| Type |
Details |
Score |
| Publication |
| First Author: |
Mouse Genome Informatics Scientific Curators |
| Year: |
2002 |
|
| Title: |
Mouse Genome Informatics Computational Sequence to Gene Associations |
|
|
|
|
•
•
•
•
•
|
| Publication |
| First Author: |
Mouse Genome Informatics Scientific Curators |
| Year: |
2010 |
| Journal: |
Database Download |
| Title: |
Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Genome U74 Array Platform (A, B, C v2). |
|
|
|
|
•
•
•
•
•
|
| Publication |
| First Author: |
MGI Genome Annotation Group and UniGene Staff |
| Year: |
2015 |
| Journal: |
Database Download |
| Title: |
MGI-UniGene Interconnection Effort |
|
|
|
|
•
•
•
•
•
|
| Publication |
| First Author: |
Marc Feuermann, Huaiyu Mi, Pascale Gaudet, Dustin Ebert, Anushya Muruganujan, Paul Thomas |
| Year: |
2010 |
|
| Title: |
Annotation inferences using phylogenetic trees |
|
|
|
|
•
•
•
•
•
|
| Publication |
| First Author: |
Mouse Genome Database and National Center for Biotechnology Information |
| Year: |
2000 |
| Journal: |
Database Release |
| Title: |
Entrez Gene Load |
|
|
|
|
•
•
•
•
•
|
| Publication |
| First Author: |
Allen Institute for Brain Science |
| Year: |
2004 |
| Journal: |
Allen Institute |
| Title: |
Allen Brain Atlas: mouse riboprobes |
|
|
|
|
•
•
•
•
•
|
| Publication |
| 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 |
|
|
|
|
•
•
•
•
•
|
| Publication |
| First Author: |
Mouse Genome Informatics (MGI) and The National Center for Biotechnology Information (NCBI) |
| Year: |
2010 |
| Journal: |
Database Download |
| Title: |
Consensus CDS project |
|
|
|
|
•
•
•
•
•
|
| Publication |
| First Author: |
Mouse Genome Informatics Group |
| Year: |
2003 |
| Journal: |
Database Procedure |
| Title: |
Automatic Encodes (AutoE) Reference |
|
|
|
|
•
•
•
•
•
|
| Publication |
| First Author: |
Bairoch A |
| Year: |
1999 |
| Journal: |
Database Release |
| Title: |
SWISS-PROT Annotated protein sequence database |
|
|
|
|
•
•
•
•
•
|
| Publication |
| First Author: |
Mouse Genome Informatics Scientific Curators |
| Year: |
2005 |
|
| Title: |
Obtaining and Loading Genome Assembly Coordinates from Ensembl Annotations |
|
|
|
|
•
•
•
•
•
|
| Publication |
| First Author: |
Mouse Genome Informatics |
| Year: |
2010 |
| Journal: |
Database Release |
| Title: |
Protein Ontology Association Load. |
|
|
|
|
•
•
•
•
•
|
| Publication |
| First Author: |
Mouse Genome Informatics Scientific Curators |
| Year: |
2005 |
|
| Title: |
Obtaining and loading genome assembly coordinates from NCBI annotations |
|
|
|
|
•
•
•
•
•
|
| Publication |
| First Author: |
Mouse Genome Informatics Scientific Curators |
| Year: |
2009 |
| Journal: |
Database Download |
| Title: |
Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Genome 430 2.0 Array Platform |
|
|
|
|
•
•
•
•
•
|
| Allele |
| Name: |
caveolin 3; targeted mutation 1, Michael P Lisanti |
| Allele Type: |
Targeted |
| Attribute String: |
Null/knockout |
|
•
•
•
•
•
|
| Allele |
| Name: |
caveolin 3; targeted mutation 1, Tateki Kikuchi |
| Allele Type: |
Targeted |
| Attribute String: |
Null/knockout |
|
•
•
•
•
•
|
| Allele |
| Name: |
caveolin 3; endonuclease-mediated mutation 1, Shanghai Model Organisms Center |
| Allele Type: |
Endonuclease-mediated |
| Attribute String: |
Null/knockout |
|
•
•
•
•
•
|
| DO Term |
|
•
•
•
•
•
|
| Strain |
| Attribute String: |
coisogenic, endonuclease-mediated mutation, mutant strain |
|
•
•
•
•
•
|
| DO Term |
|
•
•
•
•
•
|
| Allele |
| Name: |
transgene insertion 1, Yoshihide Sunada |
| Allele Type: |
Transgenic |
| Attribute String: |
Inserted expressed sequence |
|
•
•
•
•
•
|
| Gene |
| Type: |
gene |
| Organism: |
human |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Kawakami E |
| Year: |
2013 |
| Journal: |
PLoS One |
| Title: |
Local applications of myostatin-siRNA with atelocollagen increase skeletal muscle mass and recovery of muscle function. |
| Volume: |
8 |
| Issue: |
5 |
| Pages: |
e64719 |
|
•
•
•
•
•
|
| Genotype |
| Symbol: |
Tg(Ckmm-Cav3)1Ysu/? |
| Background: |
involves: C57BL/Slc * DBA/Slc |
| Zygosity: |
ot |
| Has Mutant Allele: |
true |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Yang S |
| Year: |
2016 |
| Journal: |
Cell Rep |
| Title: |
β-Arrestin-Dependent Dopaminergic Regulation of Calcium Channel Activity in the Axon Initial Segment. |
| Volume: |
16 |
| Issue: |
6 |
| Pages: |
1518-1526 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Zhan X |
| Year: |
2024 |
| Journal: |
J Neurosci |
| Title: |
Calcium-Dependent Regulation of Neuronal Excitability Is Rescued in Fragile X Syndrome by a Tat-Conjugated N-Terminal Fragment of FMRP. |
| Volume: |
44 |
| Issue: |
21 |
|
|
•
•
•
•
•
|
| Publication |
| First Author: |
Papazoglou A |
| Year: |
2017 |
| Journal: |
Data Brief |
| Title: |
Gender specific hippocampal whole genome transcriptome data from mice lacking the Cav2.3 R-type or Cav3.2 T-type voltage-gated calcium channel. |
| Volume: |
12 |
|
| Pages: |
81-86 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
El-Yazbi AF |
| Year: |
2006 |
| Journal: |
Am J Physiol Gastrointest Liver Physiol |
| Title: |
Impact of caveolin-1 knockout on NANC relaxation in circular muscles of the mouse small intestine compared with longitudinal muscles. |
| Volume: |
290 |
| Issue: |
2 |
| Pages: |
G394-403 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Cazade M |
| Year: |
2014 |
| Journal: |
Pflugers Arch |
| Title: |
5,6-EET potently inhibits T-type calcium channels: implication in the regulation of the vascular tone. |
| Volume: |
466 |
| Issue: |
9 |
| Pages: |
1759-68 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Valasek MA |
| Year: |
2005 |
| Journal: |
J Biol Chem |
| Title: |
Caveolin-1 is not required for murine intestinal cholesterol transport. |
| Volume: |
280 |
| Issue: |
30 |
| Pages: |
28103-9 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Lundt A |
| Year: |
2019 |
| Journal: |
BMC Res Notes |
| Title: |
Gender specific click and tone burst evoked ABR datasets from mice lacking the Cav3.2 T-type voltage-gated calcium channel. |
| Volume: |
12 |
| Issue: |
1 |
| Pages: |
157 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Taniguchi T |
| Year: |
2016 |
| Journal: |
PLoS One |
| Title: |
PTRF/Cavin-1 Deficiency Causes Cardiac Dysfunction Accompanied by Cardiomyocyte Hypertrophy and Cardiac Fibrosis. |
| Volume: |
11 |
| Issue: |
9 |
| Pages: |
e0162513 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Zhang Y |
| Year: |
2011 |
| Journal: |
Cardiovasc Res |
| Title: |
MG53 participates in ischaemic postconditioning through the RISK signalling pathway. |
| Volume: |
91 |
| Issue: |
1 |
| Pages: |
108-15 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Binda F |
| Year: |
2016 |
| Journal: |
Sci Rep |
| Title: |
Inhibition promotes long-term potentiation at cerebellar excitatory synapses. |
| Volume: |
6 |
|
| Pages: |
33561 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Yoo KH |
| Year: |
2014 |
| Journal: |
Dev Biol |
| Title: |
The STAT5-regulated miR-193b locus restrains mammary stem and progenitor cell activity and alveolar differentiation. |
| Volume: |
395 |
| Issue: |
2 |
| Pages: |
245-54 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Tian C |
| Year: |
2021 |
| Journal: |
Hear Res |
| Title: |
CACHD1-deficient mice exhibit hearing and balance deficits associated with a disruption of calcium homeostasis in the inner ear. |
| Volume: |
409 |
|
| Pages: |
108327 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Nixon SJ |
| Year: |
2007 |
| Journal: |
J Cell Sci |
| Title: |
Caveolin-1 is required for lateral line neuromast and notochord development. |
| Volume: |
120 |
| Issue: |
Pt 13 |
| Pages: |
2151-61 |
|
•
•
•
•
•
|
| Protein Domain |
| 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.This entry represents all types of alpha-1 subunit. |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
2381
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
585
|
| Fragment?: |
true |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Lewis KJ |
| Year: |
2021 |
| Journal: |
Bone |
| Title: |
Estrogen depletion on In vivo osteocyte calcium signaling responses to mechanical loading. |
| Volume: |
152 |
|
| Pages: |
116072 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Catterall WA |
| Year: |
2000 |
| Journal: |
Annu Rev Cell Dev Biol |
| Title: |
Structure and regulation of voltage-gated Ca2+ channels. |
| Volume: |
16 |
|
| Pages: |
521-55 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Ertel EA |
| Year: |
2000 |
| Journal: |
Neuron |
| Title: |
Nomenclature of voltage-gated calcium channels. |
| Volume: |
25 |
| Issue: |
3 |
| Pages: |
533-5 |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
513
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
2365
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
89
|
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
138
|
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
147
|
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
229
|
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
111
|
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
114
|
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
1901
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
113
|
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
110
|
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
102
|
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
255
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
247
|
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
541
|
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
2359
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Triggle DJ |
| Year: |
2003 |
| Journal: |
Cell Mol Neurobiol |
| Title: |
1,4-Dihydropyridines as calcium channel ligands and privileged structures. |
| Volume: |
23 |
| Issue: |
3 |
| Pages: |
293-303 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Striessnig J |
| Year: |
2004 |
| Journal: |
Biochem Biophys Res Commun |
| Title: |
L-type Ca2+ channels in Ca2+ channelopathies. |
| Volume: |
322 |
| Issue: |
4 |
| Pages: |
1341-6 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Turner TJ |
| Year: |
1993 |
| Journal: |
Proc Natl Acad Sci U S A |
| Title: |
Multiple Ca2+ channel types coexist to regulate synaptosomal neurotransmitter release. |
| Volume: |
90 |
| Issue: |
20 |
| Pages: |
9518-22 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Hirning LD |
| Year: |
1988 |
| Journal: |
Science |
| Title: |
Dominant role of N-type Ca2+ channels in evoked release of norepinephrine from sympathetic neurons. |
| Volume: |
239 |
| Issue: |
4835 |
| Pages: |
57-61 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Luebke JI |
| Year: |
1993 |
| Journal: |
Neuron |
| Title: |
Multiple calcium channel types control glutamatergic synaptic transmission in the hippocampus. |
| Volume: |
11 |
| Issue: |
5 |
| Pages: |
895-902 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Snutch TP |
| Year: |
2005 |
| Journal: |
NeuroRx |
| Title: |
Targeting chronic and neuropathic pain: the N-type calcium channel comes of age. |
| Volume: |
2 |
| Issue: |
4 |
| Pages: |
662-70 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Gao S |
| Year: |
2021 |
| Journal: |
Nature |
| Title: |
Structure of human Cav2.2 channel blocked by the painkiller ziconotide. |
| Volume: |
596 |
| Issue: |
7870 |
| Pages: |
143-147 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Diriong S |
| Year: |
1995 |
| Journal: |
Genomics |
| Title: |
Chromosomal localization of the human genes for alpha 1A, alpha 1B, and alpha 1E voltage-dependent Ca2+ channel subunits. |
| Volume: |
30 |
| Issue: |
3 |
| Pages: |
605-9 |
|
•
•
•
•
•
|
| Publication |
| 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 |
|
•
•
•
•
•
|
| Publication |
| 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 |
|
•
•
•
•
•
|
| Publication |
| 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 |
|
•
•
•
•
•
|
| Publication |
| 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 |
|
•
•
•
•
•
|
| Publication |
| 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 |
|
•
•
•
•
•
|
| Publication |
| 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 |
|
•
•
•
•
•
|
| Publication |
| 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 |
|
•
•
•
•
•
|
| Publication |
| 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 |
|
•
•
•
•
•
|
| Publication |
| 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 |
|
•
•
•
•
•
|
| Publication |
| 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 |
|
•
•
•
•
•
|
| Publication |
| 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 |
|
•
•
•
•
•
|
| Protein Domain |
| 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 |
| 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 |
| 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 |
| 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 []. |
|
•
•
•
•
•
|
| Protein Domain |
| 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 []. |
|
•
•
•
•
•
|
| Protein Domain |
| 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 []. |
|
•
•
•
•
•
|
| Protein Domain |
| 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 []. |
|
•
•
•
•
•
|
| Protein Domain |
| 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. |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
2368
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
844
|
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
2321
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
2368
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
431
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
2327
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
2321
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
2321
|
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
2365
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
2457
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
1852
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
2139
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
2179
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
2063
|
| Fragment?: |
false |
|
•
•
•
•
•
|
