ID I3J9C8_ORENI Unreviewed; 920 AA.
AC I3J9C8;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 2.
DT 24-JAN-2024, entry version 65.
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:ENSONIP00000005468.2};
OS Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000005468.2, ECO:0000313|Proteomes:UP000005207};
RN [1] {ECO:0000313|Proteomes:UP000005207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Broad Institute Genome Assembly Team;
RG Broad Institute Sequencing Platform;
RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Oreochromis niloticus (Nile Tilapia).";
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSONIP00000005468.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUL-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 RefSeq; XP_003447693.1; XM_003447645.4.
DR AlphaFoldDB; I3J9C8; -.
DR STRING; 8128.ENSONIP00000046828; -.
DR Ensembl; ENSONIT00000005472.2; ENSONIP00000005468.2; ENSONIG00000004338.2.
DR GeneID; 100701920; -.
DR KEGG; onl:100701920; -.
DR CTD; 1609; -.
DR eggNOG; KOG1169; Eukaryota.
DR GeneTree; ENSGT00940000159492; -.
DR HOGENOM; CLU_003770_0_0_1; -.
DR OrthoDB; 4642163at2759; -.
DR TreeFam; TF312817; -.
DR UniPathway; UPA00230; -.
DR Proteomes; UP000005207; Linkage group LG2.
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: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; 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; -; 2.
DR InterPro; IPR017438; ATP-NAD_kinase_N.
DR InterPro; IPR046349; C1-like_sf.
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:SF34; 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 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; 2.
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; 2.
DR PROSITE; PS50081; ZF_DAG_PE_2; 3.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU361128};
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 Reference proteome {ECO:0000313|Proteomes:UP000005207};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|RuleBase:RU361128};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 45..93
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 106..153
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 168..219
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 374..473
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT DOMAIN 563..700
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 264..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 889..920
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 901..920
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 920 AA; 101884 MW; 9A0756BAB7641AF7 CRC64;
MADSGRPRPA DPDAAESRTA SPLAGKKRAQ QSPGLRSKYQ SSAPGHCFKK VTLTKPTFCH
SCSDFIWGII GFLCEVCNFM CHEKCLKTLR KVCSSMTPSL VQVPVAHCFG PAGQKKRFCC
VCRKQTEGST ALRCEVCELH VHADCAIFTC ADCRSCHLDG ILEQDTFHHH WREGNLASAA
RCEVCRRSCG SSDVLAGMRC EWCGITSHAA CYLAVPAECT LGRLRCMLLH PACVRLDSRN
FSKMHCYRIA ESCSHELDNS DDGDLSAAAA PASKDGQPAA SESGKQNLKV FDGDDAVKRG
FFRLVSITKN EEVVEAALRA FYLPDDPQDF ELHEIGGLQR LHSDDILNRN GGPDNRNSLK
DGGDSWLLKA KPRVTEVIKV YNDWPRSGVA FISVSVSDSS TTSSVLAEVL SKLDRQEEDL
SKFSLLEVCM SSKQVQRQTL TPQEKLLDKL REIRKVSLRQ MNQTRFYIVE NKNRAVRVEL
LIGGLPPLLT TEKYTQLIEE HLAIKSHLVT ISNFYLNQGA VALQISCFAE AERIYMLAKD
TSINNKTLTS LVIPGITHNT LGEDVCPLLV FVNPKSGGLK GRELLYGFRK LLNPHQVFDI
MNGGPLAGLH TFREVPRFRV LVCGGDGTVG WVLGVLEAVR HKLTCREPPI GIIPLGTGND
LARILRWGPG YSGEDPYHIL VSVYEADEVL MDRWTILLDA QDVSEDGKDN DFLEPPKIVQ
MNNYFGLGID AELSLDFHLA REDEPDKFTS RFHNKGVYVK VGLQKISHTR SLHKELQLHV
DGQEVPLPNI EGLIFLNIPS WGSGADLWGS EVDSRYEKPS IDDGLLEVVG VTGVVHMGQV
QSGFRSGIRI AQGNYIRLTL RKPIPVQVDG EPWIQPPGHI IISAAGPKVR MLRKSKQKQK
KSSANMRDGH SDSPSSRDGH
//