DGK4_ARATH
ID DGK4_ARATH Reviewed; 487 AA.
AC Q1PDI2; Q9FHH4;
DT 01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Diacylglycerol kinase 4 {ECO:0000303|PubMed:30628082};
DE Short=AtDGK4 {ECO:0000303|PubMed:30628082};
DE Short=DAG kinase 4 {ECO:0000305};
DE EC=2.7.1.107 {ECO:0000269|PubMed:32471859};
DE AltName: Full=Diglyceride kinase 4 {ECO:0000305};
DE Short=DGK 4 {ECO:0000305};
GN Name=DGK4 {ECO:0000303|PubMed:30628082};
GN OrderedLocusNames=At5g57690 {ECO:0000312|Araport:AT5G57690};
GN ORFNames=MRI1.5 {ECO:0000312|EMBL:BAB09587.1};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10470850; DOI=10.1093/dnares/6.3.183;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Kotani H.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IX. Sequence
RT features of the regions of 1,011,550 bp covered by seventeen P1 and TAC
RT clones.";
RL DNA Res. 6:183-195(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=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT "Simultaneous high-throughput recombinational cloning of open reading
RT frames in closed and open configurations.";
RL Plant Biotechnol. J. 4:317-324(2006).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=30628082; DOI=10.1111/nph.15674;
RA Vaz Dias F., Serrazina S., Vitorino M., Marchese D., Heilmann I.,
RA Godinho M., Rodrigues M., Malho R.;
RT "A role for diacylglycerol kinase 4 in signalling crosstalk during
RT Arabidopsis pollen tube growth.";
RL New Phytol. 222:1434-1446(2019).
RN [5]
RP FUNCTION.
RX PubMed=32220864; DOI=10.1242/dev.183715;
RA Wong A., Donaldson L., Portes M.T., Eppinger J., Feijo J.A., Gehring C.;
RT "Arabidopsis DIACYLGLYCEROL KINASE4 is involved in nitric oxide-dependent
RT pollen tube guidance and fertilization.";
RL Development 147:0-0(2020).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP 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:32471859). PA is required for plant development and responses
CC to abiotic stress and pathogen attack. May be involved in the
CC accumulation of PA during cold stress (By similarity). Involved in the
CC regulation of PA and phosphatidylcholine biosynthesis in growing pollen
CC tubes (PubMed:30628082). Required for nitric oxide-dependent pollen
CC tube growth and re-orientation responses (PubMed:32220864). Functions
CC together with DGK2 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 Possesses guanylyl cyclase activity in vitro (PubMed:30628082,
CC PubMed:32220864). {ECO:0000250|UniProtKB:Q9FFN7,
CC ECO:0000269|PubMed:30628082, ECO:0000269|PubMed:32220864,
CC ECO:0000269|PubMed:32471859}.
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:32471859};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10273;
CC Evidence={ECO:0000269|PubMed:32471859};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P23743}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000269|PubMed:32471859}. Cytoplasm, cytosol
CC {ECO:0000269|PubMed:30628082}. Note=Expressed in the cytosol of growing
CC pollen tubes. {ECO:0000269|PubMed:30628082}.
CC -!- TISSUE SPECIFICITY: Highly expressed in pollen grains
CC (PubMed:30628082). Expressed in roots, hypocotyls, leaf vasculature,
CC developing anthers and stigmas, and receptacles of siliques
CC (PubMed:32471859). {ECO:0000269|PubMed:30628082,
CC ECO:0000269|PubMed:32471859}.
CC -!- DISRUPTION PHENOTYPE: Reduced plant size with small and curly leaves
CC (PubMed:30628082). Reduced growth rate of pollen tubes and reduced
CC number of seeds (PubMed:30628082). No visible phenotype under normal
CC growth conditions, but the double mutants dgk2 and dgk4 exhibit
CC defective pollen growth and seed development because of non-viable male
CC gametophyte (PubMed:32471859). {ECO:0000269|PubMed:30628082,
CC ECO:0000269|PubMed:32471859}.
CC -!- SIMILARITY: Belongs to the eukaryotic diacylglycerol kinase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB09587.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB018118; BAB09587.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED96936.1; -; Genomic_DNA.
DR EMBL; DQ447086; ABE66256.1; -; mRNA.
DR RefSeq; NP_200577.2; NM_125152.3.
DR AlphaFoldDB; Q1PDI2; -.
DR STRING; 3702.AT5G57690.1; -.
DR PaxDb; Q1PDI2; -.
DR PRIDE; Q1PDI2; -.
DR ProteomicsDB; 224214; -.
DR EnsemblPlants; AT5G57690.1; AT5G57690.1; AT5G57690.
DR GeneID; 835876; -.
DR Gramene; AT5G57690.1; AT5G57690.1; AT5G57690.
DR KEGG; ath:AT5G57690; -.
DR Araport; AT5G57690; -.
DR TAIR; locus:2172575; AT5G57690.
DR eggNOG; KOG1169; Eukaryota.
DR HOGENOM; CLU_002706_46_3_1; -.
DR InParanoid; Q1PDI2; -.
DR OMA; CFYGIWH; -.
DR OrthoDB; 633642at2759; -.
DR PhylomeDB; Q1PDI2; -.
DR BioCyc; ARA:AT5G57690-MON; -.
DR BRENDA; 2.7.1.107; 399.
DR PRO; PR:Q1PDI2; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q1PDI2; baseline and differential.
DR Genevisible; Q1PDI2; AT.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
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; 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; Cytoplasm; Endoplasmic reticulum; Kinase; Nucleotide-binding;
KW Plant defense; Reference proteome; Stress response; Transferase.
FT CHAIN 1..487
FT /note="Diacylglycerol kinase 4"
FT /id="PRO_0000422112"
FT DOMAIN 86..242
FT /note="DAGKc"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
SQ SEQUENCE 487 AA; 54181 MW; 854450C00B8CE355 CRC64;
MESPSIGDSL TARMIPRHSS LDSFGAMKVS LLVNLASIRV SKAELRQRVM LPQYLRIAIR
DCILRKDDSF DASSSVAPPL ENNALTPEVP LMVFVNPKSG GRQGPLIKER LQNLISEEQV
YDLTEVKPNE FIRYGLGCLE AFASRGDECA KEIREKMRIV VAGGDGTVGW VLGCLGELNL
QNRLPVPPVS IMPLGTGNDL SRSFGWGGSF PFAWKSAIKR TLHRASVAPI SRLDSWNILI
TMPSGEIVDP PYSLKATQEC YIDQNLEIEG EIPPSTNGYE GVFYNYFSIG MDAQVAYGFH
HLRNEKPYLA NGPIANKIIY SGYGCSQGWF LTHCINDPGL RGLKNIMTLH IKKLDSSEWE
KVPVPKSVRA VVALNLHSYG SGRNPWGNLK QDYLEKRGFV EAQADDGLLE IFGLKQGWHA
SFVMVELISA KHIAQAAAIR LEIRGGDWKD AFMQMDGEPW KQPMTRDYST FVDIKRVPHQ
SLVVKGD
