ID   A0A3Q4GML1_NEOBR        Unreviewed;       731 AA.
AC   A0A3Q4GML1;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   02-OCT-2024, entry version 29.
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 (APR-2024) to UniProtKB.
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=1-O-alkyl-sn-glycerol + ATP = 1-O-alkyl-sn-glycero-3-phosphate
CC         + 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|RuleBase:RU361128};
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: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:0046486; P:glycerolipid metabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0007205; P:protein kinase 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   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
//