ID G3P3G7_GASAC Unreviewed; 1135 AA.
AC G3P3G7;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
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=DGKH {ECO:0000313|Ensembl:ENSGACP00000012140.1};
OS Gasterosteus aculeatus (Three-spined stickleback).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae;
OC Gasterosteus.
OX NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000012140.1, ECO:0000313|Proteomes:UP000007635};
RN [1] {ECO:0000313|Ensembl:ENSGACP00000012140.1, ECO:0000313|Proteomes:UP000007635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGACP00000012140.1}
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; G3P3G7; -.
DR STRING; 69293.ENSGACP00000012140; -.
DR Ensembl; ENSGACT00000012164.1; ENSGACP00000012140.1; ENSGACG00000009197.1.
DR eggNOG; KOG1170; Eukaryota.
DR GeneTree; ENSGT00940000158106; -.
DR InParanoid; G3P3G7; -.
DR OMA; VEGNLAM; -.
DR TreeFam; TF313104; -.
DR UniPathway; UPA00230; -.
DR Proteomes; UP000007635; Unassembled WGS sequence.
DR Bgee; ENSGACG00000009197; Expressed in telencephalon and 2 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: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; cd20894; C1_DGKeta_rpt2; 1.
DR Gene3D; 2.60.200.40; -; 1.
DR Gene3D; 3.30.60.20; -; 2.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR017438; ATP-NAD_kinase_N.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR047480; C1_DGKeta_rpt2.
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; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR PANTHER; PTHR11255; DIACYLGLYCEROL KINASE; 1.
DR PANTHER; PTHR11255:SF37; DIACYLGLYCEROL KINASE ETA; 1.
DR Pfam; PF00130; C1_1; 2.
DR Pfam; PF00609; DAGK_acc; 1.
DR Pfam; PF00781; DAGK_cat; 1.
DR Pfam; PF00169; PH; 1.
DR SMART; SM00109; C1; 2.
DR SMART; SM00045; DAGKa; 1.
DR SMART; SM00046; DAGKc; 1.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 2.
DR SUPFAM; SSF111331; NAD kinase/diacylglycerol kinase-like; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS50146; DAGK; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
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|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU361128};
KW Coiled coil {ECO:0000256|SAM:Coils};
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:UP000007635};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361128};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 54..177
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 165..215
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 237..288
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 319..454
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 638..667
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1107..1135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 590..617
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1114..1135
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1135 AA; 124965 MW; 81A6C9B6B7BC738E CRC64;
EKGPASAAGI HAHAVGPVAG PGAADESSDS DAEQEGAQKL IRKVSTSGQI RSKTSIKEGL
LLKQTSSFQR WKKRYFKLRG RTLYYAKDAK SLIFDEVDLS DASVAESSTK NVNNSFTFIQ
WRRRLNTHAH NRTRWEDGRG GGGGVGFPKP KEPTAQFNVE HFSGMHNWYA CSHARPTFCN
VCKDSLSGVT SHGLSCEVCK FKAHKRCAVR ATNNCKWTTL ASIGKDIIED EDGIAMPHQW
LEGNLPVSAK CAVCDKTCGS VLRLQDWRCL WCKAMVHTAC MDLYPRKCPL GQCKVSIIPP
TALNSIDSDG FWKATCPPSC ASPLLVFVNS KSGDNQGVKF LRRFKQLLNP AQVFDLVNGG
PHLGLRLFQK FDNFRILVCG GDGSVGWVLS EIDKLSLHKQ CQLGVLPLGT GNDLARVLGW
GPSCDDDTQL PQILEKLERA STKMLDRWSI MTYEIKIPPK LSCPTTPEGP EDCQFHISAY
EDSVAAHLTK ILNSEQNSVV ISSAKILCET VKDFVSKVGK SYEKSTDNSD ECDTMSLKCA
VLNEKLDSLL QTLNSESRAL PSLAHSTPPI SEESLTERCG GAPHQLFKSR EHLMLRANSL
KKALRQIIEQ TERADEEVSV KPSSFVSSPC FLSSPPPSFY PGRKSPKSPA AKSPCSPTER
RVSRSTQSYS SFTITPFTTS KENLPVLNTR IICPAGLRAG LAASIAGSSI ISKMLLANID
PFGATPFIDP DLDSLDGYME KCVMNNYFGI GLDAKISLEF NNKREEHPEK CRKLYKSMMW
NGLLGKKEPL ARTCKGSRGP ANAQCDGQYI PLPSLQGIAV LNIPSYAGGT NFWGGTKEDD
IFCAPSFDDK ILEVVAVFGS MQMAVSRVIK LQHHRIAQCR TVKITILGDE GVPIQVDGEA
WIQPPGVIKI QHKNRAQMLT RDRAFENTLK SWEDKLKYDK PPLRPHLYPQ QSVDLATEEE
AAMVQLCARA AEELITRICE AAKTNGLLEQ ELAHAVNASS HAINKTHPKF PESLTRNTAM
EVASTVKALY YETESLLLGR VSLQLDPPEE DQLSGALQSL ELELAKLGEV AWLYHILQPN
DEEDLSLGYG KRNSRSSMFR IVPKFKKEKA AKKTSPQSGS GDIESGSYEE NSPGN
//
