| Type |
Details |
Score |
| Publication |
| 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 |
|
•
•
•
•
•
|
| Protein Domain |
| 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. |
|
•
•
•
•
•
|
| Protein Domain |
| 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. |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
558
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
531
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
764
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
474
|
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
471
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Publication |
| 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 |
|
•
•
•
•
•
|
| Publication |
| 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 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Peier AM |
| Year: |
2002 |
| Journal: |
Science |
| Title: |
A heat-sensitive TRP channel expressed in keratinocytes. |
| Volume: |
296 |
| Issue: |
5575 |
| Pages: |
2046-9 |
|
•
•
•
•
•
|
| Publication |
| 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 |
|
•
•
•
•
•
|
| Publication |
| 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 |
|
•
•
•
•
•
|
| Publication |
| 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 |
|
•
•
•
•
•
|
| Publication |
| 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 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Peng JB |
| Year: |
2000 |
| Journal: |
Biochem Biophys Res Commun |
| Title: |
Human calcium transport protein CaT1. |
| Volume: |
278 |
| Issue: |
2 |
| Pages: |
326-32 |
|
•
•
•
•
•
|
| Publication |
| 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 |
|
•
•
•
•
•
|
| Publication |
| 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 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
McGoldrick LL |
| Year: |
2018 |
| Journal: |
Nature |
| Title: |
Opening of the human epithelial calcium channel TRPV6. |
| Volume: |
553 |
| Issue: |
7687 |
| Pages: |
233-237 |
|
•
•
•
•
•
|
| Publication |
| 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 |
|
•
•
•
•
•
|
| Publication |
| 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 |
|
•
•
•
•
•
|
| Publication |
| 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 |
|
•
•
•
•
•
|
| Publication |
| 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 |
|
•
•
•
•
•
|
| Publication |
| 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 |
|
•
•
•
•
•
|
| Publication |
| 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 |
|
•
•
•
•
•
|
| Publication |
| 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 |
|
•
•
•
•
•
|
| Publication |
| 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 |
|
•
•
•
•
•
|
| Publication |
| 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 |
|
•
•
•
•
•
|
| Publication |
| 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 |
|
•
•
•
•
•
|
| Publication |
| 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 |
|
•
•
•
•
•
|
| Publication |
| 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 |
|
•
•
•
•
•
|
| Publication |
| 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 |
|
•
•
•
•
•
|
| Publication |
| 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 |
|
•
•
•
•
•
|
| Publication |
| 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 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Pumroy RA |
| Year: |
2019 |
| Journal: |
Elife |
| Title: |
Molecular mechanism of TRPV2 channel modulation by cannabidiol. |
| Volume: |
8 |
|
|
|
•
•
•
•
•
|
| Publication |
| First Author: |
Huynh KW |
| Year: |
2016 |
| Journal: |
Nat Commun |
| Title: |
Structure of the full-length TRPV2 channel by cryo-EM. |
| Volume: |
7 |
|
| Pages: |
11130 |
|
•
•
•
•
•
|
| Publication |
| 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 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Vogt-Eisele AK |
| Year: |
2007 |
| Journal: |
Br J Pharmacol |
| Title: |
Monoterpenoid agonists of TRPV3. |
| Volume: |
151 |
| Issue: |
4 |
| Pages: |
530-40 |
|
•
•
•
•
•
|
| Publication |
| 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 |
|
•
•
•
•
•
|
| Protein Domain |
| 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. |
|
•
•
•
•
•
|
| Protein Domain |
| 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 [, , ]. |
|
•
•
•
•
•
|
| Protein Domain |
| 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 []. |
|
•
•
•
•
•
|
| Protein Domain |
| 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 []. |
|
•
•
•
•
•
|
| Protein Domain |
| 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 |
| 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 |
| Organism: |
Mus musculus/domesticus |
| Length: |
104
|
| Fragment?: |
true |
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•
•
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| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
756
|
| Fragment?: |
false |
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•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
791
|
| Fragment?: |
false |
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•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
839
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
871
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
767
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
790
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
729
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
779
|
| Fragment?: |
false |
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•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
839
|
| Fragment?: |
false |
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•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
811
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
791
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
824
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
767
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
727
|
| Fragment?: |
false |
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•
•
•
•
•
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