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P17898 (CPT1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:CPT1
Ordered Locus Names:YNL130C
ORF Names:N1218, N1867
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length393 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.6 Ref.7 Ref.8 Ref.9 Ref.15

Catalytic activity

CDP-choline + 1,2-diacyl-sn-glycerol = CMP + a phosphatidylcholine. Ref.7 Ref.15

Cofactor

Magnesium. Ref.7

Enzyme regulation

Requires a divalent cation activator, and is inhibited by CMP. Activated by phospholipids, especially phosphatidylcholine. Ref.7

Pathway

Phospholipid metabolism; phosphatidylcholine biosynthesis; phosphatidylcholine from phosphocholine: step 2/2.

Subcellular location

Microsome membrane; Multi-pass membrane protein. Endoplasmic reticulum membrane; Multi-pass membrane protein. Mitochondrion outer membrane; Multi-pass membrane protein Ref.5 Ref.11 Ref.13.

Induction

Repressed by inositol. Ref.7 Ref.10

Miscellaneous

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

Sequence similarities

Belongs to the CDP-alcohol phosphatidyltransferase class-I family.

Biophysicochemical properties

Kinetic parameters:

KM=100 µM for CDP-choline Ref.7

KM=137 µM for CDP-dimethylethanolamine

Vmax=0.2 nmol/min/mg enzyme for CDP-choline

Vmax=0.07 nmol/min/mg enzyme for CDP-dimethylethanolamine

Sequence caution

The sequence AAA63571.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence CAA86895.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence CAA96012.1 differs from that shown. Reason: Erroneous gene model prediction.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 393393Cholinephosphotransferase 1
PRO_0000056808

Regions

Topological domain1 – 4040Lumenal Potential
Transmembrane41 – 6121Helical; Potential
Topological domain62 – 172111Cytoplasmic Potential
Transmembrane173 – 19321Helical; Potential
Topological domain194 – 21017Lumenal Potential
Transmembrane211 – 23121Helical; Potential
Topological domain232 – 26332Cytoplasmic Potential
Transmembrane264 – 28421Helical; Potential
Topological domain2851Lumenal Potential
Transmembrane286 – 30621Helical; Potential
Topological domain307 – 32014Cytoplasmic Potential
Transmembrane321 – 34121Helical; Potential
Topological domain342 – 3487Lumenal Potential
Transmembrane349 – 36921Helical; Potential
Topological domain370 – 39324Cytoplasmic Potential

Sequences

Sequence LengthMass (Da)Tools
P17898 [UniParc].

Last modified September 5, 2006. Version 3.
Checksum: 320845FE9A79C5D6

FASTA39344,829
        10         20         30         40         50         60 
MGFFIPQSSL GNLKLYKYQS DDRSFLSNHV LRPFWRKFAT IFPLWMAPNL VTLLGFCFII 

        70         80         90        100        110        120 
FNVLTTLYYD PYFDQESPRW TYFSYAIGLF LYQTFDACDG MHARRTGQQG PLGELFDHCI 

       130        140        150        160        170        180 
DSINTTLSMI PVCSMTGMGY TYMTIFSQFA ILCSFYLSTW EEYHTHKLYL AEFCGPVEGI 

       190        200        210        220        230        240 
IVLCISFIAV GIYGPQTIWH TKVAQFSWQD FVFDVETVHL MYAFCTGALI FNIVTAHTNV 

       250        260        270        280        290        300 
VRYYESQSTK SATPSKTAEN ISKAVNGLLP FFAYFSSIFT LVLIQPSFIS LALILSIGFS 

       310        320        330        340        350        360 
VAFVVGRMII AHLTMQPFPM VNFPFLIPTI QLVLYAFMVY VLDYQKGSIV SALVWMGLGL 

       370        380        390 
TLAIHGMFIN DIIYDITTFL DIYALSIKHP KEI 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
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]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[14]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRS63075.
RefSeqNP_014269.4. NM_001182968.3.

3D structure databases

ProteinModelPortalP17898.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid35697. 57 interactions.
DIPDIP-7848N.
IntActP17898. 7 interactions.
MINTMINT-4499922.
STRING4932.YNL130C.

Proteomic databases

MaxQBP17898.
PaxDbP17898.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYNL130C; YNL130C; YNL130C.
GeneID855593.
KEGGsce:YNL130C.

Organism-specific databases

CYGDYNL130c.
SGDS000005074. CPT1.

Phylogenomic databases

eggNOGCOG5050.
GeneTreeENSGT00530000063048.
HOGENOMHOG000157893.
KOK00994.
OrthoDBEOG7W9S4H.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-13671.
YEAST:YNL130C-MONOMER.
UniPathwayUPA00753; UER00740.

Gene expression databases

GenevestigatorP17898.

Family and domain databases

InterProIPR000462. CDP-OH_P_trans.
IPR014472. CHOPT.
[Graphical view]
PANTHERPTHR10414. PTHR10414. 1 hit.
PfamPF01066. CDP-OH_P_transf. 1 hit.
[Graphical view]
PIRSFPIRSF015665. CHOPT. 1 hit.
PROSITEPS00379. CDP_ALCOHOL_P_TRANSF. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio979741.
PROP17898.

Entry information

Entry nameCPT1_YEAST
AccessionPrimary (citable) accession number: P17898
Secondary accession number(s): D6W152
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: September 5, 2006
Last modified: May 14, 2014
This is version 120 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XIV

Yeast (Saccharomyces cerevisiae) chromosome XIV: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways