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Search results 401 to 486 out of 486 for Trpc5

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Type Details Score
Publication
- | J:164563
       
First Author: The Gene Ontology Consortium
Year: 2010
Title: Automated transfer of experimentally-verified manual GO annotation data to mouse-human orthologs
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Publication
21267068 | J:153498
First Author: Diez-Roux G
Year: 2011
Journal: PLoS Biol
Title: A high-resolution anatomical atlas of the transcriptome in the mouse embryo.
Volume: 9
Issue: 1
Pages: e1000582
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Publication
- | J:157972
     
First Author: Mouse Genome Informatics Scientific Curators
Year: 2010
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Genome U74 Array Platform (A, B, C v2).
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Publication
- | J:161428
       
First Author: Marc Feuermann, Huaiyu Mi, Pascale Gaudet, Dustin Ebert, Anushya Muruganujan, Paul Thomas
Year: 2010
Title: Annotation inferences using phylogenetic trees
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Publication
- | J:63103
     
First Author: Mouse Genome Database and National Center for Biotechnology Information
Year: 2000
Journal: Database Release
Title: Entrez Gene Load
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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
- | J:144086
     
First Author: Mouse Genome Informatics Scientific Curators
Year: 2009
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Gene 1.0 ST Array Platform
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Publication
- | J:155721
     
First Author: Mouse Genome Informatics (MGI) and The National Center for Biotechnology Information (NCBI)
Year: 2010
Journal: Database Download
Title: Consensus CDS project
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Publication
- | J:85324
     
First Author: Mouse Genome Informatics Group
Year: 2003
Journal: Database Procedure
Title: Automatic Encodes (AutoE) Reference
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Publication
- | J:53168
     
First Author: Bairoch A
Year: 1999
Journal: Database Release
Title: SWISS-PROT Annotated protein sequence database
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Publication
- | J:91388
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and Loading Genome Assembly Coordinates from Ensembl Annotations
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Publication
- | J:155221
     
First Author: Mouse Genome Informatics
Year: 2010
Journal: Database Release
Title: Protein Ontology Association Load.
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Publication
- | J:90438
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and loading genome assembly coordinates from NCBI annotations
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Publication
- | J:144087
     
First Author: Mouse Genome Informatics Scientific Curators
Year: 2009
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Genome 430 2.0 Array Platform
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Protein
Q9QX29
Organism: Mus musculus/domesticus
Length: 975  
Fragment?: false
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Publication
15895247 | -
First Author: Kinoshita-Kawada M
Year: 2005
Journal: Pflugers Arch
Title: Inhibition of TRPC5 channels by Ca2+-binding protein 1 in Xenopus oocytes.
Volume: 450
Issue: 5
Pages: 345-54
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Allele
Trpc5<tm1.1(cre)Dbru> | MGI:6758141
Name: transient receptor potential cation channel, subfamily C, member 5; targeted mutation 1.1, Dieter Bruns
Allele Type: Targeted
Attribute String: Recombinase
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Genotype
Genotype
Symbol: Gt(ROSA)26Sor/Gt(ROSA)26Sor<+> Trpc5/Trpc5<+>
Background: involves: 129S1/Sv * 129X1/SvJ
Zygosity: cn
Has Mutant Allele: true
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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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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
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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Publication
24703699 | J:213147
First Author: Qiu J
Year: 2014
Journal: Cell Metab
Title: Insulin excites anorexigenic proopiomelanocortin neurons via activation of canonical transient receptor potential channels.
Volume: 19
Issue: 4
Pages: 682-93
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Publication
37265366 | J:354066
First Author: Kidokoro K
Year: 2023
Journal: Kidney360
Title: Insights into the Regulation of GFR by the Keap1-Nrf2 Pathway.
Volume: 4
Issue: 10
Pages: 1454-1466
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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
30271326 | J:267272
 
First Author: Lepannetier S
Year: 2018
Journal: Front Cell Neurosci
Title: Activation of TRPC1 Channel by Metabotropic Glutamate Receptor mGluR5 Modulates Synaptic Plasticity and Spatial Working Memory.
Volume: 12
Pages: 318
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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
29915209 | J:262942
First Author: Griffin CS
Year: 2018
Journal: Sci Rep
Title: Muscarinic receptor-induced contractions of the detrusor are impaired in TRPC4 deficient mice.
Volume: 8
Issue: 1
Pages: 9264
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Publication
16407161 | J:248210
First Author: Kawasaki BT
Year: 2006
Journal: Proc Natl Acad Sci U S A
Title: Role of Src in C3 transient receptor potential channel function and evidence for a heterogeneous makeup of receptor- and store-operated Ca2+ entry channels.
Volume: 103
Issue: 2
Pages: 335-40
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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
24563462 | J:217250
First Author: Zimmermann J
Year: 2014
Journal: J Biol Chem
Title: Trans-activation response (TAR) RNA-binding protein 2 is a novel modulator of transient receptor potential canonical 4 (TRPC4) protein.
Volume: 289
Issue: 14
Pages: 9766-80
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Protein
Q8C8A8
Organism: Mus musculus/domesticus
Length: 783  
Fragment?: true
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Publication
34489621 | J:314265
 
First Author: Carver CM
Year: 2021
Journal: Front Neurosci
Title: Blockade of TRPC Channels Limits Cholinergic-Driven Hyperexcitability and Seizure Susceptibility After Traumatic Brain Injury.
Volume: 15
Pages: 681144
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Publication
24464579 | J:210682
First Author: Lee KP
Year: 2014
Journal: J Biol Chem
Title: Molecular determinants mediating gating of Transient Receptor Potential Canonical (TRPC) channels by stromal interaction molecule 1 (STIM1).
Volume: 289
Issue: 10
Pages: 6372-82
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Publication
32028278 | J:335486
First Author: Chang R
Year: 2021
Journal: Neuroendocrinology
Title: Pituitary Adenylate Cyclase-Activating Polypeptide Excites Proopiomelanocortin Neurons: Implications for the Regulation of Energy Homeostasis.
Volume: 111
Issue: 1-2
Pages: 45-69
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Publication
29165691 | J:255597
First Author: Qiu J
Year: 2018
Journal: Endocrinology
Title: Estradiol Protects Proopiomelanocortin Neurons Against Insulin Resistance.
Volume: 159
Issue: 2
Pages: 647-664
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Publication
31446151 | J:337959
 
First Author: He Z
Year: 2019
Journal: Mol Metab
Title: Direct and indirect effects of liraglutide on hypothalamic POMC and NPY/AgRP neurons - Implications for energy balance and glucose control.
Volume: 28
Pages: 120-134
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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
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
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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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
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
36589456 | J:340916
 
First Author: Ohyama S
Year: 2022
Journal: Front Physiol
Title: Piezo1-pannexin-1-P2X(3) axis in odontoblasts and neurons mediates sensory transduction in dentinal sensitivity.
Volume: 13
Pages: 891759
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Publication
34654752 | J:335326
First Author: Qiu J
Year: 2021
Journal: J Neurosci
Title: Deletion of Stim1 in Hypothalamic Arcuate Nucleus Kiss1 Neurons Potentiates Synchronous GCaMP Activity and Protects against Diet-Induced Obesity.
Volume: 41
Issue: 47
Pages: 9688-9701
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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
Q9WVC5
Organism: Mus musculus/domesticus
Length: 862  
Fragment?: false
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Protein
Q61056
Organism: Mus musculus/domesticus
Length: 793  
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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