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Protein

Cholinephosphotransferase 1

Gene

CPT1

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-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

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
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism, Phospholipid biosynthesis, Phospholipid metabolism

Keywords - Ligandi

Magnesium, 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

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

GO - Cellular componenti

  • endoplasmic reticulum membrane Source: UniProtKB-SubCell
  • Golgi apparatus Source: SGD
  • integral component of membrane Source: UniProtKB-KW
  • mitochondrial outer membrane Source: SGD
Complete GO annotation...

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.
PRIDEiP17898.

PTM databases

iPTMnetiP17898.

Expressioni

Inductioni

Repressed by inositol.1 Publication

Interactioni

Protein-protein interaction databases

BioGridi35697. 56 interactors.
DIPiDIP-7848N.
IntActiP17898. 7 interactors.
MINTiMINT-4499922.

Structurei

3D structure databases

ProteinModelPortaliP17898.
SMRiP17898.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00530000063048.
HOGENOMiHOG000157893.
InParanoidiP17898.
KOiK00994.
OMAiHSIVAKY.
OrthoDBiEOG092C2SE7.

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.

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.

Cross-referencesi

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.

3D structure databases

ProteinModelPortaliP17898.
SMRiP17898.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35697. 56 interactors.
DIPiDIP-7848N.
IntActiP17898. 7 interactors.
MINTiMINT-4499922.

Chemistry databases

SwissLipidsiSLP:000000070.

PTM databases

iPTMnetiP17898.

Proteomic databases

MaxQBiP17898.
PRIDEiP17898.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYNL130C; YNL130C; YNL130C.
GeneIDi855593.
KEGGisce:YNL130C.

Organism-specific databases

EuPathDBiFungiDB:YNL130C.
SGDiS000005074. CPT1.

Phylogenomic databases

GeneTreeiENSGT00530000063048.
HOGENOMiHOG000157893.
InParanoidiP17898.
KOiK00994.
OMAiHSIVAKY.
OrthoDBiEOG092C2SE7.

Enzyme and pathway databases

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

Miscellaneous databases

PROiP17898.

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...

Entry informationi

Entry nameiCPT1_YEAST
AccessioniPrimary (citable) accession number: P17898
Secondary accession number(s): D6W152
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: September 5, 2006
Last modified: November 30, 2016
This is version 138 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

Complete proteome, 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 XIV
    Yeast (Saccharomyces cerevisiae) chromosome XIV: 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.