Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot Q38882 (PLDA1_ARATH)

Last modified November 3, 2009. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Phospholipase D alpha 1
      Short name=PLD alpha 1
      Short name=AtPLDalpha1
    EC=3.1.4.4
Alternative name(s):
    Choline phosphatase 1
    Phosphatidylcholine-hydrolyzing phospholipase D 1
    PLDalpha
Gene names
Name: PLDALPHA1
Synonyms: PLD1
Ordered Locus Names: At3g15730
ORF Names: MSJ11.13
OrganismArabidopsis thaliana (Mouse-ear cress) [Complete proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidseurosids IIBrassicalesBrassicaceaeArabidopsis

Protein attributes

Sequence length810 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Hydrolyzes glycerol-phospholipids at the terminal phosphodiesteric bond. Plays an important role in various cellular processes, including phytohormone action and response to stress, characterized by acidification of the cell.

Catalytic activity

A phosphatidylcholine + H2O = choline + a phosphatidate.

Cofactor

Calcium. Calcium 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).

Subcellular location

Cytoplasm. Membrane; Peripheral membrane protein. Vacuole. Cytoplasmic vesicleclathrin-coated vesicle. Note: Found in vacuoles and also associated with plasma, microsomal and mitochondrial membranes and in clathrin-coated vesicles. Not found in chloroplast or nuclei. Activation increases association of preexisting enzyme with membranes. The distribution of this conventional PLD between membrane-associated and soluble fractions varied from organ to organ and is calcium-regulated. Ref.4

Tissue specificity

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

Induction

Activated by abscisic acid (ABA), ethylene, heavy metal, cold, salt and osmotic stresses.

Domain

C2 domain is a calcium-binding fold, and the binding promotes the protein association with membranes. A lower affinity toward calcium can be anticipated for PLD alpha due to the absence of two potential calcium ligands.

Sequence similarities

Belongs to the phospholipase D family. C2-PLD subfamily.

Contains 1 C2 domain.

Contains 2 PLD phosphodiesterase domains.

Sequence caution

The sequence AAC49274.1 differs from that shown. Reason: Frameshift at positions 81, 95, 369, 381, 458 and 491.

Ontologies

Keywords
   Biological processAbscisic acid signaling pathway
Ethylene signaling pathway
Lipid degradation
   Cellular componentCytoplasm
Cytoplasmic vesicle
Membrane
Vacuole
   DomainRepeat
   LigandCalcium
   Molecular functionHydrolase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processabscisic acid mediated signaling pathway

Inferred from electronic annotation. Source: UniProtKB-KW

ethylene mediated signaling pathway

Inferred from electronic annotation. Source: UniProtKB-KW

fatty acid metabolic process

Inferred from mutant phenotype. Source: TAIR

lipid catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

phosphatidylcholine metabolic process

Inferred from electronic annotation. Source: InterPro

positive regulation of abscisic acid mediated signaling pathway

Inferred from mutant phenotype. Source: TAIR

regulation of stomatal movement

Inferred from mutant phenotype. Source: TAIR

response to cadmium ion

Inferred from expression pattern. Source: TAIR

seed germination

Inferred from mutant phenotype. Source: TAIR

   Cellular componentchloroplast

Inferred from direct assay. Source: TAIR

clathrin-coated vesicle Ref.4

Inferred from direct assay. Source: TAIR

extrinsic to membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

mitochondrion Ref.4

Inferred from direct assay. Source: TAIR

nucleus Ref.4

Inferred from direct assay. Source: TAIR

plasma membrane Ref.4

Inferred from direct assay. Source: TAIR

vacuole

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionNAPE-specific phospholipase D activity

Inferred from electronic annotation. Source: EC

calcium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

phospholipase D activity

Inferred from direct assay. Source: TAIR

protein binding

Inferred from physical interaction. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

GPA1P180643EBI-962294,EBI-443890

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 810810Phospholipase D alpha 1
PRO_0000218808

Regions

Domain1 – 110110C2
Domain327 – 36640PLD phosphodiesterase 1
Domain656 – 68328PLD phosphodiesterase 2

Sites

Active site3321 Potential
Active site3341 Potential
Active site3391 Potential
Active site6611 Potential
Active site6631 Potential
Active site6681 Potential

Experimental info

Sequence conflict3 – 42QH → HD in AAC49274. Ref.1
Sequence conflict261R → M in AAC49274. Ref.1
Sequence conflict491Q → R in AAC49274. Ref.1
Sequence conflict991N → I in AAC49274. Ref.1
Sequence conflict1211Missing in AAC49274. Ref.1
Sequence conflict2181A → T in AAC49274. Ref.1
Sequence conflict301 – 3022GS → ER in AAC49274. Ref.1
Sequence conflict4351D → E in AAC49274. Ref.1
Sequence conflict560 – 5612EK → DQ in AAC49274. Ref.1
Sequence conflict607 – 6126RAQGLE → KGLEGP in AAC49274. Ref.1
Sequence conflict735 – 7395SSLEC → KLSES in AAC49274. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q38882-1 [UniParc].

Last modified February 21, 2001. Version 2.
Checksum: 87A8692E43BD73CE

FASTA81091,848
        10         20         30         40         50         60 
MAQHLLHGTL HATIYEVDAL HGGGVRQGFL GKILANVEET IGVGKGETQL YATIDLQKAR 

        70         80         90        100        110        120 
VGRTRKIKNE PKNPKWYESF HIYCAHLASD IIFTVKDDNP IGATLIGRAY IPVDQVINGE 

       130        140        150        160        170        180 
EVDQWVEILD NDRNPIQGGS KIHVKLQYFH VEEDRNWNMG IKSAKFPGVP YTFFSQRQGC 

       190        200        210        220        230        240 
KVSLYQDAHI PDNFVPRIPL AGGKNYEPQR CWEDIFDAIS NAKHLIYITG WSVYAEIALV 

       250        260        270        280        290        300 
RDSRRPKPGG DVTIGELLKK KASEGVRVLL LVWDDRTSVD VLKKDGLMAT HDEETENFFR 

       310        320        330        340        350        360 
GSDVHCILCP RNPDDGGSIV QSLQISTMFT HHQKIVVVDS EMPSRGGSEM RRIVSFVGGI 

       370        380        390        400        410        420 
DLCDGRYDTP FHSLFRTLDT VHHDDFHQPN FTGAAITKGG PREPWHDIHS RLEGPIAWDV 

       430        440        450        460        470        480 
MYNFEQRWSK QGGKDILVKL RDLSDIIITP SPVMFQEDHD VWNVQLFRSI DGGAAAGFPE 

       490        500        510        520        530        540 
SPEAAAEAGL VSGKDNIIDR SIQDAYIHAI RRAKDFIYVE NQYFLGSSFA WAADGITPED 

       550        560        570        580        590        600 
INALHLIPKE LSLKIVSKIE KGEKFRVYVV VPMWPEGLPE SGSVQAILDW QRRTMEMMYK 

       610        620        630        640        650        660 
DVIQALRAQG LEEDPRNYLT FFCLGNREVK KDGEYEPAEK PDPDTDYMRA QEARRFMIYV 

       670        680        690        700        710        720 
HTKMMIVDDE YIIIGSANIN QRSMDGARDS EIAMGGYQPH HLSHRQPARG QIHGFRMSLW 

       730        740        750        760        770        780 
YEHLGMLDET FLDPSSLECI EKVNRISDKY WDFYSSESLE HDLPGHLLRY PIGVASEGDI 

       790        800        810 
TELPGFEFFP DTKARILGTK SDYLPPILTT 

« Hide

References

« Hide 'large scale' references
[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: 10819329] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[3]"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. expand/collapse author list , 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: 14593172] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 273-810.
Strain: cv. Columbia.
[4]"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: 10198096] [Abstract]
Cited for: SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

U36381 mRNA. Translation: AAC49274.1. Frameshift.
AB017071 Genomic DNA. Translation: BAB02304.1.
AF428278 mRNA. Translation: AAL16110.1. Different initiation.
IPIIPI00527854.
RefSeqNP_188194.1.
UniGeneAt.23882

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

IntActQ38882. 3 interactions.
STRINGQ38882.

Proteomic databases

PRIDEQ38882.

Genome annotation databases

GeneID820816.
GenomeReviewsGene locus AT3G15730 in contig BA000014_GR.
KEGGath:AT3G15730.
NMPDRfig|3702.1.peg.13739.

Organism-specific databases

TAIRAt3g15730.

Phylogenomic databases

OMAPKIPLAD.

Enzyme and pathway databases

BRENDA3.1.4.4. 302.

Gene expression databases

ArrayExpressQ38882.
GenevestigatorQ38882.
GermOnlineAT3G15730. Arabidopsis thaliana.

Family and domain databases

InterProIPR000008. C2_Ca-dep.
IPR015679. Phospholipase_D.
IPR011402. PLD_pln.
IPR001736. PLipase_D/transphosphatidylase.
[Graphical view]
PANTHERPTHR18896. Phospholipase_D. 1 hit.
PfamPF00168. C2. 1 hit.
PF00614. PLDc. 2 hits.
[Graphical view]
PIRSFPIRSF036470. PLD_plant. 1 hit.
SMARTSM00239. C2. 1 hit.
SM00155. PLDc. 2 hits.
[Graphical view]
PROSITEPS50004. C2. False negative.
PS50035. PLD. 2 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePLDA1_ARATH
AccessionPrimary (citable) accession number: Q38882
Secondary accession number(s): Q944M4, Q9LW06
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 21, 2001
Last modified: November 3, 2009
This is version 86 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents