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Search results 201 to 294 out of 294 for Trpv5

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Type Details Score
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
31488724 | J:279511
First Author: Hou J
Year: 2019
Journal: Proc Natl Acad Sci U S A
Title: Phosphorylated claudin-16 interacts with Trpv5 and regulates transcellular calcium transport in the kidney.
Volume: 116
Issue: 38
Pages: 19176-19186
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Allele
Trpv5<em1Smoc> | MGI:7293012
Name: transient receptor potential cation channel, subfamily V, member 5; endonuclease-mediated mutation 1, Shanghai Model Organisms Center
Allele Type: Endonuclease-mediated
Attribute String: Null/knockout
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Interaction Experiment
Radhakrishnan VM (2013)
Description: Post-Translational Loss of Renal TRPV5 Calcium Channel Expression, Ca2+ Wasting, and Bone Loss in Experimental Colitis.
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Strain
MGI:6476551 | C57BL/6JSmoc-Trpv5<em1Smoc>/Smoc
Attribute String: coisogenic, endonuclease-mediated mutation, mutant strain
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Publication
16380433 | -
First Author: van de Graaf SF
Year: 2006
Journal: J Am Soc Nephrol
Title: Identification of BSPRY as a novel auxiliary protein inhibiting TRPV5 activity.
Volume: 17
Issue: 1
Pages: 26-30
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Publication
23747339 | -
First Author: Radhakrishnan VM
Year: 2013
Journal: Gastroenterology
Title: Post-translational loss of renal TRPV5 calcium channel expression, Ca(2+) wasting, and bone loss in experimental colitis.
Volume: 145
Issue: 3
Pages: 613-24
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Allele
Tg(Trpv5-cre)#Prae | MGI:4888717
Name: transgene insertion, Jeppe Praetorius
Allele Type: Transgenic
Attribute String: Recombinase
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Allele
Tg(MAR-Trpv5-cre)#Prae | MGI:4888728
Name: transgene insertion, Jeppe Praetorius
Allele Type: Transgenic
Attribute String: Recombinase
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Allele
Tg(Trpv5-EGFP)1Prae | MGI:4888742
Name: transgene insertion 1, Jeppe Praetorius
Allele Type: Transgenic
Attribute String: Reporter
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Publication
25648899 | J:220522
First Author: Radhakrishnan VM
Year: 2015
Journal: J Biol Chem
Title: Experimental colitis is associated with transcriptional inhibition of Na+/Ca2+ exchanger isoform 1 (NCX1) expression by interferon γ in the renal distal convoluted tubules.
Volume: 290
Issue: 14
Pages: 8964-74
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Publication
21993891 | J:180072
First Author: Hofmeister MV
Year: 2012
Journal: Am J Physiol Renal Physiol
Title: 17β-Estradiol induces nongenomic effects in renal intercalated cells through G protein-coupled estrogen receptor 1.
Volume: 302
Issue: 3
Pages: F358-68
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Publication
30038585 | J:277421
 
First Author: Moor MB
Year: 2018
Journal: Front Physiol
Title: Renal Memo1 Differentially Regulates the Expression of Vitamin D-Dependent Distal Renal Tubular Calcium Transporters.
Volume: 9
Pages: 874
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Publication
22878123 | J:192782
First Author: Woudenberg-Vrenken TE
Year: 2012
Journal: Am J Physiol Gastrointest Liver Physiol
Title: Functional TRPV6 channels are crucial for transepithelial Ca2+ absorption.
Volume: 303
Issue: 7
Pages: G879-85
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Publication
22878961 | J:201719
First Author: Olauson H
Year: 2012
Journal: J Am Soc Nephrol
Title: Targeted deletion of Klotho in kidney distal tubule disrupts mineral metabolism.
Volume: 23
Issue: 10
Pages: 1641-51
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Publication
17299139 | J:121442
First Author: Wangemann P
Year: 2007
Journal: Am J Physiol Renal Physiol
Title: Loss of cochlear HCO3- secretion causes deafness via endolymphatic acidification and inhibition of Ca2+ reabsorption in a Pendred syndrome mouse model.
Volume: 292
Issue: 5
Pages: F1345-53
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Publication
31628396 | J:285298
First Author: Daryadel A
Year: 2019
Journal: Sci Rep
Title: Elevated FGF23 and disordered renal mineral handling with reduced bone mineralization in chronically erythropoietin over-expressing transgenic mice.
Volume: 9
Issue: 1
Pages: 14989
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Publication
32729975 | J:307389
First Author: Bøllehuus Hansen L
Year: 2020
Journal: FASEB J
Title: Influence of FGF23 and Klotho on male reproduction: Systemic vs direct effects.
Volume: 34
Issue: 9
Pages: 12436-12449
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Publication
19713312 | J:166318
First Author: Alexander RT
Year: 2009
Journal: J Am Soc Nephrol
Title: Klotho prevents renal calcium loss.
Volume: 20
Issue: 11
Pages: 2371-9
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Publication
20181799 | J:168175
First Author: Yang SS
Year: 2010
Journal: Endocrinology
Title: Mechanisms for hypercalciuria in pseudohypoaldosteronism type II-causing WNK4 knock-in mice.
Volume: 151
Issue: 4
Pages: 1829-36
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Publication
31496133 | J:293633
First Author: Ferdaus MZ
Year: 2019
Journal: Physiol Rep
Title: WNK4 limits distal calcium losses following acute furosemide treatment.
Volume: 7
Issue: 17
Pages: e14195
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Publication
24686448 | J:274997
First Author: Chen F
Year: 2014
Journal: Cell Physiol Biochem
Title: Knockout of TRPV6 causes osteopenia in mice by increasing osteoclastic differentiation and activity.
Volume: 33
Issue: 3
Pages: 796-809
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Publication
28602864 | J:254307
 
First Author: Yang H
Year: 2017
Journal: Mol Cell Endocrinol
Title: NCKX3 was compensated by calcium transporting genes and bone resorption in a NCKX3 KO mouse model.
Volume: 454
Pages: 93-102
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Publication
16895908 | J:117181
First Author: Schoeber JP
Year: 2006
Journal: J Biol Chem
Title: RGS2 inhibits the epithelial Ca2+ channel TRPV6.
Volume: 281
Issue: 40
Pages: 29669-74
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Publication
17006539 | J:119558
First Author: Gkika D
Year: 2006
Journal: EMBO J
Title: Tissue kallikrein stimulates Ca(2+) reabsorption via PKC-dependent plasma membrane accumulation of TRPV5.
Volume: 25
Issue: 20
Pages: 4707-16
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Publication
15339977 | J:206786
First Author: Loffing J
Year: 2004
Journal: J Am Soc Nephrol
Title: Altered renal distal tubule structure and renal Na(+) and Ca(2+) handling in a mouse model for Gitelman's syndrome.
Volume: 15
Issue: 9
Pages: 2276-88
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Publication
17696760 | J:136244
First Author: Lee GS
Year: 2007
Journal: J Bone Miner Res
Title: Phenotype of a calbindin-D9k gene knockout is compensated for by the induction of other calcium transporter genes in a mouse model.
Volume: 22
Issue: 12
Pages: 1968-78
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Publication
28039038 | J:243155
 
First Author: Kumar S
Year: 2017
Journal: Neuroscience
Title: Transient receptor potential vanilloid 6 (TRPV6) in the mouse brain: Distribution and estrous cycle-related changes in the hypothalamus.
Volume: 344
Pages: 204-216
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Protein Domain
IPR008347 | TrpV1-4
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 TRPV (vanilloid) subfamily can be divided into two distinct groups. The first, which comprises TrpV1, TrpV2, TrpV3, and TrpV4, with nonselective cation conducting pores, has members which can be activated by temperature as well as chemical stimuli. They are involved in a range of functions including nociception, thermosensing and osmolarity sensing. The second group, which consists of TrpV5 and TrpV6, (also known as epithelial calcium channels 1 and 2), highly calcium selective, are involved in renal Ca2+ absorption/reabsorption [, ].This entry represents the TRPV1-4 group of channels. Members of this family are found in chordates.
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Protein Domain
IPR008344 | TRPV5/TRPV6
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 othermotile functions, such as muscle contraction and vaso-motor control [].The TRPV (vanilloid) subfamily can be divided into two distinct groups. The first, which comprises TrpV1, TrpV2, TrpV3, and TrpV4, with nonselective cation conducting pores, has members which can be activated by temperature as well as chemical stimuli. They are involved in a range of functions including nociception, thermosensing and osmolarity sensing. The second group, which consists of TrpV5 and TrpV6, (also known as epithelial calcium channels 1 and 2), highly calcium selective, are involved in renal Ca2+ absorption/reabsorption [, ].This entry represetns the TRPV5/6 group of channels.
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Publication
38638279 | J:347665
 
First Author: Nie M
Year: 2024
Journal: Front Physiol
Title: Ghrelin enhances tubular magnesium absorption in the kidney.
Volume: 15
Pages: 1363708
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Protein
Q3TYG5
Organism: Mus musculus/domesticus
Length: 558  
Fragment?: false
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Protein
A0A0G3VLX9
Organism: Mus musculus/domesticus
Length: 531  
Fragment?: false
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Protein
D3Z1H6
Organism: Mus musculus/domesticus
Length: 764  
Fragment?: false
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Protein
Z4YLZ2
Organism: Mus musculus/domesticus
Length: 474  
Fragment?: true
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Protein
Z4YKR8
Organism: Mus musculus/domesticus
Length: 471  
Fragment?: false
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Publication
18695040 | -
First Author: Köttgen M
Year: 2008
Journal: J Cell Biol
Title: TRPP2 and TRPV4 form a polymodal sensory channel complex.
Volume: 182
Issue: 3
Pages: 437-47
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Publication
10559903 | J:53008
First Author: Kanzaki M
Year: 1999
Journal: Nat Cell Biol
Title: Translocation of a calcium-permeable cation channel induced by insulin-like growth factor-I.
Volume: 1
Issue: 3
Pages: 165-70
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Publication
12016205 | J:76890
First Author: Peier AM
Year: 2002
Journal: Science
Title: A heat-sensitive TRP channel expressed in keratinocytes.
Volume: 296
Issue: 5575
Pages: 2046-9
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Publication
10764638 | J:61534
First Author: Caterina MJ
Year: 2000
Journal: Science
Title: Impaired nociception and pain sensation in mice lacking the capsaicin receptor.
Volume: 288
Issue: 5464
Pages: 306-13
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Publication
11081638 | J:65606
First Author: Liedtke W
Year: 2000
Journal: Cell
Title: Vanilloid receptor-related osmotically activated channel (VR-OAC), a candidate vertebrate osmoreceptor.
Volume: 103
Issue: 3
Pages: 525-35
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Publication
23612980 | J:203496
First Author: Fecher-Trost C
Year: 2013
Journal: J Biol Chem
Title: The in vivo TRPV6 protein starts at a non-AUG triplet, decoded as methionine, upstream of canonical initiation at AUG.
Volume: 288
Issue: 23
Pages: 16629-44
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Publication
11248124 | -
First Author: Niemeyer BA
Year: 2001
Journal: Proc Natl Acad Sci U S A
Title: Competitive regulation of CaT-like-mediated Ca2+ entry by protein kinase C and calmodulin.
Volume: 98
Issue: 6
Pages: 3600-5
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Publication
11097838 | J:65748
First Author: Peng JB
Year: 2000
Journal: Biochem Biophys Res Commun
Title: Human calcium transport protein CaT1.
Volume: 278
Issue: 2
Pages: 326-32
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Publication
15184369 | -
First Author: Bödding M
Year: 2004
Journal: J Biol Chem
Title: Ca2+ dependence of the Ca2+-selective TRPV6 channel.
Volume: 279
Issue: 35
Pages: 36546-52
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Publication
29861107 | -
First Author: Suzuki Y
Year: 2018
Journal: Am J Hum Genet
Title: TRPV6 Variants Interfere with Maternal-Fetal Calcium Transport through the Placenta and Cause Transient Neonatal Hyperparathyroidism.
Volume: 102
Issue: 6
Pages: 1104-1114
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Publication
29258289 | -
First Author: McGoldrick LL
Year: 2018
Journal: Nature
Title: Opening of the human epithelial calcium channel TRPV6.
Volume: 553
Issue: 7687
Pages: 233-237
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Publication
11827975 | -
First Author: Watanabe H
Year: 2002
Journal: J Biol Chem
Title: Activation of TRPV4 channels (hVRL-2/mTRP12) by phorbol derivatives.
Volume: 277
Issue: 16
Pages: 13569-77
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Publication
12151520 | -
First Author: Güler AD
Year: 2002
Journal: J Neurosci
Title: Heat-evoked activation of the ion channel, TRPV4.
Volume: 22
Issue: 15
Pages: 6408-14
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Publication
17233610 | -
First Author: Harteneck C
Year: 2007
Journal: Biochem Soc Trans
Title: TRP channels activated by extracellular hypo-osmoticity in epithelia.
Volume: 35
Issue: Pt 1
Pages: 91-5
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Publication
21336783 | -
First Author: Berciano J
Year: 2011
Journal: J Neurol
Title: Reduced penetrance in hereditary motor neuropathy caused by TRPV4 Arg269Cys mutation.
Volume: 258
Issue: 8
Pages: 1413-21
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Publication
29899501 | -
First Author: Doñate-Macián P
Year: 2018
Journal: Nat Commun
Title: The TRPV4 channel links calcium influx to DDX3X activity and viral infectivity.
Volume: 9
Issue: 1
Pages: 2307
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Publication
18826956 | -
First Author: Garcia-Elias A
Year: 2008
Journal: J Biol Chem
Title: IP3 receptor binds to and sensitizes TRPV4 channel to osmotic stimuli via a calmodulin-binding site.
Volume: 283
Issue: 46
Pages: 31284-8
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Publication
31493693 | -
 
First Author: Li D
Year: 2020
Journal: J Mech Behav Biomed Mater
Title: The structural changes of the mutated ankyrin repeat domain of the human TRPV4 channel alter its ATP binding ability.
Volume: 101
Pages: 103407
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Publication
21457451 | -
First Author: Wang H
Year: 2011
Journal: FEMS Yeast Res
Title: Alkaline stress triggers an immediate calcium fluctuation in Candida albicans mediated by Rim101p and Crz1p transcription factors.
Volume: 11
Issue: 5
Pages: 430-9
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Publication
25308698 | -
 
First Author: Yu Q
Year: 2014
Journal: Free Radic Biol Med
Title: Interaction among the vacuole, the mitochondria, and the oxidative stress response is governed by the transient receptor potential channel in Candida albicans.
Volume: 77
Pages: 152-67
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Publication
24368068 | -
First Author: Yu Q
Year: 2014
Journal: Int J Med Microbiol
Title: A novel role of the vacuolar calcium channel Yvc1 in stress response, morphogenesis and pathogenicity of Candida albicans.
Volume: 304
Issue: 3-4
Pages: 339-50
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Publication
9768840 | -
First Author: Tominaga M
Year: 1998
Journal: Neuron
Title: The cloned capsaicin receptor integrates multiple pain-producing stimuli.
Volume: 21
Issue: 3
Pages: 531-43
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Publication
9349813 | -
First Author: Caterina MJ
Year: 1997
Journal: Nature
Title: The capsaicin receptor: a heat-activated ion channel in the pain pathway.
Volume: 389
Issue: 6653
Pages: 816-24
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Publication
18550765 | -
First Author: Qin N
Year: 2008
Journal: J Neurosci
Title: TRPV2 is activated by cannabidiol and mediates CGRP release in cultured rat dorsal root ganglion neurons.
Volume: 28
Issue: 24
Pages: 6231-8
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Publication
17850966 | -
First Author: Bang S
Year: 2007
Journal: Neurosci Lett
Title: Transient receptor potential V2 expressed in sensory neurons is activated by probenecid.
Volume: 425
Issue: 2
Pages: 120-5
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Publication
10201375 | J:54131
First Author: Caterina MJ
Year: 1999
Journal: Nature
Title: A capsaicin-receptor homologue with a high threshold for noxious heat.
Volume: 398
Issue: 6726
Pages: 436-41
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Publication
31566564 | -
   
First Author: Pumroy RA
Year: 2019
Journal: Elife
Title: Molecular mechanism of TRPV2 channel modulation by cannabidiol.
Volume: 8
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Publication
27021073 | -
 
First Author: Huynh KW
Year: 2016
Journal: Nat Commun
Title: Structure of the full-length TRPV2 channel by cryo-EM.
Volume: 7
Pages: 11130
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Publication
16617338 | J:108855
First Author: Xu H
Year: 2006
Journal: Nat Neurosci
Title: Oregano, thyme and clove-derived flavors and skin sensitizers activate specific TRP channels.
Volume: 9
Issue: 5
Pages: 628-35
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Publication
17420775 | -
First Author: Vogt-Eisele AK
Year: 2007
Journal: Br J Pharmacol
Title: Monoterpenoid agonists of TRPV3.
Volume: 151
Issue: 4
Pages: 530-40
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Publication
21593771 | -
First Author: Borbíró I
Year: 2011
Journal: J Invest Dermatol
Title: Activation of transient receptor potential vanilloid-3 inhibits human hair growth.
Volume: 131
Issue: 8
Pages: 1605-14
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Protein Domain
IPR024863 | TRPV1
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 ofvoltage-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 TRPV (vanilloid) subfamily can be divided into two distinct groups. The first, which comprises TrpV1, TrpV2, TrpV3, and TrpV4, with nonselective cation conducting pores, has members which can be activated by temperature as well as chemical stimuli. They are involved in a range of functions including nociception, thermosensing and osmolarity sensing. The second group, which consists of TrpV5 and TrpV6, (also known as epithelial calcium channels 1 and 2), highly calcium selective, are involved in renal Ca2+ absorption/reabsorption [, ].TRPV1 was the first vanilloid receptor identified. It is a nonselective cation channel with a preference for calcium and is activated by noxious stimuli, heat, protons, pH 5.9, and various, mostly obnoxious, natural products []. TRPV1 is predominantly expressed in sensory neurons []and is believed to play a crucial role in temperature sensing and nociception [], qualifying therefore as a molecular target for pain treatment.
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Protein Domain
IPR024862 | TRPV
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 TRPV (vanilloid) subfamily can be divided into two distinct groups. The first, which comprises TrpV1, TrpV2, TrpV3, and TrpV4, with nonselective cation conducting pores, has members which can be activated by temperature as well as chemical stimuli. They are involved in a range of functions including nociception, thermosensing and osmolarity sensing. The second group, which consists of TrpV5 and TrpV6, (also known as epithelial calcium channels 1 and 2), highly calcium selective, are involved in renal Ca2+ absorption/reabsorption [, ].Some calcium channel proteins from fungi also belong to this protein family, including Calcium channel YVC1 from Candida albicans. Yvc1 is a vacuolar calcium channel involved in the release of calcium ions from the vacuole in response to hyperosmotic or alkaline stress. It is required for maintaining the stability of both the mitochondria and the vacuole in a potassium- and calcium-dependent manner. This protein plays a key role in hyphal polarized growth and re-orientation to host-signals through its contribution to the localization of the Spitzenkoerper to the hyphal tips [, , ].
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Protein Domain
IPR024865 | TrpV2
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 TRPV (vanilloid) subfamily can be divided into two distinct groups. The first, which comprises TrpV1, TrpV2, TrpV3, and TrpV4, with nonselective cation conducting pores, has members which can be activated by temperature as well as chemical stimuli. They are involved in a range of functions including nociception, thermosensing and osmolarity sensing. The second group, which consists of TrpV5 and TrpV6, (also known as epithelial calcium channels 1 and 2), highly calcium selective, are involved in renal Ca2+ absorption/reabsorption [, ].Under basal conditions, TrpV2 is located mainly in intracellular pools. Stimulation of cells by insulin-like growth factor-I induces translocation of TrpV2 to the plasma membrane, where it can alter calcium influx into the cell []. This channel can be activated by temperatures above 52 oC, or alternatively, by chemicals including the plant cannabinoid cannabidiol and probenecid [, , ]. However, it is not activated by vanilloids and acidic pH []. The structure of this protein has been solve by cryo-electron microscopy [].
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Protein Domain
IPR024866 | TrpV3
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 TRPV (vanilloid) subfamily can be divided into two distinct groups. The first, which comprises TrpV1, TrpV2, TrpV3, and TrpV4, with nonselective cation conductingpores, has members which can be activated by temperature as well as chemical stimuli. They are involved in a range of functions including nociception, thermosensing and osmolarity sensing. The second group, which consists of TrpV5 and TrpV6, (also known as epithelial calcium channels 1 and 2), highly calcium selective, are involved in renal Ca2+ absorption/reabsorption [, ].TrpV3 is a thermosensitive ion channel expressed predominantly in the skin and neural tissues. It is activated at innocuous (warm) temperatures and shows an increased response at noxious temperatures. This provides a mechanism for skin cells to detect detect heat via molecules similar to those in heat-sensing neurons []. TrpV3 can also be activated by various natural compounds that cause either feelings of warmth and/or act as skin sensitisers eg carvacrol, thymol and eugenol [, ]. It suppresses keratinocyte proliferation in hair follicles and induces apoptosis and premature hair follicle regression, negatively regulating hair growth and cycling [].
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Protein Domain
IPR008345 | TrpV6
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 TRPV (vanilloid) subfamily can be divided into two distinct groups. The first, which comprises TrpV1, TrpV2, TrpV3, and TrpV4, with nonselective cation conducting pores, has memberswhich can be activated by temperature as well as chemical stimuli. They are involved in a range of functions including nociception, thermosensing and osmolarity sensing. The second group, which consists of TrpV5 and TrpV6, (also known as epithelial calcium channels 1 and 2), highly calcium selective, are involved in renal Ca2+ absorption/reabsorption [, ].TrpV6 was originally cloned from rabbit kidney cells, but has also been found in human. It is a calcium selective cation channel that mediates Ca2+ uptake in various tissues, including the intestine and epithelial tissues. [, , , , ]. TrpV6 has been related to a variety of diseases [, ]. Cryo-electron microscopy images of the open and closed states of this channel showed it adopts similar conformations in both states [].
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Protein Domain
IPR008348 | TrpV4
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 TRPV (vanilloid) subfamily can be divided into two distinct groups. The first, which comprises TrpV1, TrpV2, TrpV3, and TrpV4, with nonselective cation conducting pores, has members which can be activated by temperature as well as chemical stimuli. They are involved in a range of functions including nociception, thermosensing and osmolarity sensing. The second group, which consists of TrpV5 and TrpV6, (also known as epithelial calcium channels 1 and 2), highly calcium selective, are involved in renal Ca2+ absorption/reabsorption [, ].TrpV4 is a non-selective calcium permeant cation channel involved in osmotic sensitivity and mechanosensitivity. It is expressed at high levels in the kidney, liver, heart and central nervous system, and activated by extracellular hypo-osmoticity, leading to increased transcellular ion flux and paracellular permeability, which may allow the cells to adjust to changes in extracellular osmolarity [, , ]. TRPV4 is can also be activated chemically by metabolites of arachidonic acid and alpha-isomers of phorbol esters [], by heat []and other factors []. This protein has been related to infectious diseases []and other pathologies [, ].
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Protein
V9SH16
Organism: Mus musculus/domesticus
Length: 104  
Fragment?: true
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Protein
Q9WTR1
Organism: Mus musculus/domesticus
Length: 756  
Fragment?: false
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Protein
Q8K424
Organism: Mus musculus/domesticus
Length: 791  
Fragment?: false
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Protein
Q704Y3
Organism: Mus musculus/domesticus
Length: 839  
Fragment?: false
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Protein
Q9EPK8
Organism: Mus musculus/domesticus
Length: 871  
Fragment?: false
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Protein
Q91WD2
Organism: Mus musculus/domesticus
Length: 767  
Fragment?: false
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Protein
Q32MT9
Organism: Mus musculus/domesticus
Length: 790  
Fragment?: false
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Protein
Q9JJJ0
Organism: Mus musculus/domesticus
Length: 729  
Fragment?: false
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Protein
Z4YJD4
Organism: Mus musculus/domesticus
Length: 779  
Fragment?: false
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Protein
Q3V318
Organism: Mus musculus/domesticus
Length: 839  
Fragment?: false
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Protein
D3Z1H7
Organism: Mus musculus/domesticus
Length: 811  
Fragment?: false
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Protein
E2RUG8
Organism: Mus musculus/domesticus
Length: 791  
Fragment?: false
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Protein
E9Q7L7
Organism: Mus musculus/domesticus
Length: 824  
Fragment?: false
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Protein
A0A0J9YMK6
Organism: Mus musculus/domesticus
Length: 767  
Fragment?: false
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Protein
A2JY27
Organism: Mus musculus/domesticus
Length: 727  
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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