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Q12382 (DGK1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
CTP-dependent diacylglycerol kinase 1

EC=2.7.1.174
Alternative name(s):
Diglyceride kinase 1
Short name=DAG kinase 1
High-copy suppressor of SLY1 defect protein 1
Gene names
Name:DGK1
Synonyms:HSD1
Ordered Locus Names:YOR311C
ORF Names:O6111
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length290 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in pre-tRNA splicing By similarity. CTP-dependent diacylglycerol kinase that catalyzes the phosphorylation of diacylglycerol (DAG) to phosphatidate (PA). Controls phosphatidate levels at the nuclear envelope. Counteracts the activity of PAH1/SMP2. Involved in the resistance to nickel chloride and nalidixic acid. May be involved in vesicle trafficking between the endoplasmic reticulum and the Golgi apparatus. Ref.4 Ref.5 Ref.10

Catalytic activity

CTP + 1,2-diacyl-sn-glycerol = CDP + 1,2-diacyl-sn-glycerol 3-phosphate. Ref.10 Ref.11

Cofactor

Ca2+ or Mg2+. Ref.11

Enzyme regulation

Inhibited by N-ethylmaleimide, dCTP, and sphingoid bases including sphinganine, sphingosine and phytosphingosine. DAG pyrophosphate, cardiolipin, CDP-DAG, and lyso-PA inhibited activity by 23-66%. Also inhibited by Ca2+ concentrations of more than 1 mM, by addition of EDTA or EGTA at 5 mM, and by 5 mM Mn2+ and Zn2+. Stimulated by major membrane phospholipids including phosphatidylcholine, phosphatidylethanolamine, phosphatidylinositol, phosphatidylserine, phosphatidylglycerol, and phosphatidate. Also stimulated to a maximum by addition of TritonX-100 at a concentration of 1 mM, followed by an apparent inhibition of activity at concentrations above 1 mM. Ref.11

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein. Golgi apparatus membrane; Multi-pass membrane protein. Nucleus membrane; Multi-pass membrane protein Ref.5 Ref.6 Ref.10.

Miscellaneous

Present with 784 molecules/cell in log phase SD medium.

Rescues the lethality of dephosphorylated PAH1/SMP2. Overexpression causes the appearance of phosphatidate-enriched membranes around the nucleus, leading to expansion of the nuclear membrane without proliferation of the cortical endoplasmic reticulum membrane. Deletion restores normal nuclear structure in PAH1/SMP2 deleted cells and returns the level of INO1 mRNA to normal. Deletion does not affect the abnormal levels of phosphatidylinositol and major neutral lipid triacylglycerol seen in the PAH1/SMP2 deletion mutant.

Sequence similarities

Belongs to the DGK1 family.

Biophysicochemical properties

Kinetic parameters:

KM=0.3 mM for CTP Ref.11

KM=0.4 mM for dCTP

Vmax=0.018 nM/min/mg enzyme

pH dependence:

Optimum pH is 7.0-7.5.

Temperature dependence:

Maximum activity at 30 degrees Celsius. Labile above 40 degrees Celsius.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 290290CTP-dependent diacylglycerol kinase 1
PRO_0000240382

Regions

Topological domain1 – 7777Lumenal Potential
Transmembrane78 – 9518Helical; Potential
Topological domain96 – 1038Cytoplasmic Potential
Transmembrane104 – 12421Helical; Potential
Topological domain125 – 14016Lumenal Potential
Transmembrane141 – 16121Helical; Potential
Topological domain162 – 1632Cytoplasmic Potential
Transmembrane164 – 18421Helical; Potential
Topological domain185 – 20319Lumenal Potential
Transmembrane204 – 22421Helical; Potential
Topological domain225 – 24420Cytoplasmic Potential
Transmembrane245 – 26521Helical; Potential
Topological domain266 – 29025Lumenal Potential

Amino acid modifications

Modified residue441Phosphoserine Ref.12
Modified residue451Phosphoserine Ref.12
Modified residue461Phosphoserine Ref.12
Glycosylation111N-linked (GlcNAc...) Potential
Glycosylation1971N-linked (GlcNAc...) Potential
Glycosylation2701N-linked (GlcNAc...) Potential

Experimental info

Mutagenesis761R → A: Loss of kinase activity. Not temperature-sensitive for growth. Regular shaped nuclear membrane structure. Ref.11
Mutagenesis771K → A: Loss of kinase activity. Not temperature-sensitive for growth. Regular shaped nuclear membrane structure. Ref.11
Mutagenesis1771D → A: No kinase activity. Not temperature-sensitive for growth. Does not trigger nuclear membrane expansion. Ref.10 Ref.11
Mutagenesis1841G → A: 70% reduction in kinase activity. Not temperature-sensitive for growth. Regular shaped nuclear membrane structure. Ref.11

Sequences

Sequence LengthMass (Da)Tools
Q12382 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: F8A0EE6F1018025B

FASTA29032,840
        10         20         30         40         50         60 
MGTEDAIALP NSTLEPRTEA KQRLSSKSHQ VSAKVTIPAK EEISSSDDDA HVPVTEIHLK 

        70         80         90        100        110        120 
SHEWFGDFIT KHEIPRKVFH SSIGFITLYL YTQGINYKNV LWPLIYAFII LFILDLIRLN 

       130        140        150        160        170        180 
WPFFNMLYCR TVGALMRKKE IHTYNGVLWY ILGLIFSFNF FSKDVTLISL FLLSWSDTAA 

       190        200        210        220        230        240 
ATIGRKYGHL TPKVARNKSL AGSIAAFTVG VITCWVFYGY FVPAYSYVNK PGEIQWSPET 

       250        260        270        280        290 
SRLSLNMLSL LGGVVAALSE GIDLFNWDDN FTIPVLSSLF MNAVIKTFKK 

« Hide

References

« Hide 'large scale' references
[1]"Sequencing of a 35.71 kb DNA segment on the right arm of yeast chromosome XV reveals regions of similarity to chromosomes I and XIII."
Pearson B.M., Hernando Y., Payne J., Wolf S.S., Kalogeropoulos A., Schweizer M.
Yeast 12:1021-1031(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 96604 / S288c / FY1679.
[2]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D. expand/collapse author list , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
Nature 387:98-102(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"Chemotyping of yeast mutants using robotics."
Rieger K.-J., El-Alama M., Stein G., Bradshaw C., Slonimski P.P., Maundrell K.
Yeast 15:973-986(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[5]"Multicopy suppressors of the sly1 temperature-sensitive mutation in the ER-Golgi vesicular transport in Saccharomyces cerevisiae."
Kosodo Y., Imai K., Hirata A., Noda Y., Takatsuki A., Adachi H., Yoda K.
Yeast 18:1003-1014(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[6]"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].
[7]"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].
[8]"A global topology map of the Saccharomyces cerevisiae membrane proteome."
Kim H., Melen K., Oesterberg M., von Heijne G.
Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
Strain: ATCC 208353 / W303-1A.
[9]"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ADR376.
[10]"An unconventional diacylglycerol kinase that regulates phospholipid synthesis and nuclear membrane growth."
Han G.-S., O'Hara L., Carman G.M., Siniossoglou S.
J. Biol. Chem. 283:20433-20442(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TRANSMEMBRANE DOMAINS, OVEREXPRESSION PHENOTYPE, KNOCKOUT, MUTAGENESIS OF ASP-177.
[11]"Characterization of the yeast DGK1-encoded CTP-dependent diacylglycerol kinase."
Han G.-S., O'Hara L., Siniossoglou S., Carman G.M.
J. Biol. Chem. 283:20443-20453(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: SYNTHESIS OF 133-145 AND 188-201, CATALYTIC ACTIVITY, COFACTOR, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF 1-MET--GLY-66; 1-MET--THR-70; 1-MET--LYS-77; ARG-76; LYS-77; ASP-177 AND GLY-184.
[12]"Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44; SER-45 AND SER-46, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X90565 Genomic DNA. Translation: CAA62166.1.
Z75219 Genomic DNA. Translation: CAA99631.1.
BK006948 Genomic DNA. Translation: DAA11076.1.
PIRS58323.
RefSeqNP_014956.3. NM_001183731.3.

3D structure databases

ProteinModelPortalQ12382.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid34699. 223 interactions.
DIPDIP-5021N.
MINTMINT-561696.
STRING4932.YOR311C.

Proteomic databases

PaxDbQ12382.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYOR311C; YOR311C; YOR311C.
GeneID854488.
KEGGsce:YOR311C.

Organism-specific databases

CYGDYOR311c.
SGDS000005838. DGK1.

Phylogenomic databases

eggNOGCOG0170.
HOGENOMHOG000198978.
KOK16368.
OMAHLKSHEW.
OrthoDBEOG7VX96V.

Enzyme and pathway databases

BioCycYEAST:G3O-33794-MONOMER.
SABIO-RKQ12382.

Gene expression databases

GenevestigatorQ12382.

Family and domain databases

InterProIPR000374. PC_trans.
[Graphical view]
PfamPF01148. CTP_transf_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio976813.

Entry information

Entry nameDGK1_YEAST
AccessionPrimary (citable) accession number: Q12382
Secondary accession number(s): D6W310
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XV

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

Yeast

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

SIMILARITY comments

Index of protein domains and families