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Database: UniProt
Entry: A0A3B3TBM8_9TELE
LinkDB: A0A3B3TBM8_9TELE
Original site: A0A3B3TBM8_9TELE 
ID   A0A3B3TBM8_9TELE        Unreviewed;       683 AA.
AC   A0A3B3TBM8;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 25.
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   Paramormyrops kingsleyae.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC   Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX   NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000039716.1, ECO:0000313|Proteomes:UP000261540};
RN   [1] {ECO:0000313|Ensembl:ENSPKIP00000039716.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) 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-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   AlphaFoldDB; A0A3B3TBM8; -.
DR   Ensembl; ENSPKIT00000020728.1; ENSPKIP00000039716.1; ENSPKIG00000016878.1.
DR   GeneTree; ENSGT00940000157144; -.
DR   UniPathway; UPA00230; -.
DR   Proteomes; UP000261540; Unplaced.
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:0048468; P:cell development; IEA:UniProt.
DR   GO; GO:0046486; P:glycerolipid metabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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   Gene3D; 2.60.200.40; -; 1.
DR   Gene3D; 3.30.60.20; -; 2.
DR   Gene3D; 1.10.238.110; Diacylglycerol kinase alpha; 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; 1.
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   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; 1.
DR   PROSITE; PS50222; EF_HAND_2; 1.
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|RuleBase:RU361128};
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Kinase {ECO:0000256|RuleBase:RU361128};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU361128};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|RuleBase:RU361128};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          136..171
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   DOMAIN          185..235
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50081"
FT   DOMAIN          250..300
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50081"
FT   DOMAIN          325..459
FT                   /note="DAGKc"
FT                   /evidence="ECO:0000259|PROSITE:PS50146"
SQ   SEQUENCE   683 AA;  76453 MW;  B5C4640BE240FC82 CRC64;
     MSLLFKGALI CIHPSPRPEW TCMCLSPSSL SWSLPLPQCI TEEGFRLFLK TLLEVEDFPA
     DLCQRLFRSF QNDEHEHPDG TRPAVCLKDV SCYFSLLEDG QPREKLECES CIGLEVDRII
     AQMMHAADYL GWDVTELRPV LKDMMTAIDS DGNGTVSLDE WIEGGMKNAP LLVLLGLKMT
     QRDGQHLWRM KHFNKPVYCN VCQSMLLGLR KQGLCCTSCR YTVHGRCANK NPAPCTRTYV
     KSKKDTGVSS HDWVSGNCDS GKCDKCQKKI KSSHGLTAKH CVWCHTMRHG ECVNLEPLEC
     SCGLLRDHIL PPWAIYPVIK ISPIPDTHPL LVFVNPKSGG KQGERVLRKF QYLLNPRQVY
     NLSSGGPGPG LHFFRNLLDY RILVCGGDGT VGWILDAIDK ANLVVRPPVA VLPLGTGNDL
     ARCLRWGGGY DGEDLGRILK EIDGSCQVLM DRWSVQVIPE DSQEKGDPVP YEIINNYFSI
     GVDASIAHRF HMMREKHPQK FNSRMKNKLW YFEFATTETI SASCKKLKEC LTIECCGTPL
     DLSSLSLEGI AILNIPSMHG GSNLWGDPKK VDSKSSAERE LPEVIVDPDI LKTSHQDLSD
     KRLEVVGLEG AMEMGQIYTG LKSAGRRLAK TSQITIRTKK ALPMQIDGEP WMQPPCTIHI
     THKNQARMLM APPARSSSFF NLK
//
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