ITPR1

Last updated
ITPR1
PBB Protein ITPR1 image.jpg
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases ITPR1 , ACV, CLA4, INSP3R1, IP3R, IP3R1, PPP1R94, SCA15, SCA16, SCA29, inositol 1,4,5-trisphosphate receptor type 1
External IDs OMIM: 147265 MGI: 96623 HomoloGene: 1673 GeneCards: ITPR1
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001099952
NM_001168272
NM_002222
NM_001378452

NM_010585

RefSeq (protein)

NP_001093422
NP_001161744
NP_002213

NP_034715

Location (UCSC) Chr 3: 4.49 – 4.85 Mb Chr 6: 108.19 – 108.53 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Inositol 1,4,5-trisphosphate receptor type 1 is a protein that in humans is encoded by the ITPR1 gene. [5] [6] [7] [8] [9]

Contents

Interactions

ITPR1 has been shown to interact with:

See also

Related Research Articles

Inositol trisphosphate or inositol 1,4,5-trisphosphate abbreviated InsP3 or Ins3P or IP3 is an inositol phosphate signaling molecule. It is made by hydrolysis of phosphatidylinositol 4,5-bisphosphate (PIP2), a phospholipid that is located in the plasma membrane, by phospholipase C (PLC). Together with diacylglycerol (DAG), IP3 is a second messenger molecule used in signal transduction in biological cells. While DAG stays inside the membrane, IP3 is soluble and diffuses through the cell, where it binds to its receptor, which is a calcium channel located in the endoplasmic reticulum. When IP3 binds its receptor, calcium is released into the cytosol, thereby activating various calcium regulated intracellular signals.

<span class="mw-page-title-main">Inositol trisphosphate receptor</span> Class of transport proteins

Inositol trisphosphate receptor (InsP3R) is a membrane glycoprotein complex acting as a Ca2+ channel activated by inositol trisphosphate (InsP3). InsP3R is very diverse among organisms, and is necessary for the control of cellular and physiological processes including cell division, cell proliferation, apoptosis, fertilization, development, behavior, learning and memory. Inositol triphosphate receptor represents a dominant second messenger leading to the release of Ca2+ from intracellular store sites. There is strong evidence suggesting that the InsP3R plays an important role in the conversion of external stimuli to intracellular Ca2+ signals characterized by complex patterns relative to both space and time, such as Ca2+ waves and oscillations.

<span class="mw-page-title-main">TRPC1</span> Protein and coding gene in humans

Transient receptor potential canonical 1 (TRPC1) is a protein that in humans is encoded by the TRPC1 gene.

<span class="mw-page-title-main">ITPKB</span> Protein-coding gene in the species Homo sapiens

Inositol-trisphosphate 3-kinase B is an enzyme that in humans is encoded by the ITPKB gene.

<span class="mw-page-title-main">FKBP1A</span> Protein and coding gene in humans

Peptidyl-prolyl cis-trans isomerase FKBP1A is an enzyme that in humans is encoded by the FKBP1A gene. It is also commonly referred to as FKBP-12 or FKBP12 and is a member of a family of FK506-binding proteins (FKBPs).

<span class="mw-page-title-main">Inositol-trisphosphate 3-kinase</span> Class of enzymes

Inositol (1,4,5) trisphosphate 3-kinase (EC 2.7.1.127), abbreviated here as ITP3K, is an enzyme that facilitates a phospho-group transfer from adenosine triphosphate to 1D-myo-inositol 1,4,5-trisphosphate. This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:1D-myo-inositol-1,4,5-trisphosphate 3-phosphotransferase. ITP3K catalyzes the transfer of the gamma-phosphate from ATP to the 3-position of inositol 1,4,5-trisphosphate to form inositol 1,3,4,5-tetrakisphosphate. ITP3K is highly specific for the 1,4,5-isomer of IP3, and it exclusively phosphorylates the 3-OH position, producing Ins(1,3,4,5)P4, also known as inositol tetrakisphosphate or IP4.

<span class="mw-page-title-main">Phospholipase C</span> Class of enzymes

Phospholipase C (PLC) is a class of membrane-associated enzymes that cleave phospholipids just before the phosphate group (see figure). It is most commonly taken to be synonymous with the human forms of this enzyme, which play an important role in eukaryotic cell physiology, in particular signal transduction pathways. Phospholipase C's role in signal transduction is its cleavage of phosphatidylinositol 4,5-bisphosphate (PIP2) into diacyl glycerol (DAG) and inositol 1,4,5-trisphosphate (IP3), which serve as second messengers. Activators of each PLC vary, but typically include heterotrimeric G protein subunits, protein tyrosine kinases, small G proteins, Ca2+, and phospholipids.

<span class="mw-page-title-main">PLCE1</span> Protein-coding gene in the species Homo sapiens

Phospholipase C epsilon 1 (PLCE1) is an enzyme that in humans is encoded by the PLCE1 gene. This gene encodes a phospholipase enzyme (PLCE1) that catalyzes the hydrolysis of phosphatidylinositol-4,5-bisphosphate to generate two second messengers: inositol 1,4,5-triphosphate (IP3) and diacylglycerol (DAG). Mutations in this gene cause early-onset nephrotic syndrome and have been associated with respiratory chain deficiency with diffuse mesangial sclerosis.

<span class="mw-page-title-main">EPB41L1</span> Protein-coding gene in the species Homo sapiens

Band 4.1-like protein 1 is a protein that in humans is encoded by the EPB41L1 gene.

<span class="mw-page-title-main">PLCD3</span> Protein-coding gene in the species Homo sapiens

1-Phosphatidylinositol-4,5-bisphosphate phosphodiesterase delta-3 is an enzyme that in humans is encoded by the PLCD3 gene.

<span class="mw-page-title-main">ITPKA</span> Protein-coding gene in the species Homo sapiens

Inositol-trisphosphate 3-kinase A is an enzyme that in humans is encoded by the ITPKA gene.

<span class="mw-page-title-main">AHCYL1</span> Protein-coding gene in the species Homo sapiens

Putative adenosylhomocysteinase 2 is an enzyme that in humans is encoded by the AHCYL1 gene.

<span class="mw-page-title-main">MRVI1</span> Protein-coding gene in the species Homo sapiens

Protein MRVI1 is a protein that in humans is encoded by the MRVI1 gene.

<span class="mw-page-title-main">PRKG1</span> Protein-coding gene in the species Homo sapiens

cGMP-dependent protein kinase 1, alpha isozyme is an enzyme that in humans is encoded by the PRKG1 gene.

<span class="mw-page-title-main">Ryanodine receptor 1</span> Protein and coding gene in humans

Ryanodine receptor 1 (RYR-1) also known as skeletal muscle calcium release channel or skeletal muscle-type ryanodine receptor is one of a class of ryanodine receptors and a protein found primarily in skeletal muscle. In humans, it is encoded by the RYR1 gene.

<span class="mw-page-title-main">ITPR2</span> Protein-coding gene in humans

Inositol 1,4,5-trisphosphate receptor, type 2, also known as ITPR2, is a protein which in humans is encoded by the ITPR2 gene. The protein encoded by this gene is both a receptor for inositol triphosphate and a calcium channel.

<span class="mw-page-title-main">ITPR3</span> Protein-coding gene in the species Homo sapiens

Inositol 1,4,5-trisphosphate receptor, type 3, also known as ITPR3, is a protein which in humans is encoded by the ITPR3 gene. The protein encoded by this gene is both a receptor for inositol triphosphate and a calcium channel.

<span class="mw-page-title-main">Ryanodine receptor 3</span> Transport protein and coding gene in humans

Ryanodine receptor 3 is one of a class of ryanodine receptors and a protein that in humans is encoded by the RYR3 gene. The protein encoded by this gene is both a calcium channel and a receptor for the plant alkaloid ryanodine. RYR3 and RYR1 control the resting calcium ion concentration in skeletal muscle.

Inositol-polyphosphate multikinase is an enzyme with systematic name ATP:1D-myo-inositol-1,4,5-trisphosphate 6-phosphotransferase. This enzyme catalyses the following chemical reaction

The ryanodine-inositol 1,4,5-triphosphate receptor Ca2+ channel (RIR-CaC) family includes Ryanodine receptors and Inositol trisphosphate receptors. Members of this family are large proteins, some exceeding 5000 amino acyl residues in length. This family belongs to the Voltage-gated ion channel (VIC) superfamily. Ry receptors occur primarily in muscle cell sarcoplasmic reticular (SR) membranes, and IP3 receptors occur primarily in brain cell endoplasmic reticular (ER) membranes where they effect release of Ca2+ into the cytoplasm upon activation (opening) of the channel. They are redox sensors, possibly providing a partial explanation for how they control cytoplasmic Ca2+. Ry receptors have been identified in heart mitochondria where they provide the main pathway for Ca2+ entry. Sun et al. (2011) have demonstrated oxygen-coupled redox regulation of the skeletal muscle ryanodine receptor-Ca2+ release channel (RyR1;TC# 1.A.3.1.2) by NADPH oxidase 4.

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000150995 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000030102 - Ensembl, May 2017
  3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. Yamada N, Makino Y, Clark RA, Pearson DW, Mattei MG, Guénet JL, Ohama E, Fujino I, Miyawaki A, Furuichi T (Sep 1994). "Human inositol 1,4,5-trisphosphate type-1 receptor, InsP3R1: structure, function, regulation of expression and chromosomal localization". The Biochemical Journal. 302 (Pt 3): 781–90. doi:10.1042/bj3020781. PMC   1137299 . PMID   7945203.
  6. Nucifora FC, Li SH, Danoff S, Ullrich A, Ross CA (Sep 1995). "Molecular cloning of a cDNA for the human inositol 1,4,5-trisphosphate receptor type 1, and the identification of a third alternatively spliced variant". Brain Research. Molecular Brain Research. 32 (2): 291–6. doi: 10.1016/0169-328X(95)00089-B . PMID   7500840.
  7. van de Leemput J, Chandran J, Knight MA, Holtzclaw LA, Scholz S, Cookson MR, Houlden H, Gwinn-Hardy K, Fung HC, Lin X, Hernandez D, Simon-Sanchez J, Wood NW, Giunti P, Rafferty I, Hardy J, Storey E, Gardner RJ, Forrest SM, Fisher EM, Russell JT, Cai H, Singleton AB (Jun 2007). "Deletion at ITPR1 underlies ataxia in mice and spinocerebellar ataxia 15 in humans". PLOS Genetics. 3 (6): e108. doi: 10.1371/journal.pgen.0030108 . PMC   1892049 . PMID   17590087.
  8. Iwaki A, Kawano Y, Miura S, Shibata H, Matsuse D, Li W, Furuya H, Ohyagi Y, Taniwaki T, Kira J, Fukumaki Y (Jan 2008). "Heterozygous deletion of ITPR1, but not SUMF1, in spinocerebellar ataxia type 16". Journal of Medical Genetics. 45 (1): 32–5. doi:10.1136/jmg.2007.053942. PMID   17932120. S2CID   7730102.
  9. "Entrez Gene: ITPR1 inositol 1,4,5-triphosphate receptor, type 1".
  10. Ando H, Mizutani A, Matsu-ura T, Mikoshiba K (Mar 2003). "IRBIT, a novel inositol 1,4,5-trisphosphate (IP3) receptor-binding protein, is released from the IP3 receptor upon IP3 binding to the receptor". The Journal of Biological Chemistry. 278 (12): 10602–12. doi: 10.1074/jbc.M210119200 . PMID   12525476.
  11. Hirota J, Ando H, Hamada K, Mikoshiba K (Jun 2003). "Carbonic anhydrase-related protein is a novel binding protein for inositol 1,4,5-trisphosphate receptor type 1". The Biochemical Journal. 372 (Pt 2): 435–41. doi:10.1042/BJ20030110. PMC   1223404 . PMID   12611586.
  12. Maximov A, Tang TS, Bezprozvanny I (Feb 2003). "Association of the type 1 inositol (1,4,5)-trisphosphate receptor with 4.1N protein in neurons". Molecular and Cellular Neurosciences. 22 (2): 271–83. doi:10.1016/s1044-7431(02)00027-1. PMID   12676536. S2CID   2317354.
  13. MacMillan D, Currie S, Bradley KN, Muir TC, McCarron JG (Dec 2005). "In smooth muscle, FK506-binding protein modulates IP3 receptor-evoked Ca2+ release by mTOR and calcineurin". Journal of Cell Science. 118 (Pt 23): 5443–51. doi: 10.1242/jcs.02657 . PMID   16278292.
  14. Cameron AM, Nucifora FC, Fung ET, Livingston DJ, Aldape RA, Ross CA, Snyder SH (Oct 1997). "FKBP12 binds the inositol 1,4,5-trisphosphate receptor at leucine-proline (1400-1401) and anchors calcineurin to this FK506-like domain". The Journal of Biological Chemistry. 272 (44): 27582–8. doi: 10.1074/jbc.272.44.27582 . PMID   9346894.
  15. 1 2 Schlossmann J, Ammendola A, Ashman K, Zong X, Huber A, Neubauer G, Wang GX, Allescher HD, Korth M, Wilm M, Hofmann F, Ruth P (Mar 2000). "Regulation of intracellular calcium by a signalling complex of IRAG, IP3 receptor and cGMP kinase Ibeta". Nature. 404 (6774): 197–201. Bibcode:2000Natur.404..197S. doi:10.1038/35004606. PMID   10724174. S2CID   205004996.
  16. Mehta D, Ahmmed GU, Paria BC, Holinstat M, Voyno-Yasenetskaya T, Tiruppathi C, Minshall RD, Malik AB (Aug 2003). "RhoA interaction with inositol 1,4,5-trisphosphate receptor and transient receptor potential channel-1 regulates Ca2+ entry. Role in signaling increased endothelial permeability". The Journal of Biological Chemistry. 278 (35): 33492–500. doi: 10.1074/jbc.M302401200 . PMID   12766172.
  17. Yuan JP, Kiselyov K, Shin DM, Chen J, Shcheynikov N, Kang SH, Dehoff MH, Schwarz MK, Seeburg PH, Muallem S, Worley PF (Sep 2003). "Homer binds TRPC family channels and is required for gating of TRPC1 by IP3 receptors". Cell. 114 (6): 777–89. doi: 10.1016/s0092-8674(03)00716-5 . PMID   14505576. S2CID   10552676.
  18. Mery L, Magnino F, Schmidt K, Krause KH, Dufour JF (Jan 2001). "Alternative splice variants of hTrp4 differentially interact with the C-terminal portion of the inositol 1,4,5-trisphosphate receptors". FEBS Letters. 487 (3): 377–83. doi: 10.1016/s0014-5793(00)02362-0 . PMID   11163362. S2CID   44945442.
  19. Argent L, Winter F, Prickett L, Carrasquero-Ordaz M, Olsen AL, Kramer H, Lancaster E, Becker EB (Sep 2020). "Caspr2 interacts with type 1 inositol 1,4,5-trisphosphate receptor in the developing cerebellum and regulatesPurkinje cell morphology". The Journal of Biological Chemistry. 295 (36): 12716–26. doi: 10.1074/jbc.RA120.012655 . PMC   7476715 . PMID   32675284.

Further reading