CTP-dependent diacylglycerol kinase 1 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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Q12382 (DGK1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 81. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length	290 AA.
Sequence status	Complete.
Protein existence	Evidence 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.9
Catalytic activity	CTP + 1,2-diacyl-sn-glycerol = CDP + 1,2-diacyl-sn-glycerol 3-phosphate. Ref.9 Ref.10
Cofactor	Ca²⁺ or Mg²⁺. Ref.10
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.10
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.9.
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: K_M=0.3 mM for CTP Ref.10 K_M=0.4 mM for dCTP V_max=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.

Ontologies

Keywords
Biological process	ER-Golgi transport Transport
Cellular component	Endoplasmic reticulum Golgi apparatus Membrane Nucleus
Domain	Transmembrane Transmembrane helix
Ligand	Calcium Magnesium
Molecular function	Kinase Transferase
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	phosphatidic acid biosynthetic process Inferred from direct assay Ref.10. Source: SGD vesicle-mediated transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	Golgi membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to endoplasmic reticulum membrane Inferred from direct assay Ref.5. Source: SGD nuclear membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	diacylglycerol kinase activity Inferred from direct assay Ref.9 Ref.10. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 290

290

CTP-dependent diacylglycerol kinase 1

PRO_0000240382

Regions

Topological domain

1 – 77

Lumenal Potential

Transmembrane

78 – 95

Helical; Potential

Topological domain

96 – 103

Cytoplasmic Potential

Transmembrane

104 – 124

Helical; Potential

Topological domain

125 – 140

Lumenal Potential

Transmembrane

141 – 161

Helical; Potential

Topological domain

162 – 163

Cytoplasmic Potential

Transmembrane

164 – 184

Helical; Potential

Topological domain

185 – 203

Lumenal Potential

Transmembrane

204 – 224

Helical; Potential

Topological domain

225 – 244

Cytoplasmic Potential

Transmembrane

245 – 265

Helical; Potential

Topological domain

266 – 290

Lumenal Potential

Amino acid modifications

Glycosylation

N-linked (GlcNAc...) Potential

Glycosylation

197

N-linked (GlcNAc...) Potential

Glycosylation

270

N-linked (GlcNAc...) Potential

Experimental info

Mutagenesis

R → A: Loss of kinase activity. Not temperature-sensitive for growth. Regular shaped nuclear membrane structure. Ref.10

Mutagenesis

K → A: Loss of kinase activity. Not temperature-sensitive for growth. Regular shaped nuclear membrane structure. Ref.10

Mutagenesis

177

D → A: No kinase activity. Not temperature-sensitive for growth. Does not trigger nuclear membrane expansion. Ref.9 Ref.10

Mutagenesis

184

G → A: 70% reduction in kinase activity. Not temperature-sensitive for growth. Regular shaped nuclear membrane structure. Ref.10

Sequences

Sequence

Length

Mass (Da)

Tools

Q12382 [UniParc].

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

FASTA

290

32,840

        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' referencesShow '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. Kleine K. Nature 387:98-102(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[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]	"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.
[10]	"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.
+	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.
PIR	S58323.
RefSeq	NP_014956.3. NM_001183731.3.
3D structure databases
ProteinModelPortal	Q12382.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-5021N.
MINT	MINT-561696.
STRING	4932.YOR311C.
Proteomic databases
PaxDb	Q12382.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YOR311C; YOR311C; YOR311C.
GeneID	854488.
KEGG	sce:YOR311C. sce:YOR313C.
Organism-specific databases
CYGD	YOR311c.
SGD	S000005838. DGK1.
Phylogenomic databases
eggNOG	COG0170.
HOGENOM	HOG000198978.
KO	K12772. K16368.
OMA	EWFGDFI.
OrthoDB	EOG4TJ038.
Enzyme and pathway databases
SABIO-RK	Q12382.
Gene expression databases
Genevestigator	Q12382.
GermOnline	YOR311C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR000374. PC_trans. [Graphical view]
Pfam	PF01148. CTP_transf_1. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	976813.

Entry information

Entry name

DGK1_YEAST

Accession

Primary (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 3, 2013
This is version 81 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

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

Yeast chromosome XV

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

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents