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Protein

Choline/ethanolaminephosphotransferase 1

Gene

EPT1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the final step in the CDP-ethanolamine route leading to phosphatidylethanolamine (PE). Can also catalyze the formation of phosphatidylcholine (PC) from CDP-choline, but does not substantially contribute to PC biosynthesis. Preferentially uses CDP-dimethylethanolamine and CDP-propanolamine as aminoalcohol substrates. Shows highest activity toward di-unsaturated diacylglycerol species as lipid substrates. The CDP-ethanolamine pathway may play a role in maintaining the proper PE species distribution.5 Publications

Catalytic activityi

CDP-ethanolamine + 1,2-diacyl-sn-glycerol = CMP + a phosphatidylethanolamine.2 Publications
CDP-choline + 1,2-diacyl-sn-glycerol = CMP + a phosphatidylcholine.2 Publications

Cofactori

Mg2+1 Publication

Enzyme regulationi

Requires a divalent cation activator, and is inhibited by CMP. Activated by phospholipids, especially phosphatidylcholine.1 Publication

Kineticsi

  1. KM=120 µM for CDP-choline1 Publication
  2. KM=29 µM for CDP-dimethylethanolamine1 Publication
  3. KM=29 µM for CDP-monomethylethanolamine1 Publication
  4. KM=22 µM for CDP-ethanolamine1 Publication
  1. Vmax=0.62 nmol/min/mg enzyme for CDP-choline1 Publication
  2. Vmax=0.42 nmol/min/mg enzyme for CDP-dimethylethanolamine1 Publication
  3. Vmax=0.27 nmol/min/mg enzyme for CDP-monomethylethanolamine1 Publication
  4. Vmax=1.35 nmol/min/mg enzyme for CDP-ehylethanolamine1 Publication

Pathwayi: phosphatidylethanolamine biosynthesis

This protein is involved in step 3 of the subpathway that synthesizes phosphatidylethanolamine from ethanolamine.
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. Ethanolamine kinase (EKI1)
  2. Ethanolamine-phosphate cytidylyltransferase (ECT1)
  3. Choline/ethanolaminephosphotransferase 1 (EPT1)
This subpathway is part of the pathway phosphatidylethanolamine biosynthesis, which is itself part of Phospholipid metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes phosphatidylethanolamine from ethanolamine, the pathway phosphatidylethanolamine biosynthesis and in Phospholipid metabolism.

Pathwayi: phosphatidylcholine biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes phosphatidylcholine from phosphocholine.
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Choline-phosphate cytidylyltransferase (PCT1)
  2. Cholinephosphotransferase 1 (CPT1), Choline/ethanolaminephosphotransferase 1 (EPT1)
This subpathway is part of the pathway phosphatidylcholine biosynthesis, which is itself part of Phospholipid metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes phosphatidylcholine from phosphocholine, the pathway phosphatidylcholine biosynthesis and in Phospholipid metabolism.

GO - Molecular functioni

  • diacylglycerol cholinephosphotransferase activity Source: SGD
  • ethanolaminephosphotransferase activity Source: SGD

GO - Biological processi

  • CDP-choline pathway Source: GOC
  • phosphatidylcholine biosynthetic process Source: SGD
  • phosphatidylethanolamine biosynthetic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism, Phospholipid biosynthesis, Phospholipid metabolism

Enzyme and pathway databases

BioCyciYEAST:YHR123W-MONOMER.
ReactomeiR-SCE-1483191. Synthesis of PC.
R-SCE-1483213. Synthesis of PE.
UniPathwayiUPA00558; UER00743.
UPA00753; UER00740.

Chemistry

SwissLipidsiSLP:000000068.

Names & Taxonomyi

Protein namesi
Recommended name:
Choline/ethanolaminephosphotransferase 1 (EC:2.7.8.12 Publications, EC:2.7.8.22 Publications)
Short name:
ETHPT
Short name:
Ethanolaminephosphotransferase 1
Alternative name(s):
Aminoalcohol phosphotransferase EPT1
Gene namesi
Name:EPT1
Ordered Locus Names:YHR123W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome VIII

Organism-specific databases

EuPathDBiFungiDB:YHR123W.
SGDiS000001165. EPT1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 4949LumenalSequence analysisAdd
BLAST
Transmembranei50 – 6920HelicalSequence analysisAdd
BLAST
Topological domaini70 – 172103CytoplasmicSequence analysisAdd
BLAST
Transmembranei173 – 19321HelicalSequence analysisAdd
BLAST
Topological domaini194 – 21118LumenalSequence analysisAdd
BLAST
Transmembranei212 – 23221HelicalSequence analysisAdd
BLAST
Topological domaini233 – 26432CytoplasmicSequence analysisAdd
BLAST
Transmembranei265 – 28218HelicalSequence analysisAdd
BLAST
Topological domaini283 – 2853LumenalSequence analysis
Transmembranei286 – 30823HelicalSequence analysisAdd
BLAST
Topological domaini309 – 32113CytoplasmicSequence analysisAdd
BLAST
Transmembranei322 – 34221HelicalSequence analysisAdd
BLAST
Topological domaini343 – 3464LumenalSequence analysis
Transmembranei347 – 36721HelicalSequence analysisAdd
BLAST
Topological domaini368 – 39124CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 391391Choline/ethanolaminephosphotransferase 1PRO_0000056809Add
BLAST

Proteomic databases

MaxQBiP22140.
PeptideAtlasiP22140.

Expressioni

Inductioni

Repressed by inositol. Repression is dependent on the presence of CPT1.1 Publication

Interactioni

Protein-protein interaction databases

BioGridi36556. 71 interactions.
DIPiDIP-5619N.
IntActiP22140. 11 interactions.
MINTiMINT-475142.

Structurei

3D structure databases

ProteinModelPortaliP22140.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00530000063048.
HOGENOMiHOG000157893.
InParanoidiP22140.
KOiK00993.
OMAiHARRINQ.
OrthoDBiEOG7W9S4H.

Family and domain databases

InterProiIPR000462. CDP-OH_P_trans.
IPR014472. CHOPT.
[Graphical view]
PANTHERiPTHR10414. PTHR10414. 1 hit.
PfamiPF01066. CDP-OH_P_transf. 1 hit.
[Graphical view]
PIRSFiPIRSF015665. CHOPT. 1 hit.
PROSITEiPS00379. CDP_ALCOHOL_P_TRANSF. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P22140-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGYFVPDSHI ENLKSYKYQS EDRSLVSKYF LKPFWQRFCH IFPTWMAPNI
60 70 80 90 100
ITLSGFAFIV INVLTVFYYD PNLNTDTPRW TYFSYALGVF LYQTFDGCDG
110 120 130 140 150
VHARRINQSG PLGELFDHSI DAINSTLSIF IFASETGMGF SYNLMLSQFA
160 170 180 190 200
MLTNFYLSTW EEYHTHTLYL SEFSGPVEGI LIVCVSLILT GIYGKQVIWH
210 220 230 240 250
TYLFTITVGD KVIDVDTLDI VFSLAVFGLV MNALSAKRNV DKYYRNSTSS
260 270 280 290 300
ANNITQIEQD SAIKGLLPFF AYYASIALLV WMQPSFITLS FILSVGFTGA
310 320 330 340 350
FTVGRIIVCH LTKQSFPMFN APMLIPLCQI VLYKICLSLW GIESNKIVFA
360 370 380 390
LSWLGFGLSL GVHIMFMNDI IHEFTEYLDV YALSIKRSKL T
Length:391
Mass (Da):44,560
Last modified:February 1, 1995 - v2
Checksum:i038942A7FB9EB580
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti96 – 961D → V in AAA63572 (PubMed:1848238).Curated
Sequence conflicti98 – 981C → S in AAA63572 (PubMed:1848238).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M59311 Genomic DNA. Translation: AAA63572.1.
U10398 Genomic DNA. Translation: AAB68409.1.
BK006934 Genomic DNA. Translation: DAA06817.1.
PIRiS48967.
RefSeqiNP_011991.1. NM_001179253.1.

Genome annotation databases

EnsemblFungiiYHR123W; YHR123W; YHR123W.
GeneIDi856523.
KEGGisce:YHR123W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M59311 Genomic DNA. Translation: AAA63572.1.
U10398 Genomic DNA. Translation: AAB68409.1.
BK006934 Genomic DNA. Translation: DAA06817.1.
PIRiS48967.
RefSeqiNP_011991.1. NM_001179253.1.

3D structure databases

ProteinModelPortaliP22140.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36556. 71 interactions.
DIPiDIP-5619N.
IntActiP22140. 11 interactions.
MINTiMINT-475142.

Chemistry

SwissLipidsiSLP:000000068.

Proteomic databases

MaxQBiP22140.
PeptideAtlasiP22140.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYHR123W; YHR123W; YHR123W.
GeneIDi856523.
KEGGisce:YHR123W.

Organism-specific databases

EuPathDBiFungiDB:YHR123W.
SGDiS000001165. EPT1.

Phylogenomic databases

GeneTreeiENSGT00530000063048.
HOGENOMiHOG000157893.
InParanoidiP22140.
KOiK00993.
OMAiHARRINQ.
OrthoDBiEOG7W9S4H.

Enzyme and pathway databases

UniPathwayiUPA00558; UER00743.
UPA00753; UER00740.
BioCyciYEAST:YHR123W-MONOMER.
ReactomeiR-SCE-1483191. Synthesis of PC.
R-SCE-1483213. Synthesis of PE.

Miscellaneous databases

NextBioi982287.
PROiP22140.

Family and domain databases

InterProiIPR000462. CDP-OH_P_trans.
IPR014472. CHOPT.
[Graphical view]
PANTHERiPTHR10414. PTHR10414. 1 hit.
PfamiPF01066. CDP-OH_P_transf. 1 hit.
[Graphical view]
PIRSFiPIRSF015665. CHOPT. 1 hit.
PROSITEiPS00379. CDP_ALCOHOL_P_TRANSF. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "sn-1,2-diacylglycerol choline- and ethanolaminephosphotransferases in Saccharomyces cerevisiae. Nucleotide sequence of the EPT1 gene and comparison of the CPT1 and EPT1 gene products."
    Hjelmstad R.H., Bell R.M.
    J. Biol. Chem. 266:5094-5103(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204660 / DBY746.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "The sn-1,2-diacylglycerol ethanolaminephosphotransferase activity of Saccharomyces cerevisiae. Isolation of mutants and cloning of the EPT1 gene."
    Hjelmstad R.H., Bell R.M.
    J. Biol. Chem. 263:19748-19757(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  5. "sn-1,2-diacylglycerol choline- and ethanolaminephosphotransferases in Saccharomyces cerevisiae. Mixed micellar analysis of the CPT1 and EPT1 gene products."
    Hjelmstad R.H., Bell R.M.
    J. Biol. Chem. 266:4357-4365(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, FUNCTION, COFACTOR, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
  6. "Functional redundancy of CDP-ethanolamine and CDP-choline pathway enzymes in phospholipid biosynthesis: ethanolamine-dependent effects on steady-state membrane phospholipid composition in Saccharomyces cerevisiae."
    McGee T.P., Skinner H.B., Bankaitis V.A.
    J. Bacteriol. 176:6861-6868(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "Phosphatidylcholine biosynthesis in Saccharomyces cerevisiae. Regulatory insights from studies employing null and chimeric sn-1,2-diacylglycerol choline- and ethanolaminephosphotransferases."
    McMaster C.R., Bell R.M.
    J. Biol. Chem. 269:28010-28016(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "Studies employing Saccharomyces cerevisiae cpt1 and ept1 null mutants implicate the CPT1 gene in coordinate regulation of phospholipid biosynthesis."
    Morash S.C., McMaster C.R., Hjelmstad R.H., Bell R.M.
    J. Biol. Chem. 269:28769-28776(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  9. "The selective utilization of substrates in vivo by the phosphatidylethanolamine and phosphatidylcholine biosynthetic enzymes Ept1p and Cpt1p in yeast."
    Boumann H.A., de Kruijff B., Heck A.J., de Kroon A.I.
    FEBS Lett. 569:173-177(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY.

Entry informationi

Entry nameiEPT1_YEAST
AccessioniPrimary (citable) accession number: P22140
Secondary accession number(s): D3DL73
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: February 1, 1995
Last modified: May 11, 2016
This is version 137 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome VIII
    Yeast (Saccharomyces cerevisiae) chromosome VIII: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.