ID   DGKA_PIG                Reviewed;         734 AA.
AC   P20192;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   02-SEP-2026, entry version 188.
DE   RecName: Full=Diacylglycerol kinase alpha;
DE            Short=DAG kinase alpha;
DE            EC=2.7.1.107 {ECO:0000269|PubMed:23949095, ECO:0000269|PubMed:8034597, ECO:0000269|PubMed:8809050};
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   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   TISSUE=Lymphocyte;
RX   PubMed=2156169; DOI=10.1038/344345a0;
RA   Sakane F., Yamada K., Kanoh H., Yokoyama C., Tanabe T.;
RT   "Porcine diacylglycerol kinase sequence has zinc finger and E-F hand
RT   motifs.";
RL   Nature 344:345-348(1990).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX   PubMed=8034597; DOI=10.1016/s0021-9258(17)32336-0;
RA   Kai M., Sakane F., Imai S., Wada I., Kanoh H.;
RT   "Molecular cloning of a diacylglycerol kinase isozyme predominantly
RT   expressed in human retina with a truncated and inactive enzyme expression
RT   in most other human cells.";
RL   J. Biol. Chem. 269:18492-18498(1994).
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP   LOCATION, REGION, AND MUTAGENESIS.
RX   PubMed=8809050; DOI=10.1042/bj3180583;
RA   Sakane F., Kai M., Wada I., Imai S., Kanoh H.;
RT   "The C-terminal part of diacylglycerol kinase alpha lacking zinc fingers
RT   serves as a catalytic domain.";
RL   Biochem. J. 318:583-590(1996).
RN   [4]
RP   CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY REGULATION.
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:8034597). 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:8034597). Also plays an important
CC       role in the biosynthesis of complex lipids. Can also phosphorylate 1-
CC       alkyl-2-acylglycerol in vitro as efficiently as diacylglycerol provided
CC       it contains an arachidonoyl group. Also involved in the production of
CC       alkyl-lysophosphatidic acid, another bioactive lipid, through the
CC       phosphorylation of 1-alkyl-2-acetyl glycerol (By similarity).
CC       {ECO:0000250|UniProtKB:P23743, ECO:0000269|PubMed:8034597}.
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:8034597, ECO:0000269|PubMed:8809050};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10273;
CC         Evidence={ECO:0000305|PubMed:8034597};
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:0000250|UniProtKB:P23743};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44073;
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:0000269|PubMed:23949095, ECO:0000269|PubMed:8034597};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40328;
CC         Evidence={ECO:0000305|PubMed:8034597};
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:8034597};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40324;
CC         Evidence={ECO:0000305|PubMed:8034597};
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:8034597};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43429;
CC         Evidence={ECO:0000305|PubMed:8034597};
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:0000269|PubMed:23949095}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.13 mM for ATP (at pH 7.4) {ECO:0000269|PubMed:8809050};
CC         KM=0.1 mM for ATP (at pH 7.4 and 30 degrees Celsius)
CC         {ECO:0000269|PubMed:23949095};
CC   -!- PATHWAY: Lipid metabolism; glycerolipid metabolism.
CC       {ECO:0000305|PubMed:8034597}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P23743}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:8809050}.
CC   -!- SIMILARITY: Belongs to the eukaryotic diacylglycerol kinase family.
CC       {ECO:0000305}.
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DR   EMBL; X53256; CAA37347.1; -; mRNA.
DR   PIR; S09156; S09156.
DR   RefSeq; NP_999197.1; NM_214032.2.
DR   RefSeq; XP_005663934.1; XM_005663877.3.
DR   RefSeq; XP_020946786.1; XM_021091127.1.
DR   AlphaFoldDB; P20192; -.
DR   SMR; P20192; -.
DR   FunCoup; P20192; 518.
DR   STRING; 9823.ENSSSCP00000043702; -.
DR   BindingDB; P20192; -.
DR   ChEMBL; CHEMBL4523195; -.
DR   SwissLipids; SLP:000000924; -.
DR   iPTMnet; P20192; -.
DR   PaxDb; 9823-ENSSSCP00000043702; -.
DR   PeptideAtlas; P20192; -.
DR   Ensembl; ENSSSCT00005020961.1; ENSSSCP00005012568.1; ENSSSCG00005012782.1.
DR   Ensembl; ENSSSCT00015071712.1; ENSSSCP00015028738.1; ENSSSCG00015053448.1.
DR   Ensembl; ENSSSCT00015071920.1; ENSSSCP00015028848.1; ENSSSCG00015053448.1.
DR   Ensembl; ENSSSCT00040003422.1; ENSSSCP00040001033.1; ENSSSCG00040002738.1.
DR   Ensembl; ENSSSCT00040003461.1; ENSSSCP00040001053.1; ENSSSCG00040002738.1.
DR   Ensembl; ENSSSCT00045059915.1; ENSSSCP00045042055.1; ENSSSCG00045034839.1.
DR   Ensembl; ENSSSCT00045060222.1; ENSSSCP00045042289.1; ENSSSCG00045034839.1.
DR   Ensembl; ENSSSCT00055021361.1; ENSSSCP00055016919.1; ENSSSCG00055010666.1.
DR   Ensembl; ENSSSCT00055021423.1; ENSSSCP00055016971.1; ENSSSCG00055010666.1.
DR   Ensembl; ENSSSCT00060098048.1; ENSSSCP00060042504.1; ENSSSCG00060071679.1.
DR   Ensembl; ENSSSCT00060098153.1; ENSSSCP00060042553.1; ENSSSCG00060071679.1.
DR   Ensembl; ENSSSCT00065064046.1; ENSSSCP00065027748.1; ENSSSCG00065046800.1.
DR   Ensembl; ENSSSCT00065064056.1; ENSSSCP00065027755.1; ENSSSCG00065046800.1.
DR   Ensembl; ENSSSCT00085009704; ENSSSCP00085006994; ENSSSCG00085005157.
DR   GeneID; 397097; -.
DR   KEGG; ssc:397097; -.
DR   CTD; 1606; -.
DR   eggNOG; KOG1169; Eukaryota.
DR   HOGENOM; CLU_003770_1_1_1; -.
DR   InParanoid; P20192; -.
DR   OrthoDB; 242257at2759; -.
DR   BRENDA; 2.7.1.107; 6170.
DR   Reactome; R-SSC-114508; Effects of PIP2 hydrolysis.
DR   SABIO-RK; P20192; -.
DR   UniPathway; UPA00230; -.
DR   Proteomes; UP000008227; Unplaced.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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:0046339; P:diacylglycerol metabolic process; IDA:UniProtKB.
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   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   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.
PE   1: Evidence at protein level;
KW   Acetylation; ATP-binding; Calcium; Cytoplasm; Direct protein sequencing;
KW   Kinase; Lipid metabolism; Metal-binding; Nucleotide-binding;
KW   Reference proteome; Repeat; Transferase; Zinc; Zinc-finger.
FT   CHAIN           1..734
FT                   /note="Diacylglycerol kinase alpha"
FT                   /id="PRO_0000218455"
FT   DOMAIN          109..144
FT                   /note="EF-hand 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          154..189
FT                   /note="EF-hand 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          371..505
FT                   /note="DAGKc"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT   ZN_FING         204..252
FT                   /note="Phorbol-ester/DAG-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT   ZN_FING         268..318
FT                   /note="Phorbol-ester/DAG-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT   REGION          358..505
FT                   /note="Necessary and sufficient for the diacylglycerol
FT                   kinase activity"
FT                   /evidence="ECO:0000269|PubMed:8809050"
FT   BINDING         122
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
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         133
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         167
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
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         178
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   MOD_RES         483
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P23743"
FT   MUTAGEN         248
FT                   /note="K->R: No significant effect on diacylglycerol kinase
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:8809050"
FT   MUTAGEN         383
FT                   /note="K->N: No significant effect on diacylglycerol kinase
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:8809050"
FT   MUTAGEN         395
FT                   /note="K->N: No significant effect on diacylglycerol kinase
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:8809050"
FT   MUTAGEN         483
FT                   /note="K->N: No significant effect on diacylglycerol kinase
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:8809050"
FT   MUTAGEN         492
FT                   /note="K->R: No significant effect on diacylglycerol kinase
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:8809050"
FT   MUTAGEN         554
FT                   /note="K->N: No significant effect on diacylglycerol kinase
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:8809050"
SQ   SEQUENCE   734 AA;  82606 MW;  711C2E66FB4B4E80 CRC64;
     MSKERGLISP SDFAQLQKYM EYSTKKVSDV LKLFEDGEMA EYLQGDAIGY EGFQQFLKIY
     LEVDSVPSHL SLALFQSFQT SYCSEETVKR DVVCLSDVSC YFSLLEGGRP EDKLEFTFKL
     YDTDRNGILD SSEVDRIIIQ MMRMAEYLDW DVSELRPILQ EMMKEIDYDG SGSVSLAEWL
     RAGATTVPLL VLLGLEMTLK DNGQHMWRPK RFPRPVYCNL CESSIGLGKQ GLSCNLCKYT
     VHDQCAMKAL PCEVSTYAKS RKDIGVQTHV WVRGGCESGR CDRCQKKIRI YHSLVGLHCV
     WCHLEIHDDC LPAMGHECDC GLLRDHILPP SSIYPSVLAS GQERKVSKTS QKTTDDLNLS
     TSEALRIDPV SNTHPLLVFV NPKSGGKQGE RVLWKFQYLL NPRQVFNLLK DGPEPGLRFF
     REVPDYRILV CGGDGTVGWI LETIDKANLP FVPPVAVLPL GTGNDLARCL RWGGGYEGQN
     LGKILKDLEA SKVVHMDRWS VEVIPQQTEE KSDPVPFQII NNYFSIGVDA SIAHRFHIMR
     EKYPEKFNSR MKNKLWYFEF ATSESIFSTC KKLEESLTVE ICGKPLDLSN LSLEGIAVLN
     IPSTHGGSNL WGDTKRPHGD IHGINQALGA MAKVITDPDI LKTCVPDLSD KRLEVVGLEG
     AIEMGQIYTK LKNAGHRLAK CSEITFHTTK TLPMQIDGEP WMQTPCTIKI THRNQMPMLV
     GPPPRSSNFF GFLC
//