ID   DGK3_ARATH              Reviewed;         488 AA.
AC   Q8VZG1; Q9ZV46;
DT   01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=Diacylglycerol kinase 3;
DE            Short=AtDGK3;
DE            Short=DAG kinase 3;
DE            EC=2.7.1.107;
DE   AltName: Full=Diglyceride kinase 3;
DE            Short=DGK 3;
GN   Name=DGK3; OrderedLocusNames=At2g18730; ORFNames=MSF3.11;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
CC   -!- FUNCTION: Phosphorylates the second messenger diacylglycerol (DAG) to
CC       generate phosphatidic acid (PA), another important signaling molecule.
CC       PA is required for plant development and responses to abiotic stress
CC       and pathogen attack. May be involved in the accumulation of PA during
CC       cold stress (By similarity). {ECO:0000250}.
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   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q8VZG1; Q39026: MPK6; NbExp=4; IntAct=EBI-4441630, EBI-349548;
CC   -!- SIMILARITY: Belongs to the eukaryotic diacylglycerol kinase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD08942.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AC005724; AAD08942.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002685; AEC06799.1; -; Genomic_DNA.
DR   EMBL; AY064982; AAL57635.1; -; mRNA.
DR   EMBL; AY141990; AAM98254.1; -; mRNA.
DR   PIR; H84567; H84567.
DR   RefSeq; NP_849980.1; NM_179649.4.
DR   AlphaFoldDB; Q8VZG1; -.
DR   BioGRID; 1745; 7.
DR   IntAct; Q8VZG1; 7.
DR   STRING; 3702.AT2G18730.1; -.
DR   iPTMnet; Q8VZG1; -.
DR   SwissPalm; Q8VZG1; -.
DR   PaxDb; Q8VZG1; -.
DR   PRIDE; Q8VZG1; -.
DR   ProteomicsDB; 224037; -.
DR   EnsemblPlants; AT2G18730.1; AT2G18730.1; AT2G18730.
DR   GeneID; 816388; -.
DR   Gramene; AT2G18730.1; AT2G18730.1; AT2G18730.
DR   KEGG; ath:AT2G18730; -.
DR   Araport; AT2G18730; -.
DR   TAIR; locus:2053978; AT2G18730.
DR   eggNOG; KOG1169; Eukaryota.
DR   HOGENOM; CLU_002706_46_3_1; -.
DR   InParanoid; Q8VZG1; -.
DR   OMA; LMMPEYL; -.
DR   OrthoDB; 633642at2759; -.
DR   PhylomeDB; Q8VZG1; -.
DR   BioCyc; ARA:AT2G18730-MON; -.
DR   PRO; PR:Q8VZG1; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q8VZG1; baseline and differential.
DR   Genevisible; Q8VZG1; AT.
DR   GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004143; F:diacylglycerol kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003951; F:NAD+ kinase activity; IEA:InterPro.
DR   GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
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   Gene3D; 3.40.50.10330; -; 1.
DR   InterPro; IPR017438; ATP-NAD_kinase_N.
DR   InterPro; IPR037607; DGK.
DR   InterPro; IPR000756; Diacylglycerol_kin_accessory.
DR   InterPro; IPR001206; Diacylglycerol_kinase_cat_dom.
DR   InterPro; IPR016961; Diacylglycerol_kinase_pln.
DR   InterPro; IPR016064; NAD/diacylglycerol_kinase_sf.
DR   PANTHER; PTHR11255; PTHR11255; 1.
DR   Pfam; PF00609; DAGK_acc; 1.
DR   Pfam; PF00781; DAGK_cat; 1.
DR   PIRSF; PIRSF030829; Diacylglycerol_kinase_pln; 1.
DR   SMART; SM00045; DAGKa; 1.
DR   SMART; SM00046; DAGKc; 1.
DR   SUPFAM; SSF111331; SSF111331; 1.
DR   PROSITE; PS50146; DAGK; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Kinase; Nucleotide-binding; Plant defense; Reference proteome;
KW   Stress response; Transferase.
FT   CHAIN           1..488
FT                   /note="Diacylglycerol kinase 3"
FT                   /id="PRO_0000422111"
FT   DOMAIN          87..245
FT                   /note="DAGKc"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   488 AA;  53881 MW;  126012C84473CA3F CRC64;
     MDSPVSKTDA SKEKFVASRP STADSKTMRG CGLANLAWVG VDKVELRQRL MMPEYLRLAM
     RDCIKRKDSS AIPDHLLLPG GAVADMAPHA PMVVFINPNS GGRHGPVLKE RLQQLMSEEQ
     VFDLTEVKPH EFVRYGLGCL EKVAAEGDEC AKECRARLRI MVAGGDGTVG WVLGCLGELN
     KDGKSQIPPV GVIPLGTGND LSRSFGWGGS FPFAWRSAVK RTLHRASMGP VARLDSWKIL
     VSMPSGEVVD PPYSLKPAEE NELDQGLDAG IDAPPLAKAY EGVFYNYLSI GMDAQVAYGF
     HHLRNTKPYL AQGPISNKII YSSFGCSQGW FCTPCVNDPG LRGLRNIMKI HIKKVNCSQW
     EEIAVPKNVR SIVALNLHSY GSGSHPWGNL KPDYLEKRGF VEAHCDDGLI EIFGFKQGWH
     ASFVMAELIS AKHIAQAAAV RFELRGGDWR DAFLQMDGEP WKQPMSTEYS TFVEIKKVPY
     QSLMINNE