PLDD1_ARATH
ID PLDD1_ARATH Reviewed; 868 AA.
AC Q9C5Y0; Q0WUE7; Q8L891; Q944P8; Q947R2; Q9FS18; Q9SZS7;
DT 03-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2002, sequence version 2.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Phospholipase D delta {ECO:0000303|PubMed:11891260};
DE Short=AtPLDdelta {ECO:0000303|PubMed:11891260};
DE Short=PLD delta {ECO:0000303|PubMed:11891260};
DE EC=3.1.4.4 {ECO:0000269|PubMed:11706190, ECO:0000269|PubMed:12397060};
GN Name=PLDDELTA {ECO:0000303|PubMed:11891260};
GN OrderedLocusNames=At4g35790 {ECO:0000312|Araport:AT4G35790};
GN ORFNames=F4B14.60 {ECO:0000312|EMBL:CAA21465.1};
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] (ISOFORM 2), MUTAGENESIS OF ARG-410 AND ARG-622,
RP ACTIVITY REGULATION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND FUNCTION.
RX PubMed=11549769; DOI=10.2307/3871433;
RA Gardiner J.C., Harper J.D.I., Weerakoon N.D., Collings D.A., Ritchie S.,
RA Gilroy S., Cyr R.J., Marc J.;
RT "A 90-kD phospholipase D from tobacco binds to microtubules and the plasma
RT membrane.";
RL Plant Cell 13:2143-2158(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INDUCTION, AND TISSUE
RP SPECIFICITY.
RX PubMed=11489173; DOI=10.1046/j.1365-313x.2001.01060.x;
RA Katagiri T., Takahashi S., Shinozaki K.;
RT "Involvement of a novel Arabidopsis phospholipase D, AtPLDdelta, in
RT dehydration-inducible accumulation of phosphatidic acid in stress
RT signalling.";
RL Plant J. 26:595-605(2001).
RN [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [8]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY
RP REGULATION.
RX PubMed=12397060; DOI=10.1074/jbc.m209598200;
RA Qin C., Wang C., Wang X.;
RT "Kinetic analysis of Arabidopsis phospholipase Ddelta. Substrate preference
RT and mechanism of activation by Ca2+ and phosphatidylinositol 4,5-
RT biphosphate.";
RL J. Biol. Chem. 277:49685-49690(2002).
RN [9]
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 [10]
RP DISRUPTION PHENOTYPE, AND ACTIVITY REGULATION.
RX PubMed=14508007; DOI=10.1105/tpc.013961;
RA Zhang W., Wang C., Qin C., Wood T., Olafsdottir G., Welti R., Wang X.;
RT "The oleate-stimulated phospholipase D, PLDdelta, and phosphatidic acid
RT decrease H2O2-induced cell death in Arabidopsis.";
RL Plant Cell 15:2285-2295(2003).
RN [11]
RP FUNCTION.
RX PubMed=12881496; DOI=10.1093/pcp/pcg095;
RA Gardiner J., Collings D.A., Harper J.D., Marc J.;
RT "The effects of the phospholipase D-antagonist 1-butanol on seedling
RT development and microtubule organisation in Arabidopsis.";
RL Plant Cell Physiol. 44:687-696(2003).
RN [12]
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 [13]
RP FUNCTION, TISSUE SPECIFICITY, INDUCTION BY ABSCISIC ACID, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=22932846; DOI=10.1007/s00425-012-1745-4;
RA Distefano A.M., Scuffi D., Garcia-Mata C., Lamattina L., Laxalt A.M.;
RT "Phospholipase Ddelta is involved in nitric oxide-induced stomatal
RT closure.";
RL Planta 236:1899-1907(2012).
RN [14]
RP FUNCTION, INTERACTION WITH GAPC1 AND GAPC2, AND ACTIVITY REGULATION.
RX PubMed=22589465; DOI=10.1105/tpc.111.094946;
RA Guo L., Devaiah S.P., Narasimhan R., Pan X., Zhang Y., Zhang W., Wang X.;
RT "Cytosolic glyceraldehyde-3-phosphate dehydrogenases interact with
RT phospholipase Ddelta to transduce hydrogen peroxide signals in the
RT Arabidopsis response to stress.";
RL Plant Cell 24:2200-2212(2012).
RN [15]
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 [16]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23762411; DOI=10.1371/journal.pone.0065687;
RA Jia Y., Tao F., Li W.;
RT "Lipid profiling demonstrates that suppressing Arabidopsis phospholipase
RT Ddelta retards ABA-promoted leaf senescence by attenuating lipid
RT degradation.";
RL PLoS ONE 8:E65687-E65687(2013).
RN [17]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=23979971; DOI=10.1104/pp.113.223503;
RA Pinosa F., Buhot N., Kwaaitaal M., Fahlberg P., Thordal-Christensen H.,
RA Ellerstrom M., Andersson M.X.;
RT "Arabidopsis phospholipase ddelta is involved in basal defense and nonhost
RT resistance to powdery mildew fungi.";
RL Plant Physiol. 163:896-906(2013).
CC -!- FUNCTION: Hydrolyzes glycerol-phospholipids at the terminal
CC phosphodiesteric bond to generate phosphatidic acids (PA). May be
CC involved in PA accumulation in the dehydration stress response and in
CC the transduction of hormonal and environmental signals to the
CC microtubules cytoskeleton (PubMed:11549769, PubMed:11489173,
CC PubMed:12881496). Prefers phosphatidylethanolamine to
CC phosphatidylcholine as substrate (PubMed:12397060). Involved in
CC H(2)O(2) and abscisic acid (ABA)-induced stomatal closure
CC (PubMed:22589465, PubMed:22392280). Involved in nitric oxide (NO)
CC signaling during stomatal closure (PubMed:22932846). Plays a positive
CC role in ABA-promoted senescence (PubMed:23762411). Involved in basal
CC defense and nonhost resistance (PubMed:23979971).
CC {ECO:0000269|PubMed:11489173, ECO:0000269|PubMed:11549769,
CC ECO:0000269|PubMed:12397060, ECO:0000269|PubMed:12881496,
CC ECO:0000269|PubMed:22392280, ECO:0000269|PubMed:22589465,
CC ECO:0000269|PubMed:22932846, ECO:0000269|PubMed:23762411,
CC ECO:0000269|PubMed:23979971}.
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:11706190, ECO:0000269|PubMed:12397060};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:11706190};
CC Note=Ca(2+). Requires millimolar level (PIP2-dependent).
CC {ECO:0000269|PubMed:11706190};
CC -!- ACTIVITY REGULATION: Activated by free oleic acid in a dose-dependent
CC manner and less effectively by other unsaturated fatty acids such as
CC linoleic and linolenic acids (PubMed:11706190). Not activated by the
CC saturated fatty acids stearic and palmitic acids (PubMed:11706190).
CC PIP2 and Ca(2+) stimulate activity by promoting lipid substrate binding
CC to the active site (PubMed:12397060). Activated by H(2)O(2) and by
CC binding to GAPC (PubMed:14508007, PubMed:22589465).
CC {ECO:0000269|PubMed:11706190, ECO:0000269|PubMed:12397060,
CC ECO:0000269|PubMed:14508007, ECO:0000269|PubMed:22589465}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Vmax=1.0 umol/min/mg enzyme with phosphatidylcholine as substrate
CC {ECO:0000269|PubMed:12397060};
CC Vmax=1.5 umol/min/mg enzyme with phosphatidylethanolamine as
CC substrate {ECO:0000269|PubMed:12397060};
CC pH dependence:
CC Optimum pH is between 6.0 and 7.0. {ECO:0000269|PubMed:11706190};
CC -!- SUBUNIT: Interacts with GAPC1 and GAPC2. Increased interaction in the
CC presence of H(2)O(2). {ECO:0000269|PubMed:22589465}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11706190,
CC ECO:0000269|PubMed:23979971}; Peripheral membrane protein.
CC Note=Colocalization with cortical microtubules also occurs.
CC {ECO:0000269|PubMed:11549769}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=PLD delta a;
CC IsoId=Q9C5Y0-1; Sequence=Displayed;
CC Name=2; Synonyms=PLD delta b;
CC IsoId=Q9C5Y0-2; Sequence=VSP_005029;
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems, siliques and
CC flowers (PubMed:11706190, PubMed:11489173). Strongly expressed in the
CC vascular tissues of cotyledons and leaves under dehydration stress
CC conditions (PubMed:11489173). Expression is higher in old leaves than
CC in young leaves (PubMed:11706190). Expressed in leaves and guard cells
CC (PubMed:22932846). The isoform 2 may not be present in siliques.
CC {ECO:0000269|PubMed:11489173, ECO:0000269|PubMed:11706190,
CC ECO:0000269|PubMed:22932846}.
CC -!- INDUCTION: By salt stress or dehydration, in vascular tissues of roots,
CC cotyledons and leaves (PubMed:11489173, PubMed:19017627). Not induced
CC cold stress (PubMed:11489173). Up-regulated by abscisic acid in rosette
CC leaves (PubMed:22932846, PubMed:22392280).
CC {ECO:0000269|PubMed:11489173, ECO:0000269|PubMed:19017627,
CC ECO:0000269|PubMed:22392280, ECO:0000269|PubMed:22932846}.
CC -!- DOMAIN: C2 domain is a calcium-binding fold, and the binding promotes
CC the protein association with membranes. In PLD delta, all the calcium-
CC coordinating acidic amino acids are conserved. {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype when grown under standard
CC conditions (PubMed:22932846). Loss of oleate-activated PLD activity and
CC increased sensitivity to stress damage and to H(2)O(2)-induced cell
CC death (PubMed:14508007). Hypersensitivity to hyperosmotic stress
CC (PubMed:19017627). Impaired stomatal closure in response to nitric
CC oxide donor (PubMed:22932846). Attenuated lipid degradation retarding
CC abscisic acid (ABA)-promoted leaf senescence (PubMed:23762411).
CC Decreased penetration resistance against non-host fungi
CC (PubMed:23979971). No effect on ABA-induced stomatal closure
CC (PubMed:22392280). Pldalpha1 and plddelta double mutants have a
CC suppressed ABA-induced stomatal closure (PubMed:22392280).
CC {ECO:0000269|PubMed:14508007, ECO:0000269|PubMed:19017627,
CC ECO:0000269|PubMed:22392280, ECO:0000269|PubMed:22932846,
CC ECO:0000269|PubMed:23762411, ECO:0000269|PubMed:23979971}.
CC -!- SIMILARITY: Belongs to the phospholipase D family. C2-PLD subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL11625.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAA21465.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB81488.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF322228; AAG53975.1; -; mRNA.
DR EMBL; AF274239; AAL02150.1; -; mRNA.
DR EMBL; AF306345; AAL11978.1; -; mRNA.
DR EMBL; AB031047; BAB19130.1; -; mRNA.
DR EMBL; AL031986; CAA21465.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161588; CAB81488.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE86571.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86572.1; -; Genomic_DNA.
DR EMBL; AF424632; AAL11625.1; ALT_FRAME; mRNA.
DR EMBL; AY113045; AAM47353.1; -; mRNA.
DR EMBL; AK227213; BAE99251.1; -; mRNA.
DR RefSeq; NP_567989.1; NM_119745.3. [Q9C5Y0-1]
DR RefSeq; NP_849501.1; NM_179170.3. [Q9C5Y0-2]
DR AlphaFoldDB; Q9C5Y0; -.
DR SMR; Q9C5Y0; -.
DR BioGRID; 15015; 5.
DR IntAct; Q9C5Y0; 1.
DR STRING; 3702.AT4G35790.1; -.
DR SwissPalm; Q9C5Y0; -.
DR PaxDb; Q9C5Y0; -.
DR PRIDE; Q9C5Y0; -.
DR ProteomicsDB; 236633; -. [Q9C5Y0-1]
DR EnsemblPlants; AT4G35790.1; AT4G35790.1; AT4G35790. [Q9C5Y0-1]
DR EnsemblPlants; AT4G35790.2; AT4G35790.2; AT4G35790. [Q9C5Y0-2]
DR GeneID; 829733; -.
DR Gramene; AT4G35790.1; AT4G35790.1; AT4G35790. [Q9C5Y0-1]
DR Gramene; AT4G35790.2; AT4G35790.2; AT4G35790. [Q9C5Y0-2]
DR KEGG; ath:AT4G35790; -.
DR Araport; AT4G35790; -.
DR TAIR; locus:2125314; AT4G35790.
DR eggNOG; KOG1329; Eukaryota.
DR InParanoid; Q9C5Y0; -.
DR OMA; CAPHTAL; -.
DR OrthoDB; 181485at2759; -.
DR PhylomeDB; Q9C5Y0; -.
DR BioCyc; ARA:AT4G35790-MON; -.
DR BioCyc; MetaCyc:AT4G35790-MON; -.
DR BRENDA; 3.1.4.4; 399.
DR PRO; PR:Q9C5Y0; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9C5Y0; baseline and differential.
DR Genevisible; Q9C5Y0; AT.
DR GO; GO:0090395; C:plant cell papilla; IDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0070290; F:N-acylphosphatidylethanolamine-specific phospholipase D activity; IEA:UniProtKB-EC.
DR GO; GO:0004630; F:phospholipase D activity; IDA:TAIR.
DR GO; GO:0046473; P:phosphatidic acid metabolic process; 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:0012501; P:programmed cell death; IMP:TAIR.
DR GO; GO:0090333; P:regulation of stomatal closure; IMP:TAIR.
DR GO; GO:0009409; P:response to cold; 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 Alternative splicing; Calcium; Cell membrane; Hydrolase; Lipid degradation;
KW Lipid metabolism; Membrane; Metal-binding; Reference proteome; Repeat;
KW Stress response.
FT CHAIN 1..868
FT /note="Phospholipase D delta"
FT /id="PRO_0000218815"
FT DOMAIN 1..154
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 368..403
FT /note="PLD phosphodiesterase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT DOMAIN 713..740
FT /note="PLD phosphodiesterase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 373
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 375
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 380
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 718
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 720
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 725
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT BINDING 216
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q38882"
FT BINDING 373
FT /ligand="a 1,2-diacyl-sn-glycero-3-phosphate"
FT /ligand_id="ChEBI:CHEBI:58608"
FT /evidence="ECO:0000250|UniProtKB:Q38882"
FT BINDING 409
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q38882"
FT BINDING 440
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q38882"
FT BINDING 588
FT /ligand="a 1,2-diacyl-sn-glycero-3-phosphate"
FT /ligand_id="ChEBI:CHEBI:58608"
FT /evidence="ECO:0000250|UniProtKB:Q38882"
FT BINDING 718
FT /ligand="a 1,2-diacyl-sn-glycero-3-phosphate"
FT /ligand_id="ChEBI:CHEBI:58608"
FT /evidence="ECO:0000250|UniProtKB:Q38882"
FT BINDING 781
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q38882"
FT VAR_SEQ 354..364
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11549769,
FT ECO:0000303|PubMed:11706190, ECO:0000303|PubMed:14593172,
FT ECO:0000303|Ref.7"
FT /id="VSP_005029"
FT MUTAGEN 410
FT /note="R->P: Total loss of activity."
FT /evidence="ECO:0000269|PubMed:11706190"
FT MUTAGEN 622
FT /note="R->D: Loss of 80% of PIP2-stimulated activity and
FT only 50% of oleate-stimulated activity."
FT /evidence="ECO:0000269|PubMed:11706190"
SQ SEQUENCE 868 AA; 98917 MW; AC18289664685178 CRC64;
MAEKVSEDVM LLHGDLDLKI VKARRLPNMD MFSEHLRRLF TACNACARPT DTDDVDPRDK
GEFGDKNIRS HRKVITSDPY VTVVVPQATL ARTRVLKNSQ EPLWDEKFNI SIAHPFAYLE
FQVKDDDVFG AQIIGTAKIP VRDIASGERI SGWFPVLGAS GKPPKAETAI FIDMKFTPFD
QIHSYRCGIA GDPERRGVRR TYFPVRKGSQ VRLYQDAHVM DGTLPAIGLD NGKVYEHGKC
WEDICYAISE AHHMIYIVGW SIFHKIKLVR ETKVPRDKDM TLGELLKYKS QEGVRVLLLV
WDDKTSHDKF GIKTPGVMGT HDEETRKFFK HSSVICVLSP RYASSKLGLF KQQASPSSSI
YIMTVVGTLF THHQKCVLVD TQAVGNNRKV TAFIGGLDLC DGRYDTPEHR ILHDLDTVFK
DDFHNPTFPA GTKAPRQPWH DLHCRIDGPA AYDVLINFEQ RWRKATRWKE FSLRLKGKTH
WQDDALIRIG RISWILSPVF KFLKDGTSII PEDDPCVWVS KEDDPENWHV QIFRSIDSGS
VKGFPKYEDE AEAQHLECAK RLVVDKSIQT AYIQTIRSAQ HFIYIENQYF LGSSYAWPSY
RDAGADNLIP MELALKIVSK IRAKERFAVY VVIPLWPEGD PKSGPVQEIL YWQSQTMQMM
YDVIAKELKA VQSDAHPLDY LNFYCLGKRE QLPDDMPATN GSVVSDSYNF QRFMIYVHAK
GMIVDDEYVL MGSANINQRS MAGTKDTEIA MGAYQPNHTW AHKGRHPRGQ VYGYRMSLWA
EHLGKTGDEF VEPSDLECLK KVNTISEENW KRFIDPKFSE LQGHLIKYPL QVDVDGKVSP
LPDYETFPDV GGKIIGAHSM ALPDTLTT
