ID   A0A3Q4GML1_NEOBR        Unreviewed;       731 AA.
AC   A0A3Q4GML1;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-NOV-2024, entry version 30.
DE   RecName: Full=Diacylglycerol kinase {ECO:0000256|RuleBase:RU361128};
DE            Short=DAG kinase {ECO:0000256|RuleBase:RU361128};
DE            EC=2.7.1.107 {ECO:0000256|RuleBase:RU361128};
OS   Neolamprologus brichardi (Fairy cichlid) (Lamprologus brichardi).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Lamprologini; Neolamprologus.
OX   NCBI_TaxID=32507 {ECO:0000313|Ensembl:ENSNBRP00000008003.1, ECO:0000313|Proteomes:UP000261580};
RN   [1] {ECO:0000313|Ensembl:ENSNBRP00000008003.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (AUG-2024) to UniProtKB.
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:0000256|ARBA:ARBA00045593}.
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:0000256|ARBA:ARBA00023371};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40328;
CC         Evidence={ECO:0000256|ARBA:ARBA00023371};
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:0000256|ARBA:ARBA00023395};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43429;
CC         Evidence={ECO:0000256|ARBA:ARBA00023395};
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:0000256|ARBA:ARBA00034632};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63325;
CC         Evidence={ECO:0000256|ARBA:ARBA00034632};
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:0000256|ARBA:ARBA00034642};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44073;
CC         Evidence={ECO:0000256|ARBA:ARBA00034642};
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:0000256|ARBA:ARBA00043787};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16938;
CC         Evidence={ECO:0000256|ARBA:ARBA00043787};
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:0000256|ARBA:ARBA00034624};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40404;
CC         Evidence={ECO:0000256|ARBA:ARBA00034624};
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:0000256|ARBA:ARBA00034638};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40408;
CC         Evidence={ECO:0000256|ARBA:ARBA00034638};
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:0000256|ARBA:ARBA00034647};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41677;
CC         Evidence={ECO:0000256|ARBA:ARBA00034647};
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:0000256|ARBA:ARBA00034614};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41673;
CC         Evidence={ECO:0000256|ARBA:ARBA00034614};
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:0000256|ARBA:ARBA00034636};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43417;
CC         Evidence={ECO:0000256|ARBA:ARBA00034636};
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:0000256|ARBA:ARBA00023400};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40324;
CC         Evidence={ECO:0000256|ARBA:ARBA00023400};
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:0000256|ARBA:ARBA00034613};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63329;
CC         Evidence={ECO:0000256|ARBA:ARBA00034613};
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:0000256|ARBA:ARBA00023411};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10273;
CC         Evidence={ECO:0000256|ARBA:ARBA00023411};
CC   -!- PATHWAY: Lipid metabolism; glycerolipid metabolism.
CC       {ECO:0000256|ARBA:ARBA00005175}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000256|ARBA:ARBA00004514}.
CC   -!- SIMILARITY: Belongs to the eukaryotic diacylglycerol kinase family.
CC       {ECO:0000256|ARBA:ARBA00009280, ECO:0000256|RuleBase:RU361128}.
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DR   RefSeq; XP_006794133.1; XM_006794070.1.
DR   AlphaFoldDB; A0A3Q4GML1; -.
DR   STRING; 32507.ENSNBRP00000008003; -.
DR   Ensembl; ENSNBRT00000008226.1; ENSNBRP00000008003.1; ENSNBRG00000006079.1.
DR   GeneID; 102798251; -.
DR   CTD; 724010; -.
DR   GeneTree; ENSGT00940000157144; -.
DR   OMA; KAMPCEV; -.
DR   OrthoDB; 4642163at2759; -.
DR   UniPathway; UPA00230; -.
DR   Proteomes; UP000261580; Unplaced.
DR   Bgee; ENSNBRG00000006079; Expressed in zone of skin and 7 other cell types or tissues.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:TreeGrafter.
DR   GO; GO:0047649; F:alkylglycerol kinase activity; IEA:RHEA.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004143; F:ATP-dependent diacylglycerol kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0046339; P:diacylglycerol metabolic process; IEA:TreeGrafter.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:TreeGrafter.
DR   GO; GO:0046834; P:lipid phosphorylation; IEA:TreeGrafter.
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:000006; Diacylglycerol kinase; 1.
DR   FunFam; 2.60.200.40:FF:000003; Diacylglycerol kinase; 1.
DR   FunFam; 3.30.60.20:FF:000060; 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   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; PE/DAG-bd.
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; 1.
DR   PROSITE; PS50081; ZF_DAG_PE_2; 2.
PE   3: Inferred from homology;
KW   Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU361128};
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU361128};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU361128};
KW   Reference proteome {ECO:0000313|Proteomes:UP000261580};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361128};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          113..148
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   DOMAIN          158..193
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   DOMAIN          207..257
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50081"
FT   DOMAIN          272..322
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50081"
FT   DOMAIN          376..510
FT                   /note="DAGKc"
FT                   /evidence="ECO:0000259|PROSITE:PS50146"
SQ   SEQUENCE   731 AA;  81944 MW;  B0B1B991C30C47E4 CRC64;
     MSSPTNPEVK ELNPVDFIQL QQYIEYNNLK VKDVLREFYA DGSLARHRHG ECINEEGFRL
     FLKTYLEVED FPVDLCQRLF RSFQNSEPGQ EDSTKEVFLK DVSCYFSLLE DGQPRDKLEF
     AFRLYDRDGN GVLDSSEVDR IIAQMMHAAE YLDWDVSELK PVLKDMMTAI DADSSGTVSL
     DEWVQGGMNN VPLLVLLGLK MTQKDGQHLW RMKNFNKPVY CNVCHSMLLG LRKQGLCCTS
     CKYTVHGRCA NKNPAPCART YVKSKKEIGV STHDWVSGNC DSRKCDKCQK KIKSLQGLTG
     KHCVWCHTMR HDQCVDQEST QCTCGLLRDH ILPPWAIYPV IKERPNNVKN GCSGSGDDSE
     LNTTPDGQVL QICPVLNAHP LLVFVNPKSG GKQGERVLRK FQFLLNPRQV YNLSNGGPGP
     GLSFFRNLKE YRILVCGGDG TVGWILDAID KGNLLVRPPV AVLPLGTGND LARCLRWGGG
     YDGEDLNRIL KDIEGSSQVL MDRWSVQVIT DENQEEGDPV PYEIINNYFS IGVDASIAHR
     FHTMREKHPQ KFNSRMKNKL WYFEFATSET ISASCKKLSE NLTIECCGTA LDLSGVSLEG
     VAILNIPSMH GGSNLWGETK KVDTKGLTAQ EEPEVIVNPE ILKVTSQDLS DRRLEVVGLE
     GAMEMGQIYT GLKSAVRLAK TSQITIRTKK ALPMQIDGEP WMQPPCTIQI THKNQACMLM
     GPPAKPSGFF K
//