PLDG2_ARATH
ID PLDG2_ARATH Reviewed; 856 AA.
AC Q9T051; Q3EA52; Q9XH77;
DT 03-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 3.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Phospholipase D gamma 2 {ECO:0000303|PubMed:11891260};
DE Short=AtPLDgamma2 {ECO:0000303|PubMed:11891260};
DE Short=PLD gamma 2 {ECO:0000303|PubMed:11891260};
DE EC=3.1.4.4 {ECO:0000269|PubMed:17098468};
GN Name=PLDGAMMA2 {ECO:0000303|PubMed:11891260};
GN OrderedLocusNames=At4g11830 {ECO:0000312|Araport:AT4G11830};
GN ORFNames=T26M18.40 {ECO:0000312|EMBL:CAB44321.1};
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).
RC STRAIN=cv. Columbia;
RA Qin W., Dyer J.H., Zheng L., Wang X.;
RT "Isolation and nucleotide sequence of the fourth phospholipase D, PLD-gamma
RT 2, from Arabidopsis thaliana.";
RL (er) Plant Gene Register PGR99-084(1999).
RN [2]
RP SEQUENCE REVISION.
RC STRAIN=cv. Columbia;
RA Qin W., Dyer J.H., Zheng L., Wang X.;
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY,
RP COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, AND INDUCTION
RP BY WOUNDING.
RX PubMed=17098468; DOI=10.1016/j.bbalip.2006.09.017;
RA Qin C., Li M., Qin W., Bahn S.C., Wang C., Wang X.;
RT "Expression and characterization of Arabidopsis phospholipase Dgamma2.";
RL Biochim. Biophys. Acta 1761:1450-1458(2006).
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 SUBCELLULAR LOCATION.
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 [7]
RP INDUCTION BY WOUNDING.
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 [8]
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 [9]
RP FUNCTION, INDUCTION BY ALUMINUM, AND DISRUPTION PHENOTYPE.
RX PubMed=22163277; DOI=10.1371/journal.pone.0028086;
RA Zhao J., Wang C., Bedair M., Welti R., Sumner L.W., Baxter I., Wang X.;
RT "Suppression of phospholipase Dgammas confers increased aluminum resistance
RT in Arabidopsis thaliana.";
RL PLoS ONE 6:E28086-E28086(2011).
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, vesicular trafficking, secretion, cytoskeletal arrangement,
CC meiosis, tumor promotion, pathogenesis, membrane deterioration and
CC senescence. Can use phosphatidylserine but prefers ethanolamine-
CC containing lipids as substrates. Can use phosphatidylcholine (PC) as
CC substrates in the presence of phosphatidylethanolamine (PE) and PIP2
CC (PubMed:17098468). Involved in membrane lipid modulation under aluminum
CC (Al) stress and negatively modulate plant tolerance to Al
CC (PubMed:22163277). {ECO:0000269|PubMed:17098468,
CC ECO:0000269|PubMed:22163277}.
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:17098468};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:17098468};
CC Note=Ca(2+). Requires micromolar level (PIP2-dependent).
CC {ECO:0000269|PubMed:17098468};
CC -!- ACTIVITY REGULATION: Inhibited by neomycin.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6.5 - 7.5. {ECO:0000269|PubMed:17098468};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10198096}. Membrane
CC {ECO:0000269|PubMed:10198096}; Peripheral membrane protein
CC {ECO:0000269|PubMed:10198096}. Note=Found mainly associated with
CC intracellular membranes but also with mitochondrial membranes, nuclei
CC and clathrin-coated vesicles. Not found in chloroplast.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=PLDgamma2a;
CC IsoId=Q9T051-1; Sequence=Displayed;
CC Name=2; Synonyms=PLDDgamma2b;
CC IsoId=Q9T051-2; Sequence=VSP_026065;
CC -!- TISSUE SPECIFICITY: Highly expressed in roots and flowers, moderately
CC in stems, leaves and seedlings and low in siliques. Not detected in
CC seeds. {ECO:0000269|PubMed:17098468}.
CC -!- INDUCTION: Activated by wounding, heavy metal, methyl salicylate,
CC osmotic and salt stresses (PubMed:11090221, PubMed:17098468). Up-
CC regulated by aluminum stress (PubMed:22163277).
CC {ECO:0000269|PubMed:11090221, ECO:0000269|PubMed:17098468,
CC ECO:0000269|PubMed:22163277}.
CC -!- DOMAIN: C2 domain is a calcium-binding fold, and the binding promotes
CC the protein association with membranes. In PLD gamma, all the calcium-
CC coordinating acidic amino acids are conserved. {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: No effect on tolerance to aluminum.
CC {ECO:0000269|PubMed:22163277}.
CC -!- SIMILARITY: Belongs to the phospholipase D family. C2-PLD subfamily.
CC {ECO:0000305}.
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DR EMBL; AF138281; AAD38519.2; -; mRNA.
DR EMBL; DQ812124; ABG88077.1; -; mRNA.
DR EMBL; AL078606; CAB44321.1; -; Genomic_DNA.
DR EMBL; AL161532; CAB78226.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE83054.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE83055.1; -; Genomic_DNA.
DR PIR; T09342; T09342.
DR RefSeq; NP_192920.3; NM_117252.6. [Q9T051-1]
DR RefSeq; NP_849539.1; NM_179208.3. [Q9T051-2]
DR AlphaFoldDB; Q9T051; -.
DR SMR; Q9T051; -.
DR BioGRID; 12087; 1.
DR STRING; 3702.AT4G11830.2; -.
DR PaxDb; Q9T051; -.
DR PRIDE; Q9T051; -.
DR ProteomicsDB; 234726; -. [Q9T051-1]
DR EnsemblPlants; AT4G11830.1; AT4G11830.1; AT4G11830. [Q9T051-2]
DR EnsemblPlants; AT4G11830.2; AT4G11830.2; AT4G11830. [Q9T051-1]
DR GeneID; 826789; -.
DR Gramene; AT4G11830.1; AT4G11830.1; AT4G11830. [Q9T051-2]
DR Gramene; AT4G11830.2; AT4G11830.2; AT4G11830. [Q9T051-1]
DR KEGG; ath:AT4G11830; -.
DR Araport; AT4G11830; -.
DR TAIR; locus:2137025; AT4G11830.
DR eggNOG; KOG1329; Eukaryota.
DR InParanoid; Q9T051; -.
DR OrthoDB; 133306at2759; -.
DR PhylomeDB; Q9T051; -.
DR BioCyc; ARA:AT4G11830-MON; -.
DR BRENDA; 3.1.4.4; 399.
DR PRO; PR:Q9T051; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9T051; baseline and differential.
DR Genevisible; Q9T051; AT.
DR GO; GO:0022626; C:cytosolic ribosome; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0006643; P:membrane lipid 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:0006979; P:response to oxidative stress; 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; Cytoplasm; Hydrolase; Lipid degradation;
KW Lipid metabolism; Membrane; Metal-binding; Reference proteome; Repeat.
FT CHAIN 1..856
FT /note="Phospholipase D gamma 2"
FT /id="PRO_0000218813"
FT DOMAIN 21..161
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 362..397
FT /note="PLD phosphodiesterase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT DOMAIN 702..729
FT /note="PLD phosphodiesterase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 367
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 369
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 374
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 707
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 709
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 714
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT BINDING 223
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q38882"
FT BINDING 367
FT /ligand="a 1,2-diacyl-sn-glycero-3-phosphate"
FT /ligand_id="ChEBI:CHEBI:58608"
FT /evidence="ECO:0000250|UniProtKB:Q38882"
FT BINDING 403
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q38882"
FT BINDING 435
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q38882"
FT BINDING 562
FT /ligand="a 1,2-diacyl-sn-glycero-3-phosphate"
FT /ligand_id="ChEBI:CHEBI:58608"
FT /evidence="ECO:0000250|UniProtKB:Q38882"
FT BINDING 707
FT /ligand="a 1,2-diacyl-sn-glycero-3-phosphate"
FT /ligand_id="ChEBI:CHEBI:58608"
FT /evidence="ECO:0000250|UniProtKB:Q38882"
FT BINDING 770
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q38882"
FT VAR_SEQ 37..68
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_026065"
SQ SEQUENCE 856 AA; 96024 MW; A03DB7F8189D2B6C CRC64;
MSMGGGSNHE FGQWLDQQLV PLATSSGSLM VELLHGNLDI WVKEAKHLPN MICYRNKLVG
GISFSELGRR IRKVDGEKSS KFTSDPYVTV SISGAVIGRT FVISNSENPV WMQHFDVPVA
HSAAEVHFVV KDNDPIGSKI IGVVGIPTKQ LCSGNRIEGL FPILNSSGKP CRKGAMLSLS
IQYTPMERMR LYQKGVGSGV ECVGVPGTYF PLRKGGRVTL YQDAHVDDGT LPSVHLDGGI
QYRHGKCWED MADAIRRARR LIYITGWSVF HPVRLVRRNN DPTEGTLGEL LKVKSQEGVR
VLVLVWDDPT SMSFPGFSTK GLMNTSDEET RRFFKHSSVQ VLLCPRYGGK GHSFIKKSEV
ETIYTHHQKT MIVDAEAAQN RRKIVAFVGG LDLCNGRFDT PKHSLFGTLK TLHKDDFHNP
NFVTTEDVGP REPWHDLHSK IDGPAAYDVL ANFEERWMAS KPRGIGKGRT SFDDSLLRIN
RIPDIMGLSE ASSANDNDPE SWHVQVFRSI DSTSVKGFPK DPEEATGRNL LCGKNILIDM
SIHAAYVKAI RSAQHFIYIE NQYFLGSSFN WDSNKDLGAN NLIPMEIALK IANKIRAREN
FAAYIVIPMW PEGAPTSKPI QRILYWQHKT MQMMYQTIYK ALLEVGLDGQ LEPQDFLNFF
CLGNREVGTR EVPDGTVNVY NCPRKPPQPN AAQVQALKSR RFMIYVHSKG MVVDDEFVLI
GSANINQRSL EGTRDTEIAM GGYQPHHSWA KKGSRPRGQI FGYRMSLWAE HLGFLEQEFE
EPENMECVRR VRQLSELNWG QYAAEEVTEM SGHLLKYPVQ VDKTGKVSSL PGCETFPDLG
GKIIGSFLTL QENLTI
