DGK1_ARATH
ID DGK1_ARATH Reviewed; 728 AA.
AC Q39017; Q9SD92;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 27-MAR-2002, sequence version 2.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Diacylglycerol kinase 1;
DE Short=AtDGK1;
DE Short=DAG kinase 1;
DE EC=2.7.1.107;
DE AltName: Full=Diglyceride kinase 1;
DE Short=DGK 1;
GN Name=DGK1; OrderedLocusNames=At5g07920; ORFNames=F13G24.120, MXM12.16;
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], AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=8605313; DOI=10.1007/bf00049339;
RA Katagiri T., Mizoguchi T., Shinozaki K.;
RT "Molecular cloning of a cDNA encoding diacylglycerol kinase (DGK) in
RT Arabidopsis thaliana.";
RL Plant Mol. Biol. 30:647-653(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [3]
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 [4]
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 [5]
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 [6]
RP INDUCTION.
RX PubMed=15879447; DOI=10.1093/pcp/pci122;
RA Kishimoto K., Matsui K., Ozawa R., Takabayashi J.;
RT "Volatile C6-aldehydes and allo-ocimene activate defense genes and induce
RT resistance against Botrytis cinerea in Arabidopsis thaliana.";
RL Plant Cell Physiol. 46:1093-1102(2005).
RN [7]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-491 AND LYS-500, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT "Multidimensional protein identification technology (MudPIT) analysis of
RT ubiquitinated proteins in plants.";
RL Mol. Cell. Proteomics 6:601-610(2007).
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, shoots, and leaves.
CC {ECO:0000269|PubMed:8605313}.
CC -!- INDUCTION: By volatile C6-aldehydes ((E)-2-hexenal, (Z)-3-hexenal, (Z)-
CC 3-hexenol), and allo-ocimene. {ECO:0000269|PubMed:15879447}.
CC -!- MISCELLANEOUS: Treatment with (E)-2-hexenal, (Z)-3-hexenal and allo-
CC ocimene increases plant resistance against the necrotrophic fungal
CC pathogen Botrytis cinerea. {ECO:0000305|PubMed:15879447}.
CC -!- SIMILARITY: Belongs to the eukaryotic diacylglycerol kinase family.
CC {ECO:0000305}.
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DR EMBL; D63787; BAA09856.1; -; mRNA.
DR EMBL; AL133421; CAB62604.1; -; Genomic_DNA.
DR EMBL; AB005249; BAB09956.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91221.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM69404.1; -; Genomic_DNA.
DR EMBL; BT004148; AAO42169.1; -; mRNA.
DR PIR; S71467; S71467.
DR RefSeq; NP_001331085.1; NM_001342968.1.
DR RefSeq; NP_196409.1; NM_120874.3.
DR AlphaFoldDB; Q39017; -.
DR STRING; 3702.AT5G07920.1; -.
DR iPTMnet; Q39017; -.
DR PaxDb; Q39017; -.
DR PRIDE; Q39017; -.
DR ProteomicsDB; 224052; -.
DR EnsemblPlants; AT5G07920.1; AT5G07920.1; AT5G07920.
DR EnsemblPlants; AT5G07920.3; AT5G07920.3; AT5G07920.
DR GeneID; 830686; -.
DR Gramene; AT5G07920.1; AT5G07920.1; AT5G07920.
DR Gramene; AT5G07920.3; AT5G07920.3; AT5G07920.
DR KEGG; ath:AT5G07920; -.
DR Araport; AT5G07920; -.
DR TAIR; locus:2142788; AT5G07920.
DR eggNOG; KOG1169; Eukaryota.
DR HOGENOM; CLU_003770_2_0_1; -.
DR InParanoid; Q39017; -.
DR OrthoDB; 1275907at2759; -.
DR PhylomeDB; Q39017; -.
DR BioCyc; ARA:AT5G07920-MON; -.
DR PRO; PR:Q39017; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q39017; baseline and differential.
DR Genevisible; Q39017; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; ISS:TAIR.
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 CDD; cd00029; C1; 2.
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 ATP-binding; Isopeptide bond; Kinase; Membrane; Metal-binding;
KW Nucleotide-binding; Plant defense; Reference proteome; Repeat;
KW Stress response; Transferase; Transmembrane; Transmembrane helix;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..728
FT /note="Diacylglycerol kinase 1"
FT /id="PRO_0000218475"
FT TRANSMEM 27..48
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 357..496
FT /note="DAGKc"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT ZN_FING 79..137
FT /note="Phorbol-ester/DAG-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT ZN_FING 149..212
FT /note="Phorbol-ester/DAG-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 265..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 308..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 319..333
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 491
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:17272265"
FT CROSSLNK 500
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:17272265"
FT CONFLICT 509
FT /note="N -> T (in Ref. 1; BAA09856)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 728 AA; 79984 MW; 9E3190721C083DE9 CRC64;
MDDDGELGMF FPSWTSKNPI DTVESRGLMF SCFVAALVGI LTIAYTAFQW RRNINLSWTK
AIARSKKNPK ARHKVPVAPH SWELDPIARA KNLNCCVCLK SMSPSQAIVA SESFFHRCTI
CGAAAHFNCS SSAPKDCKCV SMVGFEHVVH QWAVRWTEGA DQTDDSSFCS YCDESCSSSF
LGGSPIWCCL WCQRLVHVDC HSNMSNETGD ICDLGPLRRL ILCPLYVKEL TRNPSGGFLS
SITHGANELA STALASIRIQ SKKYKQTNET SADTGNSGSN CDESTESTAD TGPTVNGAHA
VLENSISVMN GDSSNGDSDS NGKLEKKPSV KRTGSFGQKE YHALRSKLKY ELADLPSDAR
PLLVFINKKS GAQRGDSLRQ RLHLHLNPVQ VFELSSVQGP EVGLFLFRKV PHFRVLVCGG
DGTAGWVLDA IEKQNFISPP AVAILPAGTG NDLSRVLNWG GGLGSVERQG GLSTVLQNIE
HAAVTVLDRW KVSILNQQGK QLQPPKYMNN YIGVGCDAKV ALEIHNLREE NPERFYSQFM
NKVLYAREGA RSIMDRTFED FPWQVRVEVD GVDIEVPEDA EGILVANIGS YMGGVDLWQN
EDETYENFDP QSMHDKIVEV VSISGTWHLG KLQVGLSRAR RLAQGSAVKI QLCAPLPVQI
DGEPWNQQPC TLTISHHGQA FMLKRAAEEP LGHAAAIITD VLENAETNQV INASQKRTLL
QEMALRLT
