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Protein

Cholinephosphotransferase 1

Gene

CPT1

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

Functioni

Catalyzes the final step in the CDP-choline route leading to phosphatidylcholin (PC). Preferentially uses CDP-monomethylethanolamine as aminoalcohol substrate. Shows highest activity toward di- and mono-unsaturated diacylglycerol species as lipid substrates. The CDP-choline pathway only contributes to net PC synthesis if exogenous choline is present. In its absence, this pathway recycles choline from PC turnover and may contribute to maintaining the proper PC species composition.5 Publications

Miscellaneous

Present with 981 molecules/cell in log phase SD medium.1 Publication

Catalytic activityi

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=100 µM for CDP-choline1 Publication
  2. KM=137 µM for CDP-dimethylethanolamine1 Publication
  1. Vmax=0.2 nmol/min/mg enzyme for CDP-choline1 Publication
  2. Vmax=0.07 nmol/min/mg enzyme for CDP-dimethylethanolamine1 Publication

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
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • CDP-choline pathway Source: SGD

Keywordsi

Molecular functionTransferase
Biological processLipid biosynthesis, Lipid metabolism, Phospholipid biosynthesis, Phospholipid metabolism
LigandMagnesium, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:YNL130C-MONOMER
YEAST:YNL130C-MONOMER
ReactomeiR-SCE-1483191 Synthesis of PC
R-SCE-1483213 Synthesis of PE
UniPathwayiUPA00753; UER00740

Chemistry databases

SwissLipidsiSLP:000000070

Names & Taxonomyi

Protein namesi
Recommended name:
Cholinephosphotransferase 1 (EC:2.7.8.2)
Alternative name(s):
Aminoalcohol phosphotransferase CPT1
Diacylglycerol cholinephosphotransferase 1
Sn-1,2-diacylglycerol cholinephosphotransferase
Short name:
CHOPT
Gene namesi
Name:CPT1
Ordered Locus Names:YNL130C
ORF Names:N1218, N1867
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XIV

Organism-specific databases

EuPathDBiFungiDB:YNL130C
SGDiS000005074 CPT1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 40LumenalSequence analysisAdd BLAST40
Transmembranei41 – 61HelicalSequence analysisAdd BLAST21
Topological domaini62 – 172CytoplasmicSequence analysisAdd BLAST111
Transmembranei173 – 193HelicalSequence analysisAdd BLAST21
Topological domaini194 – 210LumenalSequence analysisAdd BLAST17
Transmembranei211 – 231HelicalSequence analysisAdd BLAST21
Topological domaini232 – 263CytoplasmicSequence analysisAdd BLAST32
Transmembranei264 – 284HelicalSequence analysisAdd BLAST21
Topological domaini285LumenalSequence analysis1
Transmembranei286 – 306HelicalSequence analysisAdd BLAST21
Topological domaini307 – 320CytoplasmicSequence analysisAdd BLAST14
Transmembranei321 – 341HelicalSequence analysisAdd BLAST21
Topological domaini342 – 348LumenalSequence analysis7
Transmembranei349 – 369HelicalSequence analysisAdd BLAST21
Topological domaini370 – 393CytoplasmicSequence analysisAdd BLAST24

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Microsome, Mitochondrion, Mitochondrion outer membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000568081 – 393Cholinephosphotransferase 1Add BLAST393

Proteomic databases

MaxQBiP17898
PaxDbiP17898
PRIDEiP17898

PTM databases

iPTMnetiP17898

Expressioni

Inductioni

Repressed by inositol.1 Publication

Interactioni

Protein-protein interaction databases

BioGridi35697, 120 interactors
DIPiDIP-7848N
IntActiP17898, 20 interactors
MINTiP17898
STRINGi4932.YNL130C

Structurei

3D structure databases

ProteinModelPortaliP17898
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00530000063048
HOGENOMiHOG000157893
InParanoidiP17898
KOiK00994
OMAiKRICKEP
OrthoDBiEOG092C2SE7

Family and domain databases

InterProiView protein in InterPro
IPR000462 CDP-OH_P_trans
IPR014472 CHOPT
PANTHERiPTHR10414 PTHR10414, 1 hit
PfamiView protein in Pfam
PF01066 CDP-OH_P_transf, 1 hit
PIRSFiPIRSF015665 CHOPT, 1 hit
PROSITEiView protein in PROSITE
PS00379 CDP_ALCOHOL_P_TRANSF, 1 hit

Sequencei

Sequence statusi: Complete.

P17898-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGFFIPQSSL GNLKLYKYQS DDRSFLSNHV LRPFWRKFAT IFPLWMAPNL
60 70 80 90 100
VTLLGFCFII FNVLTTLYYD PYFDQESPRW TYFSYAIGLF LYQTFDACDG
110 120 130 140 150
MHARRTGQQG PLGELFDHCI DSINTTLSMI PVCSMTGMGY TYMTIFSQFA
160 170 180 190 200
ILCSFYLSTW EEYHTHKLYL AEFCGPVEGI IVLCISFIAV GIYGPQTIWH
210 220 230 240 250
TKVAQFSWQD FVFDVETVHL MYAFCTGALI FNIVTAHTNV VRYYESQSTK
260 270 280 290 300
SATPSKTAEN ISKAVNGLLP FFAYFSSIFT LVLIQPSFIS LALILSIGFS
310 320 330 340 350
VAFVVGRMII AHLTMQPFPM VNFPFLIPTI QLVLYAFMVY VLDYQKGSIV
360 370 380 390
SALVWMGLGL TLAIHGMFIN DIIYDITTFL DIYALSIKHP KEI
Length:393
Mass (Da):44,829
Last modified:September 5, 2006 - v3
Checksum:i320845FE9A79C5D6
GO

Sequence cautioni

The sequence AAA63571 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence CAA86895 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence CAA96012 differs from that shown. Reason: Erroneous gene model prediction.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05203 Genomic DNA Translation: AAA63571.1 Different initiation.
Z46843 Genomic DNA Translation: CAA86895.1 Different initiation.
Z71406 Genomic DNA Translation: CAA96012.1 Sequence problems.
BK006947 Genomic DNA Translation: DAA10418.1
PIRiS63075
RefSeqiNP_014269.4, NM_001182968.3

Genome annotation databases

EnsemblFungiiYNL130C; YNL130C; YNL130C
GeneIDi855593
KEGGisce:YNL130C

Similar proteinsi

Entry informationi

Entry nameiCPT1_YEAST
AccessioniPrimary (citable) accession number: P17898
Secondary accession number(s): D6W152
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: September 5, 2006
Last modified: March 28, 2018
This is version 146 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

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