Reviewed,
UniProtKB/Swiss-Prot P10687 (PLCB1_RAT)
Last modified
February 9, 2010.
Version 93.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta-1 EC=3.1.4.11 Alternative name(s): Phosphoinositide phospholipase C-beta-1 Phospholipase C-beta-1 Short name=PLC-beta-1 Phospholipase C-I Short name=PLC-I PLC-154 | ||
| Gene names |
| ||
| Organism | Rattus norvegicus (Rat) | ||
| 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 | 1216 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. |
| Catalytic activity | 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol. Ref.2 |
| Cofactor | Calcium. |
| Subunit structure | Interacts with DGKQ By similarity. |
| Subcellular location | |
| Tissue specificity | Highest expression in brain. Also expressed in parotid gland, liver, uterus, lung, heart, adrenal gland and ovary. Not detected in spleen, pancreas, intestine, thymus or kidney. Ref.2 |
| Miscellaneous | The receptor-mediated activation of PLC-beta-1 is mediated by two G-protein alpha subunits, alpha-Q and alpha-11. |
| 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 – 1216 | 1216 | 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta-1 | PRO_0000088488 | |||||
Regions | |||||||||
| Domain | 316 – 467 | 152 | PI-PLC X-box | ||||||
| Domain | 540 – 656 | 117 | PI-PLC Y-box | ||||||
| Domain | 663 – 761 | 99 | C2 | ||||||
Sites | |||||||||
| Active site | 331 | 1 | By similarity | ||||||
| Active site | 378 | 1 | By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 333 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 334 | 1 | Phosphotyrosine By similarity | ||||||
| Modified residue | 336 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 569 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 573 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 887 | 1 | Phosphoserine; by PKC By similarity | ||||||
| Modified residue | 972 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 976 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 1197 | 1 | Phosphoserine By similarity | ||||||
Sequences
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References
| [1] | "Cloning and sequence of multiple forms of phospholipase C." Suh P.-G., Ryu S.H., Moon K.H., Suh H.W., Rhee S.G. Cell 54:161-169(1988) [PubMed: 3390863] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
| [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: 8454637] [Abstract] Cited for: CATALYTIC ACTIVITY, TISSUE SPECIFICITY, SUBCELLULAR LOCATION. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | M20636 mRNA. Translation: AAA41885.1. |
| IPI | IPI00192534. |
| PIR | A28821. |
| RefSeq | NP_001071109.1. |
| UniGene | Rn.45523 |
3D structure databases | |
| SMR | P10687. Positions 18-797, 900-1171. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | P10687. |
PTM databases | |
| PhosphoSite | P10687. |
Genome annotation databases | |
| Ensembl | ENSRNOT00000051184; ENSRNOP00000042533; ENSRNOG00000004810; Rattus norvegicus. [Genome view] |
| GeneID | 24654. |
| KEGG | rno:24654. |
| UCSC | M20636. rat. |
Organism-specific databases | |
| CTD | 24654. |
| RGD | 3344. Plcb1. |
Phylogenomic databases | |
| eggNOG | roNOG12610. |
| HOVERGEN | P10687. |
| InParanoid | P10687. |
| OMA | YEYNGKS. |
| OrthoDB | EOG91C9FQ. |
| PhylomeDB | P10687. |
Enzyme and pathway databases | |
| BRENDA | 3.1.4.11. 248. |
Gene expression databases | |
| Genevestigator | P10687. |
| GermOnline | ENSRNOG00000004810. Rattus norvegicus. |
Family and domain databases | |
| InterPro | IPR000008. C2_Ca-dep. IPR008973. C2_Ca/lipid-bd_dom_CaLB. IPR018029. C2_membr_targeting. IPR011992. EF-hand-like_dom. IPR015359. Phospholipase_C_EF-hand-like. IPR001192. Phospholipase_C_Pinositol-sp_C. IPR001711. Phospholipase_C_Pinositol-sp_Y. IPR016280. PLC-beta. IPR017946. PLC-like_Pdiesterase_TIM-brl. IPR000909. PLipase_C_PInositol-sp_X_dom. [Graphical view] |
| Gene3D | G3DSA:1.10.238.10. EF-Hand_type. 1 hit. G3DSA:3.20.20.190. PLC-like_Pdiesterase_TIM-brl. 1 hit. |
| Pfam | PF09279. efhand_like. 1 hit. PF00388. PI-PLC-X. 1 hit. PF00387. PI-PLC-Y. 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] |
| PROSITE | PS50004. C2. 1 hit. PS50007. PIPLC_X_DOMAIN. 1 hit. PS50008. PIPLC_Y_DOMAIN. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 603984. |
Entry information
| Entry name | PLCB1_RAT | ||||||||
| Accession | Primary (citable) accession number: P10687 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||

Clusters with


