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Search results 201 to 290 out of 290 for Trpc1

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Type Details Score
Publication
- | J:262123
     
First Author: Allen Institute for Brain Science
Year: 2004
Journal: Allen Institute
Title: Allen Brain Atlas: mouse riboprobes
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Publication
19945390 | J:155746
First Author: Shim S
Year: 2009
Journal: Neuron
Title: Peptidyl-prolyl isomerase FKBP52 controls chemotropic guidance of neuronal growth cones via regulation of TRPC1 channel opening.
Volume: 64
Issue: 4
Pages: 471-83
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Publication
29615894 | J:313080
 
First Author: Wang D
Year: 2018
Journal: Front Aging Neurosci
Title: TRPC1 Deletion Causes Striatal Neuronal Cell Apoptosis and Proteomic Alterations in Mice.
Volume: 10
Pages: 72
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Publication
28185894 | J:255369
First Author: Antigny F
Year: 2017
Journal: Biochim Biophys Acta
Title: TRPC1 and TRPC4 channels functionally interact with STIM1L to promote myogenesis and maintain fast repetitive Ca2+ release in human myotubes.
Volume: 1864
Issue: 5
Pages: 806-813
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Publication
19052258 | J:146324
First Author: Sundivakkam PC
Year: 2009
Journal: Am J Physiol Cell Physiol
Title: Caveolin-1 scaffold domain interacts with TRPC1 and IP3R3 to regulate Ca2+ store release-induced Ca2+ entry in endothelial cells.
Volume: 296
Issue: 3
Pages: C403-13
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Protein
Q61056
Organism: Mus musculus/domesticus
Length: 793  
Fragment?: false
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Protein
Q61056-2
Organism: Mus musculus/domesticus
Length: 759  
Fragment?: false
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Allele
Trpc1<m1Btlr> | MGI:6283669
Name: transient receptor potential cation channel, subfamily C, member 1; mutation 1, Bruce Beutler
Allele Type: Chemically induced (ENU)
Attribute String: Not Specified
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Strain
MGI:6283670 | C57BL/6J-Trpc1<m1Btlr>
Attribute String: chemically induced mutation, coisogenic, mutant strain
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Genotype
Genotype
Symbol: Trpc1/Trpc1
Background: C57BL/6J-Trpc1
Zygosity: hm
Has Mutant Allele: true
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Publication
20188096 | -
First Author: Shimamoto S
Year: 2010
Journal: FEBS Lett
Title: S100 proteins regulate the interaction of Hsp90 with Cyclophilin 40 and FKBP52 through their tetratricopeptide repeats.
Volume: 584
Issue: 6
Pages: 1119-25
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Protein Domain
IPR031212 | FKBP4
Type: Family
Description: FKBP4 (also known as FKBP52) is an immunophilin that binds immunosuppressive drugs such as FK506 []. It interacts with Hsp90 []and has been shown to have peptidyl prolyl cis/trans isomerase activity []. It controls chemotropic guidance of neuronal growth cones via regulation of TRPC1 channel opening [].
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Publication
12032305 | J:177257
First Author: Hofmann T
Year: 2002
Journal: Proc Natl Acad Sci U S A
Title: Subunit composition of mammalian transient receptor potential channels in living cells.
Volume: 99
Issue: 11
Pages: 7461-6
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Publication
18635947 | -
First Author: Kang CB
Year: 2008
Journal: Neurosignals
Title: FKBP family proteins: immunophilins with versatile biological functions.
Volume: 16
Issue: 4
Pages: 318-25
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Publication
11350175 | -
First Author: Pirkl F
Year: 2001
Journal: J Mol Biol
Title: Functional analysis of the Hsp90-associated human peptidyl prolyl cis/trans isomerases FKBP51, FKBP52 and Cyp40.
Volume: 308
Issue: 4
Pages: 795-806
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Publication
17084381 | J:115579
First Author: Ohba T
Year: 2006
Journal: Biochem Biophys Res Commun
Title: Regulatory role of neuron-restrictive silencing factor in expression of TRPC1.
Volume: 351
Issue: 3
Pages: 764-70
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Publication
19450521 | J:148915
First Author: Riccio A
Year: 2009
Journal: Cell
Title: Essential role for TRPC5 in amygdala function and fear-related behavior.
Volume: 137
Issue: 4
Pages: 761-72
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Publication
17482476 | J:123222
First Author: Meis S
Year: 2007
Journal: Mol Cell Neurosci
Title: Postsynaptic mechanisms underlying responsiveness of amygdaloid neurons to cholecystokinin are mediated by a transient receptor potential-like current.
Volume: 35
Issue: 2
Pages: 356-67
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Protein Domain
IPR005460 | TRPC4_channel
Type: Family
Description: Transient receptor potential (TRP) channels can be described as tetramers formed by subunits with six transmembrane domains and containing cation-selective pores, which in several cases show high calcium permeability. The molecular architecture of TRP channels is reminiscent of voltage-gated channels and comprises six putative transmembrane segments (S1-S6), intracellular N- and C-termini, and a pore-forming reentrant loop between S5 and S6 [].TRP channels represent a superfamily conserved from worms to humans that comprise seven subfamilies []: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin or long TRPs), TRPA (ankyrin, whose only member is Transient receptor potential cation channel subfamily A member 1, TrpA1), TRPP (polycystin), TRPML (mucolipin) and TRPN (Nomp-C homologues), which has a single member that can be found in worms, flies, and zebrafish. TRPs are classified essentially according to their primary amino acid sequence rather than selectivity or ligand affinity, due to their heterogeneous properties and complex regulation.TRP channels are involved in many physiological functions, ranging from pure sensory functions, such as pheromone signalling, taste transduction, nociception, and temperature sensation, over homeostatic functions, such as Ca2+ and Mg2+ reabsorption and osmoregulation, to many other motile functions, such as muscle contraction and vaso-motor control [].The classical or canonical TRPC family (formerly short-TRPs, STRPs) encompasses channels presenting a large number of different activation modes. Some are store-operated, whereas others are receptor-operated channels activated by the production of diacylglicerol or redox processes. TRPC proteins also control growth cone guidance in both mammalian and amphibian model systems. All seven channels of this family share the common property of activation through phospholipase C (PLC)-coupled receptors []. It is believed that functional TRPC channels are generated in situ by association of four TRPC proteins to form either homotetramers or heterotetramers [].On the basis of sequence similarity, TRPC channels can be subdivided into four subgroups group 1 (TRPC1), group 2 (TRPC2), group 3 (TRPC3, TRPC6 and TRPC7) and group 4 (TRPC4 and TRPC5) []. While TRPC1 and TRPC2 are almost unique, TRPC4 and TRPC5 share approx. 65% identity. TRPC3, 6 and 7 form a structural and functional subfamily sharing 70-80% identity at the amino acid level and their common sensitivity towards diacylglycerol (DAG).TRPC4 and TRPC5 are thought to be receptor-operated, Ca2+-permeable, nonselective cation channels. It is likely that heteromultimers of TRPC1 and TRPC4 or TRPC5 form receptor-operated nonselective cation channels in central neurones, and that TRPC4 contributes to nonselective cation channels in intestinal smooth muscle [].
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Protein Domain
IPR005461 | TRPC5_channel
Type: Family
Description: Transient receptor potential (TRP) channels can be described as tetramers formed by subunits with six transmembrane domains and containing cation-selective pores, which in several cases show high calcium permeability. The molecular architecture of TRP channels is reminiscent of voltage-gated channels and comprises six putative transmembrane segments (S1-S6), intracellular N- and C-termini, and a pore-forming reentrant loop between S5 and S6 [].TRP channels represent a superfamily conserved from worms to humans that comprise seven subfamilies []: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin or long TRPs), TRPA (ankyrin, whose only member is Transient receptor potential cation channel subfamily A member 1, TrpA1), TRPP (polycystin), TRPML (mucolipin) and TRPN (Nomp-C homologues), which has a single member that can be found in worms, flies, and zebrafish. TRPs are classified essentially according to their primary amino acid sequence rather than selectivity or ligand affinity, due to their heterogeneous properties and complex regulation.TRP channels are involved in many physiological functions, ranging from pure sensory functions, such as pheromone signalling, taste transduction, nociception, and temperature sensation, over homeostatic functions, such as Ca2+ and Mg2+ reabsorption and osmoregulation, to many other motile functions, such as muscle contraction and vaso-motor control [].The classical or canonical TRPC family (formerly short-TRPs, STRPs) encompasses channels presenting a large number of different activation modes. Some are store-operated, whereas others are receptor-operated channels activated by the production of diacylglicerol or redox processes. TRPC proteins also control growth cone guidance in both mammalian and amphibian model systems. All seven channels of this family share the common property of activation through phospholipase C (PLC)-coupled receptors []. It is believed that functional TRPC channels are generated in situ by association of four TRPC proteins to form either homotetramers or heterotetramers [].On the basis of sequence similarity, TRPC channels can be subdivided into four subgroups group 1 (TRPC1), group 2 (TRPC2), group 3 (TRPC3, TRPC6 and TRPC7) and group 4 (TRPC4 and TRPC5) []. While TRPC1 and TRPC2 are almost unique, TRPC4 and TRPC5 share approx. 65% identity. TRPC3, 6 and 7 form a structural and functional subfamily sharing 70-80% identity at the amino acid level and their common sensitivity towards diacylglycerol (DAG).TRPC4 and TRPC5 are thought to be receptor-operated, Ca2+-permeable, nonselective cation channels. It is likely that heteromultimers of TRPC1 and TRPC4 or TRPC5 form receptor-operated nonselective cation channels in central neurones, and that TRPC4 contributes to nonselective cation channels in intestinal smooth muscle [].
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Protein
F7CAT1
Organism: Mus musculus/domesticus
Length: 187  
Fragment?: true
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Publication
12765689 | -
First Author: Plant TD
Year: 2003
Journal: Cell Calcium
Title: TRPC4 and TRPC5: receptor-operated Ca2+-permeable nonselective cation channels.
Volume: 33
Issue: 5-6
Pages: 441-50
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Publication
28646178 | J:271483
First Author: Li W
Year: 2017
Journal: Sci Rep
Title: Increased glomerular filtration rate and impaired contractile function of mesangial cells in TRPC6 knockout mice.
Volume: 7
Issue: 1
Pages: 4145
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Publication
21368296 | J:174250
First Author: Linde CI
Year: 2011
Journal: Am J Physiol Cell Physiol
Title: Dysregulation of Ca2+ signaling in astrocytes from mice lacking amyloid precursor protein.
Volume: 300
Issue: 6
Pages: C1502-12
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Publication
23203809 | J:200237
First Author: Pani B
Year: 2013
Journal: J Cell Sci
Title: Impairment of TRPC1-STIM1 channel assembly and AQP5 translocation compromise agonist-stimulated fluid secretion in mice lacking caveolin1.
Volume: 126
Issue: Pt 2
Pages: 667-75
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Publication
28324107 | J:245610
First Author: Beck A
Year: 2017
Journal: Endocrinology
Title: Functional Characterization of Transient Receptor Potential (TRP) Channel C5 in Female Murine Gonadotropes.
Volume: 158
Issue: 4
Pages: 887-902
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Publication
22037305 | J:346502
First Author: Gilliam JC
Year: 2011
Journal: Vision Res
Title: TRP channel gene expression in the mouse retina.
Volume: 51
Issue: 23-24
Pages: 2440-52
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Publication
18990707 | J:145902
First Author: Bair AM
Year: 2009
Journal: J Biol Chem
Title: Ca2+ entry via TRPC channels is necessary for thrombin-induced NF-kappaB activation in endothelial cells through AMP-activated protein kinase and protein kinase Cdelta.
Volume: 284
Issue: 1
Pages: 563-74
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Publication
24599464 | J:209620
First Author: Riccio A
Year: 2014
Journal: J Neurosci
Title: Decreased anxiety-like behavior and Gαq/11-dependent responses in the amygdala of mice lacking TRPC4 channels.
Volume: 34
Issue: 10
Pages: 3653-67
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Publication
26221052 | J:260186
First Author: Desai PN
Year: 2015
Journal: Sci Signal
Title: Multiple types of calcium channels arising from alternative translation initiation of the Orai1 message.
Volume: 8
Issue: 387
Pages: ra74
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Publication
20093626 | J:172147
First Author: Ma X
Year: 2010
Journal: Arterioscler Thromb Vasc Biol
Title: Functional role of vanilloid transient receptor potential 4-canonical transient receptor potential 1 complex in flow-induced Ca2+ influx.
Volume: 30
Issue: 4
Pages: 851-8
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Publication
24731445 | J:211094
First Author: Sonneveld R
Year: 2014
Journal: Am J Pathol
Title: Glucose specifically regulates TRPC6 expression in the podocyte in an AngII-dependent manner.
Volume: 184
Issue: 6
Pages: 1715-26
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Publication
26236150 | J:226572
 
First Author: Choi HJ
Year: 2015
Journal: Mol Vis
Title: Astrocytes in the optic nerve head express putative mechanosensitive channels.
Volume: 21
Pages: 749-66
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Publication
25824146 | J:257129
First Author: Wang J
Year: 2015
Journal: Cardiovasc Res
Title: Hypoxia inducible factor-1-dependent up-regulation of BMP4 mediates hypoxia-induced increase of TRPC expression in PASMCs.
Volume: 107
Issue: 1
Pages: 108-18
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Publication
31099508 | J:289230
First Author: Kong W
Year: 2019
Journal: Cell Physiol Biochem
Title: Renal Fibrosis, Immune Cell Infiltration and Changes of TRPC Channel Expression after Unilateral Ureteral Obstruction in Trpc6-/- Mice.
Volume: 52
Issue: 6
Pages: 1484-1502
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Publication
32153426 | J:312222
 
First Author: Lopez JR
Year: 2020
Journal: Front Physiol
Title: Contribution of TRPC Channels to Intracellular Ca2 + Dyshomeostasis in Smooth Muscle From mdx Mice.
Volume: 11
Pages: 126
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Publication
24908566 | J:214738
First Author: He F
Year: 2014
Journal: Diabetologia
Title: MiR-135a promotes renal fibrosis in diabetic nephropathy by regulating TRPC1.
Volume: 57
Issue: 8
Pages: 1726-36
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Publication
31982426 | J:288285
 
First Author: Hu Q
Year: 2020
Journal: J Mol Cell Cardiol
Title: Location and function of transient receptor potential canonical channel 1 in ventricular myocytes.
Volume: 139
Pages: 113-123
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Publication
18184877 | J:309851
First Author: Shan D
Year: 2008
Journal: Am J Physiol Cell Physiol
Title: Overexpression of TRPC3 increases apoptosis but not necrosis in response to ischemia-reperfusion in adult mouse cardiomyocytes.
Volume: 294
Issue: 3
Pages: C833-41
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Publication
23171960 | J:318155
First Author: Schmid E
Year: 2012
Journal: Cell Physiol Biochem
Title: SGK3 regulates Ca(2+) entry and migration of dendritic cells.
Volume: 30
Issue: 6
Pages: 1423-35
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Publication
15909153 | -
First Author: Dietrich A
Year: 2005
Journal: Naunyn Schmiedebergs Arch Pharmacol
Title: Functional characterization and physiological relevance of the TRPC3/6/7 subfamily of cation channels.
Volume: 371
Issue: 4
Pages: 257-65
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Publication
11864597 | J:74749
First Author: Montell C
Year: 2002
Journal: Mol Cell
Title: A unified nomenclature for the superfamily of TRP cation channels.
Volume: 9
Issue: 2
Pages: 229-31
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Publication
9930701 | -
First Author: Hofmann T
Year: 1999
Journal: Nature
Title: Direct activation of human TRPC6 and TRPC3 channels by diacylglycerol.
Volume: 397
Issue: 6716
Pages: 259-63
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Publication
32037396 | -
First Author: Hu Y
Year: 2020
Journal: Hypertens Res
Title: High-salt intake increases TRPC3 expression and enhances TRPC3-mediated calcium influx and systolic blood pressure in hypertensive patients.
Volume: 43
Issue: 7
Pages: 679-687
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Publication
20095964 | -
First Author: Woo JS
Year: 2010
Journal: Biochem J
Title: S165F mutation of junctophilin 2 affects Ca2+ signalling in skeletal muscle.
Volume: 427
Issue: 1
Pages: 125-34
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Protein Domain
IPR005457 | TRPC1_channel
Type: Family
Description: Transient receptor potential (TRP) channels can be described as tetramers formed by subunits with six transmembrane domains and containing cation-selective pores, which in several cases show high calcium permeability. The molecular architecture of TRP channels is reminiscent of voltage-gated channels and comprises six putative transmembrane segments (S1-S6), intracellular N- and C-termini, and a pore-forming reentrant loop between S5 and S6 [].TRP channels represent a superfamily conserved from worms to humans that comprise seven subfamilies []: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin or long TRPs), TRPA (ankyrin, whose only member is Transient receptor potential cation channel subfamily A member 1, TrpA1), TRPP (polycystin), TRPML (mucolipin) and TRPN (Nomp-C homologues), which has a single member that can be found in worms, flies, and zebrafish. TRPs are classified essentially according to their primary amino acid sequence rather than selectivity or ligand affinity, due to their heterogeneous properties and complex regulation.TRP channels are involved in many physiological functions, ranging from pure sensory functions, such as pheromone signalling, taste transduction, nociception, and temperature sensation, over homeostatic functions, such as Ca2+ and Mg2+ reabsorption and osmoregulation, to many other motile functions, such as muscle contraction and vaso-motor control [].The classical or canonical TRPC family (formerly short-TRPs, STRPs) encompasses channels presenting a large number of different activation modes. Some are store-operated, whereas others are receptor-operated channels activated by the production of diacylglicerol or redox processes. TRPC proteins also control growth cone guidance in both mammalian and amphibian model systems. All seven channels of this family share the common property of activation through phospholipase C (PLC)-coupled receptors []. It is believed that functional TRPC channels are generated in situ by association of four TRPC proteins to form either homotetramers or heterotetramers [].On the basis of sequence similarity, TRPC channels can be subdivided into four subgroups group 1 (TRPC1), group 2 (TRPC2), group 3 (TRPC3, TRPC6 and TRPC7) and group 4 (TRPC4 and TRPC5) []. While TRPC1 and TRPC2 are almost unique, TRPC4 and TRPC5 share approx. 65% identity. TRPC3, 6 and 7 form a structural and functional subfamily sharing 70-80% identity at the amino acid level and their common sensitivity towards diacylglycerol (DAG).
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Protein Domain
IPR005458 | TRPC2_channel
Type: Family
Description: Transient receptor potential (TRP) channels can be described as tetramers formed by subunits with six transmembrane domains and containing cation-selective pores, which in several cases show high calcium permeability. The molecular architecture of TRP channels is reminiscent of voltage-gated channels and comprises six putative transmembrane segments (S1-S6), intracellular N- and C-termini, and a pore-forming reentrant loop between S5 and S6 [].TRP channels represent a superfamily conserved from worms to humans that comprise seven subfamilies []: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin or long TRPs), TRPA (ankyrin, whose only member is Transient receptor potential cation channel subfamily A member 1, TrpA1), TRPP (polycystin), TRPML (mucolipin) and TRPN (Nomp-C homologues), which has a single member that can be found in worms, flies, and zebrafish. TRPs are classified essentially according to their primary amino acid sequence rather than selectivity or ligand affinity, due to their heterogeneous properties and complex regulation.TRP channels are involved in many physiological functions, ranging from pure sensory functions, such as pheromone signalling, taste transduction, nociception, and temperature sensation, over homeostatic functions, such as Ca2+ and Mg2+ reabsorption and osmoregulation, to many other motile functions, such as muscle contraction and vaso-motor control [].The classical or canonical TRPC family (formerly short-TRPs, STRPs) encompasses channels presenting a large number of different activation modes. Some are store-operated, whereas others are receptor-operated channels activated by the production of diacylglicerol or redox processes. TRPC proteins also control growth cone guidance in both mammalian and amphibian model systems. All seven channels of this family share the common property of activation through phospholipase C (PLC)-coupled receptors []. It is believed that functional TRPC channels are generated in situ by association of four TRPC proteins to form either homotetramers or heterotetramers [].On the basis of sequence similarity, TRPC channels can be subdivided into four subgroups group 1 (TRPC1), group 2 (TRPC2), group 3 (TRPC3, TRPC6 and TRPC7) and group 4 (TRPC4 and TRPC5) []. While TRPC1 and TRPC2 are almost unique, TRPC4 and TRPC5 share approx. 65% identity. TRPC3, 6 and 7 form a structural and functional subfamily sharing 70-80% identity at the amino acid level and their common sensitivity towards diacylglycerol (DAG).
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Protein Domain
IPR005459 | TRPC3_channel
Type: Family
Description: Transient receptor potential (TRP) channels can be described as tetramers formed by subunits with six transmembrane domains and containing cation-selective pores, which in several cases show high calcium permeability. The molecular architecture of TRP channels is reminiscent of voltage-gated channels and comprises six putative transmembrane segments (S1-S6), intracellular N- and C-termini, and a pore-forming reentrant loop between S5 and S6 [].TRP channels represent a superfamily conserved from worms to humans that comprise seven subfamilies []: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin or long TRPs), TRPA (ankyrin, whose only member is Transient receptor potential cation channel subfamily A member 1, TrpA1), TRPP (polycystin), TRPML (mucolipin) and TRPN (Nomp-C homologues), which has a single member that can be found in worms, flies, and zebrafish. TRPs are classified essentially according to their primary amino acid sequence rather than selectivity or ligand affinity, due to their heterogeneous properties and complex regulation.TRP channels are involved in many physiological functions, ranging from pure sensory functions, such as pheromone signalling, taste transduction, nociception, and temperature sensation, over homeostatic functions, such as Ca2+ and Mg2+ reabsorption and osmoregulation, to many other motile functions, such as muscle contraction and vaso-motor control [].The classical or canonical TRPC family (formerly short-TRPs, STRPs) encompasses channels presenting a large number of different activation modes. Some are store-operated, whereas others are receptor-operated channels activated by the production of diacylglicerol or redox processes. TRPC proteins also control growth cone guidance in both mammalian and amphibian model systems. All seven channels of this family share the common property of activation through phospholipase C (PLC)-coupled receptors []. It is believed that functional TRPC channels are generated in situ by association of four TRPC proteins to form either homotetramers or heterotetramers [].On the basis of sequence similarity, TRPC channels can be subdivided into four subgroups group 1 (TRPC1), group 2 (TRPC2), group 3 (TRPC3, TRPC6 and TRPC7) and group 4 (TRPC4 and TRPC5) []. While TRPC1 and TRPC2 are almost unique, TRPC4 and TRPC5 share approx. 65% identity. TRPC3, 6 and 7 form a structural and functional subfamily sharing 70-80% identity at the amino acid level and their common sensitivity towards diacylglycerol (DAG).TRPC3, 6, and 7 interact physically and, upon coexpression, coassemble to form functional tetrameric channels [].TRPC3 is likely to be operated by a phosphatidylinositol second messenger system activated by receptor tyrosine kinases or G-protein coupled receptors. It is activated by diacylglycerol (DAG) in a membrane-delimited fashion, independently of protein kinase C, and by inositol 1,4,5-triphosphate receptors (ITPR) with bound IP3 [, ]. High levels of TRPC3 mRNA have been related to elevated salt intake and increased blood pressure [].
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Protein Domain
IPR005462 | TRPC6_channel
Type: Family
Description: Transient receptor potential (TRP) channels can be described as tetramers formed by subunits with six transmembrane domains and containing cation-selective pores, which in several cases show high calcium permeability. The molecular architecture of TRP channels is reminiscent of voltage-gated channels and comprises six putative transmembrane segments (S1-S6), intracellular N- and C-termini, and a pore-forming reentrant loop between S5 and S6 [].TRP channels represent a superfamily conserved from worms to humans that comprise seven subfamilies []: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin or long TRPs), TRPA (ankyrin, whose only member is Transient receptor potential cation channel subfamily A member 1, TrpA1), TRPP (polycystin), TRPML (mucolipin) and TRPN (Nomp-C homologues), which has a single member that can be found in worms, flies, and zebrafish. TRPs are classified essentially according to their primary amino acid sequence rather than selectivity or ligand affinity, due to their heterogeneous properties and complex regulation.TRP channels are involved in many physiological functions, ranging from pure sensory functions, such as pheromone signalling, taste transduction, nociception, and temperature sensation, over homeostatic functions, such as Ca2+ and Mg2+ reabsorption and osmoregulation, to many other motile functions, such as muscle contraction and vaso-motor control [].The classical or canonical TRPC family (formerly short-TRPs, STRPs) encompasses channels presenting a large number of different activation modes. Some are store-operated, whereas others are receptor-operated channels activated by the production of diacylglicerol or redox processes. TRPC proteins also control growth cone guidance in both mammalian and amphibian model systems. All seven channels of this family share the common property of activation through phospholipase C (PLC)-coupled receptors []. It is believed that functional TRPC channels are generated in situ by association of four TRPC proteins to form either homotetramers or heterotetramers [].On the basis of sequence similarity, TRPC channels can be subdivided into four subgroups group 1 (TRPC1), group 2 (TRPC2), group 3 (TRPC3, TRPC6 and TRPC7) and group 4 (TRPC4 and TRPC5) []. While TRPC1 and TRPC2 are almost unique, TRPC4 and TRPC5 share approx. 65% identity. TRPC3, 6 and 7 form a structural and functional subfamily sharing 70-80% identity at the amino acid level and their common sensitivity towards diacylglycerol (DAG).TRPC3, 6, and 7 interact physically and, upon coexpression, coassemble to form functional tetrameric channels [].
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Protein Domain
IPR005463 | TRPC7_channel
Type: Family
Description: Transient receptor potential (TRP) channels can be described as tetramers formed by subunits with six transmembrane domains and containing cation-selective pores, which in several cases show high calcium permeability. The molecular architecture of TRP channels is reminiscent of voltage-gated channels and comprises six putative transmembrane segments (S1-S6), intracellular N- and C-termini, and a pore-forming reentrant loop between S5 and S6 [].TRP channels represent a superfamily conserved from worms to humans that comprise seven subfamilies []: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin or long TRPs), TRPA (ankyrin, whose only member is Transient receptor potential cation channel subfamily A member 1, TrpA1), TRPP (polycystin), TRPML (mucolipin) and TRPN (Nomp-C homologues), which has a single member that can be found in worms, flies, and zebrafish. TRPs are classified essentially according to their primary amino acid sequence rather than selectivity or ligand affinity, due to their heterogeneous properties and complex regulation.TRP channels are involved in many physiological functions, ranging from pure sensory functions, such as pheromone signalling, taste transduction, nociception, and temperature sensation, over homeostatic functions, such as Ca2+ and Mg2+ reabsorption and osmoregulation, to many other motile functions, such as muscle contraction and vaso-motor control [].The classical or canonical TRPC family (formerly short-TRPs, STRPs) encompasses channels presenting a large number of different activation modes. Some are store-operated, whereas others are receptor-operated channels activated by the production of diacylglicerol or redox processes. TRPC proteins also control growth cone guidance in both mammalian and amphibian model systems. All seven channels of this family share the common property of activation through phospholipase C (PLC)-coupled receptors []. It is believed that functional TRPC channels are generated in situ by association of four TRPC proteins to form either homotetramers or heterotetramers [].On the basis of sequence similarity, TRPC channels can be subdivided into four subgroups group 1 (TRPC1), group 2 (TRPC2), group 3 (TRPC3, TRPC6 and TRPC7) and group 4 (TRPC4 and TRPC5) []. While TRPC1 and TRPC2 are almost unique, TRPC4 and TRPC5 share approx. 65% identity. TRPC3, 6 and 7 form a structural and functional subfamily sharing 70-80% identity at the amino acid level and their common sensitivity towards diacylglycerol (DAG).TRPC3, 6, and 7 interact physically and, upon coexpression, coassemble to form functional tetrameric channels [].
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Publication
27614169 | J:321384
First Author: Morine KJ
Year: 2016
Journal: Cardiovasc Pathol
Title: Endoglin selectively modulates transient receptor potential channel expression in left and right heart failure.
Volume: 25
Issue: 6
Pages: 478-482
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Protein
Q8C8A8
Organism: Mus musculus/domesticus
Length: 783  
Fragment?: true
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Protein
Q9QX29
Organism: Mus musculus/domesticus
Length: 975  
Fragment?: false
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Protein
Q9QUQ5
Organism: Mus musculus/domesticus
Length: 974  
Fragment?: false
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Protein
Q2KHN9
Organism: Mus musculus/domesticus
Length: 975  
Fragment?: false
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Protein
Q8BNB6
Organism: Mus musculus/domesticus
Length: 432  
Fragment?: false
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Protein
Q8BNT2
Organism: Mus musculus/domesticus
Length: 974  
Fragment?: false
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Protein
A0A0G2JEV6
Organism: Mus musculus/domesticus
Length: 400  
Fragment?: false
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Protein
Q0VB97
Organism: Mus musculus/domesticus
Length: 974  
Fragment?: false
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Publication
18535090 | -
First Author: Gaudet R
Year: 2008
Journal: J Physiol
Title: TRP channels entering the structural era.
Volume: 586
Issue: 15
Pages: 3565-75
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Publication
20025796 | -
First Author: Latorre R
Year: 2009
Journal: Q Rev Biophys
Title: Structure-functional intimacies of transient receptor potential channels.
Volume: 42
Issue: 3
Pages: 201-46
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Publication
20861159 | -
First Author: Gees M
Year: 2010
Journal: Cold Spring Harb Perspect Biol
Title: The role of transient receptor potential cation channels in Ca2+ signaling.
Volume: 2
Issue: 10
Pages: a003962
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Protein
Q61057
Organism: Mus musculus/domesticus
Length: 105  
Fragment?: true
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Protein
A0A087WSD0
Organism: Mus musculus/domesticus
Length: 255  
Fragment?: true
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Protein
F6S2D5
Organism: Mus musculus/domesticus
Length: 260  
Fragment?: true
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Protein
P30416
Organism: Mus musculus/domesticus
Length: 458  
Fragment?: false
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Protein
Q9WVC5
Organism: Mus musculus/domesticus
Length: 862  
Fragment?: false
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Protein
Q9QZC1
Organism: Mus musculus/domesticus
Length: 836  
Fragment?: false
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Protein
Q61143
Organism: Mus musculus/domesticus
Length: 930  
Fragment?: false
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Protein
Q9R244
Organism: Mus musculus/domesticus
Length: 1172  
Fragment?: false
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Protein
Q32MT5
Organism: Mus musculus/domesticus
Length: 836  
Fragment?: false
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Protein
Q6NV56
Organism: Mus musculus/domesticus
Length: 406  
Fragment?: false
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Protein
G3UZW6
Organism: Mus musculus/domesticus
Length: 746  
Fragment?: true
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Protein
Q0VFY2
Organism: Mus musculus/domesticus
Length: 862  
Fragment?: false
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Protein
G3UYZ6
Organism: Mus musculus/domesticus
Length: 380  
Fragment?: true
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Protein
G3UZF9
Organism: Mus musculus/domesticus
Length: 261  
Fragment?: true
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Protein
Q3UXW9
Organism: Mus musculus/domesticus
Length: 861  
Fragment?: false
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Protein
F8VQM8
Organism: Mus musculus/domesticus
Length: 1264  
Fragment?: false
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Protein
E9PVJ9
Organism: Mus musculus/domesticus
Length: 861  
Fragment?: false
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Protein
E6Y6Q0
Organism: Mus musculus/domesticus
Length: 808  
Fragment?: false
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Protein
Q8CCQ1
Organism: Mus musculus/domesticus
Length: 880  
Fragment?: false
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Protein
G3UWT1
Organism: Mus musculus/domesticus
Length: 801  
Fragment?: false
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Protein
Q8BNT8
Organism: Mus musculus/domesticus
Length: 836  
Fragment?: false
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Protein
Q2VPD3
Organism: Mus musculus/domesticus
Length: 835  
Fragment?: true
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Protein
Q5F0M4
Organism: Mus musculus/domesticus
Length: 1119  
Fragment?: false
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Protein
G3UWI6
Organism: Mus musculus/domesticus
Length: 807  
Fragment?: false
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Protein
D6RI84
Organism: Mus musculus/domesticus
Length: 451  
Fragment?: false
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Protein
B2RPS7
Organism: Mus musculus/domesticus
Length: 809  
Fragment?: false
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Protein
Q3UZG1
Organism: Mus musculus/domesticus
Length: 852  
Fragment?: false
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Protein
B7ZMP6
Organism: Mus musculus/domesticus
Length: 775  
Fragment?: false
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