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Protein

Phospholipase D alpha 1

Gene

PLDALPHA1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Hydrolyzes glycerol-phospholipids at the terminal phosphodiesteric bond to generate phosphatidic acids (PA). Plays an important role in various cellular processes, including phytohormone action and response to stress, characterized by acidification of the cell (PubMed:9437863). Involved in wound induction of jasmonic acid (PubMed:11090221). May be involved in membrane lipid remodeling (PubMed:11239826). Probably involved in freezing tolerance by modulating the cold-responsive genes and accumulation of osmolytes (PubMed:16949955). Can use phosphatidylcholine (PC), phosphatidylethanolamine (PE) and phosphatidylglycerol (PG) as substrates, both in presence or in absence of PIP2 (PubMed:9578608). Its main substrate is phosphatidylcholine (PubMed:11239826). Stimulates the intrinsic GTPase activity of GPA1 upon binding (PubMed:14594812). Mediates the abscisic acid effects on stomata through interaction with GPA1 and the production of phosphatidic acid that bind to ABI1 (PubMed:17261695, PubMed:17565616). Involved in seed aging and deterioration (PubMed:17565616). Involved in microtubule stabilization and salt tolerance (PubMed:23150630). Involved in abscisic acid-induced stomatal closure (PubMed:22392280).12 Publications

Catalytic activityi

A phosphatidylcholine + H2O = choline + a phosphatidate.2 Publications

Cofactori

Ca2+1 PublicationNote: Ca2+ requirement for activity depends on pH. Active either under acidic conditions with micromolar levels of calcium (PIP2-dependent) or at neutral pH with millimolar levels of calcium (PIP2-independent).1 Publication

Enzyme regulationi

Not inhibited by neomycin.1 Publication

pH dependencei

Optimum pH is 4.5 to 5.0 in the presence of micromolar levels of Ca2+ and PIP2. Optimum pH is 5.5 to 6.5 in the presence of millimolar levels of Ca2+.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei332 – 3321PROSITE-ProRule annotation
Active sitei334 – 3341PROSITE-ProRule annotation
Active sitei339 – 3391PROSITE-ProRule annotation
Active sitei661 – 6611PROSITE-ProRule annotation
Active sitei663 – 6631PROSITE-ProRule annotation
Active sitei668 – 6681PROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

  • abscisic acid-activated signaling pathway Source: UniProtKB-KW
  • ethylene-activated signaling pathway Source: UniProtKB-KW
  • fatty acid metabolic process Source: TAIR
  • lipid catabolic process Source: UniProtKB-KW
  • phosphatidylcholine metabolic process Source: InterPro
  • positive regulation of abscisic acid-activated signaling pathway Source: TAIR
  • regulation of stomatal movement Source: TAIR
  • response to abscisic acid Source: TAIR
  • response to cadmium ion Source: TAIR
  • seed germination Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Abscisic acid signaling pathway, Ethylene signaling pathway, Lipid degradation, Lipid metabolism

Keywords - Ligandi

Calcium

Enzyme and pathway databases

BioCyciARA:AT3G15730-MONOMER.
MetaCyc:AT3G15730-MONOMER.
BRENDAi3.1.4.4. 399.

Names & Taxonomyi

Protein namesi
Recommended name:
Phospholipase D alpha 11 Publication (EC:3.1.4.42 Publications)
Short name:
AtPLDalpha11 Publication
Short name:
PLD alpha 11 Publication
Alternative name(s):
Choline phosphatase 1
PLDalpha1 Publication
Phosphatidylcholine-hydrolyzing phospholipase D 1
Gene namesi
Name:PLDALPHA11 Publication
Synonyms:PLD1
Ordered Locus Names:At3g15730Imported
ORF Names:MSJ11.13Imported
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 3

Organism-specific databases

TAIRiAT3G15730.

Subcellular locationi

GO - Cellular componenti

  • chloroplast Source: TAIR
  • clathrin-coated vesicle Source: TAIR
  • cytosol Source: TAIR
  • endoplasmic reticulum Source: UniProtKB-KW
  • membrane Source: TAIR
  • mitochondrial membrane Source: UniProtKB-SubCell
  • mitochondrion Source: TAIR
  • nucleus Source: TAIR
  • plasma membrane Source: TAIR
  • plasmodesma Source: TAIR
  • vacuole Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoplasmic vesicle, Endoplasmic reticulum, Membrane, Microsome, Mitochondrion, Vacuole

Pathology & Biotechi

Disruption phenotypei

No visible phenotype under normal growth conditions, but improved resistance of the seeds to deterioration during storage (PubMed:17565616). Insensitivity to abscisic acid for both promotion of stomatal closure and inhibition of stomatal opening (PubMed:16614222). Hypersensitivity to hyperosmotic stress (PubMed:19017627). Increased NaCl-induced disorganization of microtubules (PubMed:23150630). No effect on abscisic acid-induced stomatal closure (PubMed:22392280). Pldalpha1 and plddelta double mutants have a suppressed abscisic acid-induced stomatal closure (PubMed:22392280).5 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi563 – 5631E → A: Decreased GPA1 binding. 1 Publication
Mutagenesisi564 – 5641K → A: Loss of GPA1 binding. 1 Publication
Mutagenesisi565 – 5651F → A: Decreased GPA1 binding. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 810810Phospholipase D alpha 1PRO_0000218808Add
BLAST

Proteomic databases

PaxDbiQ38882.
PRIDEiQ38882.

PTM databases

iPTMnetiQ38882.

Expressioni

Tissue specificityi

Highly expressed in roots, stems and flowers, moderately in leaves, seedlings and siliques. Not detected in seeds.1 Publication

Inductioni

Up-regulated by abscisic acid and ethylene (PubMed:9437863). Up-regulated by salt, dehydration and osmotic stresses (PubMed:19017627). Not regulated by abscisic acid (PubMed:22392280).3 Publications

Gene expression databases

ExpressionAtlasiQ38882. baseline and differential.
GenevisibleiQ38882. AT.

Interactioni

Subunit structurei

Interacts with GPA1 (PubMed:14594812, PubMed:16614222, PubMed:23913032). This binding inhibits PLDALPHA1 activity and is relieved by GTP (PubMed:14594812).3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
GPA1P180643EBI-962294,EBI-443890

Protein-protein interaction databases

BioGridi6150. 9 interactions.
IntActiQ38882. 5 interactions.
STRINGi3702.AT3G15730.1.

Structurei

3D structure databases

ProteinModelPortaliQ38882.
SMRiQ38882. Positions 7-136.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 110110C2Add
BLAST
Domaini327 – 36640PLD phosphodiesterase 1PROSITE-ProRule annotationAdd
BLAST
Domaini656 – 68328PLD phosphodiesterase 2PROSITE-ProRule annotationAdd
BLAST

Domaini

C2 domain is a calcium-binding fold, and the binding induces conformational changes, promoting the protein association with membranes. These conformational changes occure at millimolar Ca2+ concentrations. Binds also PIP2. A lower affinity toward calcium can be anticipated for PLD alpha due to the absence of two potential calcium ligands.1 Publication

Sequence similaritiesi

Contains 1 C2 domain.Curated
Contains 2 PLD phosphodiesterase domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG1329. Eukaryota.
COG1502. LUCA.
HOGENOMiHOG000240112.
InParanoidiQ38882.
KOiK01115.
OMAiRISDKYW.
PhylomeDBiQ38882.

Family and domain databases

Gene3Di2.60.40.150. 1 hit.
InterProiIPR000008. C2_dom.
IPR001736. PLipase_D/transphosphatidylase.
IPR024632. PLipase_D_C.
IPR015679. PLipase_D_fam.
IPR011402. PLipase_D_pln.
[Graphical view]
PANTHERiPTHR18896. PTHR18896. 2 hits.
PfamiPF00168. C2. 1 hit.
PF12357. PLD_C. 1 hit.
PF00614. PLDc. 2 hits.
[Graphical view]
PIRSFiPIRSF036470. PLD_plant. 1 hit.
SMARTiSM00239. C2. 1 hit.
SM00155. PLDc. 2 hits.
[Graphical view]
SUPFAMiSSF49562. SSF49562. 1 hit.
PROSITEiPS50035. PLD. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q38882-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAQHLLHGTL HATIYEVDAL HGGGVRQGFL GKILANVEET IGVGKGETQL
60 70 80 90 100
YATIDLQKAR VGRTRKIKNE PKNPKWYESF HIYCAHLASD IIFTVKDDNP
110 120 130 140 150
IGATLIGRAY IPVDQVINGE EVDQWVEILD NDRNPIQGGS KIHVKLQYFH
160 170 180 190 200
VEEDRNWNMG IKSAKFPGVP YTFFSQRQGC KVSLYQDAHI PDNFVPRIPL
210 220 230 240 250
AGGKNYEPQR CWEDIFDAIS NAKHLIYITG WSVYAEIALV RDSRRPKPGG
260 270 280 290 300
DVTIGELLKK KASEGVRVLL LVWDDRTSVD VLKKDGLMAT HDEETENFFR
310 320 330 340 350
GSDVHCILCP RNPDDGGSIV QSLQISTMFT HHQKIVVVDS EMPSRGGSEM
360 370 380 390 400
RRIVSFVGGI DLCDGRYDTP FHSLFRTLDT VHHDDFHQPN FTGAAITKGG
410 420 430 440 450
PREPWHDIHS RLEGPIAWDV MYNFEQRWSK QGGKDILVKL RDLSDIIITP
460 470 480 490 500
SPVMFQEDHD VWNVQLFRSI DGGAAAGFPE SPEAAAEAGL VSGKDNIIDR
510 520 530 540 550
SIQDAYIHAI RRAKDFIYVE NQYFLGSSFA WAADGITPED INALHLIPKE
560 570 580 590 600
LSLKIVSKIE KGEKFRVYVV VPMWPEGLPE SGSVQAILDW QRRTMEMMYK
610 620 630 640 650
DVIQALRAQG LEEDPRNYLT FFCLGNREVK KDGEYEPAEK PDPDTDYMRA
660 670 680 690 700
QEARRFMIYV HTKMMIVDDE YIIIGSANIN QRSMDGARDS EIAMGGYQPH
710 720 730 740 750
HLSHRQPARG QIHGFRMSLW YEHLGMLDET FLDPSSLECI EKVNRISDKY
760 770 780 790 800
WDFYSSESLE HDLPGHLLRY PIGVASEGDI TELPGFEFFP DTKARILGTK
810
SDYLPPILTT
Length:810
Mass (Da):91,848
Last modified:February 21, 2001 - v2
Checksum:i87A8692E43BD73CE
GO

Sequence cautioni

The sequence AAC49274.1 differs from that shown. Reason: Frameshift at positions 81, 95, 369, 381, 458 and 491. Curated
The sequence AAL16110.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti3 – 42QH → HD in AAC49274 (Ref. 1) Curated
Sequence conflicti26 – 261R → M in AAC49274 (Ref. 1) Curated
Sequence conflicti49 – 491Q → R in AAC49274 (Ref. 1) Curated
Sequence conflicti99 – 991N → I in AAC49274 (Ref. 1) Curated
Sequence conflicti121 – 1211Missing in AAC49274 (Ref. 1) Curated
Sequence conflicti218 – 2181A → T in AAC49274 (Ref. 1) Curated
Sequence conflicti301 – 3022GS → ER in AAC49274 (Ref. 1) Curated
Sequence conflicti435 – 4351D → E in AAC49274 (Ref. 1) Curated
Sequence conflicti560 – 5612EK → DQ in AAC49274 (Ref. 1) Curated
Sequence conflicti607 – 6126RAQGLE → KGLEGP in AAC49274 (Ref. 1) Curated
Sequence conflicti735 – 7395SSLEC → KLSES in AAC49274 (Ref. 1) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U36381 mRNA. Translation: AAC49274.1. Frameshift.
AB017071 Genomic DNA. Translation: BAB02304.1.
CP002686 Genomic DNA. Translation: AEE75720.1.
AK226887 mRNA. Translation: BAE98964.1.
AF428278 mRNA. Translation: AAL16110.1. Different initiation.
RefSeqiNP_188194.1. NM_112443.2.
UniGeneiAt.23882.

Genome annotation databases

EnsemblPlantsiAT3G15730.1; AT3G15730.1; AT3G15730.
GeneIDi820816.
GrameneiAT3G15730.1; AT3G15730.1; AT3G15730.
KEGGiath:AT3G15730.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U36381 mRNA. Translation: AAC49274.1. Frameshift.
AB017071 Genomic DNA. Translation: BAB02304.1.
CP002686 Genomic DNA. Translation: AEE75720.1.
AK226887 mRNA. Translation: BAE98964.1.
AF428278 mRNA. Translation: AAL16110.1. Different initiation.
RefSeqiNP_188194.1. NM_112443.2.
UniGeneiAt.23882.

3D structure databases

ProteinModelPortaliQ38882.
SMRiQ38882. Positions 7-136.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi6150. 9 interactions.
IntActiQ38882. 5 interactions.
STRINGi3702.AT3G15730.1.

PTM databases

iPTMnetiQ38882.

Proteomic databases

PaxDbiQ38882.
PRIDEiQ38882.

Protocols and materials databases

DNASUi820816.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT3G15730.1; AT3G15730.1; AT3G15730.
GeneIDi820816.
GrameneiAT3G15730.1; AT3G15730.1; AT3G15730.
KEGGiath:AT3G15730.

Organism-specific databases

TAIRiAT3G15730.

Phylogenomic databases

eggNOGiKOG1329. Eukaryota.
COG1502. LUCA.
HOGENOMiHOG000240112.
InParanoidiQ38882.
KOiK01115.
OMAiRISDKYW.
PhylomeDBiQ38882.

Enzyme and pathway databases

BioCyciARA:AT3G15730-MONOMER.
MetaCyc:AT3G15730-MONOMER.
BRENDAi3.1.4.4. 399.

Miscellaneous databases

PROiQ38882.

Gene expression databases

ExpressionAtlasiQ38882. baseline and differential.
GenevisibleiQ38882. AT.

Family and domain databases

Gene3Di2.60.40.150. 1 hit.
InterProiIPR000008. C2_dom.
IPR001736. PLipase_D/transphosphatidylase.
IPR024632. PLipase_D_C.
IPR015679. PLipase_D_fam.
IPR011402. PLipase_D_pln.
[Graphical view]
PANTHERiPTHR18896. PTHR18896. 2 hits.
PfamiPF00168. C2. 1 hit.
PF12357. PLD_C. 1 hit.
PF00614. PLDc. 2 hits.
[Graphical view]
PIRSFiPIRSF036470. PLD_plant. 1 hit.
SMARTiSM00239. C2. 1 hit.
SM00155. PLDc. 2 hits.
[Graphical view]
SUPFAMiSSF49562. SSF49562. 1 hit.
PROSITEiPS50035. PLD. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and nucleotide sequence of a cDNA encoding phospholipase D from Arabidopsis."
    Dyer J.H., Zheng L., Wang X.
    Plant Gene Register PGR95-096
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: cv. Columbia.
  2. "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence features of the regions of 4,504,864 bp covered by sixty P1 and TAC clones."
    Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.
    DNA Res. 7:131-135(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  4. "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
    Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.
    , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
    Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  5. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 273-810.
    Strain: cv. Columbia.
  6. "Molecular heterogeneity of phospholipase D (PLD). Cloning of PLDgamma and regulation of plant PLDgamma, -beta, and -alpha by polyphosphoinositides and calcium."
    Qin W., Pappan K., Wang X.
    J. Biol. Chem. 272:28267-28273(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, COFACTOR, ENZYME REGULATION.
  7. "Antisense suppression of phospholipase D alpha retards abscisic acid- and ethylene-promoted senescence of postharvest Arabidopsis leaves."
    Fan L., Zheng S., Wang X.
    Plant Cell 9:2183-2196(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION BY ABSCISIC ACID AND ETHYLENE.
  8. "Substrate selectivities and lipid modulation of plant phospholipase D alpha, -beta, and -gamma."
    Pappan K., Austin-Brown S., Chapman K.D., Wang X.
    Arch. Biochem. Biophys. 353:131-140(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBSTRATE SPECIFICITY.
  9. "Plant phospholipase Dalpha is an acidic phospholipase active at near-physiological Ca(2+) concentrations."
    Pappan K., Wang X.
    Arch. Biochem. Biophys. 368:347-353(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
  10. "Subcellular distribution and tissue expression of phospholipase Dalpha, Dbeta, and Dgamma in Arabidopsis."
    Fan L., Zheng S., Cui D., Wang X.
    Plant Physiol. 119:1371-1378(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  11. "Distinct Ca2+ binding properties of novel C2 domains of plant phospholipase dalpha and beta."
    Zheng L., Krishnamoorthi R., Zolkiewski M., Wang X.
    J. Biol. Chem. 275:19700-19706(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAIN, 3D-STRUCTURE MODELING.
  12. "Involvement of phospholipase D in wound-induced accumulation of jasmonic acid in arabidopsis."
    Wang C., Zien C.A., Afitlhile M., Welti R., Hildebrand D.F., Wang X.
    Plant Cell 12:2237-2246(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  13. "In vivo substrates and the contribution of the common phospholipase D, PLDalpha, to wound-induced metabolism of lipids in Arabidopsis."
    Zien C.A., Wang C., Wang X., Welti R.
    Biochim. Biophys. Acta 1530:236-248(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  14. "A novel phospholipase d of Arabidopsis that is activated by oleic acid and associated with the plasma membrane."
    Wang C., Wang X.
    Plant Physiol. 127:1102-1112(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
    Strain: cv. Columbia.
  15. "The Arabidopsis phospholipase D family. Characterization of a calcium-independent and phosphatidylcholine-selective PLD zeta 1 with distinct regulatory domains."
    Qin C., Wang X.
    Plant Physiol. 128:1057-1068(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENE FAMILY, NOMENCLATURE.
  16. "Arabidopsis phospholipase Dalpha1 interacts with the heterotrimeric G-protein alpha-subunit through a motif analogous to the DRY motif in G-protein-coupled receptors."
    Zhao J., Wang X.
    J. Biol. Chem. 279:1794-1800(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH GPA1, MUTAGENESIS OF GLU-563; LYS-564 AND PHE-565.
  17. "Suppression of phospholipase Dalpha1 induces freezing tolerance in Arabidopsis: response of cold-responsive genes and osmolyte accumulation."
    Rajashekar C.B., Zhou H.E., Zhang Y., Li W., Wang X.
    J. Plant Physiol. 163:916-926(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  18. "A bifurcating pathway directs abscisic acid effects on stomatal closure and opening in Arabidopsis."
    Mishra G., Zhang W., Deng F., Zhao J., Wang X.
    Science 312:264-266(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH GPA1.
  19. "Early PLDalpha-mediated events in response to progressive drought stress in Arabidopsis: a transcriptome analysis."
    Mane S.P., Vasquez-Robinet C., Sioson A.A., Heath L.S., Grene R.
    J. Exp. Bot. 58:241-252(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  20. "Enhancing seed quality and viability by suppressing phospholipase D in Arabidopsis."
    Devaiah S.P., Pan X., Hong Y., Roth M., Welti R., Wang X.
    Plant J. 50:950-957(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  21. Cited for: INDUCTION, DISRUPTION PHENOTYPE.
  22. "Phosphatidic acid regulates microtubule organization by interacting with MAP65-1 in response to salt stress in Arabidopsis."
    Zhang Q., Lin F., Mao T., Nie J., Yan M., Yuan M., Zhang W.
    Plant Cell 24:4555-4576(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  23. "Cooperative function of PLDdelta and PLDalpha1 in abscisic acid-induced stomatal closure in Arabidopsis."
    Uraji M., Katagiri T., Okuma E., Ye W., Hossain M.A., Masuda C., Miura A., Nakamura Y., Mori I.C., Shinozaki K., Murata Y.
    Plant Physiol. 159:450-460(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION BY ABSCISIC ACID, DISRUPTION PHENOTYPE.
  24. "Biochemical analysis of the interaction between phospholipase Dalpha1 and GTP-binding protein alpha-subunit from Arabidopsis thaliana."
    Zhao J., Wang X.
    Methods Mol. Biol. 1043:21-35(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GPA1.

Entry informationi

Entry nameiPLDA1_ARATH
AccessioniPrimary (citable) accession number: Q38882
Secondary accession number(s): Q0WV84, Q944M4, Q9LW06
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 21, 2001
Last modified: February 17, 2016
This is version 138 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.