ID DGKQ_HUMAN Reviewed; 942 AA. AC P52824; Q6P3W4; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-SEP-2009, sequence version 2. DT 27-MAR-2024, entry version 183. DE RecName: Full=Diacylglycerol kinase theta {ECO:0000305}; DE Short=DAG kinase theta; DE Short=DGKtheta {ECO:0000303|PubMed:9099683}; DE EC=2.7.1.107 {ECO:0000269|PubMed:10066731, ECO:0000269|PubMed:11309392, ECO:0000269|PubMed:15164764, ECO:0000269|PubMed:22627129, ECO:0000269|PubMed:23949095, ECO:0000269|PubMed:9099683}; DE EC=2.7.1.93 {ECO:0000269|PubMed:22627129}; DE AltName: Full=Diglyceride kinase theta; DE Short=DGK-theta {ECO:0000303|PubMed:11309392}; GN Name=DGKQ {ECO:0000312|HGNC:HGNC:2856}; GN Synonyms=DAGK4 {ECO:0000303|PubMed:7607687}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=7607687; DOI=10.1016/0888-7543(95)80182-l; RA Pilz A., Schaap D., Hunt D., Fitzgibbon J.; RT "Chromosomal localization of three mouse diacylglycerol kinase (DAGK) RT genes: genes sharing sequence homology to the Drosophila retinal RT degeneration A (rdgA) gene."; RL Genomics 26:599-601(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT LEU-27. RC TISSUE=Uterus; 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 [4] RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY. RX PubMed=9099683; DOI=10.1074/jbc.272.16.10422; RA Houssa B., Schaap D., van der Wal J., Goto K., Kondo H., Yamakawa A., RA Shibata M., Takenawa T., van Blitterswijk W.J.; RT "Cloning of a novel human diacylglycerol kinase (DGKtheta) containing three RT cysteine-rich domains, a proline-rich region, and a pleckstrin homology RT domain with an overlapping Ras-associating domain."; RL J. Biol. Chem. 272:10422-10428(1997). RN [5] RP CATALYTIC ACTIVITY, INTERACTION WITH RHOA, AND SUBCELLULAR LOCATION. RX PubMed=10066731; DOI=10.1074/jbc.274.11.6820; RA Houssa B., de Widt J., Kranenburg O., Moolenaar W.H., RA van Blitterswijk W.J.; RT "Diacylglycerol kinase theta binds to and is negatively regulated by active RT RhoA."; RL J. Biol. Chem. 274:6820-6822(1999). RN [6] RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, INTERACTION WITH RHOA, RP AND SUBCELLULAR LOCATION. RX PubMed=11309392; DOI=10.1074/jbc.m101501200; RA Bregoli L., Baldassare J.J., Raben D.M.; RT "Nuclear diacylglycerol kinase-theta is activated in response to alpha- RT thrombin."; RL J. Biol. Chem. 276:23288-23295(2001). RN [7] RP SUBCELLULAR LOCATION, AND INTERACTION WITH PLCB1. RX PubMed=12799190; DOI=10.1016/s0014-4827(03)00115-0; RA Tabellini G., Bortul R., Santi S., Riccio M., Baldini G., Cappellini A., RA Billi A.M., Berezney R., Ruggeri A., Cocco L., Martelli A.M.; RT "Diacylglycerol kinase-theta is localized in the speckle domains of the RT nucleus."; RL Exp. Cell Res. 287:143-154(2003). RN [8] RP CATALYTIC ACTIVITY, INTERACTION WITH RHOA, AND MUTAGENESIS OF GLY-237; RP SER-241; LEU-242; PRO-245; PRO-246 AND GLY-648. RX PubMed=15164764; DOI=10.1016/j.bbalip.2003.11.008; RA Los A.P., van Baal J., de Widt J., Divecha N., van Blitterswijk W.J.; RT "Structure-activity relationship of diacylglycerol kinase theta."; RL Biochim. Biophys. Acta 1636:169-174(2004). RN [9] RP INTERACTION WITH PRKCE AND PRKCH, SUBCELLULAR LOCATION, PHOSPHORYLATION, RP AND MUTAGENESIS OF CYS-100; CYS-160; CYS-226 AND GLY-237. RX PubMed=15632189; DOI=10.1074/jbc.m409301200; RA van Baal J., de Widt J., Divecha N., van Blitterswijk W.J.; RT "Translocation of diacylglycerol kinase theta from cytosol to plasma RT membrane in response to activation of G protein-coupled receptors and RT protein kinase C."; RL J. Biol. Chem. 280:9870-9878(2005). RN [10] RP FUNCTION, INTERACTION WITH NR5A1, MOTIF, AND DOMAIN. RX PubMed=17664281; DOI=10.1128/mcb.00355-07; RA Li D., Urs A.N., Allegood J., Leon A., Merrill A.H. Jr., Sewer M.B.; RT "Cyclic AMP-stimulated interaction between steroidogenic factor 1 and RT diacylglycerol kinase theta facilitates induction of CYP17."; RL Mol. Cell. Biol. 27:6669-6685(2007). RN [11] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=22627129; DOI=10.1016/j.bbrc.2012.05.077; RA Gellett A.M., Kharel Y., Sunkara M., Morris A.J., Lynch K.R.; RT "Biosynthesis of alkyl lysophosphatidic acid by diacylglycerol kinases."; RL Biochem. Biophys. Res. Commun. 422:758-763(2012). RN [12] RP CATALYTIC ACTIVITY. RX PubMed=23949095; DOI=10.1159/000351849; RA Sato M., Liu K., Sasaki S., Kunii N., Sakai H., Mizuno H., Saga H., RA Sakane F.; RT "Evaluations of the selectivities of the diacylglycerol kinase inhibitors RT R59022 and R59949 among diacylglycerol kinase isozymes using a new non- RT radioactive assay method."; RL Pharmacology 92:99-107(2013). RN [13] RP FUNCTION, AND MUTAGENESIS OF GLY-648. RX PubMed=26748701; DOI=10.1016/j.celrep.2015.12.022; RA Goldschmidt H.L., Tu-Sekine B., Volk L., Anggono V., Huganir R.L., RA Raben D.M.; RT "DGKtheta Catalytic Activity Is Required for Efficient Recycling of RT Presynaptic Vesicles at Excitatory Synapses."; RL Cell Rep. 14:200-207(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:9099683, PubMed:11309392, CC PubMed:22627129). Thereby, acts as a central switch between the CC signaling pathways activated by these second messengers with different CC cellular targets and opposite effects in numerous biological processes CC (PubMed:11309392, PubMed:17664281, PubMed:26748701). Within the CC adrenocorticotropic hormone signaling pathway, produces phosphatidic CC acid which in turn activates NR5A1 and subsequent steroidogenic gene CC transcription (PubMed:17664281). Also functions downstream of the nerve CC growth factor signaling pathway being specifically activated in the CC nucleus by the growth factor (By similarity). Through its CC diacylglycerol activity also regulates synaptic vesicle endocytosis CC (PubMed:26748701). {ECO:0000250|UniProtKB:D3ZEY4, CC ECO:0000269|PubMed:11309392, ECO:0000269|PubMed:17664281, CC ECO:0000269|PubMed:22627129, ECO:0000269|PubMed:26748701, CC ECO:0000269|PubMed:9099683}. 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:10066731, ECO:0000269|PubMed:11309392, CC ECO:0000269|PubMed:15164764, ECO:0000269|PubMed:22627129, CC ECO:0000269|PubMed:23949095, ECO:0000269|PubMed:9099683}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10273; CC Evidence={ECO:0000305|PubMed:9099683}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-O-alkyl-sn-glycerol + ATP = 1-O-alkyl-sn-glycero-3-phosphate CC + ADP + H(+); Xref=Rhea:RHEA:16937, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:15850, ChEBI:CHEBI:30616, ChEBI:CHEBI:58014, CC ChEBI:CHEBI:456216; EC=2.7.1.93; CC Evidence={ECO:0000269|PubMed:22627129}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16938; CC Evidence={ECO:0000305|PubMed:22627129}; 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:0000269|PubMed:22627129}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44073; CC Evidence={ECO:0000305|PubMed:22627129}; 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:0000269|PubMed:11309392, ECO:0000269|PubMed:15164764, CC ECO:0000269|PubMed:22627129, ECO:0000269|PubMed:23949095, CC ECO:0000269|PubMed:9099683}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40328; CC Evidence={ECO:0000305|PubMed:9099683}; 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:0000269|PubMed:22627129}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41673; CC Evidence={ECO:0000305|PubMed:22627129}; 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:0000269|PubMed:22627129}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41677; CC Evidence={ECO:0000305|PubMed:22627129}; 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:0000269|PubMed:9099683}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40324; CC Evidence={ECO:0000305|PubMed:9099683}; CC -!- ACTIVITY REGULATION: Activated by phosphatidylserine. CC {ECO:0000269|PubMed:11309392}. CC -!- PATHWAY: Lipid metabolism; glycerolipid metabolism. CC {ECO:0000305|PubMed:9099683}. CC -!- SUBUNIT: Interacts with RHOA (constitutively activated, GTP-bound); the CC interaction inhibits DGKQ (PubMed:11309392, PubMed:15164764). Interacts CC with PRKCE (PubMed:15632189). Interacts with PRKCH (PubMed:15632189). CC Interacts with PLCB1 (PubMed:12799190). Interacts with NR5A1; the CC interaction requires both LXXLL motifs in DGKQ and is required for full CC phosphatidic acid-mediated activation of NR5A1 (PubMed:17664281). CC {ECO:0000269|PubMed:11309392, ECO:0000269|PubMed:12799190, CC ECO:0000269|PubMed:15164764, ECO:0000269|PubMed:15632189, CC ECO:0000269|PubMed:17664281}. CC -!- INTERACTION: CC P52824; P0DPK4: NOTCH2NLC; NbExp=3; IntAct=EBI-4401238, EBI-22310682; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15632189}. CC Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q6P5E8}. Cell membrane CC {ECO:0000269|PubMed:10066731, ECO:0000269|PubMed:15632189}. Synapse CC {ECO:0000250|UniProtKB:Q6P5E8}. Cytoplasm, cytoskeleton CC {ECO:0000269|PubMed:10066731}. Nucleus {ECO:0000269|PubMed:12799190}. CC Nucleus speckle {ECO:0000269|PubMed:12799190}. Nucleus matrix CC {ECO:0000250|UniProtKB:D3ZEY4}. Note=Translocates to the plasma CC membrane in response to steroid hormone receptor stimulation CC (PubMed:15632189). Translocation to the plasma membrane is dependent on CC G-protein coupled receptor stimulation and subsequent activation of CC PRKCE and probably PRKCH (PubMed:15632189). Translocates to the nucleus CC in response to thrombin stimulation (Probable). Association with the CC nuclear matrix is regulated by nerve growth factor (By similarity). CC {ECO:0000250|UniProtKB:D3ZEY4, ECO:0000269|PubMed:15632189, CC ECO:0000305|PubMed:11309392}. CC -!- DOMAIN: The L-X-X-L-L repeats are both required for binding and CC phosphatidic acid-mediated activation of the nuclear receptor NR5A1. CC {ECO:0000269|PubMed:17664281}. CC -!- PTM: Phosphorylated by PRKCE and PRKCH in vitro. CC {ECO:0000269|PubMed:15632189}. CC -!- SIMILARITY: Belongs to the eukaryotic diacylglycerol kinase family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; L38707; AAA98749.1; -; mRNA. DR EMBL; AC019103; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC063801; AAH63801.1; -; mRNA. DR CCDS; CCDS3342.1; -. DR RefSeq; NP_001338.2; NM_001347.3. DR AlphaFoldDB; P52824; -. DR SMR; P52824; -. DR BioGRID; 107979; 20. DR IntAct; P52824; 3. DR STRING; 9606.ENSP00000273814; -. DR DrugBank; DB14001; alpha-Tocopherol succinate. DR SwissLipids; SLP:000000740; -. DR GlyGen; P52824; 3 sites, 1 O-linked glycan (3 sites). DR iPTMnet; P52824; -. DR PhosphoSitePlus; P52824; -. DR BioMuta; DGKQ; -. DR DMDM; 257051005; -. DR EPD; P52824; -. DR jPOST; P52824; -. DR MassIVE; P52824; -. DR MaxQB; P52824; -. DR PaxDb; 9606-ENSP00000273814; -. DR PeptideAtlas; P52824; -. DR ProteomicsDB; 56542; -. DR Antibodypedia; 22185; 241 antibodies from 31 providers. DR DNASU; 1609; -. DR Ensembl; ENST00000273814.8; ENSP00000273814.3; ENSG00000145214.14. DR GeneID; 1609; -. DR KEGG; hsa:1609; -. DR MANE-Select; ENST00000273814.8; ENSP00000273814.3; NM_001347.4; NP_001338.2. DR UCSC; uc003gbw.5; human. DR AGR; HGNC:2856; -. DR CTD; 1609; -. DR DisGeNET; 1609; -. DR GeneCards; DGKQ; -. DR HGNC; HGNC:2856; DGKQ. DR HPA; ENSG00000145214; Low tissue specificity. DR MIM; 601207; gene. DR neXtProt; NX_P52824; -. DR OpenTargets; ENSG00000145214; -. DR PharmGKB; PA27317; -. DR VEuPathDB; HostDB:ENSG00000145214; -. DR eggNOG; KOG1169; Eukaryota. DR GeneTree; ENSGT00940000159492; -. DR InParanoid; P52824; -. DR OMA; GFHHARE; -. DR OrthoDB; 4642163at2759; -. DR PhylomeDB; P52824; -. DR TreeFam; TF312817; -. DR BRENDA; 2.7.1.107; 2681. DR PathwayCommons; P52824; -. DR Reactome; R-HSA-114508; Effects of PIP2 hydrolysis. DR SignaLink; P52824; -. DR UniPathway; UPA00230; -. DR BioGRID-ORCS; 1609; 15 hits in 1161 CRISPR screens. DR GeneWiki; DGKQ; -. DR GenomeRNAi; 1609; -. DR Pharos; P52824; Tbio. DR PRO; PR:P52824; -. DR Proteomes; UP000005640; Chromosome 4. DR RNAct; P52824; Protein. DR Bgee; ENSG00000145214; Expressed in ileal mucosa and 163 other cell types or tissues. DR ExpressionAtlas; P52824; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005856; C:cytoskeleton; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:UniProtKB. DR GO; GO:0005768; C:endosome; IDA:ParkinsonsUK-UCL. DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl. DR GO; GO:0016363; C:nuclear matrix; ISS:ParkinsonsUK-UCL. DR GO; GO:0016607; C:nuclear speck; IDA:UniProtKB. DR GO; GO:0005730; C:nucleolus; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0098794; C:postsynapse; IEA:Ensembl. DR GO; GO:0098793; C:presynapse; IEA:Ensembl. DR GO; GO:0012506; C:vesicle membrane; IDA:ParkinsonsUK-UCL. DR GO; GO:0047649; F:alkylglycerol kinase activity; IEA:RHEA. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004143; F:ATP-dependent diacylglycerol kinase activity; IDA:UniProtKB. DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:UniProtKB. DR GO; GO:0019900; F:kinase binding; IPI:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0043274; F:phospholipase binding; IPI:UniProtKB. DR GO; GO:0030297; F:transmembrane receptor protein tyrosine kinase activator activity; IGI:ParkinsonsUK-UCL. DR GO; GO:0019933; P:cAMP-mediated signaling; IDA:UniProtKB. DR GO; GO:0046339; P:diacylglycerol metabolic process; IDA:UniProtKB. DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IMP:UniProtKB. DR GO; GO:0046486; P:glycerolipid metabolic process; IDA:BHF-UCL. DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central. DR GO; GO:0046834; P:lipid phosphorylation; IDA:UniProtKB. DR GO; GO:0010629; P:negative regulation of gene expression; IMP:ParkinsonsUK-UCL. DR GO; GO:0010801; P:negative regulation of peptidyl-threonine phosphorylation; IDA:ParkinsonsUK-UCL. DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IMP:ParkinsonsUK-UCL. DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; IDA:UniProtKB. DR GO; GO:0030168; P:platelet activation; TAS:Reactome. DR GO; GO:0010628; P:positive regulation of gene expression; IMP:ParkinsonsUK-UCL. DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IDA:ParkinsonsUK-UCL. DR GO; GO:0070528; P:protein kinase C signaling; IDA:UniProtKB. DR GO; GO:0007205; P:protein kinase C-activating G protein-coupled receptor signaling pathway; IEA:InterPro. DR GO; GO:0090181; P:regulation of cholesterol metabolic process; IMP:ParkinsonsUK-UCL. DR GO; GO:2000064; P:regulation of cortisol biosynthetic process; IMP:ParkinsonsUK-UCL. DR GO; GO:0008277; P:regulation of G protein-coupled receptor signaling pathway; IDA:ParkinsonsUK-UCL. DR GO; GO:0006111; P:regulation of gluconeogenesis; IMP:ParkinsonsUK-UCL. DR GO; GO:2000182; P:regulation of progesterone biosynthetic process; IMP:ParkinsonsUK-UCL. DR GO; GO:1900242; P:regulation of synaptic vesicle endocytosis; IEA:Ensembl. DR GO; GO:1903432; P:regulation of TORC1 signaling; IMP:ParkinsonsUK-UCL. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:UniProtKB. DR GO; GO:0033198; P:response to ATP; IDA:UniProtKB. DR GO; GO:0051591; P:response to cAMP; IDA:ParkinsonsUK-UCL. DR GO; GO:0070493; P:thrombin-activated receptor signaling pathway; IDA:UniProtKB. DR CDD; cd20803; C1_DGKtheta_typeV_rpt1; 1. DR CDD; cd20804; C1_DGKtheta_typeV_rpt2; 1. DR CDD; cd20854; C1_DGKtheta_typeV_rpt3; 1. DR CDD; cd17111; RA1_DAGK-theta; 1. DR CDD; cd01783; RA2_DAGK-theta; 1. DR Gene3D; 2.60.200.40; -; 1. DR Gene3D; 3.30.60.20; -; 2. DR InterPro; IPR017438; ATP-NAD_kinase_N. DR InterPro; IPR046349; C1-like_sf. 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 InterPro; IPR000159; RA_dom. DR InterPro; IPR029071; Ubiquitin-like_domsf. DR PANTHER; PTHR11255; DIACYLGLYCEROL KINASE; 1. DR PANTHER; PTHR11255:SF54; DIACYLGLYCEROL KINASE THETA; 1. DR Pfam; PF00130; C1_1; 2. DR Pfam; PF00609; DAGK_acc; 1. DR Pfam; PF00781; DAGK_cat; 1. DR Pfam; PF00788; RA; 2. DR SMART; SM00109; C1; 3. DR SMART; SM00045; DAGKa; 1. DR SMART; SM00046; DAGKc; 1. DR SMART; SM00314; RA; 1. DR SUPFAM; SSF57889; Cysteine-rich domain; 3. DR SUPFAM; SSF111331; NAD kinase/diacylglycerol kinase-like; 1. DR SUPFAM; SSF54236; Ubiquitin-like; 1. DR PROSITE; PS50146; DAGK; 1. DR PROSITE; PS50200; RA; 1. DR PROSITE; PS00479; ZF_DAG_PE_1; 3. DR PROSITE; PS50081; ZF_DAG_PE_2; 3. DR Genevisible; P52824; HS. PE 1: Evidence at protein level; KW ATP-binding; Cell membrane; Cytoplasm; Cytoskeleton; Kinase; KW Lipid metabolism; Membrane; Metal-binding; Nucleotide-binding; Nucleus; KW Phosphoprotein; Reference proteome; Repeat; Synapse; Transferase; Zinc; KW Zinc-finger. FT CHAIN 1..942 FT /note="Diacylglycerol kinase theta" FT /id="PRO_0000218467" FT DOMAIN 395..494 FT /note="Ras-associating" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00166" FT DOMAIN 584..721 FT /note="DAGKc" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00783" FT ZN_FING 60..108 FT /note="Phorbol-ester/DAG-type 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226" FT ZN_FING 121..168 FT /note="Phorbol-ester/DAG-type 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226" FT ZN_FING 183..234 FT /note="Phorbol-ester/DAG-type 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226" FT REGION 1..59 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 269..295 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 908..942 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 555..559 FT /note="LXXLL motif 1" FT /evidence="ECO:0000305|PubMed:17664281" FT MOTIF 574..578 FT /note="LXXLL motif 2" FT /evidence="ECO:0000305|PubMed:17664281" FT COMPBIAS 922..942 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 22 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q6P5E8" FT MOD_RES 26 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q6P5E8" FT VARIANT 27 FT /note="P -> L (in dbSNP:rs17855876)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_058478" FT MUTAGEN 100 FT /note="C->G: Abolishes translocation to the plasma FT membrane." FT /evidence="ECO:0000269|PubMed:15632189" FT MUTAGEN 160 FT /note="C->G: Abolishes translocation to the plasma FT membrane." FT /evidence="ECO:0000269|PubMed:15632189" FT MUTAGEN 226 FT /note="C->G: Abolishes translocation to the plasma FT membrane." FT /evidence="ECO:0000269|PubMed:15632189" FT MUTAGEN 237 FT /note="G->R: Loss of diacylglycerol kinase activity. No FT effect on translocation to the plasma membrane." FT /evidence="ECO:0000269|PubMed:15164764, FT ECO:0000269|PubMed:15632189" FT MUTAGEN 241 FT /note="S->T: No effect on diacylglycerol kinase activity." FT /evidence="ECO:0000269|PubMed:15164764" FT MUTAGEN 242 FT /note="L->V: No effect on diacylglycerol kinase activity." FT /evidence="ECO:0000269|PubMed:15164764" FT MUTAGEN 245 FT /note="P->A,L: Decreased diacylglycerol kinase activity." FT /evidence="ECO:0000269|PubMed:15164764" FT MUTAGEN 246 FT /note="P->L: Loss of diacylglycerol kinase activity." FT /evidence="ECO:0000269|PubMed:15164764" FT MUTAGEN 648 FT /note="G->A: Loss of diacylglycerol kinase activity. Loss FT of function is synaptic endocytosis." FT /evidence="ECO:0000269|PubMed:15164764, FT ECO:0000269|PubMed:26748701" FT CONFLICT 45..46 FT /note="PE -> RD (in Ref. 1; AAA98749)" FT /evidence="ECO:0000305" FT CONFLICT 50..56 FT /note="VRAPGPA -> GVRARAR (in Ref. 1; AAA98749)" FT /evidence="ECO:0000305" FT CONFLICT 933 FT /note="A -> R (in Ref. 1; AAA98749)" FT /evidence="ECO:0000305" SQ SEQUENCE 942 AA; 101155 MW; 836D4FCBC208A5B6 CRC64; MAAAAEPGAR AWLGGGSPRP GSPACSPVLG SGGRARPGPG PGPGPERAGV RAPGPAAAPG HSFRKVTLTK PTFCHLCSDF IWGLAGFLCD VCNFMSHEKC LKHVRIPCTS VAPSLVRVPV AHCFGPRGLH KRKFCAVCRK VLEAPALHCE VCELHLHPDC VPFACSDCRQ CHQDGHQDHD THHHHWREGN LPSGARCEVC RKTCGSSDVL AGVRCEWCGV QAHSLCSAAL APECGFGRLR SLVLPPACVR LLPGGFSKTQ SFRIVEAAEP GEGGDGADGS AAVGPGRETQ ATPESGKQTL KIFDGDDAVR RSQFRLVTVS RLAGAEEVLE AALRAHHIPE DPGHLELCRL PPSSQACDAW AGGKAGSAVI SEEGRSPGSG EATPEAWVIR ALPRAQEVLK IYPGWLKVGV AYVSVRVTPK STARSVVLEV LPLLGRQAES PESFQLVEVA MGCRHVQRTM LMDEQPLLDR LQDIRQMSVR QVSQTRFYVA ESRDVAPHVS LFVGGLPPGL SPEEYSSLLH EAGATKATVV SVSHIYSSQG AVVLDVACFA EAERLYMLLK DMAVRGRLLT ALVLPDLLHA KLPPDSCPLL VFVNPKSGGL KGRDLLCSFR KLLNPHQVFD LTNGGPLPGL HLFSQVPCFR VLVCGGDGTV GWVLGALEET RYRLACPEPS VAILPLGTGN DLGRVLRWGA GYSGEDPFSV LLSVDEADAV LMDRWTILLD AHEAGSAEND TADAEPPKIV QMSNYCGIGI DAELSLDFHQ AREEEPGKFT SRLHNKGVYV RVGLQKISHS RSLHKQIRLQ VERQEVELPS IEGLIFINIP SWGSGADLWG SDSDTRFEKP RMDDGLLEVV GVTGVVHMGQ VQGGLRSGIR IAQGSYFRVT LLKATPVQVD GEPWVQAPGH MIISAAGPKV HMLRKAKQKP RRAGTTRDAR ADAAPAPESD PR //