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Diacylglycerol kinase theta (DAG kinase theta) (EC 2.7.1.107) (Diglyceride kinase theta) (DGK-theta)

 DGKQ_HUMAN              Reviewed;         942 AA.
P52824; Q6P3W4;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-SEP-2009, sequence version 2.
27-SEP-2017, entry version 147.
RecName: Full=Diacylglycerol kinase theta;
Short=DAG kinase theta;
EC=2.7.1.107;
AltName: Full=Diglyceride kinase theta;
Short=DGK-theta;
Name=DGKQ; Synonyms=DAGK4;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=7607687; DOI=10.1016/0888-7543(95)80182-L;
Pilz A., Schaap D., Hunt D., Fitzgibbon J.;
"Chromosomal localization of three mouse diacylglycerol kinase (DAGK)
genes: genes sharing sequence homology to the Drosophila retinal
degeneration A (rdgA) gene.";
Genomics 26:599-601(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT LEU-27.
TISSUE=Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
CATALYTIC ACTIVITY, INTERACTION WITH RHOA, AND SUBCELLULAR LOCATION.
PubMed=10066731; DOI=10.1074/jbc.274.11.6820;
Houssa B., de Widt J., Kranenburg O., Moolenaar W.H.,
van Blitterswijk W.J.;
"Diacylglycerol kinase theta binds to and is negatively regulated by
active RhoA.";
J. Biol. Chem. 274:6820-6822(1999).
[5]
SUBCELLULAR LOCATION, AND INTERACTION WITH PLCB1.
PubMed=12799190; DOI=10.1016/S0014-4827(03)00115-0;
Tabellini G., Bortul R., Santi S., Riccio M., Baldini G.,
Cappellini A., Billi A.M., Berezney R., Ruggeri A., Cocco L.,
Martelli A.M.;
"Diacylglycerol kinase-theta is localized in the speckle domains of
the nucleus.";
Exp. Cell Res. 287:143-154(2003).
[6]
INTERACTION WITH RHOA, AND MUTAGENESIS OF GLY-237; PRO-245 AND
PRO-246.
PubMed=15164764; DOI=10.1016/j.bbalip.2003.11.008;
Los A.P., van Baal J., de Widt J., Divecha N., van Blitterswijk W.J.;
"Structure-activity relationship of diacylglycerol kinase theta.";
Biochim. Biophys. Acta 1636:169-174(2004).
[7]
INTERACTION WITH PRKCE AND PRKCH, SUBCELLULAR LOCATION, AND
MUTAGENESIS OF CYS-100; CYS-160; CYS-226 AND GLY-237.
PubMed=15632189; DOI=10.1074/jbc.M409301200;
van Baal J., de Widt J., Divecha N., van Blitterswijk W.J.;
"Translocation of diacylglycerol kinase theta from cytosol to plasma
membrane in response to activation of G protein-coupled receptors and
protein kinase C.";
J. Biol. Chem. 280:9870-9878(2005).
[8]
FUNCTION, AND INTERACTION WITH NR5A1.
PubMed=17664281; DOI=10.1128/MCB.00355-07;
Li D., Urs A.N., Allegood J., Leon A., Merrill A.H. Jr., Sewer M.B.;
"Cyclic AMP-stimulated interaction between steroidogenic factor 1 and
diacylglycerol kinase theta facilitates induction of CYP17.";
Mol. Cell. Biol. 27:6669-6685(2007).
-!- FUNCTION: Phosphorylates diacylglycerol (DAG) to generate
phosphatidic acid (PA). May regulate the activity of protein
kinase C by controlling the balance between these two signaling
lipids. Activated in the nucleus in response to alpha-thrombin and
nerve growth factor (By similarity). May be involved in cAMP-
induced activation of NR5A1 and subsequent steroidogenic gene
transcription by delivering PA as ligand for NR5A1. Acts
synergistically with NR5A1 on CYP17 transcriptional activity.
{ECO:0000250, ECO:0000269|PubMed:17664281}.
-!- CATALYTIC ACTIVITY: ATP + 1,2-diacyl-sn-glycerol = ADP + 1,2-
diacyl-sn-glycerol 3-phosphate. {ECO:0000269|PubMed:10066731}.
-!- ENZYME REGULATION: Inactivated by binding to RHOA. Not inhibited
by phosphatidylserine.
-!- SUBUNIT: Interacts with RHOA (constitutively activated, GTP-
bound); the interaction inhibits DGKQ. Interacts with PRKCE.
Interacts with PRKCH. Interacts with PLCB1. Interacts with NR5A1;
the interaction requires the LXXLL motif 1 and LXXLL motif 2 in
DGKQ. {ECO:0000269|PubMed:10066731, ECO:0000269|PubMed:12799190,
ECO:0000269|PubMed:15164764, ECO:0000269|PubMed:15632189,
ECO:0000269|PubMed:17664281}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15632189}.
Cell membrane {ECO:0000269|PubMed:10066731,
ECO:0000269|PubMed:15632189}. Cytoplasm, cytoskeleton
{ECO:0000269|PubMed:10066731}. Nucleus
{ECO:0000269|PubMed:12799190}. Nucleus speckle
{ECO:0000269|PubMed:12799190}. Note=Translocates to the nucleus in
response to thrombin stimulation (PubMed:15632189). Translocates
to the plasma membrane in response to steroid hormone receptor
stimulation (PubMed:15632189). Translocation to the plasma
membrane is dependent on G-protein coupled receptor stimulation
and subsequent activation of PRKCE and probably PRKCH
(PubMed:15632189).
-!- DOMAIN: The L-X-X-L-L repeats are implicated in binding to the
nuclear receptor NR5A1.
-!- PTM: Phosphorylated by PRKCE and PRKCH in vitro.
-!- SIMILARITY: Belongs to the eukaryotic diacylglycerol kinase
family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; L38707; AAA98749.1; -; mRNA.
EMBL; AC019103; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC063801; AAH63801.1; -; mRNA.
CCDS; CCDS3342.1; -.
RefSeq; NP_001338.2; NM_001347.3.
UniGene; Hs.584858; -.
ProteinModelPortal; P52824; -.
SMR; P52824; -.
BioGrid; 107979; 10.
IntAct; P52824; 1.
STRING; 9606.ENSP00000273814; -.
SwissLipids; SLP:000000740; -.
iPTMnet; P52824; -.
PhosphoSitePlus; P52824; -.
BioMuta; DGKQ; -.
DMDM; 257051005; -.
EPD; P52824; -.
MaxQB; P52824; -.
PaxDb; P52824; -.
PeptideAtlas; P52824; -.
PRIDE; P52824; -.
DNASU; 1609; -.
Ensembl; ENST00000273814; ENSP00000273814; ENSG00000145214.
GeneID; 1609; -.
KEGG; hsa:1609; -.
UCSC; uc003gbw.5; human.
CTD; 1609; -.
DisGeNET; 1609; -.
EuPathDB; HostDB:ENSG00000145214.13; -.
GeneCards; DGKQ; -.
HGNC; HGNC:2856; DGKQ.
HPA; CAB033835; -.
HPA; HPA026797; -.
MIM; 601207; gene.
neXtProt; NX_P52824; -.
OpenTargets; ENSG00000145214; -.
PharmGKB; PA27317; -.
eggNOG; KOG1169; Eukaryota.
eggNOG; ENOG410XQVB; LUCA.
GeneTree; ENSGT00760000119050; -.
HOGENOM; HOG000007900; -.
HOVERGEN; HBG094675; -.
InParanoid; P52824; -.
KO; K00901; -.
OMA; TKPTFCH; -.
OrthoDB; EOG091G02NN; -.
PhylomeDB; P52824; -.
TreeFam; TF312817; -.
Reactome; R-HSA-114508; Effects of PIP2 hydrolysis.
GeneWiki; DGKQ; -.
GenomeRNAi; 1609; -.
PRO; PR:P52824; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000145214; -.
CleanEx; HS_DGKQ; -.
ExpressionAtlas; P52824; baseline and differential.
Genevisible; P52824; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005856; C:cytoskeleton; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0005768; C:endosome; IDA:ParkinsonsUK-UCL.
GO; GO:0016363; C:nuclear matrix; ISS:ParkinsonsUK-UCL.
GO; GO:0016607; C:nuclear speck; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0012506; C:vesicle membrane; IDA:ParkinsonsUK-UCL.
GO; GO:0033613; F:activating transcription factor binding; IPI:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004143; F:diacylglycerol kinase activity; IDA:UniProtKB.
GO; GO:0019900; F:kinase binding; IPI:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0003951; F:NAD+ kinase activity; IEA:InterPro.
GO; GO:0043274; F:phospholipase binding; IPI:UniProtKB.
GO; GO:0030297; F:transmembrane receptor protein tyrosine kinase activator activity; IGI:ParkinsonsUK-UCL.
GO; GO:0019933; P:cAMP-mediated signaling; IDA:UniProtKB.
GO; GO:0046339; P:diacylglycerol metabolic process; IDA:BHF-UCL.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; IMP:UniProtKB.
GO; GO:0046486; P:glycerolipid metabolic process; IDA:BHF-UCL.
GO; GO:0046834; P:lipid phosphorylation; IDA:BHF-UCL.
GO; GO:0010629; P:negative regulation of gene expression; IMP:ParkinsonsUK-UCL.
GO; GO:0010801; P:negative regulation of peptidyl-threonine phosphorylation; IDA:ParkinsonsUK-UCL.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IMP:ParkinsonsUK-UCL.
GO; GO:0006654; P:phosphatidic acid biosynthetic process; IDA:ParkinsonsUK-UCL.
GO; GO:0030168; P:platelet activation; TAS:Reactome.
GO; GO:0010628; P:positive regulation of gene expression; IMP:ParkinsonsUK-UCL.
GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IDA:ParkinsonsUK-UCL.
GO; GO:0070528; P:protein kinase C signaling; IDA:UniProtKB.
GO; GO:0007205; P:protein kinase C-activating G-protein coupled receptor signaling pathway; IEA:InterPro.
GO; GO:0090181; P:regulation of cholesterol metabolic process; IMP:ParkinsonsUK-UCL.
GO; GO:2000064; P:regulation of cortisol biosynthetic process; IMP:ParkinsonsUK-UCL.
GO; GO:0008277; P:regulation of G-protein coupled receptor protein signaling pathway; IDA:ParkinsonsUK-UCL.
GO; GO:0006111; P:regulation of gluconeogenesis; IMP:ParkinsonsUK-UCL.
GO; GO:2000182; P:regulation of progesterone biosynthetic process; IMP:ParkinsonsUK-UCL.
GO; GO:1903432; P:regulation of TORC1 signaling; IMP:ParkinsonsUK-UCL.
GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0033198; P:response to ATP; IDA:UniProtKB.
GO; GO:0051591; P:response to cAMP; IDA:ParkinsonsUK-UCL.
GO; GO:0070493; P:thrombin-activated receptor signaling pathway; IDA:UniProtKB.
CDD; cd00029; C1; 2.
Gene3D; 3.40.50.10330; -; 1.
InterPro; IPR017438; ATP-NAD_kinase_dom_1.
InterPro; IPR000756; Diacylglycerol_kin_accessory.
InterPro; IPR001206; Diacylglycerol_kinase_cat_dom.
InterPro; IPR016064; NAD/diacylglycerol_kinase.
InterPro; IPR002219; PE/DAG-bd.
InterPro; IPR000159; RA_dom.
InterPro; IPR029071; Ubiquitin-rel_dom.
Pfam; PF00130; C1_1; 2.
Pfam; PF00609; DAGK_acc; 1.
Pfam; PF00781; DAGK_cat; 1.
Pfam; PF00788; RA; 1.
SMART; SM00109; C1; 3.
SMART; SM00045; DAGKa; 1.
SMART; SM00046; DAGKc; 1.
SMART; SM00314; RA; 1.
SUPFAM; SSF111331; SSF111331; 1.
SUPFAM; SSF54236; SSF54236; 1.
PROSITE; PS50146; DAGK; 1.
PROSITE; PS50200; RA; 1.
PROSITE; PS00479; ZF_DAG_PE_1; 3.
PROSITE; PS50081; ZF_DAG_PE_2; 3.
1: Evidence at protein level;
ATP-binding; Cell membrane; Complete proteome; Cytoplasm;
Cytoskeleton; Kinase; Membrane; Metal-binding; Nucleotide-binding;
Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat;
Transferase; Zinc; Zinc-finger.
CHAIN 1 942 Diacylglycerol kinase theta.
/FTId=PRO_0000218467.
DOMAIN 395 494 Ras-associating. {ECO:0000255|PROSITE-
ProRule:PRU00166}.
DOMAIN 584 721 DAGKc. {ECO:0000255|PROSITE-
ProRule:PRU00783}.
ZN_FING 60 108 Phorbol-ester/DAG-type 1.
{ECO:0000255|PROSITE-ProRule:PRU00226}.
ZN_FING 121 168 Phorbol-ester/DAG-type 2.
{ECO:0000255|PROSITE-ProRule:PRU00226}.
ZN_FING 183 234 Phorbol-ester/DAG-type 3.
{ECO:0000255|PROSITE-ProRule:PRU00226}.
MOTIF 555 559 LXXLL motif 1.
MOTIF 574 578 LXXLL motif 2.
MOD_RES 22 22 Phosphoserine.
{ECO:0000250|UniProtKB:Q6P5E8}.
MOD_RES 26 26 Phosphoserine.
{ECO:0000250|UniProtKB:Q6P5E8}.
VARIANT 27 27 P -> L (in dbSNP:rs17855876).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_058478.
MUTAGEN 100 100 C->G: Abolishes translocation to the
plasma membrane.
{ECO:0000269|PubMed:15632189}.
MUTAGEN 160 160 C->G: Abolishes translocation to the
plasma membrane.
{ECO:0000269|PubMed:15632189}.
MUTAGEN 226 226 C->G: Abolishes translocation to the
plasma membrane.
{ECO:0000269|PubMed:15632189}.
MUTAGEN 237 237 G->R: Abolishes enzymatic activity; no
effect on translocation to the plasma
membrane. {ECO:0000269|PubMed:15164764,
ECO:0000269|PubMed:15632189}.
MUTAGEN 245 245 P->A,L: Greatly reduces enzymatic
activity. {ECO:0000269|PubMed:15164764}.
MUTAGEN 246 246 P->L: Abolishes enzymatic activity.
{ECO:0000269|PubMed:15164764}.
CONFLICT 45 46 PE -> RD (in Ref. 1; AAA98749).
{ECO:0000305}.
CONFLICT 50 56 VRAPGPA -> GVRARAR (in Ref. 1; AAA98749).
{ECO:0000305}.
CONFLICT 933 933 A -> R (in Ref. 1; AAA98749).
{ECO:0000305}.
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


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