ID   DGKB_RAT                Reviewed;         801 AA.
AC   P49621;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   04-NOV-2026, entry version 173.
DE   RecName: Full=Diacylglycerol kinase beta;
DE            Short=DAG kinase beta;
DE            EC=2.7.1.107 {ECO:0000269|PubMed:23949095, ECO:0000269|PubMed:7689223};
DE   AltName: Full=90 kDa diacylglycerol kinase;
DE   AltName: Full=Diglyceride kinase beta;
DE            Short=DGK-beta;
GN   Name=Dgkb; Synonyms=Dagk2;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, PATHWAY, SUBCELLULAR
RP   LOCATION, TOPOLOGY, AND TISSUE SPECIFICITY.
RC   STRAIN=Wistar; TISSUE=Brain;
RX   PubMed=7689223; DOI=10.1073/pnas.90.16.7598;
RA   Goto K., Kondo H.;
RT   "Molecular cloning and expression of a 90-kDa diacylglycerol kinase that
RT   predominantly localizes in neurons.";
RL   Proc. Natl. Acad. Sci. U.S.A. 90:7598-7602(1993).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-117 AND SER-417, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
RN   [3]
RP   FUNCTION, AND 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).
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:23949095, PubMed:7689223).
CC       Thereby, acts as a central switch between the signaling pathways
CC       activated by these second messengers with different cellular targets
CC       and opposite effects in numerous biological processes (Probable). Has a
CC       higher activity with long-chain diacylglycerols like 1,2-di-(9Z-
CC       octadecenoyl)-sn-glycerol compared to 1,2-didecanoyl-sn-glycerol
CC       (PubMed:7689223). Specifically expressed in brain, it regulates neuron-
CC       specific morphological changes including neurite branching and neurite
CC       spine formation (By similarity). {ECO:0000250|UniProtKB:Q6NS52,
CC       ECO:0000269|PubMed:23949095, ECO:0000269|PubMed:7689223, ECO:0000305}.
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:23949095, ECO:0000269|PubMed:7689223};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10273;
CC         Evidence={ECO:0000305|PubMed:7689223};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-octadecanoyl-2-(9Z,12Z)-octadecadienoyl-sn-glycerol + ATP =
CC         1-octadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphate +
CC         ADP + H(+); Xref=Rhea:RHEA:40339, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:77097, ChEBI:CHEBI:77098,
CC         ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:7689223};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40340;
CC         Evidence={ECO:0000305|PubMed:7689223};
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:7689223};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40324;
CC         Evidence={ECO:0000305|PubMed:7689223};
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:23949095, ECO:0000269|PubMed:7689223};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40328;
CC         Evidence={ECO:0000305|PubMed:7689223};
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:0000269|PubMed:7689223};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43429;
CC         Evidence={ECO:0000305|PubMed:7689223};
CC   -!- ACTIVITY REGULATION: Activated by calcium.
CC       {ECO:0000269|PubMed:7689223}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         Vmax=16.4 nmol/min/mg enzyme with
CC         1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycerol as
CC         substrate (in presence of 0.02 mM calcium)
CC         {ECO:0000269|PubMed:7689223};
CC   -!- PATHWAY: Lipid metabolism; glycerolipid metabolism.
CC       {ECO:0000305|PubMed:7689223}.
CC   -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane
CC       {ECO:0000305|PubMed:7689223}; Peripheral membrane protein
CC       {ECO:0000305|PubMed:7689223}. Cell membrane
CC       {ECO:0000305|PubMed:7689223}; Peripheral membrane protein
CC       {ECO:0000305|PubMed:7689223}. Cytoplasm {ECO:0000305|PubMed:7689223}.
CC       Note=Translocation to the plasma membrane is induced by phorbol esters.
CC       {ECO:0000250|UniProtKB:Q9Y6T7}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in brain where it is restricted to
CC       neuronal populations such as the caudate-putamen, the accumbens
CC       nucleus, and the olfactory tubercle (PubMed:7689223). Less abundantly
CC       expressed in adrenal gland, small intestine and heart (PubMed:7689223).
CC       {ECO:0000269|PubMed:7689223}.
CC   -!- SIMILARITY: Belongs to the eukaryotic diacylglycerol kinase family.
CC       {ECO:0000305}.
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DR   EMBL; D16100; BAA03675.1; -; mRNA.
DR   PIR; A47744; A47744.
DR   RefSeq; NP_062177.2; NM_019304.2.
DR   SMR; P49621; -.
DR   BioGRID; 248471; 2.
DR   STRING; 10116.ENSRNOP00000058842; -.
DR   SwissLipids; SLP:000000927; -.
DR   iPTMnet; P49621; -.
DR   PhosphoSitePlus; P49621; -.
DR   PaxDb; 10116-ENSRNOP00000058842; -.
DR   GeneID; 54248; -.
DR   KEGG; rno:54248; -.
DR   UCSC; RGD:2488; rat.
DR   CTD; 1607; -.
DR   AGR; RGD:2488; -.
DR   RGD; 2488; Dgkb.
DR   eggNOG; KOG1169; Eukaryota.
DR   InParanoid; P49621; -.
DR   OMA; AAPKCIP; -.
DR   PhylomeDB; P49621; -.
DR   BRENDA; 2.7.1.107; 5301.
DR   Reactome; R-RNO-114508; Effects of PIP2 hydrolysis.
DR   UniPathway; UPA00230; -.
DR   PRO; PR:P49621; -.
DR   CDD; cd20845; C1_DGKbeta_rpt1; 1.
DR   CDD; cd20891; C1_DGKbeta_rpt2; 1.
DR   CDD; cd00051; EFh; 1.
DR   FunFam; 1.10.238.10:FF:000017; Diacylglycerol kinase; 1.
DR   FunFam; 1.10.238.110:FF:000001; Diacylglycerol kinase; 1.
DR   FunFam; 1.10.238.110:FF:000003; Diacylglycerol kinase; 1.
DR   FunFam; 2.60.200.40:FF:000003; Diacylglycerol kinase; 1.
DR   FunFam; 3.30.60.20:FF:000013; Diacylglycerol kinase; 1.
DR   FunFam; 3.30.60.20:FF:000016; Diacylglycerol kinase; 1.
DR   FunFam; 3.40.50.10330:FF:000003; Diacylglycerol kinase; 1.
DR   Gene3D; 2.60.200.40; -; 2.
DR   Gene3D; 3.30.60.20; -; 2.
DR   Gene3D; 1.10.238.110; Diacylglycerol kinase alpha; 2.
DR   Gene3D; 1.10.238.10; EF-hand; 1.
DR   Gene3D; 3.40.50.10330; Probable inorganic polyphosphate/atp-NAD kinase, domain 1; 1.
DR   InterPro; IPR017438; ATP-NAD_kinase_N.
DR   InterPro; IPR046349; C1-like_sf.
DR   InterPro; IPR047471; C1_DGKbeta-like_rpt1.
DR   InterPro; IPR047470; C1_DGKbeta_rpt2.
DR   InterPro; IPR029477; DAG_kinase_typeI_N.
DR   InterPro; IPR037607; DGK.
DR   InterPro; IPR038199; DGK_typeI_N_sf.
DR   InterPro; IPR000756; Diacylglycerol_kin_accessory.
DR   InterPro; IPR001206; Diacylglycerol_kinase_cat_dom.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR002048; EF_hand_dom.
DR   InterPro; IPR016064; NAD/diacylglycerol_kinase_sf.
DR   InterPro; IPR002219; PKC_DAG/PE.
DR   PANTHER; PTHR11255; DIACYLGLYCEROL KINASE; 1.
DR   PANTHER; PTHR11255:SF32; DIACYLGLYCEROL KINASE BETA; 1.
DR   Pfam; PF00130; C1_1; 2.
DR   Pfam; PF14513; DAG_kinase_N; 2.
DR   Pfam; PF00609; DAGK_acc; 1.
DR   Pfam; PF00781; DAGK_cat; 1.
DR   Pfam; PF13499; EF-hand_7; 1.
DR   SMART; SM00109; C1; 2.
DR   SMART; SM00045; DAGKa; 1.
DR   SMART; SM00046; DAGKc; 1.
DR   SMART; SM00054; EFh; 2.
DR   SUPFAM; SSF57889; Cysteine-rich domain; 2.
DR   SUPFAM; SSF47473; EF-hand; 2.
DR   SUPFAM; SSF111331; NAD kinase/diacylglycerol kinase-like; 1.
DR   PROSITE; PS50146; DAGK; 1.
DR   PROSITE; PS00018; EF_HAND_1; 2.
DR   PROSITE; PS50222; EF_HAND_2; 2.
DR   PROSITE; PS00479; ZF_DAG_PE_1; 2.
DR   PROSITE; PS50081; ZF_DAG_PE_2; 2.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0005829; C:cytosol; ISO:RGD.
DR   GO; GO:0099147; C:extrinsic component of postsynaptic density membrane; IDA:SynGO.
DR   GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR   GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR   GO; GO:0045211; C:postsynaptic membrane; ISO:RGD.
DR   GO; GO:0098685; C:Schaffer collateral - CA1 synapse; ISO:RGD.
DR   GO; GO:0004143; F:ATP-dependent diacylglycerol kinase activity; IDA:UniProtKB.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0008289; F:lipid binding; ISO:RGD.
DR   GO; GO:0046339; P:diacylglycerol metabolic process; IDA:UniProtKB.
DR   GO; GO:0046486; P:glycerolipid metabolic process; ISO:RGD.
DR   GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR   GO; GO:0046834; P:lipid phosphorylation; IDA:UniProtKB.
DR   GO; GO:0050804; P:modulation of chemical synaptic transmission; ISO:RGD.
DR   GO; GO:0006654; P:phosphatidic acid biosynthetic process; IDA:UniProtKB.
DR   GO; GO:0046473; P:phosphatidic acid metabolic process; IDA:UniProtKB.
DR   GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; IEA:InterPro.
DR   GO; GO:0099175; P:regulation of postsynapse organization; ISO:RGD.
DR   GO; GO:0009617; P:response to bacterium; ISO:RGD.
DR   Proteomes; UP000002494; Unplaced.
DR   AlphaFoldDB; P49621; -.
DR   FunCoup; P49621; 1027.
PE   1: Evidence at protein level;
KW   ATP-binding; Calcium; Cell membrane; Cytoplasm; Kinase; Lipid metabolism;
KW   Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW   Postsynaptic cell membrane; Reference proteome; Repeat; Synapse;
KW   Transferase; Zinc; Zinc-finger.
FT   CHAIN           1..801
FT                   /note="Diacylglycerol kinase beta"
FT                   /id="PRO_0000218458"
FT   DOMAIN          148..183
FT                   /note="EF-hand 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          193..228
FT                   /note="EF-hand 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          431..565
FT                   /note="DAGKc"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT   ZN_FING         243..292
FT                   /note="Phorbol-ester/DAG-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT   ZN_FING         307..356
FT                   /note="Phorbol-ester/DAG-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT   REGION          383..415
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          670..695
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          770..801
FT                   /note="Required for association with membranes and function
FT                   in neurite spine formation"
FT                   /evidence="ECO:0000250|UniProtKB:Q6NS52"
FT   COMPBIAS        386..398
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        675..684
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        685..695
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         161
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         163
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         165
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         172
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         206
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         208
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         210
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         212
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         217
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   MOD_RES         117
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         417
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         790
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6NS52"
SQ   SEQUENCE   801 AA;  90288 MW;  F30874CD2DCE363D CRC64;
     MTNQEKWAHL SPSEFSQLQK YAEYSTKKLK DVLEEFHGNG VLAKYNPEGK QDILNQTIDF
     EGFKLFMKTF LEAELPDDFT AHLFMSFSNK FPHSSPNVKS KPALLSGGLR MNKGAITPPR
     SSPANTCFPE VIHLKDIVCY LSLLERGRPE DKLEFMFRLY DTDGNGFLDS SELENIIGQM
     MHVAEYLEWD VTELNPILHE MMEEIDYDRD GTVSLEEWIQ GGMTTIPLLV LLGLENNVKD
     DGQHVWRLKH FNKPAYCNLC LNMLIGVGKQ GLCCSFCKYT VHERCARAPP SCIKTYVKSK
     KNTDVMHHYW VEGNCPTKCD KCHKTVKCYQ GLTGLHCVWC QTTLHNKCAS HLKPECDCGP
     LKDHILPPTT ICPVVLTMPT AGTSVPEERQ STAKKEKGSS QQPNKVTDKN KMQRANSVTM
     DGQGLQITPI PGTHPLLVFV NPKSGGKQGE RIYRKFQYLL NPRQVYSLSG NGPMPGLHFF
     RDVPDFRVLA CGGDGTVGWI LDCIEKANVV KHPPVAILPL GTGNDLARCL RWGGGYEGEN
     LMKILKDIES STEIMLDRWK FEVTPNDKDE KGDPVPYSII NNYFSIGVDA SIAHRFHIMR
     EKHPEKFNSR MKNKFWYFEF GTSETFSATC KKLHESVEIE CDGVQIDLIN ISLQGIAILN
     IPSMHGGSNL WGESKKKRSH RRIEKKGSDK RPTLTDAKEL KFASQDLSDQ LLEVVGLEGA
     MEMGQIYTGL KSAGRRLAQC SSVVIRTSKS LPMQIDGEPW MQTPCTIKIT HKNQAPMLMG
     PPPKTGLFCS LIKRTRNRSK E
//