DGK2_ARATH
ID DGK2_ARATH Reviewed; 712 AA.
AC Q9FFN7; A8MRH8;
DT 01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Diacylglycerol kinase 2 {ECO:0000303|PubMed:14665624};
DE Short=AtDGK2 {ECO:0000303|PubMed:14665624};
DE Short=DAG kinase 2 {ECO:0000305};
DE EC=2.7.1.107 {ECO:0000269|PubMed:14665624};
DE AltName: Full=Diglyceride kinase 2 {ECO:0000305};
DE Short=DGK 2 {ECO:0000305};
GN Name=DGK2 {ECO:0000303|PubMed:14665624};
GN OrderedLocusNames=At5g63770 {ECO:0000312|Araport:AT5G63770};
GN ORFNames=MBK5.25 {ECO:0000312|EMBL:BAB10470.1};
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 [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, AND INDUCTION BY COLD.
RC STRAIN=cv. C24;
RX PubMed=14665624; DOI=10.1074/jbc.m312187200;
RA Gomez-Merino F.C., Brearley C.A., Ornatowska M., Abdel-Haliem M.E.,
RA Zanor M.I., Mueller-Roeber B.;
RT "AtDGK2, a novel diacylglycerol kinase from Arabidopsis thaliana,
RT phosphorylates 1-stearoyl-2-arachidonoyl-sn-glycerol and 1,2-dioleoyl-sn-
RT glycerol and exhibits cold-inducible gene expression.";
RL J. Biol. Chem. 279:8230-8241(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9330910; DOI=10.1093/dnares/4.3.215;
RA Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT features of the 1.6 Mb regions covered by twenty physically assigned P1
RT clones.";
RL DNA Res. 4:215-230(1997).
RN [3]
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 [4]
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).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, AND INDUCTION BY WOUNDING.
RX PubMed=16081412; DOI=10.1074/jbc.m506859200;
RA Gomez-Merino F.C., Arana-Ceballos F.A., Trejo-Tellez L.I., Skirycz A.,
RA Brearley C.A., Doermann P., Mueller-Roeber B.;
RT "Arabidopsis AtDGK7, the smallest member of plant diacylglycerol kinases
RT (DGKs), displays unique biochemical features and saturates at low substrate
RT concentration: the DGK inhibitor R59022 differentially affects AtDGK2 and
RT AtDGK7 activity in vitro and alters plant growth and development.";
RL J. Biol. Chem. 280:34888-34899(2005).
RN [7]
RP FUNCTION.
RX PubMed=23346092; DOI=10.3389/fpls.2013.00001;
RA Arisz S.A., van Wijk R., Roels W., Zhu J.K., Haring M.A., Munnik T.;
RT "Rapid phosphatidic acid accumulation in response to low temperature stress
RT in Arabidopsis is generated through diacylglycerol kinase.";
RL Front. Plant Sci. 4:1-1(2013).
RN [8]
RP FUNCTION.
RX PubMed=29853600; DOI=10.1104/pp.18.00402;
RA Tan W.J., Yang Y.C., Zhou Y., Huang L.P., Xu L., Chen Q.F., Yu L.J.,
RA Xiao S.;
RT "DIACYLGLYCEROL ACYLTRANSFERASE and DIACYLGLYCEROL KINASE modulate
RT triacylglycerol and phosphatidic acid production in the plant response to
RT freezing stress.";
RL Plant Physiol. 177:1303-1318(2018).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=32471859; DOI=10.1105/tpc.20.00251;
RA Angkawijaya A.E., Nguyen V.C., Gunawan F., Nakamura Y.;
RT "A pair of Arabidopsis diacylglycerol kinases essential for gametogenesis
RT and ER phospholipid metabolism in leaves and flowers.";
RL Plant Cell 32:2602-2620(2020).
CC -!- FUNCTION: Phosphorylates the second messenger diacylglycerol (DAG) to
CC generate phosphatidic acid (PA), another important signaling molecule
CC (PubMed:14665624). PA is required for plant development and responses
CC to abiotic stress and pathogen attack (Probable). May be involved in
CC the accumulation of PA during cold stress (Probable). Involved in
CC response to freezing stress by modulating the accumulation of PA
CC (PubMed:29853600). Exhibits high specificity for the unsaturated DAG
CC analogs 1-stearoyl-2-arachidonoyl-sn-glycerol (1,2-SAG) and 1,2-
CC dioleoyl-sn-glycerol (1,2-DOG) (PubMed:14665624, PubMed:16081412).
CC Exhibits high specificity for 1-palmitoyl, 2-oleoyl-sn-glycerol (1,2
CC POG), 1-stearoyl, 2-linoleoyl-sn-glycerol (1,2-SLG) and 1-oleoyl, 2-
CC palmitoyl-sn-glycerol (1,2-OPG) (PubMed:16081412). Has almost no
CC activity toward 1,2-dioctanoyl-sn-glycerol (1,2-DOCG), 1,2-dipalmitoyl-
CC sn-glycerol (1,2-DPG), 1,2-dimyristoyl-sn-glycerol (1,2-DMG) and 1-
CC oleoyl-2-acetyl-sn-glycerol (1,2-OAG) (PubMed:16081412). Functions
CC together with DGK4 in male gametophyte development and biosynthesis of
CC phosphatidylglycerol and phosphatidylinositol in the endoplasmic
CC reticulum (ER) (PubMed:32471859). Involved in PA production for pollen
CC grain growth, as well as leaf and root growth (PubMed:32471859).
CC {ECO:0000269|PubMed:14665624, ECO:0000269|PubMed:16081412,
CC ECO:0000269|PubMed:29853600, ECO:0000269|PubMed:32471859,
CC ECO:0000305|PubMed:14665624, ECO:0000305|PubMed:23346092}.
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:0000269|PubMed:14665624};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10273;
CC Evidence={ECO:0000269|PubMed:14665624};
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:0000269|PubMed:14665624};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40324;
CC Evidence={ECO:0000269|PubMed:14665624};
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:0000269|PubMed:14665624};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40328;
CC Evidence={ECO:0000269|PubMed:14665624};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=125 uM for 1,2-dioleoyl-sn-glycerol {ECO:0000269|PubMed:14665624};
CC Vmax=0.25 pmol/min/ug enzyme toward 1,2-dioleoyl-sn-glycerol
CC {ECO:0000269|PubMed:14665624};
CC pH dependence:
CC Optimum pH is 7.2. {ECO:0000269|PubMed:14665624};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P23743}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000269|PubMed:32471859}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9FFN7-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in rosette and cauline leaves, flowers,
CC siliques and roots. Highly expressed in young leaves and at lower
CC levels in older leaves. In young seedlings, expressed at the root-shoot
CC junction zone and vascular bundles of the cotyledons. In older plants,
CC expressed in root tip, central cylinder, root hair, leaf mesophyll
CC cells and guard cells, sepals, filaments of the anthers, stigma, valves
CC of young and early adult siliques and hilum of seeds.
CC {ECO:0000269|PubMed:14665624}.
CC -!- INDUCTION: Induced by cold stress (PubMed:14665624). Induced by
CC wounding (PubMed:16081412). {ECO:0000269|PubMed:14665624,
CC ECO:0000269|PubMed:16081412}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but the double mutants dgk2 and dgk4 exhibit defective
CC pollen growth and seed development because of non-viable male
CC gametophyte. {ECO:0000269|PubMed:32471859}.
CC -!- SIMILARITY: Belongs to the eukaryotic diacylglycerol kinase family.
CC {ECO:0000305}.
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DR EMBL; AY380783; AAR28755.1; -; mRNA.
DR EMBL; AB005234; BAB10470.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97795.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97796.2; -; Genomic_DNA.
DR EMBL; AY062655; AAL32733.1; -; mRNA.
DR EMBL; BT008792; AAP68231.1; -; mRNA.
DR EMBL; AK228735; BAF00636.1; -; mRNA.
DR RefSeq; NP_001318872.1; NM_001345610.1. [Q9FFN7-1]
DR RefSeq; NP_201182.1; NM_125772.5. [Q9FFN7-1]
DR AlphaFoldDB; Q9FFN7; -.
DR BioGRID; 21739; 2.
DR IntAct; Q9FFN7; 3.
DR STRING; 3702.AT5G63770.1; -.
DR SwissLipids; SLP:000001675; -.
DR iPTMnet; Q9FFN7; -.
DR PaxDb; Q9FFN7; -.
DR PRIDE; Q9FFN7; -.
DR ProteomicsDB; 224035; -. [Q9FFN7-1]
DR EnsemblPlants; AT5G63770.1; AT5G63770.1; AT5G63770. [Q9FFN7-1]
DR EnsemblPlants; AT5G63770.2; AT5G63770.2; AT5G63770. [Q9FFN7-1]
DR GeneID; 836497; -.
DR Gramene; AT5G63770.1; AT5G63770.1; AT5G63770. [Q9FFN7-1]
DR Gramene; AT5G63770.2; AT5G63770.2; AT5G63770. [Q9FFN7-1]
DR KEGG; ath:AT5G63770; -.
DR Araport; AT5G63770; -.
DR TAIR; locus:2160604; AT5G63770.
DR eggNOG; KOG1169; Eukaryota.
DR InParanoid; Q9FFN7; -.
DR OMA; GMMEVFG; -.
DR OrthoDB; 1275907at2759; -.
DR PhylomeDB; Q9FFN7; -.
DR BioCyc; ARA:AT5G63770-MON; -.
DR BioCyc; MetaCyc:AT5G63770-MON; -.
DR BRENDA; 2.7.1.107; 399.
DR SABIO-RK; Q9FFN7; -.
DR PRO; PR:Q9FFN7; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FFN7; baseline and differential.
DR Genevisible; Q9FFN7; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004143; F:diacylglycerol kinase activity; IDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003951; F:NAD+ kinase activity; IEA:InterPro.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0048366; P:leaf development; IMP:TAIR.
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 GO; GO:0009409; P:response to cold; TAS:TAIR.
DR GO; GO:0009611; P:response to wounding; IEP:TAIR.
DR GO; GO:0048364; P:root development; IMP:TAIR.
DR Gene3D; 3.40.50.10330; -; 1.
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 PANTHER; PTHR11255; PTHR11255; 1.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF00609; DAGK_acc; 1.
DR Pfam; PF00781; DAGK_cat; 1.
DR SMART; SM00109; C1; 2.
DR SMART; SM00045; DAGKa; 1.
DR SMART; SM00046; DAGKc; 1.
DR SUPFAM; SSF111331; SSF111331; 1.
DR SUPFAM; SSF57889; SSF57889; 1.
DR PROSITE; PS50146; DAGK; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Endoplasmic reticulum; Kinase;
KW Metal-binding; Nucleotide-binding; Plant defense; Reference proteome;
KW Repeat; Stress response; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..712
FT /note="Diacylglycerol kinase 2"
FT /id="PRO_0000422110"
FT DOMAIN 338..479
FT /note="DAGKc"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT ZN_FING 72..133
FT /note="Phorbol-ester/DAG-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT ZN_FING 145..208
FT /note="Phorbol-ester/DAG-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
SQ SEQUENCE 712 AA; 79405 MW; E1416E8B22836F3E CRC64;
MMEVGFSLIQ WLISSGADSP FIFGWLVTGS VGLLAVIYTF LKWQKKTSLN WVKAAAREKK
KVWKRLRVPL SHHQWTDDYG YGQQPSTCCV CLYSLVPGQN VSNKASLSIP VHRCAVCGVA
AHFYCSSSAA KDCKCVAQAG SDHVRHHWSE RWVNMDDNAD MTAFCFYCDE PCGIPFIEAS
PMWHCLWCQR LIHVKCHMIM SKESGDACDL GSLRRVILSP VHVKLNEANG VDGVLTTIKN
ELASIRGHVR RKRHRGKNGN GQSLNGKLLE DSVSDPVKTV VNGLVVKKLR RDRSIDCLKQ
VSDMPNAKGL QNGIGGHKRN KSAALNFMKK FSLVDLPPDA RPLLVFINAK SGGQLGPFLH
RRLNMLLNPV QVFELGSCQG PDAGLDLCSK VKYFRVLVCG GDGTVAWVLD AIEKRNFESP
PPVAILPLGT GNDLSRVLQW GRGISVVDGQ GSLRTFLQDI DHAAVTMLDR WSVKIVEEST
EKFPAREGHK FMMNYLGIGC DAKVAYEFHM MRQEKPEKFC SQFVNKLRYA KEGARDIMDR
ACADLPWQVW LEVDGKDIEI PKDSEGLIVL NIGSYMGGVD LWQNDYEHDD NFSIQCMHDK
TLEVVCVRGA WHLGKLQVGL SQARRLAQGK VIRIHVSSPF PVQIDGEPFI QQPGCLEITH
HGQVFMLRRA SDEPRGHAAA IMNEVLLDAE CKGVINASQK KVLLQQMALH LS
