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Reviewed, UniProtKB/Swiss-Prot P38221 (CDS1_YEAST)

Last modified November 3, 2009. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Phosphatidate cytidylyltransferase
    EC=2.7.7.41
Alternative name(s):
    CDP-diglyceride pyrophosphorylase
    CDP-diglyceride synthetase
    CDP-diacylglycerol synthase
      Short name=CDS
    CTP:phosphatidate cytidylyltransferase
    CDP-DG synthetase
    CDP-DAG synthase
Gene names
Name: CDS1
Synonyms: CDG1
Ordered Locus Names: YBR029C
ORF Names: YBR0313
OrganismSaccharomyces cerevisiae (Baker's yeast) [Complete proteome]
Taxonomic identifier4932 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length457 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Supplies CDP-diacylglycerol, which may play an important role as both a precursor to phosphoinositide biosynthesis in the plasma membrane and as a negative effector of phosphatidylinositol 4-kinase activity, thereby exerting an effect on cell proliferation via a lipid-dependent signal transduction cascade.

Catalytic activity

CTP + phosphatidate = diphosphate + CDP-diacylglycerol.

Pathway

Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 3/3.

Subunit structure

Homodimer.

Subcellular location

Mitochondrion membrane; Multi-pass membrane protein. Endoplasmic reticulum membrane; Multi-pass membrane protein.

Sequence similarities

Belongs to the CDS family.

Ontologies

Keywords
   Biological processPhospholipid biosynthesis
   Cellular componentEndoplasmic reticulum
Membrane
Mitochondrion
   DomainTransmembrane
   Molecular functionNucleotidyltransferase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processphospholipid biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentendoplasmic reticulum

Inferred from electronic annotation. Source: UniProtKB-KW

integral to membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

mitochondrion

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionphosphatidate cytidylyltransferase activity Ref.1

Inferred from direct assay. Source: SGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 457457Phosphatidate cytidylyltransferase
PRO_0000090722

Regions

Transmembrane71 – 9121 Potential
Transmembrane154 – 17421 Potential
Transmembrane188 – 20821 Potential
Transmembrane214 – 23421 Potential
Transmembrane255 – 27521 Potential
Transmembrane330 – 35021 Potential

Experimental info

Mutagenesis1021C → Y: Reduced enzyme level. Ref.5

Sequences

Sequence LengthMass (Da)Tools
P38221-1 [UniParc].

Last modified October 1, 1994. Version 1.
Checksum: F9F3613856EDE172

FASTA45751,823
        10         20         30         40         50         60 
MSDNPEMKPH GTSKEIVESV TDATSKAIDK LQEELHKDAS ESVTPVTKES TAATKESRKY 

        70         80         90        100        110        120 
NFFIRTVWTF VMISGFFITL ASGHAWCIVL ILGCQIATFK ECIAVTSASG REKNLPLTKT 

       130        140        150        160        170        180 
LNWYLLFTTI YYLDGKSLFK FFQATFYEYP VLNFIVTNHK FICYCLYLMG FVLFVCSLRK 

       190        200        210        220        230        240 
GFLKFQFGSL CVTHMVLLLV VFQAHLIIKN VLNGLFWFLL PCGLVIVNDI FAYLCGITFG 

       250        260        270        280        290        300 
KTKLIEISPK KTLEGFLGAW FFTALASIIL TRILSPYTYL TCPVEDLHTN FFSNLTCELN 

       310        320        330        340        350        360 
PVFLPQVYRL PPIFFDKVQI NSITVKPIYF HALNLATFAS LFAPFGGFFA SGLKRTFKVK 

       370        380        390        400        410        420 
DFGHSIPGHG GITDRVDCQF IMGSFANLYY ETFISEHRIT VDTVLSTILM NLNDKQIIEL 

       430        440        450 
IDILIRFLSK KGIISAKNFE KLADIFNVTK KSLTNHS 

« Hide

References

« Hide 'large scale' references
[1]"The CDS1 gene encoding CDP-diacylglycerol synthase in Saccharomyces cerevisiae is essential for cell growth."
Shen H., Heacock P.N., Clancey C.J., Dowhan W.
J. Biol. Chem. 271:789-795(1996) [PubMed: 8557688] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.
[2]"The complete sequence of a 33 kb fragment on the right arm of chromosome II from Saccharomyces cerevisiae reveals 16 open reading frames, including ten new open reading frames, five previously identified genes and a homologue of the SCO1 gene."
Smits P.H.M., de Haan M., Maat C., Grivell L.A.
Yeast 10:S75-S80(1994) [PubMed: 8091864] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]"Complete DNA sequence of yeast chromosome II."
Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C. expand/collapse author list , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.
EMBO J. 13:5795-5809(1994) [PubMed: 7813418] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae."
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.
Genome Res. 17:536-543(2007) [PubMed: 17322287] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[5]"Reduction of CDP-diacylglycerol synthase activity results in the excretion of inositol by Saccharomyces cerevisiae."
Shen H., Dowhan W.
J. Biol. Chem. 271:29043-29048(1996) [PubMed: 8910557] [Abstract]
Cited for: MUTAGENESIS OF CYS-102.
+Additional computationally mapped references.

Cross-references

Sequence databases

X76078 Genomic DNA. Translation: CAA53685.1.
Z35898 Genomic DNA. Translation: CAA84971.1.
AY693074 Genomic DNA. Translation: AAT93093.1.
PIRS45885.
RefSeqNP_009585.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

DIPDIP:7898N.
IntActP38221. 2 interactions.
STRINGP38221.

Proteomic databases

PeptideAtlasP38221.

Genome annotation databases

EnsemblYBR029C; YBR029C; YBR029C; Saccharomyces cerevisiae. [Genome view]
GeneID852317.
GenomeReviewsGene locus YBR029C in contig Y13134_GR.
KEGGsce:YBR029C.
NMPDRfig|4932.3.peg.280.

Organism-specific databases

CYGDYBR029c.
SGDS000000233. CDS1.

Phylogenomic databases

HOGENOMP38221.
OMAIEISPKK.

Enzyme and pathway databases

BRENDA2.7.7.41. 250.

Gene expression databases

ArrayExpressP38221.
GenevestigatorP38221.
GermOnlineYBR029C. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR000374. PC_trans.
IPR016720. PC_Trfase_euk.
[Graphical view]
PfamPF01148. CTP_transf_1. 1 hit.
[Graphical view]
PIRSFPIRSF018269. PC_trans_euk. 1 hit.
PROSITEPS01315. CDS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio971008.

Entry information

Entry nameCDS1_YEAST
AccessionPrimary (citable) accession number: P38221
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: November 3, 2009
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Yeast

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

Yeast chromosome II

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

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents