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Information on EC 2.7.7.14 - ethanolamine-phosphate cytidylyltransferase and Organism(s) Mus musculus and UniProt Accession Q922E4
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2.7.7.14 ethanolamine-phosphate cytidylyltransferaseSpecify your search results
Word Map
- 2.7.7.14
- phosphatidylethanolamine
- phospholipid
- cdp-ethanolamine
- diacylglycerols
-
kennedy
- cdp-choline
-
ctp:phosphocholine
- phosphocholine
-
3hethanolamine
-
ptdetn
- ethanolaminephosphotransferase
-
14cethanolamine
- drug development
The taxonomic range for the selected organisms is: Mus musculus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
pcyt2, ctp:phosphoethanolamine cytidylyltransferase, pect1, phosphoethanolamine cytidylyltransferase, ethanolamine-phosphate cytidylyltransferase, ctp:ethanolaminephosphate cytidylyltransferase, ctp:phosphoethanolamine cytidylyltransferase gene, ctp-phosphoethanolamine cytidylyltransferase, ctp:phosphoethanolamine ct, ethanolamine phosphate cytidylyltransferase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Pcyt2alpha
Pcyt2beta
CTP-phosphoethanolamine cytidylyltransferase
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cytidylyltransferase, ethanolamine phosphate
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ET
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ethanolamine phosphate cytidylyltransferase
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Pcyt2
phosphoethanolamine cytidylyltransferase
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phosphorylethanolamine transferase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
nucleotidyl group transfer
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
CTP:ethanolamine-phosphate cytidylyltransferase
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CAS REGISTRY NUMBER
COMMENTARY
9026-33-9
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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
CTP + ethanolamine phosphate
CDP-ethanolamine + diphosphate
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-
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?
CTP + ethanolamine phosphate
diphosphate + CDP-ethanolamine
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?
CTP + ethanolamine phosphate
diphosphate + CDP-ethanolamine
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Pcyt2is necessary for murine development. A single Pcyt2 allele in heterozygotes can maintain phospholipid homeostasis
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?
additional information
?
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uses N-methylated derivatives of ethanolamine phosphate less efficiently and does not react with phosphocholine
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?
additional information
?
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uses N-methylated derivatives of ethanolamine phosphate less efficiently and does not react with phosphocholine
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?
additional information
?
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Pcyt2 is the main regulatory enzyme in the CDP-ethanolamine pathwa
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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
additional information
?
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Pcyt2 is the main regulatory enzyme in the CDP-ethanolamine pathwa
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?
CTP + ethanolamine phosphate
diphosphate + CDP-ethanolamine
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Pcyt2is necessary for murine development. A single Pcyt2 allele in heterozygotes can maintain phospholipid homeostasis
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?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
does not require the presence of exogenous lipids for optimal activity
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additional information
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does not require the presence of exogenous lipids for optimal activity
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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upregulated in brown adipose tissue in comparison to white adipose tissue
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inguinal and epididymal, upregulated in brown adipose tissue in comparison to white adipose tissue
additional information
high Pcyt2 mRNA content. Negligible amount of Pcyt2beta mRNA, high amount of Pcyt2alpha mRNA
negligible amount of Pcyt2beta mRNA, high amount of Pcyt2alpha mRNA
low Pcyt2 mRNA content. Negligible amount of Pcyt2beta mRNA, high amount of Pcyt2alpha mRNA
additional information
splice variant Pcyt2gamma is ubiquitously expressed in embryonic and adult mouse tissues, and is the most abundant in the kidney, skeletal muscle and testis
additional information
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splice variant Pcyt2gamma is ubiquitously expressed in embryonic and adult mouse tissues, and is the most abundant in the kidney, skeletal muscle and testis
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
associated with the membranes of the rough endoplasmic reticulum
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
rate-limiting enzyme in mammalian phosphatidylethanolamine biosynthesis
metabolism
physiological function
additional information
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the isoforms Pcyt2alpha and Pcyt2beta are unique cytidylyltransferases, containing two CTP binding HXGH motifs and large repetitive sequences within the N- and C-domains made by gene duplication. Overexpression of Pcyt2 increases the level of CDP-ethanolamine, but phosphatidylethanolamine content remains unchanged since no adequate diacylglacerol is present
metabolism
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the enzyme is important and the main regulatory enzyme in de novo production of phosphatidylethanolamine via the CDP-ethanolamine Kennedy pathway, overview. Pcyt2 gene is a target of liver X receptor
physiological function
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the enzyme is important in de novo production of phosphatidylethanolamine, which is the most abundant lipid on the cytoplasmic layer of cellular membranes, with significant roles in cellular processes such as membrane fusion, cell cycle, autophagy, and apoptosis. Transcriptional regulation of Pcyt2, Pcyt2 expression in lipid-related disorders and cancer, and and Pcyt2 expression in the metabolic syndrome and related disorders, detailed overview
physiological function
mouse isoform Pcyt2 can be spliced at introns 7 and 8 to produce a unique isoform, Pcyt2gamma, in which the second cytidylyltransferase domain at the C-terminus becomes deleted. Pcyt2gamma is ubiquitously expressed in embryonic and adult mouse tissues, and is the most abundant in the kidney, skeletal muscle and testis. Pcyt2gamma splicing mechanism dominates over splice variant Pcyt2beta exon-skipping mechanism in most examined tissues. Pcyt2gamma maintains the N-terminal cytidylyltransferase domain, but the lack of the C-terminal cytidylyltransferase domain causes a complete loss of catalytic activity. Pcyt2gamma interacts with the active isoform, splice variant Pcyt2alpha, and significantly reduces Pcyt2alpha homodimerization and activity
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). PCY2_MOUSE
404
0
45235
Swiss-Prot
other Location (Reliability: 4)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
110000
myc-His-tagged Pcyt2beta, appears as two bands (110000 and 90000 Da), gel filtration
90000
myc-His-tagged Pcyt2beta, appears as two bands (110000 and 90000 Da), gel filtration
34000
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x * 51000, isozyme Pcyt2alpha, x * 49000, isozyme Pcyt2beta, x * 34000, isozyme Pcyt2gamma
49000
51000
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x * 51000, isozyme Pcyt2alpha, x * 49000, isozyme Pcyt2beta, x * 34000, isozyme Pcyt2gamma
49000
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x * 51000, isozyme Pcyt2alpha, x * 49000, isozyme Pcyt2beta, x * 34000, isozyme Pcyt2gamma
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
?
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x * 51000, isozyme Pcyt2alpha, x * 49000, isozyme Pcyt2beta, x * 34000, isozyme Pcyt2gamma
dimer
isozymes Pcyt2alpha and Pcyt2beta proteins can form both homodimeric and heterodimeric complexes
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H244A
inactive C-domain mutant, presence of the mutant reduces splice variant Pcyt2alpha homodimerization and activity
H244Y
inactive C-domain mutant, presence of the mutant reduces splice variant Pcyt2alpha homodimerization and activity
H35A
inactive N-domain mutant, presence of the mutant reduces splice variant Pcyt2alpha homodimerization and activity
H35Y
inactive N-domain mutant, presence of the mutant reduces splice variant Pcyt2alpha homodimerization and activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
Pcyt2, DNA and amino acid sequence and promoter determination and analysis, three splicing isoforms of Pcyt2, alpha, beta, and gamma, encoded by a single Pcyt2 gene, genetic structures. Transcriptional regulation of Pcyt2, overview
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
increased Pcyt2 mRNA levels after serum starvation are suppressed by 25-hydroxycholesterol. The suppressive effect of 25-hydroxycholesterol on mRNA transcription is ameliorated by trichostatin A. Anacardic acid, 25-hydroxycholesterol and 24(S)-hydroxycholesterol suppress the transcription by inhibiting H3K27 acetylation in the promoter. 27-Hydroxycholesterol, 22(S)-hydroxycholesterol and 22(R)-hydroxycholesterol suppress the transcription
liver X receptor, LXR, can modulate and activate promoter activity and transcription of Pcyt2. Pcyt2 is transcriptionally up-regulated by serum-deficiency induced differentiation of the skeletal muscle cells C2C12. The core mouse promoter (-111/+29)is dependent on binding of cEBP to an inverse CCAT box located at the position -82/-77 bp, ncreased amount of muscle-specific regulator, MyoD, reduced the content of Sp1 (binds to region -508/-378 bp), which, together with the decrease in ratio of Sp1 to Sp3, is responsible for the stimulation of transcription of Pcyt2 gene in differentiated C2C12 myotubes relative to undifferentiated myoblasts. The enzyme is upregulated in Sirtuin null mice and in adipose tissue of high-weight gainers
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oxysterols, 24-hydroxycholesterol, 25-hydroxycholesterol, 27-hydroxycholesterol, and 24(S),25-epoxycholesterol, and mevalonolactate are partially responsible for the inhibition of Pcyt2 transcription. 25-Hydroxycholesterol, an endogenous activator of liver X receptor, and the liver X receptor synthetic agonist TO901317 both significantly reduce the biosynthesis of phosphatidylethanolamine via the CDP-ethanolamine Kennedy pathway by inhibiting the promoter function and expression of Pcyt2 in mouse embryonic fibroblasts. The enzyme is downregulated in sphingosine 1-phosphate lyase null mice and in livers of copper-transporting ATPase ATP7B null mice, downregulation in ATF2 null mice
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the important element for transcriptional control of Pcyt2 by 25-HC resides between -56 and -36 in NIH 3T3 cells. Nuclear factor-Y binds at C(-37)CAAT(-41) and Yin Yang1 binds at C(-42)AT(-40) in the Pcyt2 promoter. Nuclear factor-Y is involved in the inhibitory effects of 25-hydroxycholesterol on Pcyt2 transcription
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bakovic, M.; Fullerton, M.D.; Michel, V.
Metabolic and molecular aspects of ethanolamine phospholipid biosynthesis: the role of CTP:phosphoethanolamine cytidylyltransferase (Pcyt2)
Biochem. Cell Biol.
85
283-300
2007
Homo sapiens, Mus musculus (Q922E4), Mus musculus, Rattus norvegicus, Saccharomyces cerevisiae
Fullerton, M.D.; Hakimuddin, F.; Bakovic, M.
Developmental and metabolic effects of disruption of the mouse CTP:phosphoethanolamine cytidylyltransferase gene (Pcyt2)
Mol. Cell. Biol.
27
3327-3336
2007
Mus musculus
Tie, A.; Bakovic, M.
Alternative splicing of CTP:phosphoethanolamine cytidylyltransferase produces two isoforms that differ in catalytic properties
J. Lipid Res.
48
2172-2181
2007
Mus musculus (Q922E4), Mus musculus
Ando, H.; Horibata, Y.; Yamashita, S.; Oyama, T.; Sugimoto, H.
Low-density lipoprotein and oxysterols suppress the transcription of CTP:Phosphoethanolamine cytidylyltransferase in vitro
Biochim. Biophys. Acta
1801
487-495
2010
Homo sapiens, Mus musculus
Zhu, L.; Michel, V.; Bakovic, M.
Regulation of the mouse CTP: phosphoethanolamine cytidylyltransferase gene Pcyt2 during myogenesis
Gene
447
51-59
2009
Mus musculus
Fullerton, M.D.; Hakimuddin, F.; Bonen, A.; Bakovic, M.
The development of a metabolic disease phenotype in CTP:phosphoethanolamine cytidylyltransferase-deficient mice
J. Biol. Chem.
284
25704-25713
2009
Mus musculus
Leonardi, R.; Frank, M.W.; Jackson, P.D.; Rock, C.O.; Jackowski, S.
Elimination of the CDP-ethanolamine pathway disrupts hepatic lipid homeostasis
J. Biol. Chem.
284
27077-27089
2009
Mus musculus
Pavlovic, Z.; Bakovic, M.
Regulation of phosphatidylethanolamine homeostasis - the critical role of CTP:phosphoethanolamine cytidylyltransferase (Pcyt2)
Int. J. Mol. Sci.
14
2529-2550
2013
Homo sapiens, Mus musculus, Mus musculus C57BL/6, Plasmodium berghei, Rattus norvegicus, Rattus norvegicus Wistar, Saccharomyces cerevisiae, Trypanosoma brucei
Ando, H.; Aoyama, C.; Horibata, Y.; Satou, M.; Mitsuhashi, S.; Itoh, M.; Hosaka, K.; Sugimoto, H.
Transcriptional suppression of CTP:phosphoethanolamine cytidylyltransferase by 25-hydroxycholesterol is mediated by nuclear factor-Y and Yin Yang 1
Biochem. J.
471
369-379
2015
Mus musculus
Pavlovic, Z.; Singh, R.K.; Bakovic, M.
A novel murine CTP:phosphoethanolamine cytidylyltransferase splice variant is a post-translational repressor and an indicator that both cytidylyltransferase domains are required for activity
Gene
543
58-68
2014
Mus musculus (Q540F5), Mus musculus
Ando, H.; Horibata, Y.; Aoyama, C.; Shimizu, H.; Shinohara, Y.; Yamashita, S.; Sugimoto, H.
Side-chain oxysterols suppress the transcription of CTP phosphoethanolamine cytidylyltransferase and 3-hydroxy-3-methylglutaryl-CoA reductase by inhibiting the interaction of p300 and NF-Y, and H3K27 acetylation
J. Steroid Biochem. Mol. Biol.
195
105482
2019
Mus musculus (Q922E4), Homo sapiens (Q99447)
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