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Search results 201 to 300 out of 309 for Trpc2

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Type Details Score
Publication
22411552 | J:181604
First Author: Seth M
Year: 2012
Journal: Dev Dyn
Title: Dynamic regulation of sarcoplasmic reticulum Ca(2+) stores by stromal interaction molecule 1 and sarcolipin during muscle differentiation.
Volume: 241
Issue: 4
Pages: 639-47
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Publication
9722956 | J:49394
First Author: Yamazaki K
Year: 1998
Journal: Genomics
Title: Genetic mapping of mouse transient receptor potential (Trrp) genes responsible for capacitative calcium entry channels to chromosomes 3, 7, 9, and X.
Volume: 51
Issue: 2
Pages: 303-5
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Publication
16460286 | J:105768
 
First Author: Ramsey IS
Year: 2006
Journal: Annu Rev Physiol
Title: An introduction to TRP channels.
Volume: 68
Pages: 619-47
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Publication
19834762 | J:161879
First Author: Asai Y
Year: 2010
Journal: J Assoc Res Otolaryngol
Title: A quantitative analysis of the spatiotemporal pattern of transient receptor potential gene expression in the developing mouse cochlea.
Volume: 11
Issue: 1
Pages: 27-37
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Publication
33884443 | J:307092
First Author: De Clercq K
Year: 2021
Journal: Cell Mol Life Sci
Title: Mapping the expression of transient receptor potential channels across murine placental development.
Volume: 78
Issue: 11
Pages: 4993-5014
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Publication
30786075 | J:294971
First Author: Fecher-Trost C
Year: 2019
Journal: J Bone Miner Res
Title: Maternal Transient Receptor Potential Vanilloid 6 (Trpv6) Is Involved In Offspring Bone Development.
Volume: 34
Issue: 4
Pages: 699-710
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Publication
19322198 | J:148796
First Author: Lechner SG
Year: 2009
Journal: EMBO J
Title: Developmental waves of mechanosensitivity acquisition in sensory neuron subtypes during embryonic development.
Volume: 28
Issue: 10
Pages: 1479-91
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Publication
19501082 | J:152865
First Author: Georgas K
Year: 2009
Journal: Dev Biol
Title: Analysis of early nephron patterning reveals a role for distal RV proliferation in fusion to the ureteric tip via a cap mesenchyme-derived connecting segment.
Volume: 332
Issue: 2
Pages: 273-86
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Publication
- | J:103485
     
First Author: Lexicon Genetics Inc
Year: 2005
Journal: MGI Direct Data Submission
Title: NIH initiative supporting placement of Lexicon Genetics, Inc. mice into public repositories
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Publication
11217851 | J:65060
First Author: Kawai J
Year: 2001
Journal: Nature
Title: Functional annotation of a full-length mouse cDNA collection.
Volume: 409
Issue: 6821
Pages: 685-90
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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
19521566 | J:177549
First Author: Willnow T
Year: 2005
Journal: Organogenesis
Title: The European renal genome project: an integrated approach towards understanding the genetics of kidney development and disease.
Volume: 2
Issue: 2
Pages: 42-7
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Publication
- | J:237616
     
First Author: MGI and IMPC
Year: 2017
Journal: MGI Direct Data Submission
Title: MGI Curation of Endonuclease-Mediated Alleles (CRISPR) from the International Mouse Phenotyping Consortium (IMPC)
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Publication
- | J:73065
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2001
Title: Gene Ontology Annotation by the MGI Curatorial Staff
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Publication
- | J:94790
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Mouse Synonym Curation
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Publication
- | J:57656
     
First Author: Lennon G
Year: 1999
Journal: Database Download
Title: WashU-HHMI Mouse EST Project
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Publication
- | J:136110
     
First Author: Velocigene
Year: 2008
Journal: MGI Direct Data Submission
Title: Alleles produced for the KOMP project by Velocigene (Regeneron Pharmaceuticals)
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Publication
- | J:171409
     
First Author: GUDMAP Consortium
Year: 2004
Journal: www.gudmap.org
Title: GUDMAP: the GenitoUrinary Development Molecular Anatomy Project
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Publication
- | J:72247
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2001
Title: Gene Ontology Annotation by the MGI Curatorial Staff
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Publication
- | J:211773
     
First Author: Mouse Genome Informatics and the International Mouse Phenotyping Consortium (IMPC)
Year: 2014
Journal: Database Release
Title: Obtaining and Loading Phenotype Annotations from the International Mouse Phenotyping Consortium (IMPC) Database
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Publication
16602821 | J:162220
First Author: Magdaleno S
Year: 2006
Journal: PLoS Biol
Title: BGEM: an in situ hybridization database of gene expression in the embryonic and adult mouse nervous system.
Volume: 4
Issue: 4
Pages: e86
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Publication
- | J:85000
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2003
Title: MGI Sequence Curation Reference
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Publication
- | J:23000
       
First Author: MGD Nomenclature Committee
Year: 1995
Title: Nomenclature Committee Use
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Publication
14610273 | J:86696
First Author: Zambrowicz BP
Year: 2003
Journal: Proc Natl Acad Sci U S A
Title: Wnk1 kinase deficiency lowers blood pressure in mice: a gene-trap screen to identify potential targets for therapeutic intervention.
Volume: 100
Issue: 24
Pages: 14109-14
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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
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: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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Protein
Q641L3
Organism: Mus musculus/domesticus
Length: 262  
Fragment?: false
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Protein
Q99L49
Organism: Mus musculus/domesticus
Length: 213  
Fragment?: false
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Protein
Q8BRU2
Organism: Mus musculus/domesticus
Length: 313  
Fragment?: false
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Publication
21854574 | J:202088
 
First Author: Frankenberg S
Year: 2011
Journal: BMC Mol Biol
Title: Identification of two distinct genes at the vertebrate TRPC2 locus and their characterisation in a marsupial and a monotreme.
Volume: 12
Pages: 39
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Protein
Q9R244
Organism: Mus musculus/domesticus
Length: 1172  
Fragment?: false
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Protein
Q9R244-3
Organism: Mus musculus/domesticus
Length: 886  
Fragment?: false
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Protein
Q9R244-4
Organism: Mus musculus/domesticus
Length: 890  
Fragment?: false
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Protein
Q9R244-2
Organism: Mus musculus/domesticus
Length: 1072  
Fragment?: false
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Publication
15589997 | -
First Author: Chu X
Year: 2005
Journal: Cell Calcium
Title: Identification of an N-terminal TRPC2 splice variant which inhibits calcium influx.
Volume: 37
Issue: 2
Pages: 173-82
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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
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
32298804 | J:304490
 
First Author: Eckstein E
Year: 2020
Journal: Mol Cell Neurosci
Title: Cyclic regulation of Trpm4 expression in female vomeronasal neurons driven by ovarian sex hormones.
Volume: 105
Pages: 103495
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Publication
28860523 | J:256462
First Author: Chamero P
Year: 2017
Journal: Sci Rep
Title: Type 3 inositol 1,4,5-trisphosphate receptor is dispensable for sensory activation of the mammalian vomeronasal organ.
Volume: 7
Issue: 1
Pages: 10260
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Publication
26670777 | J:279995
 
First Author: Saraiva LR
Year: 2015
Journal: Sci Rep
Title: Hierarchical deconstruction of mouse olfactory sensory neurons: from whole mucosa to single-cell RNA-seq.
Volume: 5
Pages: 18178
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Publication
25706994 | J:226300
First Author: Angoa-Pérez M
Year: 2015
Journal: PLoS One
Title: Brain serotonin signaling does not determine sexual preference in male mice.
Volume: 10
Issue: 2
Pages: e0118603
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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
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
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
Q61143
Organism: Mus musculus/domesticus
Length: 930  
Fragment?: false
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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
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
Q8BNB6
Organism: Mus musculus/domesticus
Length: 432  
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
Q8BNT2
Organism: Mus musculus/domesticus
Length: 974  
Fragment?: false
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Protein
E6Y6Q0
Organism: Mus musculus/domesticus
Length: 808  
Fragment?: false
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Protein
A0A0G2JEV6
Organism: Mus musculus/domesticus
Length: 400  
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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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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