ID A0A0P7TQZ3_SCLFO Unreviewed; 718 AA.
AC A0A0P7TQZ3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
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};
DE Flags: Fragment;
GN ORFNames=Z043_121801 {ECO:0000313|EMBL:KPP60214.1};
OS Scleropages formosus (Asian bonytongue) (Osteoglossum formosum).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC Osteoglossomorpha; Osteoglossiformes; Osteoglossidae; Scleropages.
OX NCBI_TaxID=113540 {ECO:0000313|EMBL:KPP60214.1, ECO:0000313|Proteomes:UP000034805};
RN [1] {ECO:0000313|EMBL:KPP60214.1, ECO:0000313|Proteomes:UP000034805}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Aro1 {ECO:0000313|EMBL:KPP60214.1};
RA Tan M.H., Gan H.M., Croft L.J., Austin C.M.;
RT "The genome of the Asian arowana (Scleropages formosus).";
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KPP60214.1}.
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DR EMBL; JARO02011016; KPP60214.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P7TQZ3; -.
DR STRING; 113540.ENSSFOP00015056823; -.
DR UniPathway; UPA00230; -.
DR Proteomes; UP000034805; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
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 CDD; cd00051; EFh; 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; 1.
DR Pfam; PF14513; DAG_kinase_N; 2.
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:UP000034805};
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 147..182
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 192..227
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 241..291
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 306..352
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 373..502
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
FT NON_TER 718
FT /evidence="ECO:0000313|EMBL:KPP60214.1"
SQ SEQUENCE 718 AA; 79995 MW; 7CBDEB328494E22D CRC64;
MPRFLDLVLS LSLADRALPP VPSSGTMSSA THTDLKKVKD LSPVDFIQLQ QYMDYSSMKV
KDVMKEFESD GKLAQHRHGE KITEEGFYLF LKTYLDVEDL PMDLCQRLFH SFLNCGQLSS
DSTALTTEQA IFLKDVSCYF SLLEDGQPRD KLEYSFKLYD KDGNGILDSK EVDRIITQMM
NAADYLGWDV TELRPVLEDM MVAMDVDKSG TVSLEEWLNG GLNNTPLLVL LGLKATETDG
QHLWRMKNFK KPVYCNVCEN MLLGLYKQGL CCTYCKCIVH GRCANKNPSP CIHSYVKSKQ
DIGVPAHAWV SGNISGKCDS CHKKVKSHTG QHCRWCQVKC HNECMSEEPT GCSCGPLRDH
ILPPWAIKII PVPGTHPLLV FVNPKSGGKQ GKRVLRKFQY LLNPRQVFNL SNGGPGPGDV
KDFRILVCGG DGTVGWVLDA IDKANLPVRP PVAVLPLGTG NDLARCLRWG GGYDGTDLTL
ILKEIEAGSS VLMDRWSVQV IPEDSQEEGD PVPYEIINNY FSVGVDASIA HRFHTMREKY
PQRFNSRTKN KLRYLEFATS ETISASCRKL KECLTIECCG TPLDLSNLSL EGIAVVNIPS
MHGGSNLWGE PKKVDSKELA DLEPQEVILN YKELKVSAQD LSDKRLEIVG LEGAIAMGQI
YTGLKSAGHR LAKTSQITIR YTDLQPMLNH IAAYIHITHK NQANMLMGPT TKSSFFSN
//
