivity
Lettuce anaphylaxis: identification of a lipid transfer protein as the major allergen.
Hypersensitivity
LTP Allergy Follow-Up Study: Development of Allergy to New Plant Foods 10 Years Later.
Hypersensitivity
Molecular characterization of Api g 2, a novel allergenic member of the lipid-transfer protein 1 family from celery stalks.
Hypersensitivity
Non-specific lipid-transfer proteins: Allergen structure and function, cross-reactivity, sensitization, and epidemiology.
Hypersensitivity
Performance of Basophil Activation Test and specific IgG4 as diagnostic tools in non-specific Lipid Transfer Protein allergy: Antwerp-Barcelona-comparison.
Hypersensitivity
Phenotyping peach-allergic patients sensitized to LTP and analysing severity biomarkers.
Hypersensitivity
Pru p 3, the nonspecific lipid transfer protein from peach, dominates the immune response to its homolog in hazelnut.
Hypotension
Isolation and partial characterization of two biologically active peptides from porcine spinal cord.
Infections
Accumulation of pathogenesis-related proteins in the apoplast of a susceptible cultivar of apple (Malus domestica cv. Elstar) after infection by Venturia inaequalis and constitutive expression of PR genes in the resistant cultivar Remo.
Infections
Identification of Differentially Expressed Proteins in Sugarcane in Response to Infection by Xanthomonas albilineans Using iTRAQ Quantitative Proteomics.
Infections
Non-Specific Lipid Transfer Proteins in Triticum kiharae Dorof. et Migush.: Identification, Characterization and Expression Profiling in Response to Pathogens and Resistance Inducers.
Infections
The involvement of Medicago truncatula non-specific lipid transfer protein N5 in the control of rhizobial infection.
Infections
The potato StLTPa7 gene displays a complex Ca-associated pattern of expression during the early stage of potato-Ralstonia solanacearum interaction.
Neoplasms
Vimentin-dependent utilization of LDL-cholesterol in human adrenal tumor cells is not associated with the level of expression of apoE, sterol carrier protein-2, or caveolin.
Peanut Hypersensitivity
The non-specific lipid transfer protein, Ara h 9, is an important allergen in peanut.
Peroxisomal Disorders
Nonspecific lipid transfer protein (sterol carrier protein-2) defective in patients with deficient peroxisomes.
propanoyl-coa c-acyltransferase deficiency
Sterol carrier protein-2 deficiency attenuates diet-induced dyslipidemia and atherosclerosis in mice.
Refsum Disease
Refsum's disease: a peroxisomal disorder affecting phytanic acid alpha-oxidation.
Yellow Fever
Characterization of the yellow fever mosquito sterol carrier protein-2 like 3 gene and ligand-bound protein structure.
Yellow Fever
Effects of mutations in Aedes aegypti sterol carrier protein-2 on the biological function of the protein.
Yellow Fever
Expression of a sterol carrier protein-x gene in the yellow fever mosquito, Aedes aegypti.
Yellow Fever
Functional analysis of AeSCP-2 using gene expression knockdown in the yellow fever mosquito, Aedes aegypti.
Yellow Fever
Identification of two sterol carrier protein-2 like genes in the yellow fever mosquito, Aedes aegypti.
Yellow Fever
In vivo functional genomic studies of sterol carrier protein-2 gene in the yellow Fever mosquito.
Yellow Fever
Isolation and expression of a sterol carrier protein-2 gene from the yellow fever mosquito, Aedes aegypti.
Yellow Fever
THAP and ATF-2 regulated sterol carrier protein-2 promoter activities in the larval midgut of the yellow fever mosquito, Aedes aegypti.
Yellow Fever
Yellow fever mosquito sterol carrier protein-2 gene structure and transcriptional regulation.
Zellweger Syndrome
Lack of requirement for sterol carrier protein-2 in the intracellular trafficking of lysosomal cholesterol.
Zellweger Syndrome
Nonspecific lipid transfer protein (sterol carrier protein-2) defective in patients with deficient peroxisomes.
Zellweger Syndrome
Sterol Carrier Protein-2, a Nonspecific Lipid-Transfer Protein, in Intracellular Cholesterol Trafficking in Testicular Leydig Cells.
Zellweger Syndrome
Synthetic High-Density Lipoprotein-Like Nanocarrier Improved Cellular Transport of Lysosomal Cholesterol in Human Sterol Carrier Protein-Deficient Fibroblasts.
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
sterol carrier protein-x/sterol carrier protein-2 gene, SCP-x/SCP-2
UniProt
brenda
sterol carrier protein 2, SCP-2; sterol carrier protein-2, SCP-2, gene
UniProt
brenda
sterol carrier protein 2/3-oxoacyl-CoA thiolase, SCP-x; sterol carrier protein-x/the sterol carrier protein-2, MsSCP-x/SCP-2, gene
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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mRNA is strongly expressed in differentiated epithelial structures of the pronephric kidney
brenda
additional information
additional information
tissue and stage expression profiles of HaSCP-2 in larvae of different stages, overview. The highest level of HaSCP-2 expression is in the midgut, whereas the epidermis and the hindgut express the lowest levels
brenda
additional information
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tissue and stage expression profiles of HaSCP-2 in larvae of different stages, overview. The highest level of HaSCP-2 expression is in the midgut, whereas the epidermis and the hindgut express the lowest levels
brenda
additional information
MsSCP-x and MsSCP-2, semi-quantitative RT-PCR expression analysis, overview
brenda
additional information
MsSCP-x and MsSCP-2, semi-quantitative RT-PCR expression analysis, overview
brenda
additional information
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MsSCP-x and MsSCP-2, semi-quantitative RT-PCR expression analysis, overview
brenda
additional information
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highly expressed in tissues involved in cholesterol trafficking and oxidation
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Scp2 localized to peroxisomes and peroxisomal targeting is necessary for its virulence function
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
physiological function
additional information
evolution
the MsSCP-x/SCP-2 protein has a high degree of homology in the SCP-2 domain to other insect SCP-2
malfunction
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disruption of either TgACBP1 (acyl-CoA binding protein) or TgSCP2 caused no obviously phenotypic changes, whereas double disruption results in defects in intracellular growth and virulence to mice. TgACBP1 or TgSCP2 disruption alone leads to decreased abundance of C18:1, whereas double disruption results in reduced abundance of C18:1, C22:1, and C24:1. Loss of TgACBP1 and TgSCP2 cause serious defects in production of glycerides and phospholipids. Collectively, TgACBP1 and TgSCP2 play synergistic roles in lipid metabolism in Toxoplasma gondii
malfunction
scp2 mutants are strongly attenuated in virulence and this defect manifested itself during penetration. Deletion of scp2 in Ustilago maydis interfers neither with growth nor with peroxisomal beta-oxidation
physiological function
overexpression enhances cholesterol uptakeinto Spli-221 cells
physiological function
HaSCPx/2 gene is important for normal development and fertility in Helicoverpa armigera
physiological function
MsSCP-2 may function as a lipid carrier protein in vivo, MsSCP-2 is involved in cholesterol uptake in vivo, overview
physiological function
inhibitor-treated larvae at young stage show a significant decrease of cholesterol uptake in vivo
physiological function
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knockdown of scp2 does not interfere with the patterning of the kidney along its proximo-distal axis, but dramatically decreases the size of the kidney, in particular the proximal tubules. This phenotype is accompanied by a reduction of lipid rafts, but is independent of the peroxisomal or transcriptional activities of scp2. Disrupting lipid microdomains by inhibiting cholesterol synthesis phenocopies the defects seen in scp2 morphants
physiological function
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SCP2 is a binding protein for endocannbinoids N-arachidonylethanolamine and 2-arachidonoylglycerol. N-arachidonylethanolamine and 2-arachidonoylglycerol associate with SCP2 at a putative cholesterol binding pocket with DeltaG values of -3.6 and -4.6 kcal per mol, respectively. SCP2-mediated transfer of cholesterol in vitro is inhibited by micromolar concentrations of N-arachidonylethanolamine, and heterologous expression of SCP2 in HEK-293 cells increases time-related accumulation of N-arachidonylethanolamine in a temperature-dependent fashion
physiological function
role of SCPX and SCP2 in intracellular cholesterol transport. Sterol carrier protein-2 is a nonspecific lipid-transfer protein in intracellular cholesterol trafficking in testicular Leydig cells
physiological function
the enzyme is important for normal development and fertility in Helicoverpa armigera
physiological function
the role of the scp2 gene during plant colonization is analyzed. Virulence function for Scp2 during penetration that is probably carried out by Scp2 in peroxisomes
additional information
effects of dsRNA interference of HaSCP-x/SCP-2 transcripts on larval development and fecundity in adults, overview
additional information
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effects of dsRNA interference of HaSCP-x/SCP-2 transcripts on larval development and fecundity in adults, overview
Show AA Sequence and Transmembrane Helices (1720 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
16000
additional information
additional information
the Scp2 gene encodes the 58 kDa sterol carrier protein-x (SCPX) and 15 kDa pro-SCP2 proteins, both of which contain a 13 kDa SCP2 domain in their C-termini
additional information
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the Scp2 gene encodes the 58 kDa sterol carrier protein-x (SCPX) and 15 kDa pro-SCP2 proteins, both of which contain a 13 kDa SCP2 domain in their C-termini
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
SCP-2 is encoded as a precursor protein with a 20-amino acid N-terminal presequence. The presequence alters SCP-2 secondary structure, tertiary structure, ligand binding site, selectivity for interaction with anionic phospholipid-rich membranes, interaction with a peroxisomal import protein, and intracellular targeting in living and fixed cells
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
NMR spectroscopy and docking simulations reveal that the folds of alpha-helices and beta-sheets interact together to form a hydrophobic cavity with putative entrance and exit openings, which serves as a tunnel for accommodation and transport of lipids
C-terminal sterol carrier protein type 2 (SCP-2) domain of human hydroxysteroid dehydrogenase-like protein 2, to 2.1 A resolution. Space group P3121 (or P3221), with unit-cell parameters a = b = 70.4, c = 60.6 A, alpha = beta = 90°, gamma = 120°
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
wild-type mice fed a cholesterol-rich diet show increased weight gain, hepatic lipid, and bileacid accumulation. SCP-2 overexpression further exacerbates hepatic lipid accumulation in cholesterol-fed females and males. Primarily in female mice, hepatic cholesterol accumulation induced by SCP-2 overexpression is associated with increased levels of LDL receptor, HDL-receptor scavenger receptor SR-B1, liver fatty acid binding protein L-FABP, and 3alpha-hydroxysteroid dehydrogenase, without alteration of other proteins involved in cholesterol uptake, esterification, efflux, or oxidation/transport of bile salts. The effects of SCP-2 overexpression and cholesterol-rich diet are downregulation of proteins involved in cholesterol transport like L-FABP and SR-B1, cholesterolsynthesis related to sterol regulatory element binding protein 2 and HMG-CoA reductase, and bile acid oxidation/transport
additional information
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wild-type mice fed a cholesterol-rich diet show increased weight gain, hepatic lipid, and bileacid accumulation. SCP-2 overexpression further exacerbates hepatic lipid accumulation in cholesterol-fed females and males. Primarily in female mice, hepatic cholesterol accumulation induced by SCP-2 overexpression is associated with increased levels of LDL receptor, HDL-receptor scavenger receptor SR-B1, liver fatty acid binding protein L-FABP, and 3alpha-hydroxysteroid dehydrogenase, without alteration of other proteins involved in cholesterol uptake, esterification, efflux, or oxidation/transport of bile salts. The effects of SCP-2 overexpression and cholesterol-rich diet are downregulation of proteins involved in cholesterol transport like L-FABP and SR-B1, cholesterolsynthesis related to sterol regulatory element binding protein 2 and HMG-CoA reductase, and bile acid oxidation/transport
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene MsSCP-x/SCP-2, from larval fat body and midgut, cDNA and amino acid sequence determination and analysis, sequence comparison
gene SCP-2, from larval fat body and midgut, cDNA and amino acid sequence determination and analysis, sequence comparison
gene SCP-x/SCP-2, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree, detailed overview
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
sterol carrier protein-2 is a validated target for development of novel insecticides due to its divergent protein structure and function from the vertebrate SCP-2. HaSCP-2 is important for normal development and fertility in Helicoverpa armigera. Chemical inhibitors of HaSCP-2 through a structure-based virtual screening are discovered. Bioassay indicates that H1 (N2,N7-di(1-naphthyl)-9H-2,7-fluorenedisulfonamide) and H14 (2,2'-diphenyl-4H,4'H-[6,6'-bibenzo[d][1,3]oxazine]-4,4'-dione) have inhibitory effect on the growth of Helicoverpa armigera larvae. H1 and H14 are promising as useful lead compounds for further optimization and development of novel SCP-2-specific pesticides
drug development
targeting insect SCP-2 may be a viable approach for the development of insecticides
medicine
nutrition
wild-type mice fed a cholesterol-rich diet show increased weight gain, hepatic lipid, and bileacid accumulation. SCP-2 overexpression further exacerbates hepatic lipid accumulation in cholesterol-fed females and males. Primarily in female mice, hepatic cholesterol accumulation induced by SCP-2 overexpression is associated with increased levels of LDL receptor, HDL-receptor scavenger receptor SR-B1, liver fatty acid binding protein L-FABP, and 3alpha-hydroxysteroid dehydrogenase, without alteration of other proteins involved in cholesterol uptake, esterification, efflux, or oxidation/transport of bile salts. The effects of SCP-2 overexpression and cholesterol-rich diet are downregulation of proteins involved in cholesterol transport like L-FABP and SR-B1, cholesterolsynthesis related to sterol regulatory element binding protein 2 and HMG-CoA reductase, and bile acid oxidation/transport
pharmacology
-
although SCP-2 was established as a protein that transfers cholesterol and phospholipids decades ago, recent findings with lipid rafts/caveolae and SCP-2 suggest that they may provide a conceptual link to metabolic processes that might be regulated through the respective signaling pathways
medicine
-
SCP2 is a binding protein for endocannbinoids N-arachidonylethanolamine and 2-arachidonoylglycerol. N-arachidonylethanolamine and 2-arachidonoylglycerol associate with SCP2 at a putative cholesterol binding pocket with DeltaG values of ?3.6 and ?4.6 kcal per mol, respectively. SCP2-mediated transfer of cholesterol in vitro is inhibited by micromolar concentrations of N-arachidonylethanolamine, and heterologous expression of SCP2 in HEK-293 cells increases time-related accumulation of N-arachidonylethanolamine in a temperature-dependent fashion
medicine
SCP2 is a critical host factor for dengue virus production in mosquito Aag2 cells. Treatment with inhibitor SCPI-1, or knockdown of SCP2 dramatically represses the virus production in mosquito but not mammalian cells.The intracellular cholesterol distribution in mosquito cells is altered by SCP2 inhibitor treatment, suggesting that SCP2-mediates cholesterol trafficking pathway that is important for dengue virus viral production. SCPI-1 treatment decreases cholesterol in both mammalian and mosquito cell lines, but this decrease in cholesterol only leads to a decline in viral titer in mosquito host cells
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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Rattus norvegicus
brenda
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1994
Homo sapiens
brenda
Kase, F.; Bjorkhem, I.; Pedersen, J.I.
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24
1560-1567
1983
Rattus norvegicus
brenda
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Mus musculus
brenda
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Biochemistry
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2008
Homo sapiens (P22307)
brenda
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Spodoptera litura (D1GJ60), Spodoptera litura
brenda
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Mus musculus (P32020), Mus musculus
brenda
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