DGKB_RAT
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 03-AUG-2022, entry version 157.
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:7689223, PubMed:23949095).
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 1-octadecanoyl-2-(5Z,8Z,11Z,14Z-
CC eicosatetraenoyl)-sn-glycerol as substrate (in presence of 0.02 mM
CC calcium) {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_062177.1; NM_019304.1.
DR AlphaFoldDB; P49621; -.
DR BioGRID; 248471; 2.
DR STRING; 10116.ENSRNOP00000058842; -.
DR SwissLipids; SLP:000000927; -.
DR iPTMnet; P49621; -.
DR PhosphoSitePlus; P49621; -.
DR PaxDb; P49621; -.
DR PRIDE; P49621; -.
DR GeneID; 54248; -.
DR KEGG; rno:54248; -.
DR UCSC; RGD:2488; rat.
DR CTD; 1607; -.
DR RGD; 2488; Dgkb.
DR eggNOG; KOG1169; Eukaryota.
DR InParanoid; P49621; -.
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 Proteomes; UP000002494; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR GO; GO:0016020; C:membrane; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; ISO:RGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004143; F:diacylglycerol kinase activity; IDA:UniProtKB.
DR GO; GO:0008289; F:lipid binding; ISO:RGD.
DR GO; GO:0003951; F:NAD+ kinase activity; IEA:InterPro.
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:0007205; P:protein kinase 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 CDD; cd00029; C1; 1.
DR CDD; cd00051; EFh; 1.
DR Gene3D; 1.10.238.110; -; 2.
DR Gene3D; 3.40.50.10330; -; 1.
DR InterPro; IPR017438; ATP-NAD_kinase_N.
DR InterPro; IPR046349; C1-like_sf.
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; PE/DAG-bd.
DR PANTHER; PTHR11255; PTHR11255; 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; SSF111331; SSF111331; 1.
DR SUPFAM; SSF47473; SSF47473; 2.
DR SUPFAM; SSF57889; SSF57889; 2.
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.
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 396..415
FT /note="Polar 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
