PLDA3_ARATH
ID PLDA3_ARATH Reviewed; 820 AA.
AC P58766;
DT 03-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2002, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Phospholipase D alpha 3 {ECO:0000303|PubMed:11891260};
DE Short=AtPLDalpha3 {ECO:0000303|PubMed:11891260};
DE Short=PLD alpha 3 {ECO:0000303|PubMed:11891260};
DE EC=3.1.4.4 {ECO:0000250|UniProtKB:Q38882};
GN Name=PLDALPHA3 {ECO:0000303|PubMed:11891260};
GN OrderedLocusNames=At5g25370 {ECO:0000312|Araport:AT5G25370};
GN ORFNames=F18G18.110;
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
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 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 [4]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=18364466; DOI=10.1105/tpc.107.056390;
RA Hong Y., Pan X., Welti R., Wang X.;
RT "Phospholipase Dalpha3 is involved in the hyperosmotic response in
RT Arabidopsis.";
RL Plant Cell 20:803-816(2008).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19704505; DOI=10.4161/psb.3.12.7003;
RA Hong Y., Pan X., Welti R., Wang X.;
RT "The effect of phospholipase Dalpha3 on Arabidopsis response to
RT hyperosmotic stress and glucose.";
RL Plant Signal. Behav. 3:1099-1100(2008).
RN [6]
RP INDUCTION BY NAC045 AND NAC086, AND TISSUE SPECIFICITY.
RX PubMed=25081480; DOI=10.1126/science.1253736;
RA Furuta K.M., Yadav S.R., Lehesranta S., Belevich I., Miyashima S.,
RA Heo J.O., Vaten A., Lindgren O., De Rybel B., Van Isterdael G.,
RA Somervuo P., Lichtenberger R., Rocha R., Thitamadee S., Taehtiharju S.,
RA Auvinen P., Beeckman T., Jokitalo E., Helariutta Y.;
RT "Plant development. Arabidopsis NAC45/86 direct sieve element morphogenesis
RT culminating in enucleation.";
RL Science 345:933-937(2014).
CC -!- FUNCTION: Hydrolyzes glycerol-phospholipids at the terminal
CC phosphodiesteric bond to generate phosphatidic acids (PA)
CC (PubMed:18364466). Active with phosphatidylcholine (PC),
CC phosphatidylethanolamine (PE), phosphatidylglycerol (PG), and
CC phosphatidylserine (PS) as substrates (PubMed:18364466). No activity
CC toward phosphatidylinositol (PI) or PIP2 (PubMed:18364466). Positively
CC mediates plant responses to hyperosmotic stresses and promotes root
CC growth, flowering, and stress avoidance (PubMed:18364466,
CC PubMed:19704505). Not involved in the abscisic acid regulation of
CC stomatal movement and transpirational water loss (PubMed:18364466).
CC {ECO:0000269|PubMed:18364466, ECO:0000269|PubMed:19704505}.
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:0000250|UniProtKB:Q38882};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:Q38882};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q38882}.
CC Membrane {ECO:0000250|UniProtKB:Q38882}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q38882}.
CC -!- TISSUE SPECIFICITY: Expressed in buds, flowers, siliques, stems, old
CC leaves and roots (PubMed:18364466). Expressed in the sieve elements
CC (PubMed:25081480). {ECO:0000269|PubMed:18364466,
CC ECO:0000269|PubMed:25081480}.
CC -!- INDUCTION: Regulated by the transcription factors NAC045 and NAC086.
CC {ECO:0000269|PubMed:25081480}.
CC -!- DOMAIN: C2 domain is a calcium-binding fold, and the binding promotes
CC the protein association with membranes. A lower affinity toward calcium
CC can be anticipated for PLD alpha due to the absence of two potential
CC calcium ligands. {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotypes when grown under normal
CC conditions, but increased sensitivity to salinity and water deficiency
CC (PubMed:18364466). Late flowering in slightly dry conditions
CC (PubMed:18364466). Decreased sensitivity to glucose (PubMed:19704505).
CC {ECO:0000269|PubMed:18364466, ECO:0000269|PubMed:19704505}.
CC -!- SIMILARITY: Belongs to the phospholipase D family. C2-PLD subfamily.
CC {ECO:0000305}.
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DR EMBL; AC006258; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED93432.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM70004.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM70005.1; -; Genomic_DNA.
DR RefSeq; NP_001318645.1; NM_001343920.1.
DR RefSeq; NP_001331647.1; NM_001343921.1.
DR RefSeq; NP_197919.1; NM_122446.2.
DR AlphaFoldDB; P58766; -.
DR SMR; P58766; -.
DR STRING; 3702.AT5G25370.1; -.
DR PaxDb; P58766; -.
DR PRIDE; P58766; -.
DR ProteomicsDB; 226199; -.
DR EnsemblPlants; AT5G25370.1; AT5G25370.1; AT5G25370.
DR EnsemblPlants; AT5G25370.2; AT5G25370.2; AT5G25370.
DR EnsemblPlants; AT5G25370.3; AT5G25370.3; AT5G25370.
DR GeneID; 832609; -.
DR Gramene; AT5G25370.1; AT5G25370.1; AT5G25370.
DR Gramene; AT5G25370.2; AT5G25370.2; AT5G25370.
DR Gramene; AT5G25370.3; AT5G25370.3; AT5G25370.
DR KEGG; ath:AT5G25370; -.
DR Araport; AT5G25370; -.
DR TAIR; locus:2145452; AT5G25370.
DR eggNOG; KOG1329; Eukaryota.
DR HOGENOM; CLU_004684_0_0_1; -.
DR InParanoid; P58766; -.
DR OrthoDB; 128697at2759; -.
DR PhylomeDB; P58766; -.
DR BioCyc; ARA:AT5G25370-MON; -.
DR PRO; PR:P58766; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; P58766; baseline and differential.
DR Genevisible; P58766; AT.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; IDA:TAIR.
DR GO; GO:0046466; P:membrane lipid catabolic 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:0009737; P:response to abscisic acid; IMP:TAIR.
DR GO; GO:0009651; P:response to salt stress; IMP:TAIR.
DR GO; GO:0009414; P:response to water deprivation; 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 2: Evidence at transcript level;
KW Calcium; Cytoplasm; Hydrolase; Lipid degradation; Lipid metabolism;
KW Membrane; Metal-binding; Reference proteome; Repeat.
FT CHAIN 1..820
FT /note="Phospholipase D alpha 3"
FT /id="PRO_0000218817"
FT DOMAIN 1..133
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 334..371
FT /note="PLD phosphodiesterase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT DOMAIN 662..689
FT /note="PLD phosphodiesterase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 339
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 341
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 346
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 667
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 669
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 674
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT BINDING 194
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q38882"
FT BINDING 339
FT /ligand="a 1,2-diacyl-sn-glycero-3-phosphate"
FT /ligand_id="ChEBI:CHEBI:58608"
FT /evidence="ECO:0000250|UniProtKB:Q38882"
FT BINDING 377
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q38882"
FT BINDING 411
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q38882"
FT BINDING 528
FT /ligand="a 1,2-diacyl-sn-glycero-3-phosphate"
FT /ligand_id="ChEBI:CHEBI:58608"
FT /evidence="ECO:0000250|UniProtKB:Q38882"
FT BINDING 667
FT /ligand="a 1,2-diacyl-sn-glycero-3-phosphate"
FT /ligand_id="ChEBI:CHEBI:58608"
FT /evidence="ECO:0000250|UniProtKB:Q38882"
FT BINDING 730
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q38882"
SQ SEQUENCE 820 AA; 93362 MW; FFB9247276BCEB7B CRC64;
MTEQLLLHGT LEVKIYRIDK LHQRSRFNLC GKGNKEPTGK KTQSQIKRLT DSCTSLFGGH
LYATIDLDRS RVARTMMRRH PKWLQSFHVY TAHSISKIIF TVKEDEPVSA SLIGRAYLPV
TEVITGQPID RWLDILDENR RPIQGGSKLH VRVKFTHVTQ DVNWNKGIIL PSFNGVPNAY
FNQREGCKVT LYQDAHVLNE YPDVTLTGGQ VIYKHHRCWE EIFDAIWEAK HLIYIAGWSV
NTDVTLVRDP KRTRPGGDLK LGELLKKKAE ENVTVLMLVW DDRTSHEVFK RDGLMMTHDQ
ETYDYFKNTK VRCVLCPRNP DNGDSIVQGF EVATMFTHHQ KTIVVDSEVD GSLTKRRIVS
FLGGIDLCDG RYDTVEHPLF GTLNSVHAND FHQPNFDGAS IKKGGPREPW HDIHCKLDGP
AAWDVLYNFE QRWMKQGSGR RYLISMAQLA EITVPPLPIV QPDNEEGWTV QVFRSIDDGA
VEGFPEDPRE AASIGLISGK DNVIERSIQD AYVNAIRRAK NFIYIENQYF LGSSFGWNSR
DINLNEINAL QLIPKEISLK IVSKIEAGER FSVYIVIPLW PEGKPGSASV QAILDWQRRT
MEMMYTDIII ALRKKGLDAN PRDYLTFFCL GNREKGKVGE YLPPEKPEAN SDYARAQESR
RFMIYVHSKM MIVDDEYIII GSANINQRSM DGGRDTEIAM GAYQPSHLLS TNNMRPVGQI
FSFRISLWLE HLRVTTNAFQ CPESEECIRM VNATADELWG LYSAQEYPRN DDLPGHLLSY
PISIGSNGEV TNLAGTEFFP DTNAKVVGEK SNYLPPILTS
