DGKQ_HUMAN
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 03-AUG-2022, entry version 174.
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 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=1,2-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}.
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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 BioGRID; 107979; 19.
DR IntAct; P52824; 3.
DR STRING; 9606.ENSP00000273814; -.
DR DrugBank; DB14001; alpha-Tocopherol succinate.
DR SwissLipids; SLP:000000740; -.
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; P52824; -.
DR PeptideAtlas; P52824; -.
DR PRIDE; P52824; -.
DR ProteomicsDB; 56542; -.
DR Antibodypedia; 22185; 219 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 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; EDYRCSE; -.
DR OrthoDB; 1275907at2759; -.
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; 14 hits in 1082 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 161 other tissues.
DR ExpressionAtlas; P52824; baseline and differential.
DR Genevisible; P52824; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
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: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:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004143; F: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:0003951; F:NAD+ kinase activity; IEA:InterPro.
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; cd00029; C1; 2.
DR Gene3D; 3.40.50.10330; -; 1.
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; PTHR11255; 2.
DR Pfam; PF00130; C1_1; 2.
DR Pfam; PF00609; DAGK_acc; 1.
DR Pfam; PF00781; DAGK_cat; 1.
DR Pfam; PF00788; RA; 1.
DR SMART; SM00109; C1; 3.
DR SMART; SM00045; DAGKa; 1.
DR SMART; SM00046; DAGKc; 1.
DR SMART; SM00314; RA; 1.
DR SUPFAM; SSF111331; SSF111331; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR SUPFAM; SSF57889; SSF57889; 3.
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.
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
