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Phospholipase D gamma 2 (AtPLDgamma2) (PLD gamma 2) (EC 3.1.4.4)

 PLDG2_ARATH             Reviewed;         856 AA.
Q9T051; Q3EA52; Q9XH77;
03-APR-2002, integrated into UniProtKB/Swiss-Prot.
12-JUN-2007, sequence version 3.
23-MAY-2018, entry version 133.
RecName: Full=Phospholipase D gamma 2 {ECO:0000303|PubMed:11891260};
Short=AtPLDgamma2 {ECO:0000303|PubMed:11891260};
Short=PLD gamma 2 {ECO:0000303|PubMed:11891260};
EC=3.1.4.4 {ECO:0000269|PubMed:17098468};
Name=PLDGAMMA2 {ECO:0000303|PubMed:11891260};
OrderedLocusNames=At4g11830 {ECO:0000312|Araport:AT4G11830};
ORFNames=T26M18.40 {ECO:0000312|EMBL:CAB44321.1};
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
STRAIN=cv. Columbia;
Qin W., Dyer J.H., Zheng L., Wang X.;
"Isolation and nucleotide sequence of the fourth phospholipase D, PLD-
gamma 2, from Arabidopsis thaliana.";
(er) Plant Gene Register PGR99-084(1999).
[2]
SEQUENCE REVISION.
STRAIN=cv. Columbia;
Qin W., Dyer J.H., Zheng L., Wang X.;
Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY,
COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, AND
INDUCTION BY WOUNDING.
PubMed=17098468; DOI=10.1016/j.bbalip.2006.09.017;
Qin C., Li M., Qin W., Bahn S.C., Wang C., Wang X.;
"Expression and characterization of Arabidopsis phospholipase
Dgamma2.";
Biochim. Biophys. Acta 1761:1450-1458(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10617198; DOI=10.1038/47134;
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G.,
Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N.,
Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M.,
Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M.,
Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T.,
Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I.,
Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P.,
Langham S.-A., McCullagh B., Bilham L., Robben J.,
van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F.,
Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E.,
Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W.,
Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P.,
Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H.,
De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R.,
van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S.,
Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R.,
Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S.,
Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H.,
Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S.,
Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A.,
Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R.,
Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S.,
Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E.,
Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A.,
Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T.,
Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C.,
Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S.,
Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K.,
Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L.,
Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J.,
Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J.,
Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D.,
Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D.,
Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C.,
Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C.,
Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R.,
Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S.,
Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A.,
Chen E., Marra M.A., Martienssen R., McCombie W.R.;
"Sequence and analysis of chromosome 4 of the plant Arabidopsis
thaliana.";
Nature 402:769-777(1999).
[5]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[6]
SUBCELLULAR LOCATION.
PubMed=10198096; DOI=10.1104/pp.119.4.1371;
Fan L., Zheng S., Cui D., Wang X.;
"Subcellular distribution and tissue expression of phospholipase
Dalpha, Dbeta, and Dgamma in Arabidopsis.";
Plant Physiol. 119:1371-1378(1999).
[7]
INDUCTION BY WOUNDING.
PubMed=11090221; DOI=10.1105/tpc.12.11.2237;
Wang C., Zien C.A., Afitlhile M., Welti R., Hildebrand D.F., Wang X.;
"Involvement of phospholipase D in wound-induced accumulation of
jasmonic acid in arabidopsis.";
Plant Cell 12:2237-2246(2000).
[8]
GENE FAMILY, AND NOMENCLATURE.
PubMed=11891260; DOI=10.1104/pp.010928;
Qin C., Wang X.;
"The Arabidopsis phospholipase D family. Characterization of a
calcium-independent and phosphatidylcholine-selective PLD zeta 1 with
distinct regulatory domains.";
Plant Physiol. 128:1057-1068(2002).
[9]
FUNCTION, INDUCTION BY ALUMINUM, AND DISRUPTION PHENOTYPE.
PubMed=22163277; DOI=10.1371/journal.pone.0028086;
Zhao J., Wang C., Bedair M., Welti R., Sumner L.W., Baxter I.,
Wang X.;
"Suppression of phospholipase Dgammas confers increased aluminum
resistance in Arabidopsis thaliana.";
PLoS ONE 6:E28086-E28086(2011).
-!- FUNCTION: Hydrolyzes glycerol-phospholipids at the terminal
phosphodiesteric bond to generate phosphatidic acids (PA). Plays
an important role in various cellular processes, including
phytohormone action, vesicular trafficking, secretion,
cytoskeletal arrangement, meiosis, tumor promotion, pathogenesis,
membrane deterioration and senescence. Can use phosphatidylserine
but prefers ethanolamine-containing lipids as substrates. Can use
phosphatidylcholine (PC) as substrates in the presence of
phosphatidylethanolamine (PE) and PIP2 (PubMed:17098468). Involved
in membrane lipid modulation under aluminum (Al) stress and
negatively modulate plant tolerance to Al (PubMed:22163277).
{ECO:0000269|PubMed:17098468, ECO:0000269|PubMed:22163277}.
-!- CATALYTIC ACTIVITY: A phosphatidylcholine + H(2)O = choline + a
phosphatidate. {ECO:0000269|PubMed:17098468}.
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
Evidence={ECO:0000269|PubMed:17098468};
Note=Ca(2+). Requires micromolar level (PIP2-dependent).
{ECO:0000269|PubMed:17098468};
-!- ENZYME REGULATION: Inhibited by neomycin.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
pH dependence:
Optimum pH is 6.5 - 7.5. {ECO:0000269|PubMed:17098468};
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10198096}.
Membrane {ECO:0000269|PubMed:10198096}; Peripheral membrane
protein {ECO:0000269|PubMed:10198096}. Note=Found mainly
associated with intracellular membranes but also with
mitochondrial membranes, nuclei and clathrin-coated vesicles. Not
found in chloroplast.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=PLDgamma2a;
IsoId=Q9T051-1; Sequence=Displayed;
Name=2; Synonyms=PLDDgamma2b;
IsoId=Q9T051-2; Sequence=VSP_026065;
-!- TISSUE SPECIFICITY: Highly expressed in roots and flowers,
moderately in stems, leaves and seedlings and low in siliques. Not
detected in seeds. {ECO:0000269|PubMed:17098468}.
-!- INDUCTION: Activated by wounding, heavy metal, methyl salicylate,
osmotic and salt stresses (PubMed:11090221, PubMed:17098468). Up-
regulated by aluminum stress (PubMed:22163277).
{ECO:0000269|PubMed:11090221, ECO:0000269|PubMed:17098468,
ECO:0000269|PubMed:22163277}.
-!- DOMAIN: C2 domain is a calcium-binding fold, and the binding
promotes the protein association with membranes. In PLD gamma, all
the calcium-coordinating acidic amino acids are conserved.
{ECO:0000305}.
-!- DISRUPTION PHENOTYPE: No effect on tolerance to aluminum.
{ECO:0000269|PubMed:22163277}.
-!- SIMILARITY: Belongs to the phospholipase D family. C2-PLD
subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF138281; AAD38519.2; -; mRNA.
EMBL; DQ812124; ABG88077.1; -; mRNA.
EMBL; AL078606; CAB44321.1; -; Genomic_DNA.
EMBL; AL161532; CAB78226.1; -; Genomic_DNA.
EMBL; CP002687; AEE83054.1; -; Genomic_DNA.
EMBL; CP002687; AEE83055.1; -; Genomic_DNA.
PIR; T09342; T09342.
RefSeq; NP_192920.3; NM_117252.6. [Q9T051-1]
RefSeq; NP_849539.1; NM_179208.3. [Q9T051-2]
UniGene; At.70227; -.
ProteinModelPortal; Q9T051; -.
SMR; Q9T051; -.
BioGrid; 12087; 1.
STRING; 3702.AT4G11830.2; -.
PaxDb; Q9T051; -.
PRIDE; Q9T051; -.
EnsemblPlants; AT4G11830.1; AT4G11830.1; AT4G11830. [Q9T051-2]
EnsemblPlants; AT4G11830.2; AT4G11830.2; AT4G11830. [Q9T051-1]
GeneID; 826789; -.
Gramene; AT4G11830.1; AT4G11830.1; AT4G11830. [Q9T051-2]
Gramene; AT4G11830.2; AT4G11830.2; AT4G11830. [Q9T051-1]
KEGG; ath:AT4G11830; -.
Araport; AT4G11830; -.
TAIR; locus:2137025; AT4G11830.
eggNOG; KOG1329; Eukaryota.
eggNOG; COG1502; LUCA.
HOGENOM; HOG000240112; -.
InParanoid; Q9T051; -.
KO; K01115; -.
OrthoDB; EOG093601WQ; -.
PhylomeDB; Q9T051; -.
BioCyc; ARA:AT4G11830-MONOMER; -.
BRENDA; 3.1.4.4; 399.
PRO; PR:Q9T051; -.
Proteomes; UP000006548; Chromosome 4.
ExpressionAtlas; Q9T051; baseline and differential.
Genevisible; Q9T051; AT.
GO; GO:0009507; C:chloroplast; IDA:TAIR.
GO; GO:0022626; C:cytosolic ribosome; IDA:TAIR.
GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0070290; F:N-acylphosphatidylethanolamine-specific phospholipase D activity; IEA:UniProtKB-EC.
GO; GO:0004630; F:phospholipase D activity; IEA:UniProtKB-EC.
GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
GO; GO:0006643; P:membrane lipid metabolic process; IMP:TAIR.
GO; GO:0046470; P:phosphatidylcholine metabolic process; IEA:InterPro.
GO; GO:0006979; P:response to oxidative stress; IMP:TAIR.
Gene3D; 2.60.40.150; -; 1.
InterPro; IPR000008; C2_dom.
InterPro; IPR035892; C2_domain_sf.
InterPro; IPR001736; PLipase_D/transphosphatidylase.
InterPro; IPR024632; PLipase_D_C.
InterPro; IPR015679; PLipase_D_fam.
InterPro; IPR011402; PLipase_D_pln.
PANTHER; PTHR18896; PTHR18896; 1.
Pfam; PF00168; C2; 1.
Pfam; PF12357; PLD_C; 1.
Pfam; PF00614; PLDc; 2.
PIRSF; PIRSF036470; PLD_plant; 1.
SMART; SM00239; C2; 1.
SMART; SM00155; PLDc; 2.
PROSITE; PS50004; C2; 1.
PROSITE; PS50035; PLD; 2.
1: Evidence at protein level;
Alternative splicing; Calcium; Complete proteome; Cytoplasm;
Hydrolase; Lipid degradation; Lipid metabolism; Membrane;
Reference proteome; Repeat.
CHAIN 1 856 Phospholipase D gamma 2.
/FTId=PRO_0000218813.
DOMAIN 46 145 C2. {ECO:0000255|PROSITE-
ProRule:PRU00041}.
DOMAIN 362 397 PLD phosphodiesterase 1.
{ECO:0000255|PROSITE-ProRule:PRU00153}.
DOMAIN 702 729 PLD phosphodiesterase 2.
{ECO:0000255|PROSITE-ProRule:PRU00153}.
ACT_SITE 367 367 {ECO:0000255|PROSITE-ProRule:PRU00153}.
ACT_SITE 369 369 {ECO:0000255|PROSITE-ProRule:PRU00153}.
ACT_SITE 374 374 {ECO:0000255|PROSITE-ProRule:PRU00153}.
ACT_SITE 707 707 {ECO:0000255|PROSITE-ProRule:PRU00153}.
ACT_SITE 709 709 {ECO:0000255|PROSITE-ProRule:PRU00153}.
ACT_SITE 714 714 {ECO:0000255|PROSITE-ProRule:PRU00153}.
VAR_SEQ 37 68 Missing (in isoform 2).
{ECO:0000303|Ref.1}.
/FTId=VSP_026065.
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


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