PLDA1_ARATH
ID PLDA1_ARATH Reviewed; 810 AA.
AC Q38882; Q0WV84; Q944M4; Q9LW06;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2001, sequence version 2.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Phospholipase D alpha 1 {ECO:0000303|PubMed:11891260};
DE Short=AtPLDalpha1 {ECO:0000303|PubMed:11891260};
DE Short=PLD alpha 1 {ECO:0000303|PubMed:11891260};
DE EC=3.1.4.4 {ECO:0000269|PubMed:10441386, ECO:0000269|PubMed:9353280};
DE AltName: Full=Choline phosphatase 1;
DE AltName: Full=PLDalpha {ECO:0000303|PubMed:11891260};
DE AltName: Full=Phosphatidylcholine-hydrolyzing phospholipase D 1;
GN Name=PLDALPHA1 {ECO:0000303|PubMed:11891260}; Synonyms=PLD1;
GN OrderedLocusNames=At3g15730 {ECO:0000312|Araport:AT3G15730};
GN ORFNames=MSJ11.13 {ECO:0000312|EMBL:BAB02304.1};
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].
RC STRAIN=cv. Columbia;
RA Dyer J.H., Zheng L., Wang X.;
RT "Cloning and nucleotide sequence of a cDNA encoding phospholipase D from
RT Arabidopsis.";
RL (er) Plant Gene Register PGR95-096(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(2000).
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;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 273-810.
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 CATALYTIC ACTIVITY, COFACTOR, AND ACTIVITY REGULATION.
RX PubMed=9353280; DOI=10.1074/jbc.272.45.28267;
RA Qin W., Pappan K., Wang X.;
RT "Molecular heterogeneity of phospholipase D (PLD). Cloning of PLDgamma and
RT regulation of plant PLDgamma, -beta, and -alpha by polyphosphoinositides
RT and calcium.";
RL J. Biol. Chem. 272:28267-28273(1997).
RN [7]
RP FUNCTION, AND INDUCTION BY ABSCISIC ACID AND ETHYLENE.
RX PubMed=9437863; DOI=10.2307/3870578;
RA Fan L., Zheng S., Wang X.;
RT "Antisense suppression of phospholipase D alpha retards abscisic acid- and
RT ethylene-promoted senescence of postharvest Arabidopsis leaves.";
RL Plant Cell 9:2183-2196(1997).
RN [8]
RP SUBSTRATE SPECIFICITY.
RX PubMed=9578608; DOI=10.1006/abbi.1998.0640;
RA Pappan K., Austin-Brown S., Chapman K.D., Wang X.;
RT "Substrate selectivities and lipid modulation of plant phospholipase D
RT alpha, -beta, and -gamma.";
RL Arch. Biochem. Biophys. 353:131-140(1998).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=10441386; DOI=10.1006/abbi.1999.1325;
RA Pappan K., Wang X.;
RT "Plant phospholipase Dalpha is an acidic phospholipase active at near-
RT physiological Ca(2+) concentrations.";
RL Arch. Biochem. Biophys. 368:347-353(1999).
RN [10]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=10198096; DOI=10.1104/pp.119.4.1371;
RA Fan L., Zheng S., Cui D., Wang X.;
RT "Subcellular distribution and tissue expression of phospholipase Dalpha,
RT Dbeta, and Dgamma in Arabidopsis.";
RL Plant Physiol. 119:1371-1378(1999).
RN [11]
RP DOMAIN, AND 3D-STRUCTURE MODELING.
RX PubMed=10777500; DOI=10.1074/jbc.m001945200;
RA Zheng L., Krishnamoorthi R., Zolkiewski M., Wang X.;
RT "Distinct Ca2+ binding properties of novel C2 domains of plant
RT phospholipase dalpha and beta.";
RL J. Biol. Chem. 275:19700-19706(2000).
RN [12]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11090221; DOI=10.2307/3871117;
RA Wang C., Zien C.A., Afitlhile M., Welti R., Hildebrand D.F., Wang X.;
RT "Involvement of phospholipase D in wound-induced accumulation of jasmonic
RT acid in arabidopsis.";
RL Plant Cell 12:2237-2246(2000).
RN [13]
RP FUNCTION.
RX PubMed=11239826; DOI=10.1016/s1388-1981(01)00091-9;
RA Zien C.A., Wang C., Wang X., Welti R.;
RT "In vivo substrates and the contribution of the common phospholipase D,
RT PLDalpha, to wound-induced metabolism of lipids in Arabidopsis.";
RL Biochim. Biophys. Acta 1530:236-248(2001).
RN [14]
RP SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=11706190; DOI=10.1104/pp.010444;
RA Wang C., Wang X.;
RT "A novel phospholipase d of Arabidopsis that is activated by oleic acid and
RT associated with the plasma membrane.";
RL Plant Physiol. 127:1102-1112(2001).
RN [15]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=11891260; DOI=10.1104/pp.010928;
RA Qin C., Wang X.;
RT "The Arabidopsis phospholipase D family. Characterization of a calcium-
RT independent and phosphatidylcholine-selective PLD zeta 1 with distinct
RT regulatory domains.";
RL Plant Physiol. 128:1057-1068(2002).
RN [16]
RP FUNCTION, INTERACTION WITH GPA1, AND MUTAGENESIS OF GLU-563; LYS-564 AND
RP PHE-565.
RX PubMed=14594812; DOI=10.1074/jbc.m309529200;
RA Zhao J., Wang X.;
RT "Arabidopsis phospholipase Dalpha1 interacts with the heterotrimeric G-
RT protein alpha-subunit through a motif analogous to the DRY motif in G-
RT protein-coupled receptors.";
RL J. Biol. Chem. 279:1794-1800(2004).
RN [17]
RP FUNCTION.
RX PubMed=16949955; DOI=10.1016/j.jplph.2005.08.006;
RA Rajashekar C.B., Zhou H.E., Zhang Y., Li W., Wang X.;
RT "Suppression of phospholipase Dalpha1 induces freezing tolerance in
RT Arabidopsis: response of cold-responsive genes and osmolyte accumulation.";
RL J. Plant Physiol. 163:916-926(2006).
RN [18]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH GPA1.
RX PubMed=16614222; DOI=10.1126/science.1123769;
RA Mishra G., Zhang W., Deng F., Zhao J., Wang X.;
RT "A bifurcating pathway directs abscisic acid effects on stomatal closure
RT and opening in Arabidopsis.";
RL Science 312:264-266(2006).
RN [19]
RP FUNCTION.
RX PubMed=17261695; DOI=10.1093/jxb/erl262;
RA Mane S.P., Vasquez-Robinet C., Sioson A.A., Heath L.S., Grene R.;
RT "Early PLDalpha-mediated events in response to progressive drought stress
RT in Arabidopsis: a transcriptome analysis.";
RL J. Exp. Bot. 58:241-252(2007).
RN [20]
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).
RN [21]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17565616; DOI=10.1111/j.1365-313x.2007.03103.x;
RA Devaiah S.P., Pan X., Hong Y., Roth M., Welti R., Wang X.;
RT "Enhancing seed quality and viability by suppressing phospholipase D in
RT Arabidopsis.";
RL Plant J. 50:950-957(2007).
RN [22]
RP INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19017627; DOI=10.1093/pcp/pcn173;
RA Bargmann B.O., Laxalt A.M., ter Riet B., van Schooten B., Merquiol E.,
RA Testerink C., Haring M.A., Bartels D., Munnik T.;
RT "Multiple PLDs required for high salinity and water deficit tolerance in
RT plants.";
RL Plant Cell Physiol. 50:78-89(2009).
RN [23]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23150630; DOI=10.1105/tpc.112.104182;
RA Zhang Q., Lin F., Mao T., Nie J., Yan M., Yuan M., Zhang W.;
RT "Phosphatidic acid regulates microtubule organization by interacting with
RT MAP65-1 in response to salt stress in Arabidopsis.";
RL Plant Cell 24:4555-4576(2012).
RN [24]
RP FUNCTION, INDUCTION BY ABSCISIC ACID, AND DISRUPTION PHENOTYPE.
RX PubMed=22392280; DOI=10.1104/pp.112.195578;
RA Uraji M., Katagiri T., Okuma E., Ye W., Hossain M.A., Masuda C., Miura A.,
RA Nakamura Y., Mori I.C., Shinozaki K., Murata Y.;
RT "Cooperative function of PLDdelta and PLDalpha1 in abscisic acid-induced
RT stomatal closure in Arabidopsis.";
RL Plant Physiol. 159:450-460(2012).
RN [25]
RP INTERACTION WITH GPA1.
RX PubMed=23913032; DOI=10.1007/978-1-62703-532-3_3;
RA Zhao J., Wang X.;
RT "Biochemical analysis of the interaction between phospholipase Dalpha1 and
RT GTP-binding protein alpha-subunit from Arabidopsis thaliana.";
RL Methods Mol. Biol. 1043:21-35(2013).
RN [26]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH
RP 1,2-DIACYL-SN-GLYCERO-3-PHOSPHATE AND CALCIUM ION, AND COFACTOR.
RX PubMed=31619765; DOI=10.1038/s41422-019-0244-6;
RA Li J., Yu F., Guo H., Xiong R., Zhang W., He F., Zhang M., Zhang P.;
RT "Crystal structure of plant PLDalpha1 reveals catalytic and regulatory
RT mechanisms of eukaryotic phospholipase D.";
RL Cell Res. 30:61-69(2020).
CC -!- FUNCTION: Hydrolyzes glycerol-phospholipids at the terminal
CC phosphodiesteric bond to generate phosphatidic acids (PA). Plays an
CC important role in various cellular processes, including phytohormone
CC action and response to stress, characterized by acidification of the
CC cell (PubMed:9437863). Involved in wound induction of jasmonic acid
CC (PubMed:11090221). May be involved in membrane lipid remodeling
CC (PubMed:11239826). Probably involved in freezing tolerance by
CC modulating the cold-responsive genes and accumulation of osmolytes
CC (PubMed:16949955). Can use phosphatidylcholine (PC),
CC phosphatidylethanolamine (PE) and phosphatidylglycerol (PG) as
CC substrates, both in presence or in absence of PIP2 (PubMed:9578608).
CC Its main substrate is phosphatidylcholine (PubMed:11239826). Stimulates
CC the intrinsic GTPase activity of GPA1 upon binding (PubMed:14594812).
CC Mediates the abscisic acid effects on stomata through interaction with
CC GPA1 and the production of phosphatidic acid that bind to ABI1
CC (PubMed:17261695, PubMed:17565616). Involved in seed aging and
CC deterioration (PubMed:17565616). Involved in microtubule stabilization
CC and salt tolerance (PubMed:23150630). Involved in abscisic acid-induced
CC stomatal closure (PubMed:22392280). {ECO:0000269|PubMed:10441386,
CC ECO:0000269|PubMed:11090221, ECO:0000269|PubMed:11239826,
CC ECO:0000269|PubMed:14594812, ECO:0000269|PubMed:16614222,
CC ECO:0000269|PubMed:16949955, ECO:0000269|PubMed:17261695,
CC ECO:0000269|PubMed:17565616, ECO:0000269|PubMed:22392280,
CC ECO:0000269|PubMed:23150630, ECO:0000269|PubMed:9437863,
CC ECO:0000269|PubMed:9578608}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1,2-diacyl-
CC sn-glycero-3-phosphate + choline + H(+); Xref=Rhea:RHEA:14445,
CC ChEBI:CHEBI:15354, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57643, ChEBI:CHEBI:58608; EC=3.1.4.4;
CC Evidence={ECO:0000269|PubMed:10441386, ECO:0000269|PubMed:9353280};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:31619765, ECO:0000269|PubMed:9353280};
CC Note=Ca(2+) requirement for activity depends on pH. Active either under
CC acidic conditions with micromolar levels of calcium (PIP2-dependent) or
CC at neutral pH with millimolar levels of calcium (PIP2-independent).
CC {ECO:0000269|PubMed:9353280};
CC -!- ACTIVITY REGULATION: Not inhibited by neomycin.
CC {ECO:0000269|PubMed:9353280}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 4.5 to 5.0 in the presence of micromolar levels of
CC Ca(2+) and PIP2. Optimum pH is 5.5 to 6.5 in the presence of
CC millimolar levels of Ca(2+). {ECO:0000269|PubMed:10441386};
CC -!- SUBUNIT: Interacts with GPA1 (PubMed:14594812, PubMed:16614222,
CC PubMed:23913032). This binding inhibits PLDALPHA1 activity and is
CC relieved by GTP (PubMed:14594812). {ECO:0000269|PubMed:14594812,
CC ECO:0000269|PubMed:16614222, ECO:0000269|PubMed:23913032}.
CC -!- INTERACTION:
CC Q38882; P18064: GPA1; NbExp=3; IntAct=EBI-962294, EBI-443890;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10198096,
CC ECO:0000269|PubMed:11706190}. Cell membrane
CC {ECO:0000269|PubMed:10198096, ECO:0000269|PubMed:11706190}; Peripheral
CC membrane protein {ECO:0000269|PubMed:10198096}. Mitochondrion membrane
CC {ECO:0000269|PubMed:11706190}. Microsome membrane
CC {ECO:0000269|PubMed:11706190}. Vacuole {ECO:0000269|PubMed:10198096}.
CC Cytoplasmic vesicle, clathrin-coated vesicle
CC {ECO:0000269|PubMed:10198096}. Note=Not found in chloroplast or nuclei.
CC The distribution of this conventional PLD between membrane-associated
CC and soluble fractions varied from organ to organ and is calcium-
CC regulated. Activation or wounding increases association of preexisting
CC enzyme with membranes. {ECO:0000269|PubMed:11090221}.
CC -!- TISSUE SPECIFICITY: Highly expressed in roots, stems and flowers,
CC moderately in leaves, seedlings and siliques. Not detected in seeds.
CC {ECO:0000269|PubMed:10198096}.
CC -!- INDUCTION: Up-regulated by abscisic acid and ethylene (PubMed:9437863).
CC Up-regulated by salt, dehydration and osmotic stresses
CC (PubMed:19017627). Not regulated by abscisic acid (PubMed:22392280).
CC {ECO:0000269|PubMed:19017627, ECO:0000269|PubMed:22392280,
CC ECO:0000269|PubMed:9437863}.
CC -!- DOMAIN: C2 domain is a calcium-binding fold, and the binding induces
CC conformational changes, promoting the protein association with
CC membranes. These conformational changes occure at millimolar Ca(2+)
CC concentrations. Binds also PIP2. A lower affinity toward calcium can be
CC anticipated for PLD alpha due to the absence of two potential calcium
CC ligands. {ECO:0000269|PubMed:10777500}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but improved resistance of the seeds to deterioration
CC during storage (PubMed:17565616). Insensitivity to abscisic acid for
CC both promotion of stomatal closure and inhibition of stomatal opening
CC (PubMed:16614222). Hypersensitivity to hyperosmotic stress
CC (PubMed:19017627). Increased NaCl-induced disorganization of
CC microtubules (PubMed:23150630). No effect on abscisic acid-induced
CC stomatal closure (PubMed:22392280). Pldalpha1 and plddelta double
CC mutants have a suppressed abscisic acid-induced stomatal closure
CC (PubMed:22392280). {ECO:0000269|PubMed:16614222,
CC ECO:0000269|PubMed:17565616, ECO:0000269|PubMed:19017627,
CC ECO:0000269|PubMed:22392280, ECO:0000269|PubMed:23150630}.
CC -!- SIMILARITY: Belongs to the phospholipase D family. C2-PLD subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC49274.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAL16110.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U36381; AAC49274.1; ALT_FRAME; mRNA.
DR EMBL; AB017071; BAB02304.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75720.1; -; Genomic_DNA.
DR EMBL; AK226887; BAE98964.1; -; mRNA.
DR EMBL; AF428278; AAL16110.1; ALT_INIT; mRNA.
DR RefSeq; NP_188194.1; NM_112443.3.
DR PDB; 6KZ8; X-ray; 2.29 A; A/B=1-810.
DR PDB; 6KZ9; X-ray; 1.80 A; A=1-810.
DR PDBsum; 6KZ8; -.
DR PDBsum; 6KZ9; -.
DR AlphaFoldDB; Q38882; -.
DR SMR; Q38882; -.
DR BioGRID; 6150; 9.
DR IntAct; Q38882; 6.
DR STRING; 3702.AT3G15730.1; -.
DR iPTMnet; Q38882; -.
DR PaxDb; Q38882; -.
DR PRIDE; Q38882; -.
DR ProteomicsDB; 236630; -.
DR DNASU; 820816; -.
DR EnsemblPlants; AT3G15730.1; AT3G15730.1; AT3G15730.
DR GeneID; 820816; -.
DR Gramene; AT3G15730.1; AT3G15730.1; AT3G15730.
DR KEGG; ath:AT3G15730; -.
DR Araport; AT3G15730; -.
DR TAIR; locus:2093227; AT3G15730.
DR eggNOG; KOG1329; Eukaryota.
DR HOGENOM; CLU_004684_0_0_1; -.
DR InParanoid; Q38882; -.
DR OMA; PNWGRGI; -.
DR OrthoDB; 128697at2759; -.
DR PhylomeDB; Q38882; -.
DR BioCyc; ARA:AT3G15730-MON; -.
DR BioCyc; MetaCyc:AT3G15730-MON; -.
DR BRENDA; 3.1.4.4; 399.
DR PRO; PR:Q38882; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q38882; baseline and differential.
DR Genevisible; Q38882; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0030136; C:clathrin-coated vesicle; IDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:TAIR.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0005773; C:vacuole; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005096; F:GTPase activator activity; IDA:TAIR.
DR GO; GO:0070290; F:N-acylphosphatidylethanolamine-specific phospholipase D activity; IEA:UniProtKB-EC.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IDA:TAIR.
DR GO; GO:0004620; F:phospholipase activity; IDA:TAIR.
DR GO; GO:0004630; F:phospholipase D activity; IDA:TAIR.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IMP:TAIR.
DR GO; GO:0009873; P:ethylene-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0006631; P:fatty acid metabolic process; IMP:TAIR.
DR GO; GO:0010358; P:leaf shaping; IMP:TAIR.
DR GO; GO:0046470; P:phosphatidylcholine metabolic process; IEA:InterPro.
DR GO; GO:0009395; P:phospholipid catabolic process; IBA:GO_Central.
DR GO; GO:0009789; P:positive regulation of abscisic acid-activated signaling pathway; IMP:TAIR.
DR GO; GO:0010119; P:regulation of stomatal movement; IMP:TAIR.
DR GO; GO:0009737; P:response to abscisic acid; IMP:TAIR.
DR GO; GO:0009845; P:seed germination; IMP:TAIR.
DR Gene3D; 2.60.40.150; -; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR InterPro; IPR024632; PLipase_D_C.
DR InterPro; IPR015679; PLipase_D_fam.
DR InterPro; IPR011402; PLipase_D_pln.
DR PANTHER; PTHR18896; PTHR18896; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF12357; PLD_C; 1.
DR Pfam; PF00614; PLDc; 2.
DR PIRSF; PIRSF036470; PLD_plant; 1.
DR SMART; SM00239; C2; 1.
DR SMART; SM00155; PLDc; 2.
DR SUPFAM; SSF49562; SSF49562; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS50035; PLD; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Abscisic acid signaling pathway; Calcium; Cell membrane;
KW Cytoplasm; Cytoplasmic vesicle; Endoplasmic reticulum;
KW Ethylene signaling pathway; Hydrolase; Lipid degradation; Lipid metabolism;
KW Membrane; Metal-binding; Microsome; Mitochondrion; Reference proteome;
KW Repeat; Vacuole.
FT CHAIN 1..810
FT /note="Phospholipase D alpha 1"
FT /id="PRO_0000218808"
FT DOMAIN 1..126
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 327..366
FT /note="PLD phosphodiesterase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT DOMAIN 656..683
FT /note="PLD phosphodiesterase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 332
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 334
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 339
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 661
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 663
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 668
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT BINDING 187
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:31619765,
FT ECO:0007744|PDB:6KZ8, ECO:0007744|PDB:6KZ9"
FT BINDING 332
FT /ligand="a 1,2-diacyl-sn-glycero-3-phosphate"
FT /ligand_id="ChEBI:CHEBI:58608"
FT /evidence="ECO:0000269|PubMed:31619765,
FT ECO:0007744|PDB:6KZ8"
FT BINDING 372
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:31619765,
FT ECO:0007744|PDB:6KZ8, ECO:0007744|PDB:6KZ9"
FT BINDING 406
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:31619765,
FT ECO:0007744|PDB:6KZ8, ECO:0007744|PDB:6KZ9"
FT BINDING 522
FT /ligand="a 1,2-diacyl-sn-glycero-3-phosphate"
FT /ligand_id="ChEBI:CHEBI:58608"
FT /evidence="ECO:0000269|PubMed:31619765,
FT ECO:0007744|PDB:6KZ8"
FT BINDING 661
FT /ligand="a 1,2-diacyl-sn-glycero-3-phosphate"
FT /ligand_id="ChEBI:CHEBI:58608"
FT /evidence="ECO:0000269|PubMed:31619765,
FT ECO:0007744|PDB:6KZ8"
FT BINDING 722
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:31619765,
FT ECO:0007744|PDB:6KZ8, ECO:0007744|PDB:6KZ9"
FT MUTAGEN 563
FT /note="E->A: Decreased GPA1 binding."
FT /evidence="ECO:0000269|PubMed:14594812"
FT MUTAGEN 564
FT /note="K->A: Loss of GPA1 binding."
FT /evidence="ECO:0000269|PubMed:14594812"
FT MUTAGEN 565
FT /note="F->A: Decreased GPA1 binding."
FT /evidence="ECO:0000269|PubMed:14594812"
FT CONFLICT 3..4
FT /note="QH -> HD (in Ref. 1; AAC49274)"
FT /evidence="ECO:0000305"
FT CONFLICT 26
FT /note="R -> M (in Ref. 1; AAC49274)"
FT /evidence="ECO:0000305"
FT CONFLICT 49
FT /note="Q -> R (in Ref. 1; AAC49274)"
FT /evidence="ECO:0000305"
FT CONFLICT 99
FT /note="N -> I (in Ref. 1; AAC49274)"
FT /evidence="ECO:0000305"
FT CONFLICT 121
FT /note="Missing (in Ref. 1; AAC49274)"
FT /evidence="ECO:0000305"
FT CONFLICT 218
FT /note="A -> T (in Ref. 1; AAC49274)"
FT /evidence="ECO:0000305"
FT CONFLICT 301..302
FT /note="GS -> ER (in Ref. 1; AAC49274)"
FT /evidence="ECO:0000305"
FT CONFLICT 435
FT /note="D -> E (in Ref. 1; AAC49274)"
FT /evidence="ECO:0000305"
FT CONFLICT 560..561
FT /note="EK -> DQ (in Ref. 1; AAC49274)"
FT /evidence="ECO:0000305"
FT CONFLICT 607..612
FT /note="RAQGLE -> KGLEGP (in Ref. 1; AAC49274)"
FT /evidence="ECO:0000305"
FT CONFLICT 735..739
FT /note="SSLEC -> KLSES (in Ref. 1; AAC49274)"
FT /evidence="ECO:0000305"
FT STRAND 4..18
FT /evidence="ECO:0007829|PDB:6KZ9"
FT STRAND 50..56
FT /evidence="ECO:0007829|PDB:6KZ9"
FT STRAND 59..63
FT /evidence="ECO:0007829|PDB:6KZ9"
FT STRAND 71..73
FT /evidence="ECO:0007829|PDB:6KZ9"
FT STRAND 75..97
FT /evidence="ECO:0007829|PDB:6KZ9"
FT STRAND 104..112
FT /evidence="ECO:0007829|PDB:6KZ9"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:6KZ9"
FT TURN 116..118
FT /evidence="ECO:0007829|PDB:6KZ9"
FT STRAND 122..127
FT /evidence="ECO:0007829|PDB:6KZ9"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:6KZ9"
FT STRAND 137..139
FT /evidence="ECO:0007829|PDB:6KZ8"
FT STRAND 141..150
FT /evidence="ECO:0007829|PDB:6KZ9"
FT HELIX 151..153
FT /evidence="ECO:0007829|PDB:6KZ9"
FT TURN 155..159
FT /evidence="ECO:0007829|PDB:6KZ9"
FT STRAND 177..188
FT /evidence="ECO:0007829|PDB:6KZ9"
FT STRAND 203..205
FT /evidence="ECO:0007829|PDB:6KZ9"
FT HELIX 211..221
FT /evidence="ECO:0007829|PDB:6KZ9"
FT STRAND 223..231
FT /evidence="ECO:0007829|PDB:6KZ9"
FT TURN 248..251
FT /evidence="ECO:0007829|PDB:6KZ9"
FT HELIX 254..263
FT /evidence="ECO:0007829|PDB:6KZ9"
FT STRAND 267..273
FT /evidence="ECO:0007829|PDB:6KZ9"
FT HELIX 275..277
FT /evidence="ECO:0007829|PDB:6KZ9"
FT HELIX 280..285
FT /evidence="ECO:0007829|PDB:6KZ9"
FT HELIX 292..299
FT /evidence="ECO:0007829|PDB:6KZ9"
FT STRAND 305..309
FT /evidence="ECO:0007829|PDB:6KZ9"
FT HELIX 319..325
FT /evidence="ECO:0007829|PDB:6KZ8"
FT STRAND 335..341
FT /evidence="ECO:0007829|PDB:6KZ9"
FT STRAND 351..359
FT /evidence="ECO:0007829|PDB:6KZ9"
FT TURN 376..381
FT /evidence="ECO:0007829|PDB:6KZ9"
FT HELIX 396..398
FT /evidence="ECO:0007829|PDB:6KZ9"
FT STRAND 408..414
FT /evidence="ECO:0007829|PDB:6KZ9"
FT HELIX 415..431
FT /evidence="ECO:0007829|PDB:6KZ9"
FT HELIX 440..443
FT /evidence="ECO:0007829|PDB:6KZ9"
FT TURN 444..446
FT /evidence="ECO:0007829|PDB:6KZ9"
FT STRAND 462..471
FT /evidence="ECO:0007829|PDB:6KZ9"
FT TURN 472..474
FT /evidence="ECO:0007829|PDB:6KZ9"
FT HELIX 482..487
FT /evidence="ECO:0007829|PDB:6KZ9"
FT STRAND 494..500
FT /evidence="ECO:0007829|PDB:6KZ9"
FT HELIX 501..512
FT /evidence="ECO:0007829|PDB:6KZ9"
FT STRAND 514..522
FT /evidence="ECO:0007829|PDB:6KZ9"
FT HELIX 528..530
FT /evidence="ECO:0007829|PDB:6KZ9"
FT STRAND 534..536
FT /evidence="ECO:0007829|PDB:6KZ9"
FT HELIX 538..540
FT /evidence="ECO:0007829|PDB:6KZ9"
FT HELIX 547..561
FT /evidence="ECO:0007829|PDB:6KZ9"
FT STRAND 566..570
FT /evidence="ECO:0007829|PDB:6KZ9"
FT HELIX 582..608
FT /evidence="ECO:0007829|PDB:6KZ9"
FT HELIX 615..617
FT /evidence="ECO:0007829|PDB:6KZ9"
FT STRAND 619..627
FT /evidence="ECO:0007829|PDB:6KZ9"
FT HELIX 646..653
FT /evidence="ECO:0007829|PDB:6KZ9"
FT STRAND 655..657
FT /evidence="ECO:0007829|PDB:6KZ9"
FT STRAND 663..667
FT /evidence="ECO:0007829|PDB:6KZ9"
FT TURN 668..670
FT /evidence="ECO:0007829|PDB:6KZ9"
FT STRAND 671..676
FT /evidence="ECO:0007829|PDB:6KZ9"
FT HELIX 681..684
FT /evidence="ECO:0007829|PDB:6KZ9"
FT STRAND 685..697
FT /evidence="ECO:0007829|PDB:6KZ9"
FT STRAND 703..706
FT /evidence="ECO:0007829|PDB:6KZ9"
FT HELIX 711..724
FT /evidence="ECO:0007829|PDB:6KZ9"
FT HELIX 729..732
FT /evidence="ECO:0007829|PDB:6KZ9"
FT HELIX 737..755
FT /evidence="ECO:0007829|PDB:6KZ9"
FT STRAND 767..769
FT /evidence="ECO:0007829|PDB:6KZ9"
FT STRAND 771..774
FT /evidence="ECO:0007829|PDB:6KZ9"
FT STRAND 780..783
FT /evidence="ECO:0007829|PDB:6KZ9"
FT STRAND 786..788
FT /evidence="ECO:0007829|PDB:6KZ9"
FT STRAND 802..804
FT /evidence="ECO:0007829|PDB:6KZ9"
FT HELIX 806..809
FT /evidence="ECO:0007829|PDB:6KZ9"
SQ SEQUENCE 810 AA; 91848 MW; 87A8692E43BD73CE CRC64;
MAQHLLHGTL HATIYEVDAL HGGGVRQGFL GKILANVEET IGVGKGETQL YATIDLQKAR
VGRTRKIKNE PKNPKWYESF HIYCAHLASD IIFTVKDDNP IGATLIGRAY IPVDQVINGE
EVDQWVEILD NDRNPIQGGS KIHVKLQYFH VEEDRNWNMG IKSAKFPGVP YTFFSQRQGC
KVSLYQDAHI PDNFVPRIPL AGGKNYEPQR CWEDIFDAIS NAKHLIYITG WSVYAEIALV
RDSRRPKPGG DVTIGELLKK KASEGVRVLL LVWDDRTSVD VLKKDGLMAT HDEETENFFR
GSDVHCILCP RNPDDGGSIV QSLQISTMFT HHQKIVVVDS EMPSRGGSEM RRIVSFVGGI
DLCDGRYDTP FHSLFRTLDT VHHDDFHQPN FTGAAITKGG PREPWHDIHS RLEGPIAWDV
MYNFEQRWSK QGGKDILVKL RDLSDIIITP SPVMFQEDHD VWNVQLFRSI DGGAAAGFPE
SPEAAAEAGL VSGKDNIIDR SIQDAYIHAI RRAKDFIYVE NQYFLGSSFA WAADGITPED
INALHLIPKE LSLKIVSKIE KGEKFRVYVV VPMWPEGLPE SGSVQAILDW QRRTMEMMYK
DVIQALRAQG LEEDPRNYLT FFCLGNREVK KDGEYEPAEK PDPDTDYMRA QEARRFMIYV
HTKMMIVDDE YIIIGSANIN QRSMDGARDS EIAMGGYQPH HLSHRQPARG QIHGFRMSLW
YEHLGMLDET FLDPSSLECI EKVNRISDKY WDFYSSESLE HDLPGHLLRY PIGVASEGDI
TELPGFEFFP DTKARILGTK SDYLPPILTT
