Reviewed,
UniProtKB/Swiss-Prot P97813 (PLD2_MOUSE)
Last modified
October 13, 2009.
Version 83.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
Customize display | text xml rdf/xml gff fasta |
Names and origin
| Protein names | Recommended name: Phospholipase D2 Short name=PLD 2 Short name=mPLD2 EC=3.1.4.4 Alternative name(s): Choline phosphatase 2 Phosphatidylcholine-hydrolyzing phospholipase D2 PLD1C | ||
| Gene names |
| ||
| Organism | Mus musculus (Mouse) | ||
| Taxonomic identifier | 10090 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus |
Protein attributes
| Sequence length | 933 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | May have a role in signal-induced cytoskeletal regulation and/or endocytosis. |
| Catalytic activity | A phosphatidylcholine + H2O = choline + a phosphatidate. |
| Enzyme regulation | Stimulated by phosphatidylinositol 4,5-bisphosphate. Is not responsive to either ADP-ribosylation factor-1 (ARF-1) or GTP-binding proteins such as RHOA. |
| Subunit structure | Interacts with PIP5K1A By similarity. Interacts with EGFR. |
| Subcellular location | |
| Tissue specificity | Ubiquitous. Highest levels in brain and lung. Ref.3 |
| Developmental stage | Expressed at high levels in the hippocampus at the earliest time at which it is defined as a structure and also in ventricular neural cells as well as differentiating neurons outside of the ventricular region. Expressed during development in lower levels in mesenchymal cells derived from the neural crest that are destined to form bones of the skull. |
| Post-translational modification | Phosphorylated on Tyr-11; most likely by EGFR. Ref.4 |
| Sequence similarities | Belongs to the phospholipase D family. Contains 1 PH domain. Contains 2 PLD phosphodiesterase domains. Contains 1 PX (phox homology) domain. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Lipid degradation |
| Cellular component | Membrane |
| Coding sequence diversity | Alternative splicing |
| Domain | Repeat |
| Molecular function | Hydrolase |
| PTM | Phosphoprotein |
| Gene Ontology (GO) | |
| Biological process | G-protein coupled receptor internalization Inferred from direct assay. Source: MGI cell communicationInferred from electronic annotation. Source: InterPro lipid catabolic processInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | brush border membrane Inferred from direct assay. Source: MGI extrinsic to membraneInferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | NAPE-specific phospholipase D activity Inferred from electronic annotation. Source: EC phosphoinositide bindingInferred from electronic annotation. Source: InterPro phospholipase D activityInferred from electronic annotation. Source: EC protein bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Alternative products
| This entry describes 1 isoform produced by alternative splicing. [Select] Note: At least 3 isoforms are produced. | ||||||
| Isoform 1 (identifier: P97813-1) This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 933 | 933 | Phospholipase D2 | PRO_0000218806 | |||||
Regions | |||||||||
| Domain | 65 – 195 | 131 | PX | ||||||
| Domain | 203 – 311 | 109 | PH | ||||||
| Domain | 437 – 464 | 28 | PLD phosphodiesterase 1 | ||||||
| Domain | 751 – 778 | 28 | PLD phosphodiesterase 2 | ||||||
| Region | 441 – 788 | 348 | Catalytic | ||||||
Amino acid modifications | |||||||||
| Modified residue | 11 | 1 | Phosphotyrosine Ref.4 | ||||||
Experimental info | |||||||||
| Mutagenesis | 11 | 1 | Y → F: 2-fold increase in basal phospholipase activity. Ref.4 | ||||||
Sequences
| ||||||||||||||||||
References
| [1] | "Phospholipase D2, a distinct phospholipase D isoform with novel regulatory properties that provokes cytoskeletal reorganization." Colley W.C., Sung T.-C., Roll R., Jenco J.M., Hammond S.M., Altshuller Y.M., Bar-Sagi D., Morris A.J., Frohman M.A. Curr. Biol. 7:191-201(1997) [PubMed: 9395408] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. Tissue: Embryo and Neonatal brain. |
| [2] | "Organization and alternative splicing of the murine phospholipase D2 gene." Redina O.E., Frohman M.A. Biochem. J. 331:845-851(1998) [PubMed: 9560313] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 129. |
| [3] | "Cloning and expression analysis of murine phospholipase D1." Colley W.C., Altshuller Y.M., Sue-Ling C.K., Copeland N.G., Gilbert D.J., Jenkins N.A., Branch K.D., Tsirka S.E., Bollag R.J., Bollag W.B., Frohman M.A. Biochem. J. 326:745-753(1997) [PubMed: 9307024] [Abstract] Cited for: TISSUE SPECIFICITY. |
| [4] | "PLD2 complexes with the EGF receptor and undergoes tyrosine phosphorylation at a single site upon agonist stimulation." Slaaby R., Jensen T., Hansen H.S., Frohman M.A., Seedorf K. J. Biol. Chem. 273:33722-33727(1998) [PubMed: 9837959] [Abstract] Cited for: PHOSPHORYLATION AT TYR-11, MUTAGENESIS OF TYR-11. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| U87557 mRNA. Translation: AAC53173.1. AF052294 AF052292 Genomic DNA. Translation: AAC24519.1. | |
| IPI | IPI00469217. |
| RefSeq | NP_032902.1. |
| UniGene | Mm.260177 |
3D structure databases | |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | P97813. |
PTM databases | |
| PhosphoSite | P97813. |
Proteomic databases | |
| PRIDE | P97813. |
Genome annotation databases | |
| Ensembl | ENSMUST00000018429; ENSMUSP00000018429; ENSMUSG00000020828; Mus musculus. [Genome view] ENSMUST00000108557; ENSMUSP00000104197; ENSMUSG00000020828; Mus musculus. [Genome view] |
| GeneID | 18806. |
| KEGG | mmu:18806. |
| UCSC | uc007jvg.1. mouse. |
Organism-specific databases | |
| CTD | 18806. |
| MGI | MGI:892877. Pld2. |
Phylogenomic databases | |
| HOVERGEN | P97813. |
Enzyme and pathway databases | |
| BRENDA | 3.1.4.4. 244. |
Gene expression databases | |
| ArrayExpress | P97813. |
| Bgee | P97813. |
| CleanEx | MM_PLD2. |
| Genevestigator | P97813. |
| GermOnline | ENSMUSG00000020828. Mus musculus. |
Family and domain databases | |
| InterPro | IPR011993. PH_type. IPR015679. Phospholipase_D. IPR001849. Pleckstrin_homology. IPR001736. PLipase_D/transphosphatidylase. IPR016555. PLipase_D_euk. IPR001683. PX. [Graphical view] |
| Gene3D | G3DSA:2.30.29.30. PH_type. 1 hit. G3DSA:3.30.1520.10. PX. 1 hit. |
| PANTHER | PTHR18896. Phospholipase_D. 1 hit. |
| Pfam | PF00169. PH. 1 hit. PF00614. PLDc. 2 hits. PF00787. PX. 1 hit. [Graphical view] |
| PIRSF | PIRSF009376. Phospholipase_D_euk. 1 hit. |
| SMART | SM00233. PH. 1 hit. SM00155. PLDc. 2 hits. SM00312. PX. 1 hit. [Graphical view] |
| PROSITE | PS50003. PH_DOMAIN. False negative. PS50035. PLD. 2 hits. PS50195. PX. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 295114. |
| SOURCE | Search... |
Entry information
| Entry name | PLD2_MOUSE | ||||||||
| Accession | Primary (citable) accession number: P97813 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| MGD cross-references Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |

Clusters with


