ID F7DE73_CALJA Unreviewed; 993 AA.
AC F7DE73;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 3.
DT 27-MAR-2024, entry version 70.
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=DGKQ {ECO:0000313|Ensembl:ENSCJAP00000003389.4};
OS Callithrix jacchus (White-tufted-ear marmoset).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Callithrix; Callithrix.
OX NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000003389.4, ECO:0000313|Proteomes:UP000008225};
RN [1] {ECO:0000313|Ensembl:ENSCJAP00000003389.4}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCJAP00000003389.4}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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=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 AlphaFoldDB; F7DE73; -.
DR Ensembl; ENSCJAT00000003577.4; ENSCJAP00000003389.4; ENSCJAG00000001866.5.
DR eggNOG; KOG1169; Eukaryota.
DR GeneTree; ENSGT00940000159492; -.
DR TreeFam; TF312817; -.
DR UniPathway; UPA00230; -.
DR Proteomes; UP000008225; Chromosome 3.
DR Bgee; ENSCJAG00000001866; Expressed in frontal cortex and 6 other cell types or tissues.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046486; P:glycerolipid metabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0030168; P:platelet activation; IEA:UniProt.
DR GO; GO:0007205; P:protein kinase C-activating G protein-coupled receptor signaling pathway; IEA:InterPro.
DR CDD; cd20803; C1_DGKtheta_typeV_rpt1; 1.
DR CDD; cd20804; C1_DGKtheta_typeV_rpt2; 1.
DR CDD; cd20854; C1_DGKtheta_typeV_rpt3; 1.
DR CDD; cd17111; RA1_DAGK-theta; 1.
DR Gene3D; 2.60.200.40; -; 1.
DR Gene3D; 3.30.60.20; -; 3.
DR InterPro; IPR017438; ATP-NAD_kinase_N.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR020454; DAG/PE-bd.
DR InterPro; IPR037607; DGK.
DR InterPro; IPR000756; Diacylglycerol_kin_accessory.
DR InterPro; IPR001206; Diacylglycerol_kinase_cat_dom.
DR InterPro; IPR016064; NAD/diacylglycerol_kinase_sf.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR000159; RA_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR11255; DIACYLGLYCEROL KINASE; 1.
DR PANTHER; PTHR11255:SF54; DIACYLGLYCEROL KINASE THETA; 1.
DR Pfam; PF00130; C1_1; 2.
DR Pfam; PF00609; DAGK_acc; 1.
DR Pfam; PF00781; DAGK_cat; 1.
DR Pfam; PF00788; RA; 1.
DR PRINTS; PR00008; DAGPEDOMAIN.
DR SMART; SM00109; C1; 3.
DR SMART; SM00045; DAGKa; 1.
DR SMART; SM00046; DAGKc; 1.
DR SMART; SM00314; RA; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 3.
DR SUPFAM; SSF111331; NAD kinase/diacylglycerol kinase-like; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS50146; DAGK; 1.
DR PROSITE; PS50200; RA; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 3.
DR PROSITE; PS50081; ZF_DAG_PE_2; 3.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU361128};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU361128};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
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:UP000008225};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361128};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 62..110
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 123..170
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 185..236
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 397..496
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT DOMAIN 586..723
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 917..947
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 924..941
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 993 AA; 106476 MW; 9F96EB61758B8651 CRC64;
MAAAAEPGAR AWLGGGSPRP GSPACSPVLG AGGRARLGPG PGPGPGPERA GARAPGPAAA
PGHSFRKVTL TKPTFCHLCS DFIWGLAGFL CDVCNFMSHE KCLKHVRTPC TSVAPSLVRV
AMAHCFGPRG LYKRKFCGVC RKVLEAPALR CEVCELHLHP DCVPFACSDC RQCHQDGHQD
HDTHHHHWRE GNLPSGARCE VCRKTCGSSD VLAGVRCEWC GVQAHSICSA ALAPECGFGR
LCSLVLPPAC VRLLPGGFSK RQSFRIAEAV EPGEGGDGAD GSAAAGPGRE TLVAPESGKK
MLKIFDGDDA VRRSQFRLIT VPRLASAEEV LEAALRAYHI PEDPGHLELR PLPPSSQACD
AWAGGKAGSA VISEEGRSPG SGEATSEAWV IRALPRAQEV LKIYPGWLKV GVAYVSVRVT
PQSTARSVVL EVLPLLGRQA EGPESFQLVE VAMGCRHVQR TVLAEEQPLL ARLQDIRQMS
IWQLSQTRFY VAESRNVAPH ISLFVGGLPP GLAPKEYSSL LLEAMATEAT MVSVSHVYSS
QGAVVLDVAC FAEAERLYAM LKDTAVRGRP LTALVLPDLL HSRLPPDSRP LLVFVNPKSG
GLKGRDLLCS FRKLLNPHQV FDLTNGGPLP GLHVFSQVPC FRVLVCGGDG TVGWVLSALE
ETRHRLACPE PSVAILPLGT GNDLGRVLRW GAGYSGEDPF SVLLSVDEAD AVLMDRWTIL
LDAHDAGSAE NGTADAEPPK IVQMSNYCGI GIDAELSLDF HQAREEEPGK FTSRLHNKGV
YVRVGLQKIS HSRGLHKEIR LQVEQQEVEL PSIEGLIFIN IPSWGSGADL WGSDNDARFE
KPRMDDGLLE VVGVTGVVHM GQVQGGLRSG IRIAQGSYFR VTLLKATPVQ VDGEPWIQAP
GHMIISAAGP KVHMLRKAKQ KPRRAGTTRD ARVDAAPAPE GDPRDSDGTL ALGGVCLCRK
PPDSLHEKWS QSPCCTLSLW GTAGLGLPFW VWP
//
