TRPP3
TRPP3, or Transient Receptor Potential Protein 3, is a member of the TRP (transient receptor potential) channel family, which consists of various ion channels that are permeable to cations such as sodium, calcium, and magnesium. TRPP3 is also known as PKD2L1 (Polycystin-2-Like 1) and is primarily expressed in certain tissues, including the inner ear and the kidneys.
TRPV
TRPV stands for "Transient Receptor Potential Vanilloid" channels, which are a group of ion channels located primarily in the cell membranes of sensory neurons. These channels play a crucial role in mediating sensations such as pain and temperature, as well as other physiological processes. The TRPV family includes several members, the most well-known of which is TRPV1.
TRPV1
TRPV1, or Transient Receptor Potential Vanilloid 1, is a protein that functions as a receptor and is part of the TRP (Transient Receptor Potential) channel family. It is primarily expressed in sensory neurons and plays a crucial role in the detection and regulation of various painful stimuli, including heat, noxious chemicals, and inflammation.
TRPV2
Transient receptor potential vanilloid 2 (TRPV2) is a member of the transient receptor potential (TRP) channel family, which consists of ion channels that play a crucial role in various physiological processes. TRPV2 is known to be a non-selective cation channel that is activated by temperature changes (specifically, it is activated by high temperatures), certain chemicals, and mechanical stimuli.
TRPV3
TRPV3, or Transient Receptor Potential Vanilloid 3, is a member of the TRP (transient receptor potential) channel family. These channels are ion channels located in the cell membrane and are known to be involved in various sensory functions, particularly in pain perception, temperature sensation, and the detection of environmental stimuli. TRPV3 is primarily expressed in the skin, hair follicles, and some parts of the nervous system.
TRPV4
TRPV4 (Transient Receptor Potential Vanilloid 4) is a type of protein that functions as a receptor involved in various physiological processes. It is a member of the transient receptor potential (TRP) family of ion channels, which are known for their roles in detecting environmental changes and regulating cellular responses. TRPV4 is particularly responsive to mechanical stress, temperature changes, and osmotic pressure.
TRPV5
TRPV5 (Transient Receptor Potential Vanilloid 5) is a member of the TRP (Transient Receptor Potential) channel family, which consists of ion channels that are involved in various physiological processes. TRPV5 is specifically known for its role as a calcium ion (Ca²⁺) channel. It is primarily expressed in the kidneys, where it plays a critical role in calcium reabsorption in the renal tubules.
TRPV6
TRPV6 (Transient Receptor Potential Vanilloid 6) is a protein that functions as an ion channel, primarily permeable to calcium ions (Ca²⁺). It is part of the TRP (Transient Receptor Potential) channel family, which is involved in various sensory processes and physiological functions.
Transient receptor potential (TRP) channels are a family of ion channels located in the cell membrane that play a crucial role in various sensory and physiological processes. They are named for their role in mediating transient (temporary) receptor potential changes in response to various stimuli. These channels are involved in sensory perception, including pain, temperature, taste, and vision.
The Transient Receptor Potential Channel-Interacting Protein Database (TRIPDB) is a specialized database that focuses on providing information related to transient receptor potential (TRP) channels and their interacting proteins. TRP channels are a group of ion channels located in various cellular membranes and are involved in a wide range of physiological processes including sensation, temperature regulation, and pain perception.
Two-pore-domain potassium channels (K2P channels) are a family of ion channels that facilitate the movement of potassium ions (K+) across cell membranes. These channels are characterized by their unique structure, which features two pore domains within a single polypeptide chain. This dual-pore configuration differentiates them from other types of potassium channels, which typically have a single pore domain.
Two-pore channels (TPCs) are a family of ion channels that are characterized by their unique structure and function. They are integral membrane proteins that form pores in the cell membrane, allowing for the selective passage of ions. TPCs are particularly notable for their ability to facilitate the movement of sodium, potassium, and other cations across the plasma membrane and intracellular membranes.
VDAC1
VDAC1, or Voltage-Dependent Anion Channel 1, is a protein that is primarily located in the outer mitochondrial membrane. It plays a crucial role in the regulation of mitochondrial metabolism and cellular homeostasis. VDAC1 is involved in the transport of ions and small metabolites across the mitochondrial membrane, facilitating the exchange of molecules such as ATP, ADP, and various metabolites between the mitochondria and the cytosol.
VDAC2
VDAC2, or Voltage-Dependent Anion Channel 2, is a protein that is part of the VDAC family, which also includes VDAC1 and VDAC3. These proteins are located in the outer mitochondrial membrane and play a critical role in mitochondrial function. VDAC2 is primarily involved in regulating the transport of ions and small molecules across the mitochondrial membrane, which is essential for maintaining cellular energy metabolism.
VDAC3
VDAC3, or Voltage-Dependent Anion Channel 3, is a protein that is part of the VDAC family, which consists of several isoforms (VDAC1, VDAC2, and VDAC3). These proteins are primarily located in the outer mitochondrial membrane and play a crucial role in regulating the transport of metabolites and ions across the mitochondrial membrane.
Voltage-dependent anion channels (VDACs) are a class of proteins that form pores in the outer mitochondrial membrane. They play a crucial role in the regulation of ionic and metabolic fluxes between the mitochondria and the cytoplasm. VDACs are primarily permeable to anions, which include negatively charged ions such as phosphate, ATP, and other metabolites, allowing them to facilitate processes such as cellular respiration and energy production.
Voltage-gated ion channels are specialized membrane proteins that open or close in response to changes in the membrane potential (voltage) of a cell. They play a crucial role in the generation and propagation of electrical signals in excitable tissues, like neurons, muscle cells, and some endocrine cells. ### Key Features: 1. **Voltage Sensitivity**: These channels have sensors that detect changes in the electrical potential across the cell membrane.
The Voltage-gated Potassium Channel Database (Kv database or Kv channel database) is a specialized online resource that provides information about voltage-gated potassium channels (Kv channels), which are crucial for various physiological processes in many organisms. These channels play a significant role in the generation and propagation of electrical signals in nerve and muscle cells by allowing potassium ions to flow across the cell membrane in response to changes in membrane potential.
Voltage-gated proton channels are specialized ion channels that allow the selective movement of protons (H⁺ ions) across the cell membrane in response to changes in membrane potential. Unlike more commonly known ion channels (such as sodium or potassium channels), voltage-gated proton channels have a unique and specific function related to human physiology and intracellular processes. ### Key Features: 1. **Function**: These channels are involved in regulating pH and electrical excitability in cells.
Volume-regulated anion channels (VRACs) are a type of ion channel found in the cell membrane that play a crucial role in cellular volume regulation. They are activated in response to cell swelling, which can occur in various physiological and pathological conditions. When cells swell, they need to release ions and other small solutes to restore their original volume.