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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

Vmax=0.2 nmol/min/mg enzyme for CDP-choline1 Publication

Vmax=0.07 nmol/min/mg enzyme for CDP-dimethylethanolamine1 Publication

Pathwayi

GO - Molecular functioni

  1. diacylglycerol cholinephosphotransferase activity Source: SGD
  2. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. 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:MONOMER-13671.
YEAST:YNL130C-MONOMER.
ReactomeiREACT_328312. Synthesis of PC.
REACT_348722. Synthesis of PE.
UniPathwayiUPA00753; UER00740.

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
ProteomesiUP000002311 Componenti: Chromosome XIV

Organism-specific databases

CYGDiYNL130c.
EuPathDBiFungiDB:YNL130C.
SGDiS000005074. CPT1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 4040LumenalSequence AnalysisAdd
BLAST
Transmembranei41 – 6121HelicalSequence AnalysisAdd
BLAST
Topological domaini62 – 172111CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei173 – 19321HelicalSequence AnalysisAdd
BLAST
Topological domaini194 – 21017LumenalSequence AnalysisAdd
BLAST
Transmembranei211 – 23121HelicalSequence AnalysisAdd
BLAST
Topological domaini232 – 26332CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei264 – 28421HelicalSequence AnalysisAdd
BLAST
Topological domaini285 – 2851LumenalSequence Analysis
Transmembranei286 – 30621HelicalSequence AnalysisAdd
BLAST
Topological domaini307 – 32014CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei321 – 34121HelicalSequence AnalysisAdd
BLAST
Topological domaini342 – 3487LumenalSequence Analysis
Transmembranei349 – 36921HelicalSequence AnalysisAdd
BLAST
Topological domaini370 – 39324CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum membrane Source: UniProtKB-SubCell
  2. Golgi apparatus Source: SGD
  3. integral component of membrane Source: UniProtKB-KW
  4. 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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 393393Cholinephosphotransferase 1PRO_0000056808Add
BLAST

Proteomic databases

MaxQBiP17898.
PaxDbiP17898.

Expressioni

Inductioni

Repressed by inositol.1 Publication

Gene expression databases

GenevestigatoriP17898.

Interactioni

Protein-protein interaction databases

BioGridi35697. 57 interactions.
DIPiDIP-7848N.
IntActiP17898. 7 interactions.
MINTiMINT-4499922.
STRINGi4932.YNL130C.

Structurei

3D structure databases

ProteinModelPortaliP17898.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG5050.
GeneTreeiENSGT00530000063048.
HOGENOMiHOG000157893.
InParanoidiP17898.
KOiK00994.
OMAiACDGMHA.
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.

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 AAA63571.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence CAA86895.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence CAA96012.1 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35697. 57 interactions.
DIPiDIP-7848N.
IntActiP17898. 7 interactions.
MINTiMINT-4499922.
STRINGi4932.YNL130C.

Proteomic databases

MaxQBiP17898.
PaxDbiP17898.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CYGDiYNL130c.
EuPathDBiFungiDB:YNL130C.
SGDiS000005074. CPT1.

Phylogenomic databases

eggNOGiCOG5050.
GeneTreeiENSGT00530000063048.
HOGENOMiHOG000157893.
InParanoidiP17898.
KOiK00994.
OMAiACDGMHA.
OrthoDBiEOG7W9S4H.

Enzyme and pathway databases

UniPathwayiUPA00753; UER00740.
BioCyciMetaCyc:MONOMER-13671.
YEAST:YNL130C-MONOMER.
ReactomeiREACT_328312. Synthesis of PC.
REACT_348722. Synthesis of PE.

Miscellaneous databases

NextBioi979741.
PROiP17898.

Gene expression databases

GenevestigatoriP17898.

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. "The sn-1,2-diacylglycerol cholinephosphotransferase of Saccharomyces cerevisiae. Nucleotide sequence, transcriptional mapping, and gene product analysis of the CPT1 gene."
    Hjelmstad R.H., Bell R.M.
    J. Biol. Chem. 265:1755-1764(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "A 43.5 kb segment of yeast chromosome XIV, which contains MFA2, MEP2, CAP/SRV2, NAM9, FKB1/FPR1/RBP1, MOM22 and CPT1, predicts an adenosine deaminase gene and 14 new open reading frames."
    Mallet L., Bussereau F., Jacquet M.
    Yeast 11:1195-1209(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications."
    Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J.
    , Bussereau F., Coster F., Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.
    Nature 387:93-98(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. "Subcellular and submitochondrial localization of phospholipid-synthesizing enzymes in Saccharomyces cerevisiae."
    Kuchler K., Daum G., Paltauf F.
    J. Bacteriol. 165:901-910(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  6. "Mutants of Saccharomyces cerevisiae defective in sn-1,2-diacylglycerol cholinephosphotransferase. Isolation, characterization, and cloning of the CPT1 gene."
    Hjelmstad R.H., Bell R.M.
    J. Biol. Chem. 262:3909-3917(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "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.
  8. "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.
  9. "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.
  10. "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.
  11. "Phospholipid-synthesizing enzymes in Golgi membranes of the yeast, Saccharomyces cerevisiae."
    Leber A., Hrastnik C., Daum G.
    FEBS Lett. 377:271-274(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  12. "Reinvestigation of the Saccharomyces cerevisiae genome annotation by comparison to the genome of a related fungus: Ashbya gossypii."
    Brachat S., Dietrich F.S., Voegeli S., Zhang Z., Stuart L., Lerch A., Gates K., Gaffney T.D., Philippsen P.
    Genome Biol. 4:R45.1-R45.13(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVISION OF GENE MODEL.
  13. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  14. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  15. "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 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: April 29, 2015
This is version 126 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

External Data

Dasty 3

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 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.