DGKZ_MOUSE
ID DGKZ_MOUSE Reviewed; 929 AA.
AC Q80UP3; A2AHJ6;
DT 22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Diacylglycerol kinase zeta {ECO:0000303|PubMed:20023381};
DE Short=DAG kinase zeta;
DE EC=2.7.1.107 {ECO:0000269|PubMed:12883552};
DE AltName: Full=Diglyceride kinase zeta;
DE Short=DGK-zeta;
GN Name=Dgkz {ECO:0000312|MGI:MGI:1278339};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND DISRUPTION PHENOTYPE.
RX PubMed=12883552; DOI=10.1038/ni958;
RA Zhong X.P., Hainey E.A., Olenchock B.A., Jordan M.S., Maltzman J.S.,
RA Nichols K.E., Shen H., Koretzky G.A.;
RT "Enhanced T cell responses due to diacylglycerol kinase zeta deficiency.";
RL Nat. Immunol. 4:882-890(2003).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP SUBCELLULAR LOCATION, AND NUCLEAR EXPORT SIGNAL.
RX PubMed=20023381; DOI=10.4161/cc.9.2.10469;
RA Evangelisti C., Gaboardi G.C., Billi A.M., Ognibene A., Goto K.,
RA Tazzari P.L., McCubrey J.A., Martelli A.M.;
RT "Identification of a functional nuclear export sequence in diacylglycerol
RT kinase-zeta.";
RL Cell Cycle 9:384-388(2010).
RN [6]
RP FUNCTION, INTERACTION WITH IRS1, AND IDENTIFICATION IN A COMPLEX WITH
RP PIP5K1A AND IRS1.
RX PubMed=27739494; DOI=10.1038/srep35438;
RA Liu T., Yu B., Kakino M., Fujimoto H., Ando Y., Hakuno F., Takahashi S.I.;
RT "A novel IRS-1-associated protein, DGKzeta regulates GLUT4 translocation in
RT 3T3-L1 adipocytes.";
RL Sci. Rep. 6:35438-35438(2016).
CC -!- FUNCTION: Diacylglycerol kinase that converts diacylglycerol/DAG into
CC phosphatidic acid/phosphatidate/PA and regulates the respective levels
CC of these two bioactive lipids (PubMed:12883552). Thereby, acts as a
CC central switch between the signaling pathways activated by these second
CC messengers with different cellular targets and opposite effects in
CC numerous biological processes (PubMed:12883552). Also plays an
CC important role in the biosynthesis of complex lipids (Probable). Does
CC not exhibit an acyl chain-dependent substrate specificity among
CC diacylglycerol species. Can also phosphorylate 1-alkyl-2-acylglycerol
CC in vitro but less efficiently and with a preference for
CC alkylacylglycerols containing an arachidonoyl group (By similarity).
CC The biological processes it is involved in include T cell activation
CC since it negatively regulates T-cell receptor signaling which is in
CC part mediated by diacylglycerol (PubMed:12883552). By generating
CC phosphatidic acid, stimulates PIP5KIA activity which regulates actin
CC polymerization (By similarity). Through the same mechanism could also
CC positively regulate insulin-induced translocation of SLC2A4 to the cell
CC membrane (PubMed:27739494). Regulates RASGRP1 activity (By similarity).
CC {ECO:0000250|UniProtKB:Q13574, ECO:0000269|PubMed:12883552,
CC ECO:0000269|PubMed:27739494, ECO:0000305|PubMed:12883552}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycerol + ATP = a 1,2-diacyl-sn-glycero-3-
CC phosphate + ADP + H(+); Xref=Rhea:RHEA:10272, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17815, ChEBI:CHEBI:30616, ChEBI:CHEBI:58608,
CC ChEBI:CHEBI:456216; EC=2.7.1.107;
CC Evidence={ECO:0000269|PubMed:12883552};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10273;
CC Evidence={ECO:0000269|PubMed:12883552};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-didecanoyl-sn-glycerol + ATP = 1,2-didecanoyl-sn-glycero-
CC 3-phosphate + ADP + H(+); Xref=Rhea:RHEA:43428, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:18155, ChEBI:CHEBI:30616, ChEBI:CHEBI:78227,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q13574};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43429;
CC Evidence={ECO:0000250|UniProtKB:Q13574};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-ditetradecanoyl-sn-glycerol + ATP = 1,2-ditetradecanoyl-
CC sn-glycero-3-phosphate + ADP + H(+); Xref=Rhea:RHEA:43444,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:80651,
CC ChEBI:CHEBI:83550, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:Q13574};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43445;
CC Evidence={ECO:0000250|UniProtKB:Q13574};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycerol + ATP = 1-
CC hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + ADP + H(+);
CC Xref=Rhea:RHEA:43416, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:64839, ChEBI:CHEBI:75466, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:Q13574};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43417;
CC Evidence={ECO:0000250|UniProtKB:Q13574};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycerol
CC + ATP = 1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC 3-phosphate + ADP + H(+); Xref=Rhea:RHEA:40335, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:72864, ChEBI:CHEBI:77096,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q13574};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40336;
CC Evidence={ECO:0000250|UniProtKB:Q13574};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-2-(9Z-octadecenoyl)-sn-glycerol + ATP = 1-
CC octadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + ADP + H(+);
CC Xref=Rhea:RHEA:43424, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:74560, ChEBI:CHEBI:75468, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:Q13574};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43425;
CC Evidence={ECO:0000250|UniProtKB:Q13574};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycerol
CC + ATP = 1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC 3-phosphate + ADP + H(+); Xref=Rhea:RHEA:40323, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:75728, ChEBI:CHEBI:77091,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q13574};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40324;
CC Evidence={ECO:0000250|UniProtKB:Q13574};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-
CC glycerol + ATP = 1-octadecanoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z-
CC docosahexaenoyl)-sn-glycero-3-phosphate + ADP + H(+);
CC Xref=Rhea:RHEA:40359, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:77129, ChEBI:CHEBI:77130, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:Q13574};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40360;
CC Evidence={ECO:0000250|UniProtKB:Q13574};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycerol + ATP = 1,2-di-(9Z-
CC octadecenoyl)-sn-glycero-3-phosphate + ADP + H(+);
CC Xref=Rhea:RHEA:40327, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:52333, ChEBI:CHEBI:74546, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:Q13574};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40328;
CC Evidence={ECO:0000250|UniProtKB:Q13574};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-2-hexadecanoyl-sn-glycerol + ATP = 1-(9Z)-
CC octadecenoyl-2-hexadecanoyl-sn-glycero-3-phosphate + ADP + H(+);
CC Xref=Rhea:RHEA:43420, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:74551, ChEBI:CHEBI:75447, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:Q13574};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43421;
CC Evidence={ECO:0000250|UniProtKB:Q13574};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-eicosanoyl-2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycerol +
CC ATP = 1-eicosanoyl-2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-
CC phosphate + ADP + H(+); Xref=Rhea:RHEA:40331, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:77093, ChEBI:CHEBI:77094,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q13574};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40332;
CC Evidence={ECO:0000250|UniProtKB:Q13574};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycerol + ATP =
CC 1,2-di-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphate + ADP
CC + H(+); Xref=Rhea:RHEA:40351, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:77125, ChEBI:CHEBI:77126, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:Q13574};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40352;
CC Evidence={ECO:0000250|UniProtKB:Q13574};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-alkyl-2-acyl-sn-glycerol + ATP = 1-O-alkyl-2-acyl-sn-
CC glycero-3-phosphate + ADP + H(+); Xref=Rhea:RHEA:44072,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:52595,
CC ChEBI:CHEBI:73332, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:Q13574};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44073;
CC Evidence={ECO:0000250|UniProtKB:Q13574};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-hexadecyl-2-acetyl-sn-glycerol + ATP = 1-O-hexadecyl-2-
CC acetyl-sn-glycero-3-phosphate + ADP + H(+); Xref=Rhea:RHEA:41676,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:75936,
CC ChEBI:CHEBI:78385, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:Q13574};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41677;
CC Evidence={ECO:0000250|UniProtKB:Q13574};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-hexadecyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycerol +
CC ATP = 1-O-hexadecyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-
CC phosphate + ADP + H(+); Xref=Rhea:RHEA:40403, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:77184, ChEBI:CHEBI:77186,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q13574};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40404;
CC Evidence={ECO:0000250|UniProtKB:Q13574};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-hexadecyl-2-(9Z-octadecenoyl)-sn-glycerol + ATP = 1-O-
CC hexadecyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + ADP + H(+);
CC Xref=Rhea:RHEA:40407, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:77185, ChEBI:CHEBI:77187, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:Q13574};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40408;
CC Evidence={ECO:0000250|UniProtKB:Q13574};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-hexadecyl-sn-glycerol + ATP = 1-O-hexadecyl-sn-glycero-3-
CC phosphate + ADP + H(+); Xref=Rhea:RHEA:41672, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:34115, ChEBI:CHEBI:77580,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q13574};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41673;
CC Evidence={ECO:0000250|UniProtKB:Q13574};
CC -!- PATHWAY: Lipid metabolism; glycerolipid metabolism.
CC {ECO:0000305|PubMed:12883552}.
CC -!- SUBUNIT: Interacts (via PDZ-binding motif) with the PDZ domain of the
CC syntrophin SNTG1 and that of SNX27 (By similarity). Interacts with IRS1
CC in the absence of insulin; insulin stimulation decreases this
CC interaction (PubMed:27739494). Found in a ternary complex with IRS1 and
CC PIP5K1A in the absence of insulin (PubMed:27739494). Interacts with
CC PIP5K1A (By similarity). Forms a signaling complex with RASGRP1 and
CC HRAS (By similarity). {ECO:0000250|UniProtKB:Q13574,
CC ECO:0000269|PubMed:27739494}.
CC -!- INTERACTION:
CC Q80UP3; P13405: Rb1; NbExp=2; IntAct=EBI-971774, EBI-971782;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20023381}. Cytoplasm,
CC cytosol {ECO:0000305|PubMed:20023381}. Cell membrane
CC {ECO:0000250|UniProtKB:Q13574}. Cell projection, lamellipodium
CC {ECO:0000250|UniProtKB:Q13574}.
CC -!- DOMAIN: The PDZ-binding motif mediates interaction with PDZ domain-
CC containing proteins like SNTG1 and SNX27.
CC {ECO:0000250|UniProtKB:Q13574}.
CC -!- DISRUPTION PHENOTYPE: Homozygous knockout mice are viable, fertile and
CC do not display overt phenotype (PubMed:12883552). Slight perturbations
CC of the cellular composition of secondary lymphoid organs with a slight
CC decrease of mature T cells is observed (PubMed:12883552). Upon TCR
CC activation the normal conversion of diacylglycerol into phosphatidic
CC acid that negatively regulates TCR signaling is partially impaired
CC (PubMed:12883552). Hyper proliferation of T-cells and the ability to
CC mount a more vigorous and effective T-cell response against pathogens
CC indicate a more profound T-cell activation in these mice
CC (PubMed:12883552). {ECO:0000269|PubMed:12883552}.
CC -!- SIMILARITY: Belongs to the eukaryotic diacylglycerol kinase family.
CC {ECO:0000305}.
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DR EMBL; AL731772; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL732484; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC049228; AAH49228.1; -; mRNA.
DR CCDS; CCDS16441.1; -.
DR RefSeq; NP_612179.2; NM_138306.2.
DR AlphaFoldDB; Q80UP3; -.
DR SMR; Q80UP3; -.
DR BioGRID; 222626; 10.
DR IntAct; Q80UP3; 2.
DR STRING; 10090.ENSMUSP00000106934; -.
DR iPTMnet; Q80UP3; -.
DR PhosphoSitePlus; Q80UP3; -.
DR EPD; Q80UP3; -.
DR MaxQB; Q80UP3; -.
DR PaxDb; Q80UP3; -.
DR PRIDE; Q80UP3; -.
DR ProteomicsDB; 279643; -.
DR Antibodypedia; 26268; 250 antibodies from 31 providers.
DR DNASU; 104418; -.
DR Ensembl; ENSMUST00000028667; ENSMUSP00000028667; ENSMUSG00000040479.
DR GeneID; 104418; -.
DR KEGG; mmu:104418; -.
DR UCSC; uc008kxc.2; mouse.
DR CTD; 8525; -.
DR MGI; MGI:1278339; Dgkz.
DR VEuPathDB; HostDB:ENSMUSG00000040479; -.
DR eggNOG; KOG0782; Eukaryota.
DR GeneTree; ENSGT00940000156152; -.
DR HOGENOM; CLU_003770_4_0_1; -.
DR InParanoid; Q80UP3; -.
DR OMA; GEPCKLT; -.
DR OrthoDB; 274339at2759; -.
DR BRENDA; 2.7.1.107; 3474.
DR Reactome; R-MMU-114508; Effects of PIP2 hydrolysis.
DR UniPathway; UPA00230; -.
DR BioGRID-ORCS; 104418; 3 hits in 75 CRISPR screens.
DR ChiTaRS; Dgkz; mouse.
DR PRO; PR:Q80UP3; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q80UP3; protein.
DR Bgee; ENSMUSG00000040479; Expressed in cerebellum lobe and 262 other tissues.
DR ExpressionAtlas; Q80UP3; baseline and differential.
DR Genevisible; Q80UP3; MM.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0030027; C:lamellipodium; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0014069; C:postsynaptic density; ISO:MGI.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IDA:SynGO.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004143; F:diacylglycerol kinase activity; IMP:UniProtKB.
DR GO; GO:0004857; F:enzyme inhibitor activity; IDA:MGI.
DR GO; GO:0016301; F:kinase activity; ISO:MGI.
DR GO; GO:0001727; F:lipid kinase activity; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003951; F:NAD+ kinase activity; IEA:InterPro.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
DR GO; GO:0046339; P:diacylglycerol metabolic process; IMP:UniProtKB.
DR GO; GO:0046486; P:glycerolipid metabolic process; ISO:MGI.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0046834; P:lipid phosphorylation; IMP:UniProtKB.
DR GO; GO:0099562; P:maintenance of postsynaptic density structure; IDA:SynGO.
DR GO; GO:0031571; P:mitotic G1 DNA damage checkpoint signaling; ISO:MGI.
DR GO; GO:0045930; P:negative regulation of mitotic cell cycle; ISO:MGI.
DR GO; GO:0046580; P:negative regulation of Ras protein signal transduction; IMP:MGI.
DR GO; GO:0050860; P:negative regulation of T cell receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; IMP:UniProtKB.
DR GO; GO:0090216; P:positive regulation of 1-phosphatidylinositol-4-phosphate 5-kinase activity; IMP:UniProtKB.
DR GO; GO:0007205; P:protein kinase C-activating G protein-coupled receptor signaling pathway; IEA:InterPro.
DR GO; GO:0007265; P:Ras protein signal transduction; IMP:MGI.
DR GO; GO:0051966; P:regulation of synaptic transmission, glutamatergic; IBA:GO_Central.
DR CDD; cd00029; C1; 1.
DR Gene3D; 1.25.40.20; -; 1.
DR Gene3D; 3.40.50.10330; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR017438; ATP-NAD_kinase_N.
DR InterPro; IPR037607; DGK.
DR InterPro; IPR000756; Diacylglycerol_kin_accessory.
DR InterPro; IPR001206; Diacylglycerol_kinase_cat_dom.
DR InterPro; IPR016064; NAD/diacylglycerol_kinase_sf.
DR InterPro; IPR002219; PE/DAG-bd.
DR PANTHER; PTHR11255; PTHR11255; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF00609; DAGK_acc; 1.
DR Pfam; PF00781; DAGK_cat; 1.
DR SMART; SM00248; ANK; 2.
DR SMART; SM00109; C1; 2.
DR SMART; SM00045; DAGKa; 1.
DR SMART; SM00046; DAGKc; 1.
DR SUPFAM; SSF111331; SSF111331; 1.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 2.
DR PROSITE; PS50146; DAGK; 1.
PE 1: Evidence at protein level;
KW ANK repeat; ATP-binding; Cell membrane; Cell projection; Cytoplasm; Kinase;
KW Lipid metabolism; Membrane; Metal-binding; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..929
FT /note="Diacylglycerol kinase zeta"
FT /id="PRO_0000218469"
FT DOMAIN 292..426
FT /note="DAGKc"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT REPEAT 823..853
FT /note="ANK 1"
FT /evidence="ECO:0000255"
FT REPEAT 858..887
FT /note="ANK 2"
FT /evidence="ECO:0000255"
FT ZN_FING 98..153
FT /note="Phorbol-ester/DAG-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT ZN_FING 173..231
FT /note="Phorbol-ester/DAG-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 59..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 257..281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 279..417
FT /note="Mediates interaction with RASGRP1"
FT /evidence="ECO:0000250|UniProtKB:Q13574"
FT REGION 421..441
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 760..785
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 362..370
FT /note="Nuclear export signal"
FT /evidence="ECO:0000269|PubMed:20023381"
FT MOTIF 925..929
FT /note="PDZ-binding"
FT /evidence="ECO:0000250|UniProtKB:Q13574"
FT COMPBIAS 12..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 706
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13574"
FT MOD_RES 782
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13574"
FT CONFLICT 908
FT /note="A -> S (in Ref. 2; AAH49228)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 929 AA; 104031 MW; AC3E48790E3C3463 CRC64;
MEPRDPSPEG RSSDSESASA SSSGSERDAG PEPDKAPRRL TKRRFPGLRL FGHRKAITKS
GLQHLAPPPP TPGAPCGESE EQIQSTVDWS ESAVYGEHIW FETNVSGDFC YVGEQHCVAK
MLPKSAPRKK CAACKIVVHT QCIKQLEKIN FRCKPSFRES GSRNVREPTF VRHHWVHRRR
QDGKCRHCGK GFQQKFTFHS KEIVAISCSW CKQAYHSKVS CFMMQQIEEP CSLGVHAAVV
IPPTWILRAR RPQNTLKASK KKKRASFKRR SSKKGPEEGR WRPFIIRPTP SPLMKPLLVF
VNPKSGGNQG AKIIQSFLWY LNPRQVFDLS QGGPREALEM YRKVHNLRIL ACGGDGTVGW
ILSTLDQLRL KPPPPVAILP LGTGNDLART LNWGGGYTDE PVSKILSHVE EGNVVQLDRW
DLRAEPNPEA GPEERDDGAT DRLPLDVFNN YFSLGFDAHV TLEFHESREA NPEKFNSRFR
NKMFYAGTAF SDFLMGSSKD LAKHIRVVCD GMDLTPKIQD LKPQCIVFLN IPRYCAGTMP
WGHPGEHHDF EPQRHDDGYL EVIGFTMTSL AALQVGGHGE RLTQCREVLL TTAKAIPVQV
DGEPCKLSAS RIRIALRNQA TMVQKAKRRS TAPLHSDQQP VPEQLRIQVS RVSMHDYEAL
HYDKEQLKEA SVPLGTVVVP GDSDLELCRA HIERLQREPD GAGAKSPMCH QLSSKWCFLD
ATTASRFYRI DRAQEHLNYV TEIAQDEIYI LDPELLGASA RPDLPTPTSP LPASPCSPTP
GSMQGDTALP QGEELIEAAK RNDCCKLQEL HRAGGDLMHR DQKSRTLLHH AVSTGSKEVV
RYLLDHAPPE ILDAVEENGE TCLHQAAALG QRTICHYIVE AGASLMKTDL QGDTPRQRAE
KAQDTELAAY LENRQHYQMI QREDQETAV
