DGKA_MOUSE
ID DGKA_MOUSE Reviewed; 730 AA.
AC O88673; Q922X2;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 27-MAR-2002, sequence version 2.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Diacylglycerol kinase alpha;
DE Short=DAG kinase alpha;
DE EC=2.7.1.107 {ECO:0000250|UniProtKB:P23743};
DE AltName: Full=80 kDa diacylglycerol kinase;
DE AltName: Full=Diglyceride kinase alpha;
DE Short=DGK-alpha;
GN Name=Dgka; Synonyms=Dagk1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Sanjuan M.A., Carrera A.C., Merida I.;
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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. Thereby, acts as a central switch
CC between the signaling pathways activated by these second messengers
CC with different cellular targets and opposite effects in numerous
CC biological processes. Also plays an important role in the biosynthesis
CC of complex lipids. Can also phosphorylate 1-alkyl-2-acylglycerol in
CC vitro as efficiently as diacylglycerol provided it contains an
CC arachidonoyl group. Also involved in the production of alkyl-
CC lysophosphatidic acid, another bioactive lipid, through the
CC phosphorylation of 1-alkyl-2-acetyl glycerol.
CC {ECO:0000250|UniProtKB:P23743}.
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:0000250|UniProtKB:P23743};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10273;
CC Evidence={ECO:0000250|UniProtKB:P23743};
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:0000250|UniProtKB:P23743};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40328;
CC Evidence={ECO:0000250|UniProtKB:P23743};
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:0000250|UniProtKB:P51556};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41677;
CC Evidence={ECO:0000250|UniProtKB:P51556};
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:0000250|UniProtKB:P51556};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41673;
CC Evidence={ECO:0000250|UniProtKB:P51556};
CC -!- ACTIVITY REGULATION: Stimulated by calcium and phosphatidylserine.
CC {ECO:0000250|UniProtKB:P23743}.
CC -!- PATHWAY: Lipid metabolism; glycerolipid metabolism.
CC {ECO:0000250|UniProtKB:P23743}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P23743}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P23743}.
CC -!- SIMILARITY: Belongs to the eukaryotic diacylglycerol kinase family.
CC {ECO:0000305}.
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DR EMBL; AF085219; AAC33483.1; -; mRNA.
DR EMBL; BC006713; AAH06713.1; -; mRNA.
DR CCDS; CCDS24290.1; -.
DR RefSeq; NP_058091.2; NM_016811.2.
DR RefSeq; XP_011241653.1; XM_011243351.1.
DR RefSeq; XP_011241662.1; XM_011243360.1.
DR RefSeq; XP_017169275.1; XM_017313786.1.
DR RefSeq; XP_017169276.1; XM_017313787.1.
DR RefSeq; XP_017169277.1; XM_017313788.1.
DR AlphaFoldDB; O88673; -.
DR BioGRID; 199049; 2.
DR STRING; 10090.ENSMUSP00000026414; -.
DR iPTMnet; O88673; -.
DR PhosphoSitePlus; O88673; -.
DR EPD; O88673; -.
DR MaxQB; O88673; -.
DR PaxDb; O88673; -.
DR PeptideAtlas; O88673; -.
DR PRIDE; O88673; -.
DR ProteomicsDB; 277321; -.
DR Antibodypedia; 27785; 458 antibodies from 31 providers.
DR DNASU; 13139; -.
DR Ensembl; ENSMUST00000026414; ENSMUSP00000026414; ENSMUSG00000025357.
DR GeneID; 13139; -.
DR KEGG; mmu:13139; -.
DR UCSC; uc007hoc.1; mouse.
DR CTD; 1606; -.
DR MGI; MGI:102952; Dgka.
DR VEuPathDB; HostDB:ENSMUSG00000025357; -.
DR eggNOG; KOG1169; Eukaryota.
DR GeneTree; ENSGT00940000157144; -.
DR HOGENOM; CLU_003770_1_1_1; -.
DR InParanoid; O88673; -.
DR OMA; HCAMKAQ; -.
DR OrthoDB; 633642at2759; -.
DR PhylomeDB; O88673; -.
DR TreeFam; TF313104; -.
DR BRENDA; 2.7.1.107; 3474.
DR Reactome; R-MMU-114508; Effects of PIP2 hydrolysis.
DR UniPathway; UPA00230; -.
DR BioGRID-ORCS; 13139; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Dgka; mouse.
DR PRO; PR:O88673; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; O88673; protein.
DR Bgee; ENSMUSG00000025357; Expressed in thymus and 255 other tissues.
DR ExpressionAtlas; O88673; baseline and differential.
DR Genevisible; O88673; MM.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
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:MGI.
DR GO; GO:0016301; F:kinase activity; ISO:MGI.
DR GO; GO:0008289; F:lipid binding; ISO:MGI.
DR GO; GO:0003951; F:NAD+ kinase activity; IEA:InterPro.
DR GO; GO:0005543; F:phospholipid binding; IDA:MGI.
DR GO; GO:0046339; P:diacylglycerol metabolic process; ISS:UniProtKB.
DR GO; GO:0046486; P:glycerolipid metabolic process; ISO:MGI.
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..730
FT /note="Diacylglycerol kinase alpha"
FT /id="PRO_0000218454"
FT DOMAIN 111..146
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 156..191
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 368..501
FT /note="DAGKc"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT ZN_FING 206..254
FT /note="Phorbol-ester/DAG-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT ZN_FING 270..320
FT /note="Phorbol-ester/DAG-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT BINDING 124
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 126
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 128
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 135
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 169
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 171
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 173
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 175
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 180
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 479
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P23743"
FT CONFLICT 317
FT /note="G -> V (in Ref. 1; AAC33483)"
FT /evidence="ECO:0000305"
FT CONFLICT 392
FT /note="K -> N (in Ref. 1; AAC33483)"
FT /evidence="ECO:0000305"
FT CONFLICT 398
FT /note="N -> D (in Ref. 1; AAC33483)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 730 AA; 82762 MW; A7808E4F8FD83350 CRC64;
MAKEKGLISP EDFAQLQKYI EYSTKRVSDV LKVFDDGEMN RFCQGDAIGY LGFEQFMKMY
LEMEEVPHHL CWALFWSFHT SQVAAEKTKS KANVICLSDV YCYFTLLEGG RPEDKLEFTF
KLYDMDRNGI LDSTEVEKII LQMMRVAEYL DWDVSELRPI LQEMMREMDQ DGSGSVSLDE
WVRAGATTVP LLVLLGMDVT MKDDGNHIWR PKRFTRLVYC NLCEQSISLG KQGLSCNFCK
YIVHDHCAMK AQPCEVSTYA KSRKDIGVQS HLWVRGGCHS GRCDRCQKKI RTYHSLTGLH
CVWCHLEIHD DCLQAVGPEC DCGLLRDHIL PPCSIYPSVL VSGQECKHKT TDDTSLCTPE
AFRIEPVSNT HPLLVFINLK SGGKQGQSVL WKFQYILNPR QVFDLKDGPE PGLRFFKDVP
QFRILVCGGD GTVGWVLETI DKANFATVPP VAVLPLGTGN DLARCLRWGR GYEGENLRKI
LKDIELSKVV YLDRWFLEVI PQQNGEKSDP VPSQIINNYF SIGVDASIAH RFHLMREKYP
EKFNSRMKNK LWYFEFATSE SIFSTCKKLE ESVTVEICGK LLDLSDLSLE GIAVLNIPST
HGGSNLWGDT KRPHGDTCEI NQALGSAAKI ITDPDILKTC VPDMSDKRLE VVGIEGAIEM
GQIYTRLKSA GHRLAKCSEI TFQTTKTLPM QIDGEPWMQA PCTIKITHKN QMPMLMGPPS
NSYNFFGFWS
