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

GO curators for mouse genes have assigned the following annotations to the gene product of Itpr1. (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.] This gene encodes an intracellular receptor for inositol 1,4,5-trisphosphate. Upon stimulation by inositol 1,4,5-trisphosphate, this receptor mediates calcium release from the endoplasmic reticulum. Mutations in this gene cause spinocerebellar ataxia type 15, a disease associated with an heterogeneous group of cerebellar disorders. Multiple transcript variants have been identified for this gene. [provided by RefSeq, Nov 2009]

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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 Itpr1
  • participates in the following biological processes:
    • calcium ion transmembrane transport ^{[6, 13]}
    • calcium ion transport ^[1]
    • inositol phosphate-mediated signaling ^{[6, 13]}
    • response to hypoxia ^[7]
  • performs the following molecular functions:
    • inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity ^{[6, 13]}
    • intracellular ligand-gated calcium channel activity ^[13]
    • phosphatidylinositol binding ^{[6, 13, 14]}
  • is located in the following cellular components:
    • calcineurin complex ^[2]
    • cytoplasm ^[3]
    • endoplasmic reticulum membrane ^[11]
    • nuclear envelope ^[1]
    • nuclear inner membrane ^[1]
    • nucleolus ^[1]
    • postsynaptic density ^[10]
    • sarcoplasmic reticulum ^[1]
• The gene product of Itpr1 has been shown to bind to the gene products of Bcl2, Car8, Epb4.1l1, Erp44, Grid2, Grm1, Homer1. ^{[4, 5, 10, 11, 15]} Researchers have inferred, based on physical interactions, that the gene product of Itpr1
  • performs the following molecular functions:
  • is located in the following cellular components:
    • protein complex ^[9]
• Researchers have inferred, based on phenotypic analysis of mouse mutants, that the gene product of Itpr1
  • participates in the following biological processes:
    • intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress ^[8]
    • post-embryonic development ^[12]
    • release of sequestered calcium ion into cytosol ^[8]
    • voluntary musculoskeletal movement ^[12]
• Researchers have inferred, based on genetic interactions, that the gene product of Itpr1
  • participates in the following biological processes:
    • endoplasmic reticulum calcium ion homeostasis based on interactions with Bak1, Bax, Bcl2 ^[11]

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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 Itpr1:
  • participates in the following biological processes:
    • elevation of cytosolic calcium ion concentration
    • inositol phosphate-mediated signaling
    • negative regulation of neuron death
    • positive regulation of calcium ion transport
    • release of sequestered calcium ion into cytosol
    • response to hypoxia
  • performs the following molecular functions:
    • inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity
    • protein C-terminus binding
    • protein complex binding
    • protein phosphatase binding
  • is located in the following cellular components:
    • cytoplasm
    • dendrite
    • endoplasmic reticulum membrane
    • intracellular membrane-bounded organelle
    • membrane raft
    • neuronal cell body
    • nuclear envelope
    • perinuclear region of cytoplasm
    • plasma membrane
    • platelet dense granule membrane
    • platelet dense tubular network
    • postsynaptic density
    • protein complex
    • sarcoplasmic reticulum
    • secretory granule membrane
    • synaptic membrane

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Summary text based on GO annotations supported by structural data

• Itpr1 encodes a protein or proteins that contain the following InterPro domains: Inositol 1,4,5-trisphosphate-binding protein receptor, Inositol 1,4,5-trisphosphate/ryanodine receptor, Intracellular calcium-release channel, Ion transport domain, MIR motif, Ryanodine receptor-related, RyR/IP3R Homology associated domain, indicating that the gene product:
  • participates in the following biological processes:
    • ion transport
    • transmembrane transport
  • performs the following molecular functions:
    • calcium channel activity
    • ion channel activity
  • is located in the following cellular components:
    • membrane

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Summary text for additional MGI annotations

• Automated translation to GO terms of SwissProt keywords that describe Itpr1 indicates that it:
  • participates in the following biological processes:
    • apoptotic process
    • ion transport
    • transport
  • performs the following molecular functions:
    • calcium channel activity
    • ion channel activity
  • is located in the following cellular components:
    • integral to membrane
    • membrane

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References

1. Cardenas C et al. (2005) Nuclear inositol 1,4,5-trisphosphate receptors regulate local Ca2+ transients and modulate cAMP response element binding protein phosphorylation. J Cell Sci, 118:3131-40. (PubMed:16014380)
2. Erin N et al. (2003) Calcium-dependent interaction of calcineurin with Bcl-2 in neuronal tissue. Neuroscience, 117:541-55. (PubMed:12617961)
3. Fissore RA et al. (1999) Differential distribution of inositol trisphosphate receptor isoforms in mouse oocytes. Biol Reprod, 60:49-57. (PubMed:9858485)
4. Higo T et al. (2005) Subtype-specific and ER lumenal environment-dependent regulation of inositol 1,4,5-trisphosphate receptor type 1 by ERp44. Cell, 120:85-98. (PubMed:15652484)
5. Hirota J et al. (2003) Carbonic anhydrase-related protein is a novel binding protein for inositol 1,4,5-trisphosphate receptor type 1. Biochem J, 372:435-41. (PubMed:12611586)
6. Iwai M et al. (2007) Molecular basis of the isoform-specific ligand-binding affinity of inositol 1,4,5-trisphosphate receptors. J Biol Chem, 282:12755-64. (PubMed:17327232)
7. Jurkovicova D et al. (2008) Hypoxia differently modulates gene expression of inositol 1,4,5-trisphosphate receptors in mouse kidney and HEK 293 cell line. Ann N Y Acad Sci, 1148:421-7. (PubMed:19120137)
8. Li G et al. (2009) Role of ERO1-alpha-mediated stimulation of inositol 1,4,5-triphosphate receptor activity in endoplasmic reticulum stress-induced apoptosis. J Cell Biol, 186:783-92. (PubMed:19752026)
9. Murata T et al. (2007) Genetic evidence supporting caveolae microdomain regulation of calcium entry in endothelial cells. J Biol Chem, 282:16631-43. (PubMed:17416589)
10. Nakamura M et al. (2004) Signaling complex formation of phospholipase Cbeta4 with metabotropic glutamate receptor type 1alpha and 1,4,5-trisphosphate receptor at the perisynapse and endoplasmic reticulum in the mouse brain. Eur J Neurosci, 20:2929-44. (PubMed:15579147)
11. Oakes SA et al. (2005) Proapoptotic BAX and BAK regulate the type 1 inositol trisphosphate receptor and calcium leak from the endoplasmic reticulum. Proc Natl Acad Sci U S A, 102:105-10. (PubMed:15613488)
12. van de Leemput J et al. (2007) Deletion at ITPR1 Underlies Ataxia in Mice and Spinocerebellar Ataxia 15 in Humans. PLoS Genet, 3:e108. (PubMed:17590087)
13. Yamazaki H et al. (2010) Tyr-167/Trp-168 in type 1/3 inositol 1,4,5-trisphosphate receptor mediates functional coupling between ligand binding and channel opening. J Biol Chem, 285:36081-91. (PubMed:20813840)
14. Yoshikawa F et al. (1996) Mutational analysis of the ligand binding site of the inositol 1,4,5-trisphosphate receptor. J Biol Chem, 271:18277-84. (PubMed:8663526)
15. Zhang S et al. (2003) Protein 4.1N is required for translocation of inositol 1,4,5-trisphosphate receptor type 1 to the basolateral membrane domain in polarized Madin-Darby canine kidney cells. J Biol Chem, 278:4048-56. (PubMed:12444087)

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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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