Reviewed,
UniProtKB/Swiss-Prot Q38882 (PLDA1_ARATH)
Last modified
November 3, 2009.
Version 86.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended 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 |
| ||||||||
| Organism | Arabidopsis thaliana (Mouse-ear cress) [Complete proteome] | ||||||||
| Taxonomic identifier | 3702 [NCBI] | ||||||||
| Taxonomic lineage | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis |
Protein attributes
| Sequence length | 810 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence 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 vesicle › clathrin-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
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 810 | 810 | Phospholipase D alpha 1 | PRO_0000218808 | |||||
Regions | |||||||||
| Domain | 1 – 110 | 110 | C2 | ||||||
| Domain | 327 – 366 | 40 | PLD phosphodiesterase 1 | ||||||
| Domain | 656 – 683 | 28 | PLD phosphodiesterase 2 | ||||||
Sites | |||||||||
| Active site | 332 | 1 | Potential | ||||||
| Active site | 334 | 1 | Potential | ||||||
| Active site | 339 | 1 | Potential | ||||||
| Active site | 661 | 1 | Potential | ||||||
| Active site | 663 | 1 | Potential | ||||||
| Active site | 668 | 1 | Potential | ||||||
Experimental info | |||||||||
| Sequence conflict | 3 – 4 | 2 | QH → HD in AAC49274. Ref.1 | ||||||
| Sequence conflict | 26 | 1 | R → M in AAC49274. Ref.1 | ||||||
| Sequence conflict | 49 | 1 | Q → R in AAC49274. Ref.1 | ||||||
| Sequence conflict | 99 | 1 | N → I in AAC49274. Ref.1 | ||||||
| Sequence conflict | 121 | 1 | Missing in AAC49274. Ref.1 | ||||||
| Sequence conflict | 218 | 1 | A → T in AAC49274. Ref.1 | ||||||
| Sequence conflict | 301 – 302 | 2 | GS → ER in AAC49274. Ref.1 | ||||||
| Sequence conflict | 435 | 1 | D → E in AAC49274. Ref.1 | ||||||
| Sequence conflict | 560 – 561 | 2 | EK → DQ in AAC49274. Ref.1 | ||||||
| Sequence conflict | 607 – 612 | 6 | RAQGLE → KGLEGP in AAC49274. Ref.1 | ||||||
| Sequence conflict | 735 – 739 | 5 | SSLEC → KLSES in AAC49274. Ref.1 | ||||||
Sequences
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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. 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. | |
| IPI | IPI00527854. |
| RefSeq | NP_188194.1. |
| UniGene | At.23882 |
3D structure databases | |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | Q38882. 3 interactions. |
| STRING | Q38882. |
Proteomic databases | |
| PRIDE | Q38882. |
Genome annotation databases | |
| GeneID | 820816. |
| GenomeReviews | Gene locus AT3G15730 in contig BA000014_GR. |
| KEGG | ath:AT3G15730. |
| NMPDR | fig|3702.1.peg.13739. |
Organism-specific databases | |
| TAIR | At3g15730. |
Phylogenomic databases | |
| OMA | PKIPLAD. |
Enzyme and pathway databases | |
| BRENDA | 3.1.4.4. 302. |
Gene expression databases | |
| ArrayExpress | Q38882. |
| Genevestigator | Q38882. |
| GermOnline | AT3G15730. Arabidopsis thaliana. |
Family and domain databases | |
| InterPro | IPR000008. C2_Ca-dep. IPR015679. Phospholipase_D. IPR011402. PLD_pln. IPR001736. PLipase_D/transphosphatidylase. [Graphical view] |
| PANTHER | PTHR18896. Phospholipase_D. 1 hit. |
| Pfam | PF00168. C2. 1 hit. PF00614. PLDc. 2 hits. [Graphical view] |
| PIRSF | PIRSF036470. PLD_plant. 1 hit. |
| SMART | SM00239. C2. 1 hit. SM00155. PLDc. 2 hits. [Graphical view] |
| PROSITE | PS50004. C2. False negative. PS50035. PLD. 2 hits. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | PLDA1_ARATH | ||||||||
| Accession | Primary (citable) accession number: Q38882 Secondary accession number(s): Q944M4, Q9LW06 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | PPAP (Plant Proteome Annotation Project) | ||||||||
Relevant documents
| Arabidopsis thaliana Arabidopsis thaliana: entries and gene names |
| SIMILARITY comments Index of protein domains and families |

Clusters with


