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Search results 701 to 800 out of 824 for Trpc6

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Type Details Score
Publication
- | J:23000
       
First Author: MGD Nomenclature Committee
Year: 1995
Title: Nomenclature Committee Use
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Publication
- | J:293217
       
First Author: GemPharmatech
Year: 2020
Title: GemPharmatech Website.
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Publication
- | J:342587
       
First Author: AgBase, BHF-UCL, Parkinson's UK-UCL, dictyBase, HGNC, Roslin Institute, FlyBase and UniProtKB curators
Year: 2011
Title: Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
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Publication
- | J:68900
     
First Author: The Jackson Laboratory Mouse Radiation Hybrid Database
Year: 2004
Journal: Database Release
Title: Mouse T31 Radiation Hybrid Data Load
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Publication
12466851 | J:80000
First Author: Okazaki Y
Year: 2002
Journal: Nature
Title: Analysis of the mouse transcriptome based on functional annotation of 60,770 full-length cDNAs.
Volume: 420
Issue: 6915
Pages: 563-73
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Publication
- | J:164563
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2010
Title: Human to Mouse ISO GO annotation transfer
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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:57747
     
First Author: MGI Genome Annotation Group and UniGene Staff
Year: 2015
Journal: Database Download
Title: MGI-UniGene Interconnection Effort
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Publication
- | J:75000
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2002
Title: Mouse Genome Informatics Computational Sequence to Gene Associations
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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: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: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: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:155221
     
First Author: Mouse Genome Informatics
Year: 2010
Journal: Database Release
Title: Protein Ontology Association Load.
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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:85324
     
First Author: Mouse Genome Informatics Group
Year: 2003
Journal: Database Procedure
Title: Automatic Encodes (AutoE) Reference
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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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Publication
17099778 | J:117376
First Author: Kuwahara K
Year: 2006
Journal: J Clin Invest
Title: TRPC6 fulfills a calcineurin signaling circuit during pathologic cardiac remodeling.
Volume: 116
Issue: 12
Pages: 3114-26
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Strain
MGI:5450899 | B6;129P2-Trpc6<tm1Dgen>/H
Attribute String: mutant stock, targeted mutation
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Publication
36672207 | J:336232
 
First Author: Hagmann H
Year: 2023
Journal: Cells
Title: Capsazepine (CPZ) Inhibits TRPC6 Conductance and Is Protective in Adriamycin-Induced Nephropathy and Diabetic Glomerulopathy.
Volume: 12
Issue: 2
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Publication
35096991 | J:319713
 
First Author: Norton N
Year: 2021
Journal: Front Cardiovasc Med
Title: Trpc6 Promotes Doxorubicin-Induced Cardiomyopathy in Male Mice With Pleiotropic Differences Between Males and Females.
Volume: 8
Pages: 757784
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Publication
26348127 | J:231400
First Author: Chauvet S
Year: 2015
Journal: Biochim Biophys Acta
Title: The Na+/K+-ATPase and the amyloid-beta peptide aβ1-40 control the cellular distribution, abundance and activity of TRPC6 channels.
Volume: 1853
Issue: 11 Pt A
Pages: 2957-65
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Allele
Tg(NPHS2-Trpc6)F419Walz | MGI:5319631
Name: transgene insertion F419, Katherina Walz
Allele Type: Transgenic
Attribute String: Inserted expressed sequence
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Allele
Tg(NPHS2-Trpc6*E896K)F75aWalz | MGI:5319640
Name: transgene insertion F75a, Katherina Walz
Allele Type: Transgenic
Attribute String: Inserted expressed sequence
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Allele
Tg(NPHS2-Trpc6*P111Q)F615Walz | MGI:5319638
Name: transgene insertion F615, Katherina Walz
Allele Type: Transgenic
Attribute String: Inserted expressed sequence
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Genotype
Genotype
Symbol: Tg(NPHS2-Trpc6)F419Walz/?
Background: involves: C57BL/6J * CBA/J
Zygosity: ot
Has Mutant Allele: true
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Genotype
Genotype
Symbol: Tg(NPHS2-Trpc6*E896K)F75aWalz/?
Background: involves: C57BL/6J * CBA/J
Zygosity: ot
Has Mutant Allele: true
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Genotype
Genotype
Symbol: Tg(NPHS2-Trpc6*P111Q)F615Walz/?
Background: involves: C57BL/6J * CBA/J
Zygosity: ot
Has Mutant Allele: true
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Allele
Trpc6<em2Smoc> | MGI:7293000
Name: transient receptor potential cation channel, subfamily C, member 6; endonuclease-mediated mutation 2, Shanghai Model Organisms Center
Allele Type: Endonuclease-mediated
Attribute String: Null/knockout
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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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Interaction Experiment
Anderson M (2013)
Description: Opposing effects of podocin on the gating of podocyte TRPC6 channels evoked by membrane stretch or diacylglycerol.
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Protein
Q61143
Organism: Mus musculus/domesticus
Length: 930  
Fragment?: false
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Transgene
MGI:5319642 | Tg(NPHS2-Trpc6*E896K)F75aWalz
Type: transgene
Organism: mouse, laboratory
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Transgene
MGI:5319643 | Tg(NPHS2-Trpc6*P111Q)F615Walz
Type: transgene
Organism: mouse, laboratory
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Transgene
MGI:5319633 | Tg(NPHS2-Trpc6)F419Walz
Type: transgene
Organism: mouse, laboratory
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DO Term
DOID:0111129 | focal segmental glomerulosclerosis 2
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Allele
Trpc6<tm1Smoc> | MGI:7293001
Name: transient receptor potential cation channel, subfamily C, member 6; targeted mutation 1, Shanghai Model Organisms Center
Allele Type: Targeted
Attribute String: Conditional ready, No functional change
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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
23657570 | -
First Author: Anderson M
Year: 2013
Journal: Am J Physiol Cell Physiol
Title: Opposing effects of podocin on the gating of podocyte TRPC6 channels evoked by membrane stretch or diacylglycerol.
Volume: 305
Issue: 3
Pages: C276-89
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Allele
Tg(Myh6-TRPC6*)1Jmol | MGI:5294560
Name: transgene insertion 1, Jeffery D Molkentin
Allele Type: Transgenic
Attribute String: Humanized sequence, Inserted expressed sequence
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Strain
MGI:6354438 | C57BL/6J-Trpc6<tm1Smoc>/Smoc
Attribute String: congenic, mutant strain, targeted mutation
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Strain
MGI:5294578 | FVB-Tg(Myh6-TRPC6*)1Jmol/J
Attribute String: coisogenic, mutant strain, transgenic
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Allele
Tg(ACTA1-TRPC6*)1Jmol | MGI:5516499
Name: transgene insertion 1, Jeffery Molkentin
Allele Type: Transgenic
Attribute String: Dominant negative, Humanized sequence, Inserted expressed sequence
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Strain
MGI:5516507 | B6;FVB-Tg(ACTA1-TRPC6*)1Jmol/J
Attribute String: transgenic, mutant stock
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Strain
MGI:5319641 | B6.Cg-Tg(NPHS2-Trpc6)F419Walz/J
Attribute String: congenic, mutant strain, transgenic
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Publication
19864620 | J:154908
First Author: Millay DP
Year: 2009
Journal: Proc Natl Acad Sci U S A
Title: Calcium influx is sufficient to induce muscular dystrophy through a TRPC-dependent mechanism.
Volume: 106
Issue: 45
Pages: 19023-8
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Publication
15664177 | J:124819
First Author: Hashimotodani Y
Year: 2005
Journal: Neuron
Title: Phospholipase Cbeta serves as a coincidence detector through its Ca2+ dependency for triggering retrograde endocannabinoid signal.
Volume: 45
Issue: 2
Pages: 257-68
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Publication
23027959 | J:190298
First Author: Li W
Year: 2012
Journal: Proc Natl Acad Sci U S A
Title: Activity-dependent BDNF release and TRPC signaling is impaired in hippocampal neurons of Mecp2 mutant mice.
Volume: 109
Issue: 42
Pages: 17087-92
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Publication
29628897 | J:275884
 
First Author: López E
Year: 2018
Journal: Front Physiol
Title: Stanniocalcin 2 Regulates Non-capacitative Ca2+ Entry and Aggregation in Mouse Platelets.
Volume: 9
Pages: 266
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Publication
30354220 | J:285069
First Author: Carnevale D
Year: 2018
Journal: Arterioscler Thromb Vasc Biol
Title: Loss of EMILIN-1 Enhances Arteriolar Myogenic Tone Through TGF-β (Transforming Growth Factor-β)-Dependent Transactivation of EGFR (Epidermal Growth Factor Receptor) and Is Relevant for Hypertension in Mice and Humans.
Volume: 38
Issue: 10
Pages: 2484-2497
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Publication
35563527 | J:337998
 
First Author: Feng Y
Year: 2022
Journal: Int J Mol Sci
Title: DOT1L Methyltransferase Regulates Calcium Influx in Erythroid Progenitor Cells in Response to Erythropoietin.
Volume: 23
Issue: 9
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Publication
22207724 | J:317565
First Author: Kusudo T
Year: 2012
Journal: J Appl Physiol (1985)
Title: TRPV4 deficiency increases skeletal muscle metabolic capacity and resistance against diet-induced obesity.
Volume: 112
Issue: 7
Pages: 1223-32
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Publication
20651158 | J:185917
First Author: Wang Y
Year: 2010
Journal: J Am Soc Nephrol
Title: Activation of NFAT signaling in podocytes causes glomerulosclerosis.
Volume: 21
Issue: 10
Pages: 1657-66
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Publication
22249312 | J:183428
First Author: Boucher I
Year: 2012
Journal: Lab Invest
Title: Gα12 activation in podocytes leads to cumulative changes in glomerular collagen expression, proteinuria and glomerulosclerosis.
Volume: 92
Issue: 5
Pages: 662-75
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Publication
28430879 | J:269273
First Author: Krauszman A
Year: 2017
Journal: Cardiovasc Res
Title: Role of phosphatase and tensin homolog in hypoxic pulmonary vasoconstriction.
Volume: 113
Issue: 8
Pages: 869-878
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Publication
25829545 | J:220528
First Author: Tabeling C
Year: 2015
Journal: Proc Natl Acad Sci U S A
Title: CFTR and sphingolipids mediate hypoxic pulmonary vasoconstriction.
Volume: 112
Issue: 13
Pages: E1614-23
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Publication
12114324 | J:109706
First Author: Tiruppathi C
Year: 2002
Journal: Circ Res
Title: Impairment of store-operated Ca2+ entry in TRPC4(-/-) mice interferes with increase in lung microvascular permeability.
Volume: 91
Issue: 1
Pages: 70-6
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Publication
19279558 | J:162696
First Author: Catanuto P
Year: 2009
Journal: Kidney Int
Title: 17 beta-estradiol and tamoxifen upregulate estrogen receptor beta expression and control podocyte signaling pathways in a model of type 2 diabetes.
Volume: 75
Issue: 11
Pages: 1194-201
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Publication
31118506 | J:297186
First Author: Kang JS
Year: 2019
Journal: Sci Rep
Title: Angiotensin II-mediated MYH9 downregulation causes structural and functional podocyte injury in diabetic kidney disease.
Volume: 9
Issue: 1
Pages: 7679
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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
17884814 | J:128342
First Author: Semtner M
Year: 2007
Journal: J Biol Chem
Title: Potentiation of TRPC5 by protons.
Volume: 282
Issue: 46
Pages: 33868-78
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Publication
28442546 | J:247778
First Author: Wright JD
Year: 2017
Journal: FASEB J
Title: Modeled structural basis for the recognition of α2-3-sialyllactose by soluble Klotho.
Volume: 31
Issue: 8
Pages: 3574-3586
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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
29960052 | J:266063
 
First Author: Shimizu N
Year: 2018
Journal: Neurosci Lett
Title: Effects of nerve growth factor neutralization on TRP channel expression in laser-captured bladder afferent neurons in mice with spinal cord injury.
Volume: 683
Pages: 100-103
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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
23734001 | J:218651
First Author: Sah R
Year: 2013
Journal: Circulation
Title: Timing of myocardial trpm7 deletion during cardiogenesis variably disrupts adult ventricular function, conduction, and repolarization.
Volume: 128
Issue: 2
Pages: 101-14
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Publication
25171374 | J:219239
First Author: Matsushita N
Year: 2014
Journal: PLoS One
Title: Cardiac overexpression of constitutively active Galpha q causes angiotensin II type1 receptor activation, leading to progressive heart failure and ventricular arrhythmias in transgenic mice.
Volume: 9
Issue: 8
Pages: e106354
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Publication
33849280 | J:345532
First Author: Gammons J
Year: 2021
Journal: J Am Heart Assoc
Title: Cardiac-Specific Deletion of Orai3 Leads to Severe Dilated Cardiomyopathy and Heart Failure in Mice.
Volume: 10
Issue: 8
Pages: e019486
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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
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 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
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
32116663 | J:319809
 
First Author: Liu B
Year: 2019
Journal: Front Pharmacol
Title: Role of TG2-Mediated SERCA2 Serotonylation on Hypoxic Pulmonary Vein Remodeling.
Volume: 10
Pages: 1611
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Publication
30974795 | J:290976
 
First Author: Kameda T
Year: 2019
Journal: Int J Mol Sci
Title: Expression and Activity of TRPA1 and TRPV1 in the Intervertebral Disc: Association with Inflammation and Matrix Remodeling.
Volume: 20
Issue: 7
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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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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
Q8C8A8
Organism: Mus musculus/domesticus
Length: 783  
Fragment?: true
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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
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
Q9QX29
Organism: Mus musculus/domesticus
Length: 975  
Fragment?: false
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Protein
Q9R244
Organism: Mus musculus/domesticus
Length: 1172  
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
Q32MT5
Organism: Mus musculus/domesticus
Length: 836  
Fragment?: false
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MouseMine is a collaboration between MGI at The Jackson Laboratory and the InterMine project at the Cambridge Systems Biology Centre. MouseMine is funded through a grant from the NIH/NHGRI.The Jackson Laboratory makes no representation about the suitability or accuracy of this software or data for any purpose, and makes no warranties, either express or implied, including merchantability and fitness for a particular purpose or that the use of this software or data will not infringe any third party patents, copyrights, trademarks, or other rights. the software and data are provided "as is". This software and data are provided to enhance knowledge and encourage progress in the scientific community and are to be used only for research and educational purposes. Any reproduction or use for commercial purpose is prohibited without the prior express written permission of the Jackson Laboratory.

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