DGK7_ARATH
ID DGK7_ARATH Reviewed; 492 AA.
AC F4JQ95; B0KYU1; Q9C5L2; Q9M0C6;
DT 01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Diacylglycerol kinase 7;
DE Short=AtDGK7;
DE Short=DAG kinase 7;
DE EC=2.7.1.107;
DE AltName: Full=Diglyceride kinase 7;
DE Short=DGK 7;
GN Name=DGK7; OrderedLocusNames=At4g30340; ORFNames=F17I23.320;
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, AND TISSUE SPECIFICITY.
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RA Arana-Ceballos F.A., Gomez-Merino F., Krebs J., Skirycz A.,
RA Mueller-Roeber B.;
RT "Arabidopsis AtDGK7 regulates lateral root formation.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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 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).
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 xhibits high specificity for 1,2-dioleoyl-sn-glycerol (1,2-
CC DOG), 1-palmitoyl, 2-oleoyl-sn-glycerol (1,2 POG), 1-stearoyl, 2-
CC linoleoyl-sn-glycerol (1,2-SLG) and 1-oleoyl, 2-palmitoyl-sn-glycerol
CC (1,2-OPG). {ECO:0000269|PubMed:16081412, ECO:0000269|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:16081412};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.74 mM for ATP {ECO:0000269|PubMed:16081412};
CC Vmax=0.34 pmol/min/ug enzyme toward 1,2-dioleoyl-sn-glycerol
CC {ECO:0000269|PubMed:16081412};
CC pH dependence:
CC Optimum pH is 6.8. {ECO:0000269|PubMed:16081412};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Highly expressed in flowers, and at low levels in
CC roots, stems and leaves. {ECO:0000269|PubMed:16081412}.
CC -!- SIMILARITY: Belongs to the eukaryotic diacylglycerol kinase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK25884.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
CC Sequence=AAM44963.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
CC Sequence=AAU04880.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
CC Sequence=CAB81027.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY686593; AAU04880.1; ALT_SEQ; mRNA.
DR EMBL; DQ350135; ABC71078.1; -; mRNA.
DR EMBL; AL161576; CAB81027.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE85754.1; -; Genomic_DNA.
DR EMBL; AF360174; AAK25884.1; ALT_SEQ; mRNA.
DR EMBL; AY113915; AAM44963.1; ALT_SEQ; mRNA.
DR PIR; G85354; G85354.
DR RefSeq; NP_001328552.1; NM_001342006.1.
DR RefSeq; NP_567845.4; NM_119180.6.
DR AlphaFoldDB; F4JQ95; -.
DR BioGRID; 14444; 1.
DR IntAct; F4JQ95; 1.
DR STRING; 3702.AT4G30340.1; -.
DR iPTMnet; F4JQ95; -.
DR PaxDb; F4JQ95; -.
DR PRIDE; F4JQ95; -.
DR ProteomicsDB; 224102; -.
DR EnsemblPlants; AT4G30340.1; AT4G30340.1; AT4G30340.
DR GeneID; 829157; -.
DR Gramene; AT4G30340.1; AT4G30340.1; AT4G30340.
DR KEGG; ath:AT4G30340; -.
DR Araport; AT4G30340; -.
DR TAIR; locus:2118791; AT4G30340.
DR eggNOG; KOG1169; Eukaryota.
DR HOGENOM; CLU_002706_46_3_1; -.
DR InParanoid; F4JQ95; -.
DR OMA; WFFAPCS; -.
DR OrthoDB; 633642at2759; -.
DR BioCyc; MetaCyc:AT4G30340-MON; -.
DR PRO; PR:F4JQ95; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; F4JQ95; baseline and differential.
DR Genevisible; F4JQ95; AT.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004143; F:diacylglycerol kinase activity; IDA:TAIR.
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:0048364; P:root development; IMP:TAIR.
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..492
FT /note="Diacylglycerol kinase 7"
FT /id="PRO_0000422115"
FT DOMAIN 90..248
FT /note="DAGKc"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT CONFLICT 274
FT /note="D -> G (in Ref. 1; ABC71078)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 492 AA; 54572 MW; 7E5577CA2799D3A2 CRC64;
MEETPRSVGE ASTTNFVAAR PSAKTDDAVT MRGCGFANLA LVGIDKEELR GRLAMPEYLR
IAMRDCIKRK DSTEISDHLL LPGGAAADMA PHAPMVVFIN PKSGGRHGPV LKERLQQLMT
EEQVFDLTEV KPHEFVRYGL GCLDTLAAKG DECARECREK IRIMVAGGDG TVGWVLGCLG
ELHKDGKSHI PPVGVIPLGT GNDLSRSFSW GGSFPFAWRS AMKRTLHRAT LGSIARLDSW
KIVVSMPSGE VVDPPYSLKP TIEETALDQA LDADGDVPPK AKSYEGVFYN YFSIGMDAQV
AYGFHHLRNE KPYLAQGPVT NKIIYSSYSC TQGWFCTPCV NNPALRGLRN IMKIHIKKAN
CSEWEEIHVP KSVRSIVVLN LYNYGSGRHP WGNLRPKYLE KRGFVEAHCD DGLIEIFGLK
QGWHASFVMA EIISAKHIAQ AAAIRFELRG GDWKNAFLQM DGEPWKQPMK SDYSTFVEIK
KVPFQSLMIN GE
