Q07722 (PLCB4_BOVIN) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 108.
History...
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-4 EC=3.1.4.11 Alternative name(s): PCL-C1 Phosphoinositide phospholipase C-beta-4 Phospholipase C-beta-4 Short name=PLC-beta-4 | ||
| Gene names |
| ||
| Organism | Bos taurus (Bovine) [Reference proteome] | ||
| Taxonomic identifier | 9913 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos![]() |
Protein attributes
| Sequence length | 1023 AA. |
| Sequence status | Fragment. |
| 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. This form has a role in retina signal transduction. |
| Catalytic activity | 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol. |
| Cofactor | Calcium. |
| Tissue specificity | Preferentially expressed in the retina. |
| Post-translational modification | The N-terminus is blocked. |
| Sequence similarities | Contains 1 C2 domain. Contains 1 PI-PLC X-box domain. Contains 1 PI-PLC Y-box domain. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Lipid degradation Lipid metabolism |
| Coding sequence diversity | Alternative splicing |
| Ligand | Calcium |
| Molecular function | Hydrolase Transducer |
| PTM | Phosphoprotein |
| Technical term | Complete proteome Direct protein sequencing Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | intracellular signal transduction Inferred from electronic annotation. Source: InterPro lipid catabolic processInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular_function | calcium ion binding Inferred from electronic annotation. Source: InterPro phosphatidylinositol phospholipase C activityInferred from electronic annotation. Source: EC signal transducer activityInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Alternative products
| This entry describes 4 isoforms produced by alternative splicing. [Align] [Select] Note: Additional isoforms seem to exist. | ||||||
| Isoform 1B (identifier: Q07722-1) 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. | ||||||
| Isoform 1A (identifier: Q07722-2) The sequence of this isoform differs from the canonical sequence as follows: 372-383: Missing. | ||||||
| Isoform 2A (identifier: Q07722-3) The sequence of this isoform differs from the canonical sequence as follows: 1-104: Missing. 372-383: Missing. | ||||||
| Isoform 2B (identifier: Q07722-4) The sequence of this isoform differs from the canonical sequence as follows: 1-104: Missing. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | ‹1 – 1023 | ›1023 | 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-4 | PRO_0000088494 | |||||
Regions | |||||||||
| Domain | 149 – 299 | 151 | PI-PLC X-box | ||||||
| Domain | 413 – 529 | 117 | PI-PLC Y-box | ||||||
| Domain | 536 – 634 | 99 | C2 | ||||||
Sites | |||||||||
| Active site | 164 | 1 | By similarity | ||||||
| Active site | 211 | 1 | By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 734 | 1 | Phosphothreonine By similarity | ||||||
Natural variations | |||||||||
| Alternative sequence | ‹1 – 104 | ›104 | Missing in isoform 2A and isoform 2B. | VSP_004719 | |||||
| Alternative sequence | 372 – 383 | 12 | Missing in isoform 1A and isoform 2A. | VSP_004720 | |||||
Experimental info | |||||||||
| Sequence conflict | 24 | 1 | E → D AA sequence Ref.2 | ||||||
| Sequence conflict | 32 | 1 | N → D AA sequence Ref.2 | ||||||
| Sequence conflict | 36 | 1 | E → L AA sequence Ref.2 | ||||||
| Sequence conflict | 328 | 1 | M → I AA sequence Ref.2 | ||||||
| Non-terminal residue | 1 | 1 | |||||||
Sequences
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References
| [1] | "Distinctive subtypes of bovine phospholipase C that have preferential expression in the retina and high homology to the norpA gene product of Drosophila." Ferreira P.A., Shortridge R.D., Pak W.L. Proc. Natl. Acad. Sci. U.S.A. 90:6042-6046(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1A; 1B; 2A AND 2B). Tissue: Retina. |
| [2] | "Purification of a novel phospholipase C isozyme from bovine cerebellum." Min D.S., Kim D.M., Lee Y.H., Seo J., Suh P.-G., Ryu S.H. J. Biol. Chem. 268:12207-12212(1993) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 20-37; 259-269; 315-337; 386-391; 604-623 AND 634-639. Tissue: Cerebellum. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | L13936 mRNA. Translation: AAA30699.1. L13935 mRNA. Translation: AAC37304.1. L13937 mRNA. Translation: AAA30700.1. L13938 mRNA. Translation: AAA30701.1. |
| IPI | IPI00696189. IPI00708128. IPI00708692. IPI00911649. |
| PIR | B38932. |
| UniGene | Bt.4552. |
3D structure databases | |
| ProteinModelPortal | Q07722. |
| ModBase | Search... |
Proteomic databases | |
| PRIDE | Q07722. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Phylogenomic databases | |
| eggNOG | NOG149692. |
| HOGENOM | HOG000232046. |
| HOVERGEN | HBG053609. |
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. 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. [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 | PLCB4_BOVIN | ||||||||
| Accession | Primary (citable) accession number: Q07722 Secondary accession number(s): Q07721, Q07723, Q07724 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with
