CACNA1F Membrane Protein Introduction

Introduction of CACNA1F

CACNA1F, voltage-dependent, L type alpha 1F subunit, also known as Cav1.4, is a protein that in human is encoded by CACNA1F gene. It is a member of the alpha-1 subunit family, and it’s one of the proteins involved in the voltage-dependent calcium channel complex. CACNA1F mediates the calcium influx into the cell once membrane polarization. In addition, CACNA1F is a complex which consists of alpha-1, alpha-2/delta, beta, and gamma subunits as a 1 to 1 to 1 to 1 ratio. The alpha-1 subunit includes 24 transmembrane segments and forms the pore by which ions pass into the cell. Multiple isoforms of each protein in the complex are available, either encoded by different genes or the result of alternative splicing of transcripts.

Basic Information of CACNA1F
Protein Name Voltage-dependent L-type calcium channel subunit alpha-1F
Gene Name CACNA1F
Aliases Voltage-gated calcium channel subunit alpha Cav1.4, CACNAF1
Organism Homo sapiens (Human)
UniProt ID O60840
Transmembrane Times 24
Length (aa) 1977

Function of CACNA1F Membrane Protein

CACNA1F, calcium channel is a voltage-dependent, L-type calcium channel subunit alpha-1F. Mediating the entry of calcium ions into excitable cells, voltage-sensitive calcium channels (VSCC) are also involved in a variety of calcium-dependent processes, including muscle contraction, hormone or neurotransmitter release, gene expression, cell motility, cell division and cell death. The isoform alpha-1F can cause L-type calcium currents. Researchers have reported that long-lasting (L-type) calcium channels are members of the 'high-voltage activated' (HVA) group. They are blocked by dihydropyridines (DHP), benzothiazepines, as well as phenylalkylamines and omega-agatoxin-IIIA (omega-Aga-IIIA). CACNA1F is insensitive to omega-agatoxin-IVA (omega-Aga-IVA), as well as omega-conotoxin-GVIA (omega-CTx-GVIA). Furthermore, CACNA1F is also activated at more negative voltages and does not process calcium-dependent inactivation (CDI), due to incoming calcium ions during depolarization.

Protein topology of Ca<sub>v</sub>1.4. Fig.1 Protein topology of Cav1.4. (Waldner, 2018)

Application of CACNA1F Membrane Protein in Literature

  1. Waldner D.M., et al. Channeling Vision: Cav1.4-A Critical Link in Retinal Signal Transmission. Biomed Res Int. 2018, 2018: 7272630. PubMed ID: 29854783

    This article addresses the special properties of one L-type VGCC, Cav1.4, with particular emphasis on its role in the transmission of visual signals from rod and cone photoreceptors to the second-order retinal neurons, and the pathological effects of mutations in the CACNA1F gene which codes for the pore-forming α1F subunit of Cav1.4.

  2. Men C.J., et al. The importance of genetic testing as demonstrated by two cases of CACNA1F-associated retinal generation misdiagnosed as LCA. Mol Vis. 2017, 23: 695-706. PubMed ID: 29062221

    This article is to describe in detail cases with an initial diagnosis of Leber congenital amaurosis that is later found to have a hemizygous mutation in the CACNA1F gene.

  3. Schön C., et al. Cav1.4 L-Type Calcium Channels Contribute to Calpain Activation in Degenerating Photoreceptors of rd1 Mice. PLoS One. 2016, 11(6): e0156974. PubMed ID: 27270916

    This study shows that genetic deletion of the synaptic Cav1.4 L-type VGCCs impairs calpain activation and leads to a short-term preservation of photoreceptors in the rd1 mouse.

  4. Haeseleer F., et al. Characterization of C-terminal Splice Variants of Cav1.4 Ca2+ Channels in Human Retina. J Biol Chem. 2016, 291(30): 15663-73. PubMed ID: 27226626

    This article concludes that exon 47 encodes structural determinants that regulate CDI and voltage-dependent activation of Cav1.4, and is necessary for modulation of channel activation by CaBP4.

  5. Grabner C.P., et al. RIM1/2-Mediated Facilitation of Cav1.4 Channel Opening Is Required for Ca2+-Stimulated Release in Mouse Rod Photoreceptors. J Neurosci. 2015, 35(38): 13133-47. PubMed ID: 26400943

    This article shows that a key function of RIM1/2 at rod ribbons is to enhance Cav1.4 channel activity, possibly through direct or indirect modulation of the channel.

CACNA1F Preparation Options

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  1. Waldner D M, et al. (2018). Channeling Vision: Cav1.4-A Critical Link in Retinal Signal Transmission. Biomed Res Int. 2018:7272630.

All listed customized services & products are for research use only, not intended for pharmaceutical, diagnostic, therapeutic or any in vivo human use.

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