Go Annotations as Summary Text (Tabular View) (GO Graph)

GO curators for mouse genes have assigned the following annotations to the gene product of Plcb1. (This text reflects annotations as of Wednesday, January 23, 2013.)

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Summary from NCBI RefSeq

[Summary is not available for the mouse gene. This summary is for the human ortholog.] The protein encoded by this gene catalyzes the formation of inositol 1,4,5-trisphosphate and diacylglycerol from phosphatidylinositol 4,5-bisphosphate. This reaction uses calcium as a cofactor and plays an important role in the intracellular transduction of many extracellular signals. This gene is activated by two G-protein alpha subunits, alpha-q and alpha-11. Two transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jul 2008]

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Summary text based on GO annotations supported by experimental evidence in mouse

• Researchers have inferred from direct assay, that the gene product of Plcb1
  • participates in the following biological processes:
    • activation of meiosis involved in egg activation ^[1]
    • fat cell differentiation ^[16]
    • G1 phase ^[8]
    • G2/M transition of mitotic cell cycle ^[10]
    • insulin-like growth factor receptor signaling pathway ^[14]
    • negative regulation of monocyte extravasation ^[18]
    • negative regulation of transcription, DNA-dependent ^{[3, 7]}
    • positive regulation of CD24 biosynthetic process ^[9]
    • positive regulation of myoblast differentiation ^[6]
    • positive regulation of transcription, DNA-dependent ^[9]
  • performs the following molecular functions:
    • phosphatidylinositol phospholipase C activity ^[5]
  • is located in the following cellular components:
    • cytoplasm ^{[9, 13]}
    • nuclear chromatin ^[10]
    • nuclear speck ^[3]
    • nucleus ^{[1, 6, 8, 9, 13]}
• The gene product of Plcb1 has been shown to bind to the gene products of Srsf3. ^[3] Researchers have inferred, based on physical interactions, that the gene product of Plcb1
  • performs the following molecular functions:
    • lamin binding ^[10]
• Researchers have inferred, based on phenotypic analysis of mouse mutants, that the gene product of Plcb1
  • participates in the following biological processes:
    • cerebral cortex development ^[11]
    • G-protein coupled acetylcholine receptor signaling pathway ^[12]
    • glutamate receptor signaling pathway ^[11]
    • memory ^[15]
    • positive regulation of acrosome reaction ^[4]
    • positive regulation of developmental growth ^[2]
    • positive regulation of embryonic development ^[4]
    • positive regulation of interleukin-12 production ^[17]
    • regulation of fertilization ^[4]
    • regulation of G-protein coupled receptor protein signaling pathway ^[15]
• Based on the experimental annotations above, MGI curators have inferred, that the gene product of Plcb1
  • participates in the following biological processes:
    • cell adhesion ^[9]

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Summary text based on GO annotations supported by experimental evidence in other organisms

• From comparative sequence analysis (see table for details), MGI curators have determined that the gene product of Plcb1:
  • participates in the following biological processes:
    • interleukin-1-mediated signaling pathway
    • interleukin-12-mediated signaling pathway
    • interleukin-15-mediated signaling pathway
    • positive regulation of GTPase activity
    • positive regulation of JNK cascade
    • response to monosaccharide stimulus
    • response to peptide hormone stimulus
  • performs the following molecular functions:
    • calcium ion binding
    • calmodulin binding
    • enzyme binding
    • GTPase activator activity
    • phosphatidylinositol phospholipase C activity
    • phosphatidylinositol-4,5-bisphosphate binding
    • protein homodimerization activity
  • is located in the following cellular components:
    • cytoplasm
    • cytosol
    • membrane
    • nuclear speck

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Summary text based on GO annotations supported by structural data

• Plcb1 encodes a protein or proteins that contain the following InterPro domains: C2 calcium-dependent membrane targeting, C2 calcium/lipid-binding domain, CaLB, C2 membrane targeting protein, EF-hand-like domain, Phosphatidylinositol-4, 5-bisphosphate phosphodiesterase beta, Phosphatidylinositol-4, 5-bisphosphate phosphodiesterase beta, conserved site, Phosphoinositide phospholipase C, Phospholipase C, phosphatidylinositol-specific , X domain, Phospholipase C, phosphatidylinositol-specific, Y domain, Phospholipase C, phosphoinositol-specific, EF-hand-like, PLC-beta, C-terminal, PLC-like phosphodiesterase, TIM beta/alpha-barrel domain, Pleckstrin homology-like domain, indicating that the gene product:
  • participates in the following biological processes:
    • intracellular signal transduction
    • lipid catabolic process
    • lipid metabolic process
  • performs the following molecular functions:
    • phosphoric diester hydrolase activity

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Summary text for additional MGI annotations

• Automated translation to GO terms of SwissProt keywords that describe Plcb1 indicates that it:
  • participates in the following biological processes:
    • lipid catabolic process
    • lipid metabolic process
  • performs the following molecular functions:
    • hydrolase activity
    • signal transducer activity

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References

1. Avazeri N et al. (2003) Meiosis resumption, calcium-sensitive period, and PLC-beta1 relocation into the nucleus in the mouse oocyte. Cell Signal, 15:1003-10. (PubMed:14499343)
2. Ballester M et al. (2004) Disruption of the mouse phospholipase C-beta1 gene in a beta-lactoglobulin transgenic line affects viability, growth, and fertility in mice. Gene, 341:279-89. (PubMed:15474310)
3. Bavelloni A et al. (2006) Proteomic-based analysis of nuclear signaling: PLCbeta1 affects the expression of the splicing factor SRp20 in Friend erythroleukemia cells. Proteomics, 6:5725-34. (PubMed:17022104)
4. Choi D et al. (2001) The biological significance of phospholipase C beta 1 gene mutation in mouse sperm in the acrosome reaction, fertilization, and embryo development. J Assist Reprod Genet, 18:305-10. (PubMed:11464583)
5. Cocco L et al. (1998) Inositides in the nucleus: taking stock of PLC beta 1. Adv Enzyme Regul, 38:351-63. (PubMed:9762362)
6. Faenza I et al. (2004) Expression of phospholipase C beta family isoenzymes in C2C12 myoblasts during terminal differentiation. J Cell Physiol, 200:291-6. (PubMed:15174099)
7. Faenza I et al. (2002) Nuclear PLCbeta(1) acts as a negative regulator of p45/NF-E2 expression levels in Friend erythroleukemia cells. Biochim Biophys Acta, 1589:305-10. (PubMed:12031797)
8. Faenza I et al. (2000) A role for nuclear phospholipase Cbeta 1 in cell cycle control. J Biol Chem, 275:30520-4. (PubMed:10913438)
9. Fiume R et al. (2005) Nuclear phospholipase C beta1 (PLCbeta1) affects CD24 expression in murine erythroleukemia cells. J Biol Chem, 280:24221-6. (PubMed:15849202)
10. Fiume R et al. (2009) Involvement of nuclear PLCbeta1 in lamin B1 phosphorylation and G2/M cell cycle progression. FASEB J, 23:957-66. (PubMed:19028838)
11. Hannan AJ et al. (2001) PLC-beta1, activated via mGluRs, mediates activity-dependent differentiation in cerebral cortex. Nat Neurosci, 4:282-8. (PubMed:11224545)
12. Kim D et al. (1997) Phospholipase C isozymes selectively couple to specific neurotransmitter receptors. Nature, 389:290-3. (PubMed:9305844)
13. Lefevre B et al. (2007) The phosphoinositide-phospholipase C (PI-PLC) pathway in the mouse oocyte. Crit Rev Eukaryot Gene Expr, 17:259-69. (PubMed:17725492)
14. Manzoli L et al. (1997) Essential role for nuclear phospholipase C beta1 in insulin-like growth factor I-induced mitogenesis. Cancer Res, 57:2137-9. (PubMed:9187110)
15. McOmish CE et al. (2008) PLC-beta1 knockout mice as a model of disrupted cortical development and plasticity: behavioral endophenotypes and dysregulation of RGS4 gene expression. Hippocampus, 18:824-34. (PubMed:18493969)
16. O'Carroll SJ et al. (2009) Nuclear PLCbeta1 is required for 3T3-L1 adipocyte differentiation and regulates expression of the cyclin D3-cdk4 complex. Cell Signal, 21:926-35. (PubMed:19385066)
17. Rudnicka W et al. (1997) The host response to Listeria monocytogenes mutants defective in genes encoding phospholipases C (plcA, plcB) and actin assembly (actA). Microbiol Immunol, 41:847-53. (PubMed:9444325)
18. Seehaus S et al. (2009) Hypercoagulability inhibits monocyte transendothelial migration through protease-activated receptor-1-, phospholipase-Cbeta-, phosphoinositide 3-kinase-, and nitric oxide-dependent signaling in monocytes and promotes plaque stability. Circulation, 120:774-84. (PubMed:19687358)

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Gene Ontology Evidence Code Abbreviations:

EXP Inferred from experiment

IC Inferred by curator

IDA Inferred from direct assay

IEA Inferred from electronic annotation

IGI Inferred from genetic interaction

IMP Inferred from mutant phenotype

IPI Inferred from physical interaction

ISS Inferred from sequence or structural similarity

ISO Inferred from sequence orthology

ISA Inferred from sequence alignment

ISM Inferred from sequence model

NAS Non-traceable author statement

ND No biological data available

RCA Reviewed computational analysis

TAS Traceable author statement

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