Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Phospholipase D beta 1

Gene

PLDBETA1

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, vesicular trafficking, secretion, cytoskeletal arrangement, meiosis, tumor promotion, pathogenesis, membrane deterioration and senescence. Involved in regulating stomatal movement and plant-water status (PubMed:11722757). Can use phosphatidylserine (PS) and phosphatidylethanolamine (PE) as substrates only in the presence of PIP2. Can use phosphatidylcholine (PC), phosphatidylglycerol (PG) or N-acylphosphatidylethanolamine (NAPE) as substrates in the presence of PE and PIP2 (PubMed:9578608). Modulates defense responses to bacterial and fungal pathogens (PubMed:23577648).3 Publications

Catalytic activityi

A phosphatidylcholine + H2O = choline + a phosphatidate.3 Publications

Cofactori

Ca2+2 PublicationsNote: Ca2+. Requires micromolar level (PIP2-dependent).2 Publications

Enzyme regulationi

Inhibited by neomycin. Up-regulated by PIP2 binding.2 Publications

pH dependencei

Optimum pH is 6.5 to 7.5.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei600 – 6001PROSITE-ProRule annotation
Active sitei602 – 6021PROSITE-ProRule annotation
Active sitei607 – 6071PROSITE-ProRule annotation
Active sitei934 – 9341PROSITE-ProRule annotation
Active sitei936 – 9361PROSITE-ProRule annotation
Active sitei941 – 9411PROSITE-ProRule annotation

GO - Molecular functioni

  • N-acylphosphatidylethanolamine-specific phospholipase D activity Source: UniProtKB-EC
  • phosphatidylinositol-4,5-bisphosphate binding Source: TAIR
  • phospholipase D activity Source: TAIR

GO - Biological processi

  • defense response to bacterium, incompatible interaction Source: TAIR
  • lipid catabolic process Source: UniProtKB-KW
  • response to cadmium ion Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Keywords - Ligandi

Calcium

Enzyme and pathway databases

BioCyciARA:AT2G42010-MONOMER.
MetaCyc:AT2G42010-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Phospholipase D beta 11 Publication (EC:3.1.4.43 Publications)
Short name:
AtPLDbeta11 Publication
Short name:
PLD beta 11 Publication
Short name:
PLDbeta1 Publication
Gene namesi
Name:PLDBETA11 Publication
Ordered Locus Names:At2g42010Imported
ORF Names:T6D20.10Imported
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 2

Organism-specific databases

TAIRiAT2G42010.

Subcellular locationi

  • Cytoplasm By similarity
  • Membrane By similarity; Peripheral membrane protein By similarity

GO - Cellular componenti

  • cytoplasm Source: UniProtKB-SubCell
  • membrane Source: UniProtKB-SubCell
  • plasmodesma Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10831083Phospholipase D beta 1PRO_0000218810Add
BLAST

Proteomic databases

PaxDbiP93733.
PRIDEiP93733.

PTM databases

iPTMnetiP93733.

Expressioni

Tissue specificityi

Expressed in stems, and to a lower amount in leaves, flowers and siliques.1 Publication

Inductioni

Activated by wounding, methyl jasmonate, heavy metal, osmotic and salt stresses.1 Publication

Gene expression databases

GenevisibleiP93733. AT.

Interactioni

Protein-protein interaction databases

BioGridi4139. 3 interactions.
IntActiP93733. 1 interaction.
MINTiMINT-8064634.
STRINGi3702.AT2G42010.1.

Structurei

3D structure databases

ProteinModelPortaliP93733.
SMRiP93733. Positions 273-416.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini260 – 377118C2PROSITE-ProRule annotationAdd
BLAST
Domaini595 – 63036PLD phosphodiesterase 1PROSITE-ProRule annotationAdd
BLAST
Domaini929 – 95628PLD phosphodiesterase 2PROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi6 – 147142Pro-richAdd
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 micromolar Ca2+ concentrations. Exhibits three Ca2+-binding sites. Binds also PIP2.1 Publication

Sequence similaritiesi

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

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG1329. Eukaryota.
COG1502. LUCA.
HOGENOMiHOG000240112.
InParanoidiP93733.
KOiK01115.
OMAiCPESLEC.

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.
[Graphical view]
PANTHERiPTHR18896. PTHR18896. 2 hits.
PfamiPF00168. C2. 1 hit.
PF12357. PLD_C. 1 hit.
PF00614. PLDc. 2 hits.
[Graphical view]
SMARTiSM00239. C2. 1 hit.
SM00155. PLDc. 2 hits.
[Graphical view]
SUPFAMiSSF49562. SSF49562. 1 hit.
PROSITEiPS50004. C2. 1 hit.
PS50035. PLD. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P93733-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDNHGPRYPY PYGQYPYPYP YPAPYRPPSS EPYPPPPTNQ YSAPYYPYPP
60 70 80 90 100
PPYATPPPYA SPPPPHQHTS GSHSGPLDYS HNPQPSSLAA APPEYHRHSF
110 120 130 140 150
DYQPSPYPYQ PQGNFGAYGP PPPHYSYQEP AQYPPPETKP QEPLPPPQQT
160 170 180 190 200
QGFQEYRRQD CLSTGGTGHD NVSNSGSSYP PVDELLGGLH ISTNQPGPSV
210 220 230 240 250
PQLSSLPSNS WQSRPGDLYG YPNSSFPSNS HLPQLGRVDS SSSYYASTES
260 270 280 290 300
PHSADMQMTL FGKGSLKVLL LHGNLDIWIY HAKNLPNMDM FHKTLGDMFG
310 320 330 340 350
RLPGKIEGQL TSKITSDPYV SVSVAGAVIG RTYVMSNSEN PVWMQHFYVP
360 370 380 390 400
VAHHAAEVHF VVKDSDVVGS QLIGLVTIPV EQIYSGAKIE GTYPILNSNG
410 420 430 440 450
KPCKPGANLS LSIQYTPMDK LSVYHHGVGA GPDYQGVPGT YFPLRKGGTV
460 470 480 490 500
RLYQDAHVPE GMLPGIRLDN GMSYEHGKCW HDMFDAIRQA RRLIYITGWS
510 520 530 540 550
VWHKVKLIRD KLGPASECTL GELLRSKSQE GVRVLLLIWD DPTSRSILGY
560 570 580 590 600
KTDGVMATHD EETRRFFKHS SVQVLLCPRN AGKRHSWVKQ REVGTIYTHH
610 620 630 640 650
QKNVIVDADA GGNRRKIIAF VGGLDLCDGR YDTPQHPLFR TLQTIHKDDF
660 670 680 690 700
HNPTFTGNLS GCPREPWHDL HSKIDGPAAY DVLTNFEERW LKAAKPSGIK
710 720 730 740 750
KFKTSYDDAL LRIDRIPDIL GVSDTPTVSE NDPEAWHVQI FRSIDSNSVK
760 770 780 790 800
GFPKDPKDAT CKNLVCGKNV LIDMSIHTAY VKAIRAAQHF IYIENQYFIG
810 820 830 840 850
SSYNWNAHKD IGANNLIPME IALKIAEKIR ANERFAAYIV IPMWPEGVPT
860 870 880 890 900
GAATQRILYW QHKTIQMMYE TIYKALVETG LEGAFSPQDY LNFFCLGNRE
910 920 930 940 950
MVDGIDNSGT GSPSNANTPQ ALSRKSRRFM VYVHSKGMVV DDEYVVIGSA
960 970 980 990 1000
NINQRSMEGT RDTEIAMGAY QPQHTWARKH SGPRGQIYGY RMSLWAEHMA
1010 1020 1030 1040 1050
TLDDCFTQPE SIECVRKVRT MGERNWKQFA AEEVSDMRGH LLKYPVEVDR
1060 1070 1080
KGKVRPLPGS ETFPDVGGNI VGSFIAIQEN LTI
Length:1,083
Mass (Da):121,101
Last modified:January 25, 2012 - v4
Checksum:i4A3558560FF8CFEB
GO

Sequence cautioni

The sequence AAB63542.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAC49656.2 differs from that shown.Sequencing errors.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U90439 Genomic DNA. Translation: AAB63542.2. Different initiation.
CP002685 Genomic DNA. Translation: AEC10063.1.
U84568 mRNA. Translation: AAC49656.2. Sequence problems.
PIRiH84848.
RefSeqiNP_565963.2. NM_129765.3.
UniGeneiAt.14711.

Genome annotation databases

EnsemblPlantsiAT2G42010.1; AT2G42010.1; AT2G42010.
GeneIDi818802.
GrameneiAT2G42010.1; AT2G42010.1; AT2G42010.
KEGGiath:AT2G42010.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U90439 Genomic DNA. Translation: AAB63542.2. Different initiation.
CP002685 Genomic DNA. Translation: AEC10063.1.
U84568 mRNA. Translation: AAC49656.2. Sequence problems.
PIRiH84848.
RefSeqiNP_565963.2. NM_129765.3.
UniGeneiAt.14711.

3D structure databases

ProteinModelPortaliP93733.
SMRiP93733. Positions 273-416.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4139. 3 interactions.
IntActiP93733. 1 interaction.
MINTiMINT-8064634.
STRINGi3702.AT2G42010.1.

PTM databases

iPTMnetiP93733.

Proteomic databases

PaxDbiP93733.
PRIDEiP93733.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT2G42010.1; AT2G42010.1; AT2G42010.
GeneIDi818802.
GrameneiAT2G42010.1; AT2G42010.1; AT2G42010.
KEGGiath:AT2G42010.

Organism-specific databases

TAIRiAT2G42010.

Phylogenomic databases

eggNOGiKOG1329. Eukaryota.
COG1502. LUCA.
HOGENOMiHOG000240112.
InParanoidiP93733.
KOiK01115.
OMAiCPESLEC.

Enzyme and pathway databases

BioCyciARA:AT2G42010-MONOMER.
MetaCyc:AT2G42010-MONOMER.

Miscellaneous databases

PROiP93733.

Gene expression databases

GenevisibleiP93733. 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.
[Graphical view]
PANTHERiPTHR18896. PTHR18896. 2 hits.
PfamiPF00168. C2. 1 hit.
PF12357. PLD_C. 1 hit.
PF00614. PLDc. 2 hits.
[Graphical view]
SMARTiSM00239. C2. 1 hit.
SM00155. PLDc. 2 hits.
[Graphical view]
SUPFAMiSSF49562. SSF49562. 1 hit.
PROSITEiPS50004. C2. 1 hit.
PS50035. PLD. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  2. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  3. "Molecular cloning and functional analysis of polyphosphoinositide-dependent phospholipase D, PLDbeta, from Arabidopsis."
    Pappan K., Qin W., Dyer J.H., Zheng L., Wang X.
    J. Biol. Chem. 272:7055-7061(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 60-1083, CATALYTIC ACTIVITY.
    Strain: cv. Columbia.
    Tissue: Hypocotyl.
  4. Wang X.
    Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  5. "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.
  6. "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.
  7. "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: CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
  8. "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: TISSUE SPECIFICITY.
  9. "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.
  10. "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: INDUCTION BY WOUNDING.
  11. "Regulation of plant water loss by manipulating the expression of phospholipase Dalpha."
    Sang Y., Zheng S., Li W., Huang B., Wang X.
    Plant J. 28:135-144(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. "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.
  13. "Arabidopsis phospholipase Dbeta1 modulates defense responses to bacterial and fungal pathogens."
    Zhao J., Devaiah S.P., Wang C., Li M., Welti R., Wang X.
    New Phytol. 199:228-240(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiPLDB1_ARATH
AccessioniPrimary (citable) accession number: P93733
Secondary accession number(s): F4ILZ0, P93745
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 3, 2002
Last sequence update: January 25, 2012
Last modified: July 6, 2016
This is version 129 of the entry and version 4 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.