Q99JE6 (PLCB3_RAT) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 93.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-3 EC=3.1.4.11 Alternative name(s): Phosphoinositide phospholipase C-beta-3 Phospholipase C-beta-3 Short name=PLC-beta-3 | ||
| Gene names |
| ||
| Organism | Rattus norvegicus (Rat) [Reference proteome] | ||
| Taxonomic identifier | 10116 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus![]() |
Protein attributes
| Sequence length | 1234 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. Ref.2 UniProtKB P51432 |
| Catalytic activity | 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol. Ref.2 |
| Cofactor | Calcium. Ref.2 |
| Subunit structure | Interacts with LPAR2 By similarity. Interacts with SHANK2. Ref.3 |
| Subcellular location | |
| Tissue specificity | Expressed in parotid gland, brain, liver, uterus, lung, heart, adrenal gland, and ovary. Not detected in spleen, pancreas, intestine, thymus or kidney. Ref.2 |
| Sequence similarities | Contains 1 C2 domain. Contains 1 PI-PLC X-box domain. Contains 1 PI-PLC Y-box domain. |
Ontologies
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 1234 | 1234 | 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-3 | PRO_0000088493 | |||||
Regions | |||||||||
| Domain | 315 – 466 | 152 | PI-PLC X-box | ||||||
| Domain | 589 – 705 | 117 | PI-PLC Y-box | ||||||
| Domain | 712 – 809 | 98 | C2 | ||||||
| Region | 1231 – 1234 | 4 | Interaction with SHANK2 | ||||||
Sites | |||||||||
| Active site | 330 | 1 | By similarity | ||||||
| Active site | 377 | 1 | By similarity UniProtKB P10688 | ||||||
Amino acid modifications | |||||||||
| Modified residue | 472 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 535 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1105 | 1 | Phosphoserine By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 17 | 1 | T → A in AAK14906. Ref.2 | ||||||
Sequences
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References
| [1] | "The 5'-upstream region of the rat phospholipase C-beta 3 gene contains two critical Sp1 sites and an HIV Inr-like element." Kang J.S., Lee H.B., Rhee S.G., Park K., Yoo O.J. Gene 197:19-28(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-33. |
| [2] | "Cloning, sequencing, purification, and Gq-dependent activation of phospholipase C-beta 3." Jhon D.-Y., Lee H.-H., Park D., Lee C.-W., Lee K.-H., Yoo O.J., Rhee S.G. J. Biol. Chem. 268:6654-6661(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 17-1234, FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION. Strain: Fischer. Tissue: Thyroid. |
| [3] | "The interaction of phospholipase C-beta3 with Shank2 regulates mGluR-mediated calcium signal." Hwang J.-I., Kim H.S., Lee J.R., Kim E., Ryu S.H., Suh P.-G. J. Biol. Chem. 280:12467-12473(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SHANK2. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | U41411 Genomic DNA. Translation: AAC53366.1. M99567 mRNA. Translation: AAK14906.1. |
| IPI | IPI00209033. |
| PIR | A45493. |
| UniGene | Rn.16983. |
3D structure databases | |
| ProteinModelPortal | Q99JE6. |
| ModBase | Search... |
PTM databases | |
| PhosphoSite | Q99JE6. |
Proteomic databases | |
| PaxDb | Q99JE6. |
| PRIDE | Q99JE6. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| UCSC | RGD:61993. rat. |
Organism-specific databases | |
| RGD | 61993. Plcb3. |
Phylogenomic databases | |
| eggNOG | NOG149692. |
| HOVERGEN | HBG053609. |
| InParanoid | Q99JE6. |
| OrthoDB | EOG41RPT7. |
Enzyme and pathway databases | |
| BRENDA | 3.1.4.11. 5301. |
Gene expression databases | |
| ArrayExpress | Q99JE6. |
| Genevestigator | Q99JE6. |
| GermOnline | ENSRNOG00000021150. Rattus norvegicus. |
Family and domain databases | |
| Gene3D | 1.10.238.10. 1 hit. 3.20.20.190. 2 hits. |
| InterPro | IPR000008. C2_Ca-dep. IPR008973. C2_Ca/lipid-bd_dom_CaLB. IPR018029. C2_membr_targeting. IPR011992. EF-hand-like_dom. IPR001192. Pinositol_PLipase_C. IPR016280. PLC-beta. IPR014815. PLC-beta_C. IPR009535. PLC-beta_CS. IPR017946. PLC-like_Pdiesterase_TIM-brl. IPR015359. PLipase_C_EF-hand-like. IPR000909. PLipase_C_PInositol-sp_X_dom. IPR001711. PLipase_C_Pinositol-sp_Y. [Graphical view] |
| PANTHER | PTHR10336. PTHR10336. 1 hit. |
| Pfam | PF00168. C2. 1 hit. PF06631. DUF1154. 1 hit. PF09279. efhand_like. 1 hit. PF00388. PI-PLC-X. 1 hit. PF00387. PI-PLC-Y. 1 hit. PF08703. PLC-beta_C. 1 hit. [Graphical view] |
| PIRSF | PIRSF000956. PLC-beta. 1 hit. |
| PRINTS | PR00390. PHPHLIPASEC. |
| SMART | SM00239. C2. 1 hit. SM00148. PLCXc. 1 hit. SM00149. PLCYc. 1 hit. [Graphical view] |
| SUPFAM | SSF49562. C2_CaLB. 1 hit. SSF51695. PLC-like_Pdiesterase_TIM-brl. 1 hit. |
| PROSITE | PS50004. C2. 1 hit. PS50007. PIPLC_X_DOMAIN. 1 hit. PS50008. PIPLC_Y_DOMAIN. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | PLCB3_RAT | ||||||||
| Accession | Primary (citable) accession number: Q99JE6 Secondary accession number(s): Q62887, Q9QW29 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with
