ID   DGKA_HUMAN              Reviewed;         735 AA.
AC   P23743; O75481; O75482; O75483; O95217; Q3ZE25; Q8IZ56; Q8N5Q2;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2009, sequence version 3.
DT   04-NOV-2026, entry version 233.
DE   RecName: Full=Diacylglycerol kinase alpha;
DE            Short=DAG kinase alpha;
DE            EC=2.7.1.107 {ECO:0000269|PubMed:15544348, ECO:0000269|PubMed:2175712};
DE            EC=2.7.1.93 {ECO:0000250|UniProtKB:P51556};
DE   AltName: Full=80 kDa diacylglycerol kinase;
DE   AltName: Full=Diglyceride kinase alpha;
DE            Short=DGK-alpha;
GN   Name=DGKA; Synonyms=DAGK, DAGK1;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY,
RP   SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, PATHWAY, SUBUNIT, SUBCELLULAR
RP   LOCATION, AND TISSUE SPECIFICITY.
RC   TISSUE=Lymphocyte;
RX   PubMed=2175712; DOI=10.1016/0014-5793(90)81461-v;
RA   Schaap D., de Widt J., van der Wal J., Vandekerckhove J., van Damme J.,
RA   Gussow D., Ploegh H.L., van Blitterswijk W.J., van der Bendl R.L.;
RT   "Purification, cDNA-cloning and expression of human diacylglycerol
RT   kinase.";
RL   FEBS Lett. 275:151-158(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND ALTERNATIVE SPLICING.
RC   TISSUE=Uterus;
RA   Champagne C.M.E., Maeda H., Takashiba S., van Dyke T.E.;
RT   "Alternative splicing of diacylglycerol kinase alpha expressed in human
RT   neutrophils.";
RL   Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RA   Batista E.L. Jr., Van Dyke T.E.;
RT   "Characterization of a novel DGK alpha transcript generated by alternative
RT   splicing.";
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16541075; DOI=10.1038/nature04569;
RA   Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA   Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA   Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA   Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA   Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA   Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA   Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA   Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA   Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA   Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA   Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA   Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA   Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA   Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA   Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA   Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA   Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA   David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA   D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA   Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA   Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA   Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA   LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA   Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA   Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA   Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA   Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA   Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA   Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA   Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA   Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA   Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA   Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA   Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA   Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA   Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA   Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA   Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA   Gibbs R.A.;
RT   "The finished DNA sequence of human chromosome 12.";
RL   Nature 440:346-351(2006).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT TYR-538.
RC   TISSUE=Brain;
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   [6]
RP   CHROMOSOMAL LOCATION.
RX   PubMed=8180475; DOI=10.1007/bf00292343;
RA   Hart T.C., Champagne C., Zhou J., van Dyke T.E.;
RT   "Assignment of the gene for diacylglycerol kinase (DAGK) to human
RT   chromosome 12.";
RL   Mamm. Genome 5:123-124(1994).
RN   [7]
RP   CHROMOSOMAL LOCATION.
RX   PubMed=7959783; DOI=10.1006/geno.1994.1376;
RA   Hart T.C., Zhou J., Champagne C., van Dyke T.E., Rao P.N., Pettenati M.J.;
RT   "Assignment of the human diacylglycerol kinase gene (DAGK) to 12q13.3 using
RT   fluorescence in situ hybridization analysis.";
RL   Genomics 22:246-247(1994).
RN   [8]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND PATHWAY.
RX   PubMed=15544348; DOI=10.1021/bi0484724;
RA   Epand R.M., Kam A., Bridgelal N., Saiga A., Topham M.K.;
RT   "The alpha isoform of diacylglycerol kinase exhibits arachidonoyl
RT   specificity with alkylacylglycerol.";
RL   Biochemistry 43:14778-14783(2004).
RN   [9]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-484, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA   Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [11]
RP   FUNCTION, AND PATHWAY.
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).
RN   [12]
RP   STRUCTURE BY NMR OF 1-118.
RG   Northeast structural genomics consortium (NESG);
RT   "NMR structure of diacylglycerol kinase alpha, NESGC target HR532.";
RL   Submitted (JAN-2005) to the PDB data bank.
RN   [13] {ECO:0007744|PDB:6IIE}
RP   X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH CALCIUM, SUBUNIT, AND MUTAGENESIS OF
RP   GLU-134 AND GLU-179.
RX   PubMed=30653270; DOI=10.1002/pro.3572;
RA   Takahashi D., Suzuki K., Sakamoto T., Iwamoto T., Murata T., Sakane F.;
RT   "Crystal structure and calcium-induced conformational changes of
RT   diacylglycerol kinase alpha EF-hand domains.";
RL   Protein Sci. 28:694-706(2019).
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:15544348, PubMed:2175712).
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 (PubMed:15544348,
CC       PubMed:2175712). Also plays an important role in the biosynthesis of
CC       complex lipids (Probable). Can also phosphorylate 1-alkyl-2-
CC       acylglycerol in vitro as efficiently as diacylglycerol provided it
CC       contains an arachidonoyl group (PubMed:15544348). Also involved in the
CC       production of alkyl-lysophosphatidic acid, another bioactive lipid,
CC       through the phosphorylation of 1-alkyl-2-acetyl glycerol
CC       (PubMed:22627129). {ECO:0000269|PubMed:15544348,
CC       ECO:0000269|PubMed:2175712, ECO:0000269|PubMed:22627129, 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:15544348, ECO:0000269|PubMed:2175712};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10273;
CC         Evidence={ECO:0000305|PubMed:2175712};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1-O-alkyl-sn-glycerol + ATP = a 1-O-alkyl-sn-glycero-3-
CC         phosphate + ADP + H(+); Xref=Rhea:RHEA:16937, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15850, ChEBI:CHEBI:30616, ChEBI:CHEBI:58014,
CC         ChEBI:CHEBI:456216; EC=2.7.1.93;
CC         Evidence={ECO:0000250|UniProtKB:P51556};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16938;
CC         Evidence={ECO:0000250|UniProtKB:P51556};
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:0000269|PubMed:15544348, ECO:0000269|PubMed:2175712};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44073;
CC         Evidence={ECO:0000305|PubMed:2175712};
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:0000269|PubMed:2175712};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63325;
CC         Evidence={ECO:0000305|PubMed:2175712};
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:0000269|PubMed:2175712};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43417;
CC         Evidence={ECO:0000305|PubMed:2175712};
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:0000269|PubMed:2175712};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63329;
CC         Evidence={ECO:0000305|PubMed:2175712};
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:15544348, ECO:0000269|PubMed:2175712};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40328;
CC         Evidence={ECO:0000305|PubMed:2175712};
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:15544348,
CC         ECO:0000269|PubMed:2175712};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40324;
CC         Evidence={ECO:0000305|PubMed:2175712};
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-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:0000269|PubMed:15544348};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40404;
CC         Evidence={ECO:0000305|PubMed:15544348};
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:0000269|PubMed:15544348, ECO:0000269|PubMed:2175712};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40408;
CC         Evidence={ECO:0000305|PubMed:2175712};
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:0000269|PubMed:2175712}.
CC   -!- PATHWAY: Lipid metabolism; glycerolipid metabolism.
CC       {ECO:0000305|PubMed:15544348, ECO:0000305|PubMed:2175712,
CC       ECO:0000305|PubMed:22627129}.
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:2175712,
CC       ECO:0000269|PubMed:30653270}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:2175712}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=P23743-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P23743-2; Sequence=VSP_032212, VSP_032213;
CC       Name=3;
CC         IsoId=P23743-3; Sequence=VSP_047702, VSP_047703;
CC   -!- TISSUE SPECIFICITY: Expressed in lymphocytes.
CC       {ECO:0000269|PubMed:2175712}.
CC   -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC       premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC       decay. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the eukaryotic diacylglycerol kinase family.
CC       {ECO:0000305}.
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DR   EMBL; X62535; CAA44396.1; -; mRNA.
DR   EMBL; AF064767; AAC34802.1; -; mRNA.
DR   EMBL; AF064768; AAC34803.1; -; mRNA.
DR   EMBL; AF064769; AAC34804.1; -; mRNA.
DR   EMBL; AF064771; AAC34806.1; -; mRNA.
DR   EMBL; AY930112; AAY20994.1; -; mRNA.
DR   EMBL; AC025162; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC023523; AAH23523.1; -; mRNA.
DR   EMBL; BC031870; AAH31870.1; -; mRNA.
DR   CCDS; CCDS8896.1; -. [P23743-1]
DR   PIR; S12969; S12969.
DR   RefSeq; NP_001336.2; NM_001345.5. [P23743-1]
DR   RefSeq; NP_001337962.1; NM_001351033.2. [P23743-1]
DR   RefSeq; NP_001337963.1; NM_001351034.2. [P23743-1]
DR   RefSeq; NP_001400525.1; NM_001413596.1. [P23743-1]
DR   RefSeq; NP_001400526.1; NM_001413597.1. [P23743-1]
DR   RefSeq; NP_001400527.1; NM_001413598.1. [P23743-1]
DR   RefSeq; NP_958852.1; NM_201444.3. [P23743-1]
DR   RefSeq; NP_958853.1; NM_201445.2. [P23743-1]
DR   RefSeq; NP_963848.1; NM_201554.2. [P23743-1]
DR   RefSeq; XP_047284390.1; XM_047428434.1. [P23743-1]
DR   RefSeq; XP_047284391.1; XM_047428435.1. [P23743-1]
DR   RefSeq; XP_054227261.1; XM_054371286.1. [P23743-1]
DR   PDB; 1TUZ; NMR; -; A=1-118.
DR   PDB; 6IIE; X-ray; 2.14 A; A=107-197.
DR   SASBDB; P23743; -.
DR   BMRB; P23743; -.
DR   SMR; P23743; -.
DR   BioGRID; 107976; 38.
DR   IntAct; P23743; 10.
DR   STRING; 9606.ENSP00000377703; -.
DR   NDEx; IQUERY-CP-DGKA; 2 NDEx IQuery Curated Pathways.
DR   BindingDB; P23743; -.
DR   ChEMBL; CHEMBL4105787; -.
DR   DrugBank; DB14001; alpha-Tocopherol succinate.
DR   DrugBank; DB00163; Vitamin E.
DR   GuidetoPHARMACOLOGY; 3256; -.
DR   SwissLipids; SLP:000000555; -.
DR   SwissLipids; SLP:000000739; -.
DR   GlyGen; P23743; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P23743; -.
DR   PhosphoSitePlus; P23743; -.
DR   MetOSite; P23743; -.
DR   BioMuta; DGKA; -.
DR   DMDM; 281185505; -.
DR   PaxDb; 9606-ENSP00000377703; -.
DR   PeptideAtlas; P23743; -.
DR   ProteomicsDB; 54146; -. [P23743-1]
DR   ProteomicsDB; 54147; -. [P23743-2]
DR   Pumba; P23743; -.
DR   jPOST; P23743; -.
DR   MassIVE; P23743; -.
DR   DNASU; 1606; -.
DR   Ensembl; ENST00000331886.10; ENSP00000328405.5; ENSG00000065357.21. [P23743-1]
DR   Ensembl; ENST00000394147.5; ENSP00000377703.1; ENSG00000065357.21. [P23743-1]
DR   Ensembl; ENST00000402956.7; ENSP00000385792.3; ENSG00000065357.21. [P23743-3]
DR   Ensembl; ENST00000548549.5; ENSP00000448565.1; ENSG00000065357.21. [P23743-2]
DR   Ensembl; ENST00000551156.5; ENSP00000450359.1; ENSG00000065357.21. [P23743-1]
DR   Ensembl; ENST00000553084.5; ENSP00000446605.1; ENSG00000065357.21. [P23743-2]
DR   GeneID; 1606; -.
DR   KEGG; hsa:1606; -.
DR   MANE-Select; ENST00000331886.10; ENSP00000328405.5; NM_001345.5; NP_001336.2.
DR   UCSC; uc001sij.4; human. [P23743-1]
DR   CTD; 1606; -.
DR   DisGeNET; 1606; -.
DR   VEuPathDB; HostDB:ENSG00000065357; -.
DR   GeneCards; DGKA; -.
DR   HGNC; HGNC:2849; DGKA.
DR   AGR; HGNC:2849; -.
DR   HPA; ENSG00000065357; Tissue enhanced (lymphoid).
DR   MIM; 125855; gene.
DR   OpenTargets; ENSG00000065357; -.
DR   ClinPGx; PA27310; -.
DR   eggNOG; KOG1169; Eukaryota.
DR   GeneTree; ENSGT00940000157144; -.
DR   HOGENOM; CLU_059202_0_0_1; -.
DR   InParanoid; P23743; -.
DR   OMA; ACAMAKF; -.
DR   OrthoDB; 242257at2759; -.
DR   PhylomeDB; P23743; -.
DR   BRENDA; 2.7.1.107; 2681.
DR   Reactome; R-HSA-114508; Effects of PIP2 hydrolysis.
DR   SABIO-RK; P23743; -.
DR   SignaLink; P23743; -.
DR   SIGNOR; P23743; -.
DR   UniPathway; UPA00230; -.
DR   ChiTaRS; DGKA; human.
DR   EvolutionaryTrace; P23743; -.
DR   Agora; ENSG00000065357; -.
DR   GeneWiki; DGKA; -.
DR   GenomeRNAi; 1606; -.
DR   PRO; PR:P23743; -.
DR   Bgee; ENSG00000065357; Expressed in lower esophagus mucosa and 180 other cell types or tissues.
DR   ExpressionAtlas; P23743; baseline and differential.
DR   CDD; cd20799; C1_DGK_typeI_rpt1; 1.
DR   CDD; cd20890; C1_DGKalpha_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:000004; Diacylglycerol kinase; 1.
DR   FunFam; 2.60.200.40:FF:000003; Diacylglycerol kinase; 1.
DR   FunFam; 3.30.60.20:FF:000039; Diacylglycerol kinase; 1.
DR   FunFam; 3.30.60.20:FF:000047; Diacylglycerol kinase; 1.
DR   FunFam; 3.40.50.10330:FF:000003; Diacylglycerol kinase; 1.
DR   Gene3D; 2.60.200.40; -; 1.
DR   Gene3D; 3.30.60.20; -; 2.
DR   Gene3D; 1.10.238.110; Diacylglycerol kinase alpha; 1.
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; IPR047469; C1_DGKalpha_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:SF38; DIACYLGLYCEROL KINASE ALPHA; 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   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:0005829; C:cytosol; IDA:UniProtKB.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0047620; F:acylglycerol kinase activity; IEA:RHEA.
DR   GO; GO:0047649; F:alkylglycerol kinase activity; IEA:UniProtKB-EC.
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:0016301; F:kinase activity; IDA:BHF-UCL.
DR   GO; GO:0008289; F:lipid binding; IDA:BHF-UCL.
DR   GO; GO:0046339; P:diacylglycerol metabolic process; IDA:UniProtKB.
DR   GO; GO:0046486; P:glycerolipid metabolic process; IDA:BHF-UCL.
DR   GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR   GO; GO:0046834; P:lipid phosphorylation; IDA:UniProtKB.
DR   GO; GO:0006654; P:phosphatidic acid biosynthetic process; IDA:UniProtKB.
DR   GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; IEA:InterPro.
DR   GO; GO:0030168; P:platelet activation; TAS:Reactome.
DR   Proteomes; UP000005640; Chromosome 12.
DR   PathwayCommons; P23743; -.
DR   Pharos; P23743; Tbio.
DR   Antibodypedia; 27785; 529 antibodies from 36 providers.
DR   RNAct; P23743; protein.
DR   BioGRID-ORCS; 1606; 26 hits in 1162 CRISPR screens.
DR   AlphaFoldDB; P23743; -.
DR   FunCoup; P23743; 734.
DR   PAN-GO; P23743; 5 GO annotations based on evolutionary models.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; ATP-binding; Calcium;
KW   Cytoplasm; Kinase; Lipid metabolism; Metal-binding; Nucleotide-binding;
KW   Proteomics identification; Reference proteome; Repeat; Transferase; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..735
FT                   /note="Diacylglycerol kinase alpha"
FT                   /id="PRO_0000218453"
FT   DOMAIN          110..145
FT                   /note="EF-hand 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          155..190
FT                   /note="EF-hand 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          372..506
FT                   /note="DAGKc"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT   ZN_FING         205..253
FT                   /note="Phorbol-ester/DAG-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT   ZN_FING         269..319
FT                   /note="Phorbol-ester/DAG-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
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                   ECO:0000269|PubMed:30653270"
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                   ECO:0000269|PubMed:30653270"
FT   BINDING         127
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT                   ECO:0000269|PubMed:30653270"
FT   BINDING         134
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT                   ECO:0000269|PubMed:30653270"
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                   ECO:0000269|PubMed:30653270"
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                   ECO:0000269|PubMed:30653270"
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                   ECO:0000269|PubMed:30653270"
FT   BINDING         174
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT                   ECO:0000269|PubMed:30653270"
FT   BINDING         179
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT                   ECO:0000269|PubMed:30653270"
FT   MOD_RES         484
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   VAR_SEQ         117..118
FT                   /note="FT -> WS (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.2"
FT                   /id="VSP_032212"
FT   VAR_SEQ         119..735
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.2"
FT                   /id="VSP_032213"
FT   VAR_SEQ         237..247
FT                   /note="LCKYTVHDQCA -> RPITCVGARRL (in isoform 3)"
FT                   /evidence="ECO:0000303|Ref.3"
FT                   /id="VSP_047702"
FT   VAR_SEQ         248..735
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|Ref.3"
FT                   /id="VSP_047703"
FT   VARIANT         538
FT                   /note="H -> Y (in dbSNP:rs17852990)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_031563"
FT   MUTAGEN         134
FT                   /note="E->Q: Binds calcium but with decreased affinity."
FT                   /evidence="ECO:0000269|PubMed:30653270"
FT   MUTAGEN         179
FT                   /note="E->Q: Loss of calcium-binding."
FT                   /evidence="ECO:0000269|PubMed:30653270"
FT   CONFLICT        339
FT                   /note="L -> P (in Ref. 2; AAC34804)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        379
FT                   /note="V -> L (in Ref. 2; AAC34802)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        385
FT                   /note="S -> W (in Ref. 2; AAC34802)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        684
FT                   /note="E -> G (in Ref. 2; AAC34803)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        699
FT                   /note="G -> V (in Ref. 1; CAA44396)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        715
FT                   /note="N -> K (in Ref. 2; AAC34803)"
FT                   /evidence="ECO:0000305"
FT   HELIX           10..22
FT                   /evidence="ECO:0007829|PDB:1TUZ"
FT   HELIX           27..35
FT                   /evidence="ECO:0007829|PDB:1TUZ"
FT   HELIX           38..42
FT                   /evidence="ECO:0007829|PDB:1TUZ"
FT   HELIX           50..60
FT                   /evidence="ECO:0007829|PDB:1TUZ"
FT   HELIX           68..77
FT                   /evidence="ECO:0007829|PDB:1TUZ"
FT   HELIX           96..107
FT                   /evidence="ECO:0007829|PDB:1TUZ"
FT   HELIX           112..122
FT                   /evidence="ECO:0007829|PDB:6IIE"
FT   STRAND          127..130
FT                   /evidence="ECO:0007829|PDB:6IIE"
FT   HELIX           132..148
FT                   /evidence="ECO:0007829|PDB:6IIE"
FT   TURN            154..156
FT                   /evidence="ECO:0007829|PDB:6IIE"
FT   HELIX           157..167
FT                   /evidence="ECO:0007829|PDB:6IIE"
FT   STRAND          173..176
FT                   /evidence="ECO:0007829|PDB:6IIE"
FT   HELIX           177..186
FT                   /evidence="ECO:0007829|PDB:6IIE"
FT   HELIX           190..193
FT                   /evidence="ECO:0007829|PDB:6IIE"
SQ   SEQUENCE   735 AA;  82630 MW;  ACAA0AD186EE64A0 CRC64;
     MAKERGLISP SDFAQLQKYM EYSTKKVSDV LKLFEDGEMA KYVQGDAIGY EGFQQFLKIY
     LEVDNVPRHL SLALFQSFET GHCLNETNVT KDVVCLNDVS CYFSLLEGGR PEDKLEFTFK
     LYDTDRNGIL DSSEVDKIIL QMMRVAEYLD WDVSELRPIL QEMMKEIDYD GSGSVSQAEW
     VRAGATTVPL LVLLGLEMTL KDDGQHMWRP KRFPRPVYCN LCESSIGLGK QGLSCNLCKY
     TVHDQCAMKA LPCEVSTYAK SRKDIGVQSH VWVRGGCESG RCDRCQKKIR IYHSLTGLHC
     VWCHLEIHDD CLQAVGHECD CGLLRDHILP PSSIYPSVLA SGPDRKNSKT SQKTMDDLNL
     STSEALRIDP VPNTHPLLVF VNPKSGGKQG QRVLWKFQYI LNPRQVFNLL KDGPEIGLRL
     FKDVPDSRIL VCGGDGTVGW ILETIDKANL PVLPPVAVLP LGTGNDLARC LRWGGGYEGQ
     NLAKILKDLE MSKVVHMDRW SVEVIPQQTE EKSDPVPFQI INNYFSIGVD ASIAHRFHIM
     REKYPEKFNS RMKNKLWYFE FATSESIFST CKKLEESLTV EICGKPLDLS NLSLEGIAVL
     NIPSMHGGSN LWGDTRRPHG DIYGINQALG ATAKVITDPD ILKTCVPDLS DKRLEVVGLE
     GAIEMGQIYT KLKNAGRRLA KCSEITFHTT KTLPMQIDGE PWMQTPCTIK ITHKNQMPML
     MGPPPRSTNF FGFLS
//