ID A0A2Y9T3W6_PHYMC Unreviewed; 802 AA.
AC A0A2Y9T3W6;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 26.
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};
GN Name=DGKB {ECO:0000313|RefSeq:XP_023985018.1};
OS Physeter macrocephalus (Sperm whale) (Physeter catodon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Physeteridae; Physeter.
OX NCBI_TaxID=9755 {ECO:0000313|Proteomes:UP000248484, ECO:0000313|RefSeq:XP_023985018.1};
RN [1] {ECO:0000313|RefSeq:XP_023985018.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_023985018.1};
RG RefSeq;
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-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=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 -!- SIMILARITY: Belongs to the eukaryotic diacylglycerol kinase family.
CC {ECO:0000256|ARBA:ARBA00009280, ECO:0000256|RuleBase:RU361128}.
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DR RefSeq; XP_023985018.1; XM_024129250.1.
DR AlphaFoldDB; A0A2Y9T3W6; -.
DR UniPathway; UPA00230; -.
DR Proteomes; UP000248484; Chromosome 5.
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: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; cd20845; C1_DGKbeta_rpt1; 1.
DR CDD; cd20891; C1_DGKbeta_rpt2; 1.
DR CDD; cd00051; EFh; 1.
DR Gene3D; 2.60.200.40; -; 2.
DR Gene3D; 3.30.60.20; -; 2.
DR Gene3D; 1.10.238.110; Diacylglycerol kinase alpha; 2.
DR Gene3D; 1.10.238.10; EF-hand; 1.
DR InterPro; IPR017438; ATP-NAD_kinase_N.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR047471; C1_DGKbeta-like_rpt1.
DR InterPro; IPR047470; C1_DGKbeta_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:SF32; DIACYLGLYCEROL KINASE BETA; 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 ATP-binding {ECO:0000256|RuleBase:RU361128};
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Kinase {ECO:0000256|RuleBase:RU361128, ECO:0000313|RefSeq:XP_023985018.1};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU361128};
KW Reference proteome {ECO:0000313|Proteomes:UP000248484};
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 148..183
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 193..228
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 243..293
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 308..357
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 432..566
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
FT REGION 671..693
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 802 AA; 90396 MW; CC91D2C40673FE46 CRC64;
MTNQEKWAHL SPSEFSQLQK YAEYSTKKLK DVLEEFHGNG VLAKYNPEGK QDVLKQTIDF
EGFKLFMKTF LEAELPDDFT THLFMSFSNK FPHSSPMVKS KPALLSGGLR MNKGAITSPR
TSPANTCSPE VIHLKDIVCY LSLLERGRPE DKLEFMFRLY DTDGNGFLDS SELENIISQM
MHVAEYLEWD VTELNPILHE MMEEIDYDHD GTVSLEEWIQ GGMTTIPLLV LLGLENNVKD
DGQHVWRLKH FNKPAYCNLC LNMLIGVGKQ GLCCSFCKYT VHERCVARAP PSCIKTYVKS
KKNTDVMHHY WVEGNCPTKC DKCHKTVKCY QGLTGLHCVW CQITLHNKCA SHLKPECDCG
PLKDHILPPT TICPVVLTLP TSGVSVPEER QATVKKEKGG SQQPNKVIDK NKMQRANSVT
VDGQGLQITP VPGTHPLLVF VNPKSGGKQG ERIYRKFQYL LNPRQVYSLA GNGPMPGLNF
FRDVPDFRVL ACGGDGTVGW ILDCIEKANV VKHPPVAILP LGTGNDLARC LRWGGGYEGE
NLMKILKDIE NSTEIMLDRW KFEVIPNDKD EKGDPVPYSI INNYFSIGVD ASIAHRFHIM
REKHPEKFNS RMKNKFWYFE FGTSETFSAT CKKLHESVEI ECDGVQIDLI NISLEGIAIL
NIPSMHGGSN LWGESKKRRS HRRTEKKGSD KRTTLTDAKE LKFASQDLSD QLLEVVGLEG
AMEMGQIYTG LKSAGRRLAQ CSSVVIRTSK SLPMQIDGEP WMQTPCTIKI MHKNQAPMLM
GPPPKTGLFC SLLKRTRNRS KE
//