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Database: UniProt
Entry: E1BGA9_BOVIN
LinkDB: E1BGA9_BOVIN
Original site: E1BGA9_BOVIN 
ID   E1BGA9_BOVIN            Unreviewed;       942 AA.
AC   E1BGA9;
DT   02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 3.
DT   27-MAR-2024, entry version 79.
DE   RecName: Full=Diacylglycerol kinase {ECO:0000256|RuleBase:RU361128};
DE            Short=DAG kinase {ECO:0000256|RuleBase:RU361128};
DE            EC=2.7.1.107 {ECO:0000256|RuleBase:RU361128};
GN   Name=DGKQ {ECO:0000313|Ensembl:ENSBTAP00000022905.5,
GN   ECO:0000313|VGNC:VGNC:28031};
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913 {ECO:0000313|Ensembl:ENSBTAP00000022905.5, ECO:0000313|Proteomes:UP000009136};
RN   [1] {ECO:0000313|Ensembl:ENSBTAP00000022905.5, ECO:0000313|Proteomes:UP000009136}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000022905.5,
RC   ECO:0000313|Proteomes:UP000009136};
RA   Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA   Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA   Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT   "ARS-UCD1.2.";
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSBTAP00000022905.5}
RP   IDENTIFICATION.
RC   STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000022905.5};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00023371};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40328;
CC         Evidence={ECO:0000256|ARBA:ARBA00023371};
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:0000256|RuleBase:RU361128};
CC   -!- PATHWAY: Lipid metabolism; glycerolipid metabolism.
CC       {ECO:0000256|ARBA:ARBA00005175}.
CC   -!- SIMILARITY: Belongs to the eukaryotic diacylglycerol kinase family.
CC       {ECO:0000256|ARBA:ARBA00009280, ECO:0000256|RuleBase:RU361128}.
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DR   AlphaFoldDB; E1BGA9; -.
DR   SMR; E1BGA9; -.
DR   STRING; 9913.ENSBTAP00000022905; -.
DR   PaxDb; 9913-ENSBTAP00000022905; -.
DR   Ensembl; ENSBTAT00000022905.5; ENSBTAP00000022905.5; ENSBTAG00000017240.5.
DR   VEuPathDB; HostDB:ENSBTAG00000017240; -.
DR   VGNC; VGNC:28031; DGKQ.
DR   eggNOG; KOG1169; Eukaryota.
DR   GeneTree; ENSGT00940000159492; -.
DR   HOGENOM; CLU_003770_0_0_1; -.
DR   InParanoid; E1BGA9; -.
DR   OMA; GFHHARE; -.
DR   TreeFam; TF312817; -.
DR   Reactome; R-BTA-114508; Effects of PIP2 hydrolysis.
DR   UniPathway; UPA00230; -.
DR   Proteomes; UP000009136; Chromosome 6.
DR   Bgee; ENSBTAG00000017240; Expressed in esophagus and 101 other cell types or tissues.
DR   GO; GO:0005856; C:cytoskeleton; IEA:Ensembl.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005768; C:endosome; IEA:Ensembl.
DR   GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR   GO; GO:0016607; C:nuclear speck; IEA:Ensembl.
DR   GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR   GO; GO:0098794; C:postsynapse; IEA:Ensembl.
DR   GO; GO:0098793; C:presynapse; IEA:Ensembl.
DR   GO; GO:0012506; C:vesicle membrane; IEA:Ensembl.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004143; F:ATP-dependent diacylglycerol kinase activity; IBA:GO_Central.
DR   GO; GO:0140297; F:DNA-binding transcription factor binding; IEA:Ensembl.
DR   GO; GO:0019900; F:kinase binding; IEA:Ensembl.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0043274; F:phospholipase binding; IEA:Ensembl.
DR   GO; GO:0030297; F:transmembrane receptor protein tyrosine kinase activator activity; IEA:Ensembl.
DR   GO; GO:0019933; P:cAMP-mediated signaling; IEA:Ensembl.
DR   GO; GO:0046339; P:diacylglycerol metabolic process; IBA:GO_Central.
DR   GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR   GO; GO:0046834; P:lipid phosphorylation; IBA:GO_Central.
DR   GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
DR   GO; GO:0010801; P:negative regulation of peptidyl-threonine phosphorylation; IEA:Ensembl.
DR   GO; GO:0006654; P:phosphatidic acid biosynthetic process; IEA:Ensembl.
DR   GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR   GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IEA:Ensembl.
DR   GO; GO:0070528; P:protein kinase C signaling; IEA:Ensembl.
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; IEA:Ensembl.
DR   GO; GO:2000064; P:regulation of cortisol biosynthetic process; IEA:Ensembl.
DR   GO; GO:0008277; P:regulation of G protein-coupled receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0006111; P:regulation of gluconeogenesis; IEA:Ensembl.
DR   GO; GO:2000182; P:regulation of progesterone biosynthetic process; IEA:Ensembl.
DR   GO; GO:1900242; P:regulation of synaptic vesicle endocytosis; IEA:Ensembl.
DR   GO; GO:1903432; P:regulation of TORC1 signaling; IEA:Ensembl.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR   GO; GO:0033198; P:response to ATP; IEA:Ensembl.
DR   GO; GO:0051591; P:response to cAMP; IEA:Ensembl.
DR   GO; GO:0070493; P:thrombin-activated receptor signaling pathway; IEA:Ensembl.
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; cd01783; RA2_DAGK-theta; 1.
DR   Gene3D; 2.60.200.40; -; 1.
DR   Gene3D; 3.30.60.20; -; 3.
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; 1.
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.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU361128};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU361128};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU361128};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009136};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361128};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          61..109
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50081"
FT   DOMAIN          122..169
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50081"
FT   DOMAIN          184..235
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50081"
FT   DOMAIN          395..494
FT                   /note="Ras-associating"
FT                   /evidence="ECO:0000259|PROSITE:PS50200"
FT   DOMAIN          584..721
FT                   /note="DAGKc"
FT                   /evidence="ECO:0000259|PROSITE:PS50146"
FT   REGION          1..63
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          270..300
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          913..942
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        922..942
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   942 AA;  101668 MW;  9039F03318515079 CRC64;
     MAAAAEPGAR GWLGGGSPRP GSPTSSPELG AGSRSRSGPG SGPGSGPERS GSRPPGPAAP
     SHSFRKVTLT KPTFCHLCSD FIWGLAGILC DVCNFMSHEK CLKHVKTPCT SVAPSLVRVP
     VAHCFGPRGL YKRRFCSVCR KGLEAPGLRC EVCELHVHPD CVPFACSDCR QCHQDGHRDH
     DAHLHHWREG TLPSGARCEL CRKTCGSSDV PAGVRCEWCG IQAHSVCSAA LAPECTFGRL
     RTLVLPPACV RLLSRNFSKM HCFRIPESAA PEPGEWGGGE GADGSVPAGP GREVGTPESG
     KQTLKIFDGS DAMQRNHFRA VTVPRLARSQ EVLEAALRAY YISEDPQGFQ LQALPTPVQL
     GDTAAAGRVW STGPAEEEGG RAAPEAWVLR ALPRTQEILK IYPAWLKVGV AYVSIRVTPQ
     STARSVVLEV LPLLGRQAEG AEGFQLVEVL MGSRQVQRTV LADEEPLLDR LREIRQTSLR
     QMSQTRFYVA ESRVPAPRVS LFVGGLPPGL SPQEYRRLLD EAVTSKAALV TVSHVYSAQG
     AVVLDVACFA EAERLYMLIR DTAVRGRPLT ALVLPEVLHT KLAPDCRPLL VFVNPRSGGL
     KGRDLLCSFR KLLNPHQVFE LTNGGPLPGF HVFSRVPCFR VLVCGGDGTV GWVLAALEDL
     RHHLACPEPA VAILPLGTGN DLGRVLRWGA GYSGEDPFSV LLSVDEADAV LVDRWTILLD
     AHESACGEDS EADAEPPKIV QMSNYCGIGI DAELSLDFHQ AREEEPGKFT SRFHNKGVYV
     RVGLQKISHS RSLHRALRLQ VEQQEVELPS IEGLIFINIP SWGSGADLWG SDSDSRFEKP
     RMDDGLLEVV GVTGVVHMGQ VQSGLRSGIR IAQGSYFRVT LLKATPVQVD GEPWVQAPGH
     LIISAAGPKV HMLRKAKQKP RKAGPAKDAR ADGAPAPEGD PK
//
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