DGKA_RAT
ID DGKA_RAT Reviewed; 727 AA.
AC P51556;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Diacylglycerol kinase alpha;
DE Short=DAG kinase alpha;
DE EC=2.7.1.107 {ECO:0000269|PubMed:22627129};
DE AltName: Full=80 kDa diacylglycerol kinase;
DE AltName: Full=Diglyceride kinase alpha;
DE Short=DGK-alpha;
GN Name=Dgka; Synonyms=Dagk, Dagk1;
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], AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=1339302; DOI=10.1016/0169-328x(92)90196-i;
RA Goto K., Watanabe M., Kondo H., Yuasa H., Sakane F., Kanoh H.;
RT "Gene cloning, sequence, expression and in situ localization of 80 kDa
RT diacylglycerol kinase specific to oligodendrocyte of rat brain.";
RL Brain Res. Mol. Brain Res. 16:75-87(1992).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, ACTIVITY REGULATION, AND SUBCELLULAR
RP LOCATION.
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).
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:22627129). Thereby, acts as a
CC central switch between the signaling pathways activated by these second
CC messengers with different cellular targets and opposite effects in
CC numerous biological processes (PubMed:22627129). Also plays an
CC important role in the biosynthesis of complex lipids. Can also
CC phosphorylate 1-alkyl-2-acylglycerol in vitro as efficiently as
CC diacylglycerol provided it contains an arachidonoyl group (By
CC similarity). Also involved in the production of alkyl-lysophosphatidic
CC acid, another bioactive lipid, through the phosphorylation of 1-alkyl-
CC 2-acetyl glycerol (PubMed:22627129). {ECO:0000250|UniProtKB:P23743,
CC ECO:0000269|PubMed:22627129}.
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:22627129};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10273;
CC Evidence={ECO:0000305|PubMed:22627129};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dihexadecanoyl-sn-glycerol + ATP = 1,2-dihexadecanoyl-sn-
CC glycero-3-phosphate + ADP + H(+); Xref=Rhea:RHEA:63324,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:72859,
CC ChEBI:CHEBI:82929, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:P23743};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63325;
CC Evidence={ECO:0000250|UniProtKB:P23743};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycerol + ATP = 1-
CC hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + ADP + H(+);
CC Xref=Rhea:RHEA:43416, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:64839, ChEBI:CHEBI:75466, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:P23743};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43417;
CC Evidence={ECO:0000250|UniProtKB:P23743};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-(9Z-octadecenoyl)-glycerol + ATP = 2-(9Z-octadecenoyl)-sn-
CC glycero-3-phosphate + ADP + H(+); Xref=Rhea:RHEA:63328,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:73990,
CC ChEBI:CHEBI:77593, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:P23743};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63329;
CC Evidence={ECO:0000250|UniProtKB:P23743};
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:22627129};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40328;
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:0000250|UniProtKB:P23743};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40324;
CC Evidence={ECO:0000250|UniProtKB:P23743};
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:0000250|UniProtKB:P20192};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43429;
CC Evidence={ECO:0000250|UniProtKB:P20192};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-alkyl-2-acyl-sn-glycerol + ATP = 1-O-alkyl-2-acyl-sn-
CC glycero-3-phosphate + ADP + H(+); Xref=Rhea:RHEA:44072,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:52595,
CC ChEBI:CHEBI:73332, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:P23743};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44073;
CC Evidence={ECO:0000250|UniProtKB:P23743};
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-O-hexadecyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycerol +
CC ATP = 1-O-hexadecyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-
CC phosphate + ADP + H(+); Xref=Rhea:RHEA:40403, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:77184, ChEBI:CHEBI:77186,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:P23743};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40404;
CC Evidence={ECO:0000250|UniProtKB:P23743};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-hexadecyl-2-(9Z-octadecenoyl)-sn-glycerol + ATP = 1-O-
CC hexadecyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + ADP + H(+);
CC Xref=Rhea:RHEA:40407, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:77185, ChEBI:CHEBI:77187, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:P23743};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40408;
CC Evidence={ECO:0000250|UniProtKB:P23743};
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 -!- ACTIVITY REGULATION: Stimulated by calcium and phosphatidylserine (By
CC similarity). Activated by sphingosine (PubMed:22627129).
CC {ECO:0000250|UniProtKB:P23743, ECO:0000269|PubMed:22627129}.
CC -!- PATHWAY: Lipid metabolism; glycerolipid metabolism.
CC {ECO:0000305|PubMed:22627129}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P23743}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:22627129}.
CC -!- TISSUE SPECIFICITY: Lymphocytes and oligodendroglial cells.
CC {ECO:0000269|PubMed:1339302}.
CC -!- SIMILARITY: Belongs to the eukaryotic diacylglycerol kinase family.
CC {ECO:0000305}.
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DR EMBL; S49760; AAB24434.1; -; mRNA.
DR PIR; A56879; A56879.
DR RefSeq; NP_542965.1; NM_080787.1.
DR AlphaFoldDB; P51556; -.
DR STRING; 10116.ENSRNOP00000038628; -.
DR BindingDB; P51556; -.
DR ChEMBL; CHEMBL4523237; -.
DR SwissLipids; SLP:000000738; -.
DR PhosphoSitePlus; P51556; -.
DR PaxDb; P51556; -.
DR PRIDE; P51556; -.
DR GeneID; 140866; -.
DR KEGG; rno:140866; -.
DR UCSC; RGD:70904; rat.
DR CTD; 1606; -.
DR RGD; 70904; Dgka.
DR VEuPathDB; HostDB:ENSRNOG00000022943; -.
DR eggNOG; KOG1169; Eukaryota.
DR HOGENOM; CLU_003770_1_1_1; -.
DR InParanoid; P51556; -.
DR OMA; HCAMKAQ; -.
DR OrthoDB; 633642at2759; -.
DR PhylomeDB; P51556; -.
DR BRENDA; 2.7.1.107; 5301.
DR Reactome; R-RNO-114508; Effects of PIP2 hydrolysis.
DR UniPathway; UPA00230; -.
DR PRO; PR:P51556; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000022943; Expressed in thymus and 20 other tissues.
DR Genevisible; P51556; RN.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; 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; ISS:UniProtKB.
DR GO; GO:0016301; F:kinase activity; ISO:RGD.
DR GO; GO:0008289; F:lipid binding; ISO:RGD.
DR GO; GO:0003951; F:NAD+ kinase activity; IEA:InterPro.
DR GO; GO:0005543; F:phospholipid binding; ISO:RGD.
DR GO; GO:0046339; P:diacylglycerol metabolic process; ISS: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; ISS:UniProtKB.
DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; ISS:UniProtKB.
DR GO; GO:0007205; P:protein kinase C-activating G protein-coupled receptor signaling pathway; IEA:InterPro.
DR CDD; cd00029; C1; 1.
DR CDD; cd00051; EFh; 1.
DR Gene3D; 1.10.238.110; -; 1.
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; 1.
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 Acetylation; ATP-binding; Calcium; Cytoplasm; Kinase; Lipid metabolism;
KW Metal-binding; Nucleotide-binding; Reference proteome; Repeat; Transferase;
KW Zinc; Zinc-finger.
FT CHAIN 1..727
FT /note="Diacylglycerol kinase alpha"
FT /id="PRO_0000218456"
FT DOMAIN 108..143
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 153..188
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 365..498
FT /note="DAGKc"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT ZN_FING 203..251
FT /note="Phorbol-ester/DAG-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT ZN_FING 267..317
FT /note="Phorbol-ester/DAG-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT BINDING 121
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 123
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 125
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 132
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 166
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 168
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 170
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 172
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 177
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 476
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P23743"
SQ SEQUENCE 727 AA; 82199 MW; B5A248ADD2F61C1D CRC64;
MAKDKGLISP EDFAQLQKYI DYSTKSVSDV LKVFEMNKYC QGDEIGYLGF EQFLKMYLEV
EEVPHHLCWT LFWSFHSSQD LDEETESKAN VICLSDVYCY FTLLEGGSPE DKLEFTFKLY
DMDRNGILDS TEVEKIILQM MRVAEYLDWD VSELRPILQE MMKEMDRDGS GCVSLAEWVR
AGATTVPLLV LLGIDMTMKD DGHHIWRPKR FSRPVYCNLC ELSIGLGKQG LSCNLCKYIV
HDHCAMKAQP CEVSTYAKSR KDIGVQPHVW VRGGCHSGRC DRCQKKIRTY HSLTGLHCVW
CHLEIHDDCL QAVGPECDCG LLRDHILPPC SIYPRVLVSG QECKQKTTDV TSLCTPEAFR
IEPVSNTHPL LVFINPKSGG KQGQSVLWKF QYILNPRQVF NLKDGPEPGL RFFKDVPQFR
VLVCGGDGTV GWILETIDKA NFPIVPPVAV LPLGTGNDLA RCLRWGRGYE GENLRKILKD
IEISKVVYLD RWLLEVIPQQ NGEKSDPVPS QIINNYFSIG VDASIAHRFH LMREKYPEKF
NSRMKNKLWY LEFATSESIF STCKKLEESV TVEICGKLLD LSDLSLEGIA VLNIPSMHGG
SNLWGDTKRP HGDTCGINQA LGSVAKIITD PDILKTCVPD MSDKRLEVVG IEGVIEMGQI
YTRLKSAGHR LAKCSEITFQ TTKTLPMQVD GEPWMQAPCT IKITHKNQMP MLMGPAPSSS
NFFGFWS
