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Search results 1001 to 1100 out of 1104 for Cav1

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Type Details Score
Publication
9257934 | -
First Author: Randall AD
Year: 1997
Journal: Neuropharmacology
Title: Contrasting biophysical and pharmacological properties of T-type and R-type calcium channels.
Volume: 36
Issue: 7
Pages: 879-93
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Publication
11067968 | -
First Author: Foehring RC
Year: 2000
Journal: J Neurophysiol
Title: Unique properties of R-type calcium currents in neocortical and neostriatal neurons.
Volume: 84
Issue: 5
Pages: 2225-36
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Publication
11698583 | -
First Author: Gasparini S
Year: 2001
Journal: J Neurosci
Title: Presynaptic R-type calcium channels contribute to fast excitatory synaptic transmission in the rat hippocampus.
Volume: 21
Issue: 22
Pages: 8715-21
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Publication
3037387 | -
First Author: Tanabe T
Year: 1987
Journal: Nature
Title: Primary structure of the receptor for calcium channel blockers from skeletal muscle.
Volume: 328
Issue: 6128
Pages: 313-8
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Publication
9013606 | -
First Author: Soldatov NM
Year: 1997
Journal: J Biol Chem
Title: Molecular structures involved in L-type calcium channel inactivation. Role of the carboxyl-terminal region encoded by exons 40-42 in alpha1C subunit in the kinetics and Ca2+ dependence of inactivation.
Volume: 272
Issue: 6
Pages: 3560-6
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Publication
9065969 | -
First Author: Wei X
Year: 1996
Journal: Receptors Channels
Title: Increase in Ca2+ channel expression by deletions at the amino terminus of the cardiac alpha 1C subunit.
Volume: 4
Issue: 4
Pages: 205-15
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Publication
9405178 | -
First Author: Takimoto K
Year: 1997
Journal: J Mol Cell Cardiol
Title: Distribution, splicing and glucocorticoid-induced expression of cardiac alpha 1C and alpha 1D voltage-gated Ca2+ channel mRNAs.
Volume: 29
Issue: 11
Pages: 3035-42
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Publication
11285265 | -
First Author: Koschak A
Year: 2001
Journal: J Biol Chem
Title: alpha 1D (Cav1.3) subunits can form l-type Ca2+ channels activating at negative voltages.
Volume: 276
Issue: 25
Pages: 22100-6
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Publication
10639174 | -
First Author: Moser T
Year: 2000
Journal: Proc Natl Acad Sci U S A
Title: Kinetics of exocytosis and endocytosis at the cochlear inner hair cell afferent synapse of the mouse.
Volume: 97
Issue: 2
Pages: 883-8
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Publication
8930286 | -
First Author: Magee JC
Year: 1996
Journal: J Neurophysiol
Title: Dihydropyridine-sensitive, voltage-gated Ca2+ channels contribute to the resting intracellular Ca2+ concentration of hippocampal CA1 pyramidal neurons.
Volume: 76
Issue: 5
Pages: 3460-70
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Publication
28472301 | -
First Author: Pinggera A
Year: 2017
Journal: Hum Mol Genet
Title: New gain-of-function mutation shows CACNA1D as recurrently mutated gene in autism spectrum disorders and epilepsy.
Volume: 26
Issue: 15
Pages: 2923-2932
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Protein Domain
IPR005446 | VDCC_L_a1su
Type: Family
Description: Ca2+ ions are unique in that they not only carry charge but they are also the most widely used of diffusible second messengers. Voltage-dependent Ca2+ channels (VDCC) are a family of molecules that allow cells to couple electrical activity to intracellular Ca2+ signalling. The opening and closing of these channels by depolarizing stimuli, such as action potentials, allows Ca2+ ions to enter neurons down a steep electrochemical gradient, producing transient intracellular Ca2+ signals. Many of the processes that occur in neurons, including transmitter release, gene transcription and metabolism are controlled by Ca2+ influx occurring simultaneously at different cellular locales. The pore is formed by the alpha-1 subunit which incorporates the conduction pore, the voltage sensor and gating apparatus, and the known sites of channel regulation by second messengers, drugs, and toxins []. The activity of this pore is modulated by four tightly-coupled subunits: an intracellular beta subunit; a transmembrane gamma subunit; and a disulphide-linked complex of alpha-2 and delta subunits, which are proteolytically cleaved from the same gene product. Properties of the protein including gating voltage-dependence, G protein modulation and kinase susceptibility can be influenced by these subunits.Voltage-gated calcium channels are classified as T, L, N, P, Q and R, and are distinguished by their sensitivity to pharmacological blocks, single-channel conductance kinetics, and voltage-dependence. On the basis of their voltage activation properties, the voltage-gated calcium classes can be further divided into two broad groups: the low (T-type) and high (L, N, P, Q and R-type) threshold-activated channels.The alpha-1 subunit forms the pore for the import of extracellular calcium ions and, though regulated by the other subunits, is primarily responsible for the pharmacological properties of the channel []. It shares sequence characteristics with all voltage-dependent cation channels, and exploits the same 6-helix bundle structural motif - in both sodium and calcium channels, this motif is repeated 4 times within the sequence to give a 24-helix bundle. Within each of these repeats, 5 of the transmembrane (TM) segments (S1, S2, S3, S5, S6) are hydrophobic, while the other (S4) is positively charged and serves as the voltage-sensor. Several genes encoding alpha-1 subunits have been identified and can be divided into three functionally distinct families based on sequence homology - Cav1, Cav2 and Cav3 []. The Cav1 family forms channels mediating L-type calcium currents, the Cav2 family mediates P/Q-, N-, and R-type calcium currents, while the Cav3 family mediates T-type calcium currents.L-type calcium channels are formed from alpha-1S, alpha-1C, alpha-1D, and alpha-1F subunits. They are widely distributed and are well characterised in the heart, smooth and skeletal muscle, and some neurons. Their primary functions are in both excitation-contraction and excitation-secretion coupling. In skeletal muscle, the L-type calcium channels act as a voltage sensor for excitation-contraction coupling, and in cardiac muscle, they provide a pathway for calcium influx. Mutations affecting L-type channel subunits result in three diseases: (1) muscular dystrophy, which is characterised by a lack of functional skeletal muscle; (2) hypokalaemic periodic paralysis, which is characterised by episodic attacks of skeletal muscle weakness; and (3) malignant hyperthermia, which is the main cause of death due to anaesthesia. 1,4-dihydropyridines act as antagonists of these channels [, ].
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Protein Domain
IPR005447 | VDCC_N_a1su
Type: Family
Description: Ca2+ ions are unique in that they not only carry charge but they are also the most widely used of diffusible second messengers. Voltage-dependent Ca2+ channels (VDCC) are a family of molecules that allow cells to couple electrical activity to intracellular Ca2+ signalling. The opening and closing of these channels by depolarizing stimuli, such as action potentials, allows Ca2+ ions to enter neurons down a steep electrochemical gradient, producing transient intracellular Ca2+ signals. Many of the processes that occur in neurons, including transmitter release, gene transcription and metabolism are controlled by Ca2+ influx occurring simultaneously at different cellular locales. The pore is formed by the alpha-1 subunit which incorporates the conduction pore, the voltage sensor and gating apparatus, and the known sites of channel regulation by second messengers, drugs, and toxins []. The activity of this pore is modulated by four tightly-coupled subunits: an intracellular beta subunit; a transmembrane gamma subunit; and a disulphide-linked complex of alpha-2 and delta subunits, which are proteolytically cleaved from the same gene product. Properties of the protein including gating voltage-dependence, G protein modulation and kinase susceptibility can be influenced by these subunits.Voltage-gated calcium channels are classified as T, L, N, P, Q and R, and are distinguished by their sensitivity to pharmacological blocks, single-channel conductance kinetics, and voltage-dependence. On the basis of their voltage activation properties, the voltage-gated calcium classes can be further divided into two broad groups: the low (T-type) and high (L, N, P, Q and R-type) threshold-activated channels.The alpha-1 subunit forms the pore for the import of extracellular calcium ions and, though regulated by the other subunits, is primarily responsible for the pharmacological properties of the channel []. It shares sequence characteristics with all voltage-dependent cation channels, and exploits the same 6-helix bundle structural motif - in both sodium and calcium channels, this motif is repeated 4 times within the sequence to give a 24-helix bundle. Within each of these repeats, 5 of the transmembrane (TM) segments (S1, S2, S3, S5, S6) are hydrophobic, while the other (S4) is positively charged and serves as the voltage-sensor. Several genes encoding alpha-1 subunits have been identified and can be divided into three functionally distinct families based on sequence homology - Cav1, Cav2 and Cav3 []. The Cav1 family forms channels mediating L-type calcium currents, the Cav2 family mediates P/Q-, N-, and R-type calcium currents, while the Cav3 family mediates T-type calcium currents.N-type calcium channels are composed from alpha-1B subunits. Experiments employing CTX have demonstrated the physiological importance of the N-type calcium channels in the nervous system, where they have a significant developmental role in the migration of immature neurons before the establishment of their synaptic circuit. In peripheral neurons, such as autonomic neurons, motor neurons and spinal cord neurons, they have also been shown to be critically involved in the release of neurotransmitters, including glutamate [], gamma-amino-butyric acid, acetylcholine, dopamine []and norepinephrine []. N-type calcium channels are promising targets for the development of drugs to relieve chronic and neuropathic pain []. Recently, it has been shown to be specifically blocked by ziconotide [].
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Protein Domain
IPR005448 | CACNA1A
Type: Family
Description: Ca2+ ions are unique in that they not only carry charge but they are also the most widely used of diffusible second messengers. Voltage-dependent Ca2+ channels (VDCC) are a family of molecules that allow cells to couple electrical activity to intracellular Ca2+ signalling. The opening and closing of these channels by depolarizing stimuli, such as action potentials, allows Ca2+ ions to enter neurons down a steep electrochemical gradient, producing transient intracellular Ca2+ signals. Many of the processes that occur in neurons, including transmitter release, gene transcription and metabolism are controlled by Ca2+ influx occurring simultaneously at different cellular locales. The pore is formed by the alpha-1 subunit which incorporates the conduction pore, the voltage sensor and gating apparatus, and the known sites of channel regulation by second messengers, drugs, and toxins []. The activity of this pore is modulated by four tightly-coupled subunits: an intracellular beta subunit; a transmembrane gamma subunit; and a disulphide-linked complex of alpha-2 and delta subunits, which are proteolytically cleaved from the same gene product. Properties of the protein including gating voltage-dependence, G protein modulation and kinase susceptibility can be influenced by these subunits.Voltage-gated calcium channels are classified as T, L, N, P, Q and R, and are distinguished by their sensitivity to pharmacological blocks, single-channel conductance kinetics, and voltage-dependence. On the basis of their voltage activation properties, the voltage-gated calcium classes can be further divided into two broad groups: the low (T-type) and high (L, N, P, Q and R-type) threshold-activated channels.The alpha-1 subunit forms the pore for the import of extracellular calcium ions and, though regulated by the other subunits, is primarily responsible for the pharmacological properties of the channel []. It shares sequence characteristics with all voltage-dependent cation channels, and exploits the same 6-helix bundle structural motif - in both sodium and calcium channels, this motif is repeated 4 times within the sequence to give a 24-helix bundle. Within each of these repeats, 5 of the transmembrane (TM) segments (S1, S2, S3, S5, S6) are hydrophobic, while the other (S4) is positively charged and serves as the voltage-sensor. Several genes encoding alpha-1 subunits have been identified and can be divided into three functionally distinct families based on sequence homology - Cav1, Cav2 and Cav3 []. The Cav1 family forms channels mediating L-type calcium currents, the Cav2 family mediates P/Q-, N-, and R-type calcium currents, while the Cav3 family mediates T-type calcium currents.Several genes encoding alpha-1 subunits have been identified, each forming a distinct electrophysiological channel. P- and Q-type channels are formed from alpha-1A subunits and function in transmitter release []. P-type channels are prevalent in cerebellar Purkinje cells, but are also expressed in many central and peripheral neurons, such as the spinal cord and visual cortex. By contrast, Q-type channels are found in cerebellar granule neurones and the hippocampus. Different mutations in the alpha-1A subunit can produce the following human diseases: episodic ataxia type-2familial hemiplegic migrainespinocerebellar ataxia type-6All 3 diseases result in cerebellar atrophy, but they differ in the extent and rate of progression of neuronal degeneration.
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Protein Domain
IPR005449 | VDCC_R_a1su
Type: Family
Description: Ca2+ ions are unique in that they not only carry charge but they are also the most widely used of diffusible second messengers. Voltage-dependent Ca2+ channels (VDCC) are a family of molecules that allow cells to couple electrical activity to intracellular Ca2+ signalling. The opening and closing of these channels by depolarizing stimuli, such as action potentials, allows Ca2+ ions to enter neurons down a steep electrochemical gradient, producing transient intracellular Ca2+ signals. Many of the processes that occur in neurons, including transmitter release, gene transcription and metabolism are controlled by Ca2+ influx occurring simultaneously at different cellular locales. The pore is formed by the alpha-1 subunit which incorporates the conduction pore, the voltage sensor and gating apparatus, and the known sites of channel regulation by second messengers, drugs, and toxins []. The activity of this pore is modulated by four tightly-coupled subunits: an intracellular beta subunit; a transmembrane gamma subunit; and a disulphide-linked complex of alpha-2 and delta subunits, which are proteolytically cleaved from the same gene product. Properties of the protein including gating voltage-dependence, G protein modulation and kinase susceptibility can be influenced by these subunits.Voltage-gated calcium channels are classified as T, L, N, P, Q and R, and are distinguished by their sensitivity to pharmacological blocks, single-channel conductance kinetics, and voltage-dependence. On the basis of their voltage activation properties, the voltage-gated calcium classes can be further divided into two broad groups: the low (T-type) and high (L, N, P, Q and R-type) threshold-activated channels.The alpha-1 subunit forms the pore for the import of extracellular calcium ions and, though regulated by the other subunits, is primarily responsible for the pharmacological properties of the channel []. It shares sequence characteristics with all voltage-dependent cation channels, and exploits the same 6-helix bundle structural motif - in both sodium and calcium channels, this motif is repeated 4 times within the sequence to give a 24-helix bundle. Within each of these repeats, 5 of the transmembrane (TM) segments (S1, S2, S3, S5, S6) are hydrophobic, while the other (S4) is positively charged and serves as the voltage-sensor. Several genes encoding alpha-1 subunits have been identified and can be divided into three functionally distinct families based on sequence homology - Cav1, Cav2 and Cav3 []. The Cav1 family forms channels mediating L-type calcium currents, the Cav2 family mediates P/Q-, N-, and R-type calcium currents, while the Cav3 family mediates T-type calcium currents.R-type calcium channels are composed of alpha-1E subunits and are found in a variety of neuronal populations, such as cerebellar granule neurons and dendrites of hippocampal pyrimidal neurons []. They are believed to play an important role in the body's natural communication network, where they contribute to the regulation of brain function by synaptic integration []. Their hypolarised inactivation range and rapid kinetics of inactivation make R-type channels more suited to providing a transient surge of Ca2+ influx [].
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Protein Domain
IPR005445 | VDCC_T_a1
Type: Family
Description: Ca2+ ions are unique in that they not only carry charge but they are also the most widely used of diffusible second messengers. Voltage-dependent Ca2+ channels (VDCC) are a family of molecules that allow cells to couple electrical activity to intracellular Ca2+ signalling. The opening and closing of these channels by depolarizing stimuli, such as action potentials, allows Ca2+ ions to enter neurons down a steep electrochemical gradient, producing transient intracellular Ca2+ signals. Many of the processes that occur in neurons, including transmitter release, gene transcription and metabolism are controlled by Ca2+ influx occurring simultaneously at different cellular locales. The pore is formed by the alpha-1 subunit which incorporates the conduction pore, the voltage sensor and gating apparatus, and the known sites of channel regulation by second messengers, drugs, and toxins []. The activity of this pore is modulated by four tightly-coupled subunits: an intracellular beta subunit; a transmembrane gamma subunit; and a disulphide-linked complex of alpha-2 and delta subunits, which are proteolytically cleaved from the same gene product. Properties of the protein including gating voltage-dependence, G protein modulation and kinase susceptibility can be influenced by these subunits.Voltage-gated calcium channels are classified as T, L, N, P, Q and R, and are distinguished by their sensitivity to pharmacological blocks, single-channel conductance kinetics, and voltage-dependence. On the basis of their voltage activation properties, the voltage-gated calcium classes can be further divided into two broad groups: the low (T-type) and high (L, N, P, Q and R-type) threshold-activated channels.The alpha-1 subunit forms the pore for the import of extracellular calcium ions and, though regulated by the other subunits, is primarily responsible for the pharmacological properties of the channel []. It shares sequence characteristics with all voltage-dependent cation channels, and exploits the same 6-helix bundle structural motif - in both sodium and calcium channels, this motif is repeated 4 times within the sequence to give a 24-helix bundle. Within each of these repeats, 5 of the transmembrane (TM) segments (S1, S2, S3, S5, S6) are hydrophobic, while the other (S4) is positively charged and serves as the voltage-sensor. Several genes encoding alpha-1 subunits have been identified and can be divided into three functionally distinct families based on sequence homology - Cav1, Cav2 and Cav3 []. The Cav1 family forms channels mediating L-type calcium currents, the Cav2 family mediates P/Q-, N-, and R-type calcium currents, while the Cav3 family mediates T-type calcium currents.T-type calcium channels exhibit unique voltage-dependent kinetics, small single channel conductance, rapid inactivation, slow deactivation and a relatively high permeability to calcium []. They are primarily responsible for rebound burst firing in central neurons and are implicated in normal brain functions, such as slow wave sleep, and in diseased states, such as epilepsy []. They also play an important role in hormone secretion []and smooth muscle excitability [].
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Protein Domain
IPR005451 | VDCC_L_a1csu
Type: Family
Description: Ca2+ ions are unique in that they not only carry charge but they are also the most widely used of diffusible second messengers. Voltage-dependent Ca2+ channels (VDCC) are a family of molecules that allow cells to couple electrical activity to intracellular Ca2+ signalling. The opening and closing of these channels by depolarizing stimuli, such as action potentials, allows Ca2+ ions to enter neurons down a steep electrochemical gradient, producing transient intracellular Ca2+ signals. Many of the processes that occur in neurons, including transmitter release, gene transcription and metabolism are controlled by Ca2+ influx occurring simultaneously at different cellular locales. The pore is formed by the alpha-1 subunit which incorporates the conduction pore, the voltage sensor and gating apparatus, and the known sites of channel regulation by second messengers, drugs, and toxins []. The activity of this pore is modulated by four tightly-coupled subunits: an intracellular beta subunit; a transmembrane gamma subunit; and a disulphide-linked complex of alpha-2 and delta subunits, which are proteolytically cleaved from the same gene product. Properties of the protein including gating voltage-dependence, G protein modulation and kinase susceptibility can be influenced by these subunits.Voltage-gated calcium channels are classified as T, L, N, P, Q and R, and are distinguished by their sensitivity to pharmacological blocks, single-channel conductance kinetics, and voltage-dependence. On the basis of their voltage activation properties, the voltage-gated calcium classes can be further divided into two broad groups: the low (T-type) and high (L, N, P, Q and R-type) threshold-activated channels.The alpha-1 subunit forms the pore for the import of extracellular calcium ions and, though regulated by the other subunits, is primarily responsible for the pharmacological properties of the channel []. It shares sequence characteristics with all voltage-dependent cation channels, and exploits the same 6-helix bundle structural motif - in both sodium and calcium channels, this motif is repeated 4 times within the sequence to give a 24-helix bundle. Within each of these repeats, 5 of the transmembrane (TM) segments (S1, S2, S3, S5, S6) are hydrophobic, while the other (S4) is positively charged and serves as the voltage-sensor. Several genes encoding alpha-1 subunits have been identified and can be divided into three functionally distinct families based on sequence homology - Cav1, Cav2 and Cav3 []. The Cav1 family forms channels mediating L-type calcium currents, the Cav2 family mediates P/Q-, N-, and R-type calcium currents, while the Cav3 family mediates T-type calcium currents.L-type calcium channels are formed from alpha-1S, alpha-1C, alpha-1D, and alpha-1F subunits. They are widely distributed and are well characterised in the heart, smooth and skeletal muscle, and some neurons. Their primary functions are in both excitation-contraction and excitation-secretion coupling. In skeletal muscle, the L-type calcium channels act as a voltage sensor for excitation-contraction coupling, and in cardiac muscle, they provide a pathway for calcium influx. Mutations affecting L-type channel subunits result in three diseases: (1) muscular dystrophy, which is characterised by a lack of functional skeletal muscle; (2) hypokalaemic periodic paralysis, which is characterised by episodic attacks of skeletal muscle weakness; and (3) malignant hyperthermia, which is the main cause of death due to anaesthesia. 1,4-dihydropyridines act as antagonists of these channels [, ].Alpha-1C subunits can be found in a number of excitable tissues, as well as the heart and lungs []. The variability in the C-terminal region of the alpha-1C subunit generated by alternative splicing influences the kinetics, calcium- and voltage-dependence of L-type channels []. The N terminus is also a site of significant structural diversity [].
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Protein Domain
IPR005452 | LVDCC_a1dsu
Type: Family
Description: Ca2+ ions are unique in that they not only carry charge but they are also the most widely used of diffusible second messengers. Voltage-dependent Ca2+ channels (VDCC) are a family of molecules that allow cells to couple electrical activity to intracellular Ca2+ signalling. The opening and closing of these channels by depolarizing stimuli, such as action potentials, allows Ca2+ ions to enter neurons down a steep electrochemical gradient, producing transient intracellular Ca2+ signals. Many of the processes that occur in neurons, including transmitter release, gene transcription and metabolism are controlled by Ca2+ influx occurring simultaneously at different cellular locales. The pore is formed by the alpha-1 subunit which incorporates the conduction pore, the voltage sensor and gating apparatus, and the known sites of channel regulation by second messengers, drugs, and toxins []. The activity of this pore is modulated by four tightly-coupled subunits: an intracellular beta subunit; a transmembrane gamma subunit; and a disulphide-linked complex of alpha-2 and delta subunits, which are proteolytically cleaved from the same gene product. Properties of the protein including gating voltage-dependence, G protein modulation and kinase susceptibility can be influenced by these subunits.Voltage-gated calcium channels are classified as T, L, N, P, Q and R, and are distinguished by their sensitivity to pharmacological blocks, single-channel conductance kinetics, and voltage-dependence. On the basis of their voltage activation properties, the voltage-gated calcium classes can be further divided into two broad groups: the low (T-type) and high (L, N, P, Q and R-type) threshold-activated channels.The alpha-1 subunit forms the pore for the import of extracellular calcium ions and, though regulated by the other subunits, is primarily responsible for the pharmacological properties of the channel []. It shares sequence characteristics with all voltage-dependent cation channels, and exploits the same 6-helix bundle structural motif - in both sodium and calcium channels, this motif is repeated 4 times within the sequence to give a 24-helix bundle. Within each of these repeats, 5 of the transmembrane (TM) segments (S1, S2, S3, S5, S6) are hydrophobic, while the other (S4) is positively charged and serves as the voltage-sensor. Several genes encoding alpha-1 subunits have been identified and can be divided into three functionally distinct families based on sequence homology - Cav1, Cav2 and Cav3 []. The Cav1 family forms channels mediating L-type calcium currents, the Cav2 family mediates P/Q-, N-, and R-type calcium currents, while the Cav3 family mediates T-type calcium currents.L-type calcium channels are formed from alpha-1S, alpha-1C, alpha-1D, and alpha-1F subunits. They are widely distributed and are well characterised in the heart, smooth and skeletal muscle, and some neurons. Their primary functions are in both excitation-contraction and excitation-secretion coupling. In skeletal muscle, the L-type calcium channels act as a voltage sensor for excitation-contraction coupling, and in cardiac muscle, they provide a pathway for calcium influx. Mutations affecting L-type channel subunits result in three diseases: (1) muscular dystrophy, which is characterised by a lack of functional skeletal muscle; (2) hypokalaemic periodic paralysis, which is characterised by episodic attacks of skeletal muscle weakness; and (3) malignant hyperthermia, which is the main cause of death due to anaesthesia. 1,4-dihydropyridines act as antagonists of these channels [, ].Alpha-1D subunits allow cells to slowly inactivate voltage-gated Ca2+ influx to weak depolarisations []. This property allows them to participate in important physiological functions, such as tonic neurotransmitter release in cochlear inner hair cells []. In addition, these properties make them ideally suited to contribute to subthreshold Ca2+ signalling, for example in hippocampal pyramidal cells []. Mutations in this channel have been associated with autism spectrum disorders and epilepsy [].
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Protein Domain
IPR005450 | VDCC_L_a1ssu
Type: Family
Description: Ca2+ ions are unique in that they not only carry charge but they are also the most widely used of diffusible second messengers. Voltage-dependent Ca2+ channels (VDCC) are a family of molecules that allow cells to couple electrical activity to intracellular Ca2+ signalling. The opening and closing of these channels by depolarizing stimuli, such as action potentials, allows Ca2+ ions to enter neurons down a steep electrochemical gradient, producing transient intracellular Ca2+ signals. Many of the processes that occur in neurons, including transmitter release, gene transcription and metabolism are controlled by Ca2+ influx occurring simultaneously at different cellular locales. The pore is formed by the alpha-1 subunit which incorporates the conduction pore, the voltage sensor and gating apparatus, and the known sites of channel regulation by second messengers, drugs, and toxins []. The activity of this pore is modulated by four tightly-coupled subunits: an intracellular beta subunit; a transmembrane gamma subunit; and a disulphide-linked complex of alpha-2 and delta subunits, which are proteolytically cleaved from the same gene product. Properties of the protein including gating voltage-dependence, G protein modulation and kinase susceptibility can be influenced by these subunits.Voltage-gated calcium channels are classified as T, L, N, P, Q and R, and are distinguished by their sensitivity to pharmacological blocks, single-channel conductance kinetics, and voltage-dependence. On the basis of their voltage activation properties, the voltage-gated calcium classes can be further divided into two broad groups: the low (T-type) and high (L, N, P, Q and R-type) threshold-activated channels.The alpha-1 subunit forms the pore for the import of extracellular calcium ions and, though regulated by the other subunits, is primarily responsible for the pharmacological properties of the channel []. It shares sequence characteristics with all voltage-dependent cation channels, and exploits the same 6-helix bundle structural motif - in both sodium and calcium channels, this motif is repeated 4 times within the sequence to give a 24-helix bundle. Within each of these repeats, 5 of the transmembrane (TM) segments (S1, S2, S3, S5, S6) are hydrophobic, while the other (S4) is positively charged and serves as the voltage-sensor. Several genes encoding alpha-1 subunits have been identified and can be divided into three functionally distinct families based on sequence homology - Cav1, Cav2 and Cav3 []. The Cav1 family forms channels mediating L-type calcium currents, the Cav2 family mediates P/Q-, N-, and R-type calcium currents, while the Cav3 family mediates T-type calcium currents.L-type calcium channels are formed from alpha-1S, alpha-1C, alpha-1D, and alpha-1F subunits. They are widely distributed and are well characterised in the heart, smooth and skeletal muscle, and some neurons. Their primary functions are in both excitation-contraction and excitation-secretion coupling. In skeletal muscle, the L-type calcium channels act as a voltage sensor for excitation-contraction coupling, and in cardiac muscle, they provide a pathway for calcium influx. Mutations affecting L-type channel subunits result in three diseases: (1) muscular dystrophy, which is characterised by a lack of functional skeletal muscle; (2) hypokalaemic periodic paralysis, which is characterised by episodic attacks of skeletal muscle weakness; and (3) malignant hyperthermia, which is the main cause of death due to anaesthesia. 1,4-dihydropyridines act as antagonists of these channels [, ].The alpha-1S subunit is present in skeletal muscle and has also been detected in kidney and brain []. In the skeletal muscle, it is present in two size variants, a full-length, minor (~5%) form of ~212kDa, and a major (~95%) species of ~190kDa, derived from the longer protein by post-translational cleavage.
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Protein
P97445
Organism: Mus musculus/domesticus
Length: 2368  
Fragment?: false
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Protein
Q8C8Q4
Organism: Mus musculus/domesticus
Length: 844  
Fragment?: true
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Protein
Q3UHA5
Organism: Mus musculus/domesticus
Length: 2321  
Fragment?: false
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Protein
Q3UHN4
Organism: Mus musculus/domesticus
Length: 2368  
Fragment?: false
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Protein
S4R182
Organism: Mus musculus/domesticus
Length: 431  
Fragment?: false
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Protein
Q8R5M7
Organism: Mus musculus/domesticus
Length: 2327  
Fragment?: false
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Protein
E9Q1R5
Organism: Mus musculus/domesticus
Length: 2321  
Fragment?: false
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Protein
A0A1L1SQZ2
Organism: Mus musculus/domesticus
Length: 2321  
Fragment?: true
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Protein
Q8R5M6
Organism: Mus musculus/domesticus
Length: 2365  
Fragment?: false
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Protein
A0A571BET0
Organism: Mus musculus/domesticus
Length: 2457  
Fragment?: false
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Protein
Q02789
Organism: Mus musculus/domesticus
Length: 1852  
Fragment?: false
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Protein
Q01815
Organism: Mus musculus/domesticus
Length: 2139  
Fragment?: false
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Protein
Q99246
Organism: Mus musculus/domesticus
Length: 2179  
Fragment?: false
•
•
•
•
•
Protein
A0A1W2P731
Organism: Mus musculus/domesticus
Length: 2063  
Fragment?: false
•
•
•
•
•
Protein
C7TQ62
Organism: Mus musculus/domesticus
Length: 2222  
Fragment?: false
•
•
•
•
•
Protein
Q0PCR6
Organism: Mus musculus/domesticus
Length: 2169  
Fragment?: false
•
•
•
•
•
Protein
F7CNJ1
Organism: Mus musculus/domesticus
Length: 1507  
Fragment?: true
•
•
•
•
•
Protein
A0A589Q4M7
Organism: Mus musculus/domesticus
Length: 2135  
Fragment?: false
•
•
•
•
•
Protein
A0A087WPP1
Organism: Mus musculus/domesticus
Length: 2167  
Fragment?: false
•
•
•
•
•
Protein
A0A087WRZ6
Organism: Mus musculus/domesticus
Length: 2159  
Fragment?: false
•
•
•
•
•
Protein
B7ZN95
Organism: Mus musculus/domesticus
Length: 2139  
Fragment?: false
•
•
•
•
•
Protein
A0A087WS40
Organism: Mus musculus/domesticus
Length: 2153  
Fragment?: false
•
•
•
•
•
Protein
A0A571BDT1
Organism: Mus musculus/domesticus
Length: 1647  
Fragment?: false
•
•
•
•
•
Protein
A0A087WR02
Organism: Mus musculus/domesticus
Length: 2139  
Fragment?: false
•
•
•
•
•
Protein
A0A087WPZ8
Organism: Mus musculus/domesticus
Length: 2139  
Fragment?: false
•
•
•
•
•
Protein
C7TQ58
Organism: Mus musculus/domesticus
Length: 2194  
Fragment?: false
•
•
•
•
•
Protein
A0A2C9F2E5
Organism: Mus musculus/domesticus
Length: 2187  
Fragment?: false
•
•
•
•
•
Protein
A0A087WS67
Organism: Mus musculus/domesticus
Length: 2164  
Fragment?: false
•
•
•
•
•
Protein
A0A087WQT9
Organism: Mus musculus/domesticus
Length: 2135  
Fragment?: false
•
•
•
•
•
Protein
A0A1W2P6Z7
Organism: Mus musculus/domesticus
Length: 2005  
Fragment?: false
•
•
•
•
•
Protein
A0A8I4RSM0
Organism: Mus musculus/domesticus
Length: 1850  
Fragment?: false
•
•
•
•
•
Protein
A0A087WQJ4
Organism: Mus musculus/domesticus
Length: 2156  
Fragment?: false
•
•
•
•
•
Protein
Q3UQQ0
Organism: Mus musculus/domesticus
Length: 1473  
Fragment?: false
•
•
•
•
•
Protein
A0A286YD72
Organism: Mus musculus/domesticus
Length: 2159  
Fragment?: false
•
•
•
•
•
Protein
C7TQ61
Organism: Mus musculus/domesticus
Length: 2156  
Fragment?: false
•
•
•
•
•
Protein
F8WJL1
Organism: Mus musculus/domesticus
Length: 2139  
Fragment?: false
•
•
•
•
•
Protein
A0A087WSE7
Organism: Mus musculus/domesticus
Length: 2194  
Fragment?: false
•
•
•
•
•
Protein
A0A087WRM3
Organism: Mus musculus/domesticus
Length: 2187  
Fragment?: false
•
•
•
•
•
Protein
C7TQ60
Organism: Mus musculus/domesticus
Length: 2153  
Fragment?: false
•
•
•
•
•
Protein
A0A1W2P6T3
Organism: Mus musculus/domesticus
Length: 1969  
Fragment?: false
•
•
•
•
•
Protein
F7C376
Organism: Mus musculus/domesticus
Length: 2222  
Fragment?: false
•
•
•
•
•
Protein
A0A1W2P805
Organism: Mus musculus/domesticus
Length: 1980  
Fragment?: false
•
•
•
•
•
Protein
A0A571BEQ4
Organism: Mus musculus/domesticus
Length: 1643  
Fragment?: true
•
•
•
•
•
Protein
Q5S8D1
Organism: Mus musculus/domesticus
Length: 2139  
Fragment?: false
•
•
•
•
•
Protein
C7TQ57
Organism: Mus musculus/domesticus
Length: 2169  
Fragment?: false
•
•
•
•
•
Protein
C7TQ59
Organism: Mus musculus/domesticus
Length: 2169  
Fragment?: false
•
•
•
•
•
Protein
O55017
Organism: Mus musculus/domesticus
Length: 2327  
Fragment?: false
•
•
•
•
•
Protein
Q61290
Organism: Mus musculus/domesticus
Length: 2272  
Fragment?: false
•
•
•
•
•
Protein
Q9JIS7
Organism: Mus musculus/domesticus
Length: 1985  
Fragment?: false
•
•
•
•
•
Protein
A2AIR7
Organism: Mus musculus/domesticus
Length: 2328  
Fragment?: false
•
•
•
•
•
Protein
A0A087WS83
Organism: Mus musculus/domesticus
Length: 2273  
Fragment?: false
•
•
•
•
•
Protein
E9QK20
Organism: Mus musculus/domesticus
Length: 1965  
Fragment?: false
•
•
•
•
•
Protein
A0A1D5RLU3
Organism: Mus musculus/domesticus
Length: 2254  
Fragment?: false
•
•
•
•
•
Protein
A2AIS0
Organism: Mus musculus/domesticus
Length: 2288  
Fragment?: false
•
•
•
•
•
Protein
Q5SUG0
Organism: Mus musculus/domesticus
Length: 2277  
Fragment?: false
•
•
•
•
•
Protein
A2AIR9
Organism: Mus musculus/domesticus
Length: 2325  
Fragment?: false
•
•
•
•
•
Protein
B1AVA4
Organism: Mus musculus/domesticus
Length: 1977  
Fragment?: false
•
•
•
•
•
Protein
E9PWL1
Organism: Mus musculus/domesticus
Length: 2272  
Fragment?: false
•
•
•
•
•
Protein
Q5SUG4
Organism: Mus musculus/domesticus
Length: 2295  
Fragment?: false
•
•
•
•
•
Protein
Q9WUT2
Organism: Mus musculus/domesticus
Length: 2295  
Fragment?: false
•
•
•
•
•
Protein
B2RWX7
Organism: Mus musculus/domesticus
Length: 2273  
Fragment?: false
•
•
•
•
•
Protein
E9Q7P2
Organism: Mus musculus/domesticus
Length: 2199  
Fragment?: false
•
•
•
•
•
Protein
Q5SUG3
Organism: Mus musculus/domesticus
Length: 2270  
Fragment?: false
•
•
•
•
•
Protein
Q5SUF6
Organism: Mus musculus/domesticus
Length: 2288  
Fragment?: false
•
•
•
•
•
Protein
E0CXK2
Organism: Mus musculus/domesticus
Length: 1835  
Fragment?: false
•
•
•
•
•
Protein
Q7TNI3
Organism: Mus musculus/domesticus
Length: 1984  
Fragment?: false
•
•
•
•
•
Protein
Q5SUF5
Organism: Mus musculus/domesticus
Length: 2247  
Fragment?: false
•
•
•
•
•
Protein
Q6PDD2
Organism: Mus musculus/domesticus
Length: 859  
Fragment?: false
•
•
•
•
•
Protein
B9VVV1
Organism: Mus musculus/domesticus
Length: 81  
Fragment?: true
•
•
•
•
•
Protein
Q5SUF8
Organism: Mus musculus/domesticus
Length: 2254  
Fragment?: false
•
•
•
•
•
Protein
Q5SUG1
Organism: Mus musculus/domesticus
Length: 2248  
Fragment?: false
•
•
•
•
•
Protein
Q27YN9
Organism: Mus musculus/domesticus
Length: 2265  
Fragment?: false
•
•
•
•
•
Protein
Q6ZPX4
Organism: Mus musculus/domesticus
Length: 1389  
Fragment?: true
•
•
•
•
•
Protein
Q6PFV8
Organism: Mus musculus/domesticus
Length: 2248  
Fragment?: false
•
•
•
•
•
Protein
Q5SUF9
Organism: Mus musculus/domesticus
Length: 2265  
Fragment?: false
•
•
•
•
•
Protein
Q5SUG2
Organism: Mus musculus/domesticus
Length: 2176  
Fragment?: false
•
•
•
•
•
Protein
Q3UWK7
Organism: Mus musculus/domesticus
Length: 771  
Fragment?: true
•
•
•
•
•
Protein
A2AIZ9
Organism: Mus musculus/domesticus
Length: 228  
Fragment?: true
•
•
•
•
•
Publication
8815798 | -
 
First Author: Huguenard JR
Year: 1996
Journal: Annu Rev Physiol
Title: Low-threshold calcium currents in central nervous system neurons.
Volume: 58
Pages: 329-48
•
•
•
•
•
Publication
8232302 | -
First Author: Enyeart JJ
Year: 1993
Journal: Mol Endocrinol
Title: T-type Ca2+ channels are required for adrenocorticotropin-stimulated cortisol production by bovine adrenal zona fasciculata cells.
Volume: 7
Issue: 8
Pages: 1031-40
•
•
•
•
•
Publication
2557425 | -
 
First Author: Akaike N
Year: 1989
Journal: J Physiol
Title: Dihydropyridine-sensitive low-threshold calcium channels in isolated rat hypothalamic neurones.
Volume: 412
Pages: 181-95
•
•
•
•
•




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.

Copyright © 2017 by The Jackson Laboratory. All Rights Reserved

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