Nomenclature: Cav1.4

Family: Voltage-gated calcium channels

Annotation status:  image of an orange circle Annotated and awaiting review. Please contact us if you can help with reviewing. 

Contents

Gene and Protein Information
Species TM P Loops AA Chromosomal Location Gene Symbol Gene Name Reference
Human 24 4 1977 Xp11.23 CACNA1F calcium channel, voltage-dependent, L type, alpha 1F subunit 3,31,34
Mouse 24 4 1984 X A1.1 Cacna1f calcium channel, voltage-dependent, alpha 1F subunit 27,35
Rat 24 4 1981 Xq13 Cacna1f calcium channel, voltage-dependent, L type, alpha 1F subunit 23
Previous and Unofficial Names
Names References
Cav1.4
L-type
α1F
CSNB2
AIED
JM8
JMC8
CSNBX2
CORDX3
CSNB2A
COD4
OA2
Aland island eye disease (Forsius-Eriksson ocular albinism, ocular albinism type 2)
calcium channel, voltage-dependent, L type, alpha 1F subunit
calcium channel, voltage-dependent, alpha 1F subunit
voltage-dependent L-type calcium channel subunit alpha-1F
Sfc17
nerg1
nob2
Cav1.4α1
alpha1F
class F L-type calcium channel 3
Database Links
ChEMBL Target
DrugBank Target
Ensembl Gene
Entrez Gene
GeneCards
GenitoUrinary Development Molecular Anatomy Project
HomoloGene
Human Protein Reference Database
InterPro
KEGG Gene
OMIM
Orphanet Gene
PharmGKB Gene
PhosphoSitePlus
Protein Ontology (PRO)
RefSeq Nucleotide
RefSeq Protein
TreeFam
UniGene Hs.
UniProtKB
Wikipedia
Associated Proteins
Heteromeric Pore-forming Subunits
Name References
Not determined
Auxiliary Subunits
Name References
α 17,29
β (likely β2) 1
Other Associated Proteins
Name References
Calcium binding protein 4 11,30
Calmodulin 10,31
Functional Characteristics
Moderate voltage-activated, slow inactivation (Ca2+ independent)
Ion Selectivity and Conductance
Species:  Human
Rank order:  Cs+ [21.0 pS] > Ba2+ [4.0 pS]
References:  8
Voltage Dependence
  V0.5 (mV)  τ (msec)  Reference  Cell type  Species 
Activation  -15.1 – -1.1 (median: -12.0) 0.65 – 3.6 2,11 HEK 293 cells. Mouse
Inactivation  -15.4 - 2
Comments  Data are for ICa2+, except for τ which was determined for IBa2+. V0.5 for activation is more positive with Ca2+ as a charge carrier than with Ba2+.
  V0.5 (mV)  τ (msec)  Reference  Cell type  Species 
Activation  -11.6 – 0.6 0.43 – 6.6 18,22,31 tsA-201 cells. Human
Inactivation  -9.3 9.8 22
Comments  Data are for ICa2+, except for inactivation data (IBa2+). V0.5 for activation is more positive with Ca2+ as a charge carrier than with Ba2+. Unlike for other Ca2+ channels, Ca2+-dependent inactivation (CDI) is absent due to inhibition of CDI by a C-terminal modulatory domain [31,35]. This inhibitory effect can be overcome by excess calmodulin resulting in CDI [20]. ICa2+ inactivates by about 80% during 10-s depolarisations to Vmax [18,31,35]. Activation is biexponential with β2 subunits (τ for fast and slow phase are given).
Activators
Key to terms and symbols View all chemical structures Click column headers to sort
Ligand Sp. Action Affinity Units Concentration range (M) Holding voltage (mV) Reference
BAYK 8644 Hs - - - 5x10-6 - 1x10-5 -100.0 – -80.0 14,18,22
Conc range: 5x10-6 - 1x10-5 M [14,18,22]
Holding voltage: -100.0 – -80.0 mV
BAYK 8644 Mm - - - 1x10-6 -80.0 2
Conc range: 1x10-6 M [2]
Holding voltage: -80.0 mV
(-)-(S)-BayK8644 Hs - - - - -
View species-specific activator tables
Activator Comments
BAYK 8644 shifts the I-V relationship 5-10mV in the hyperpolarised direction.
Gating inhibitors
Key to terms and symbols View all chemical structures Click column headers to sort
Ligand Sp. Action Affinity Units Concentration range (M) Holding voltage (mV) Reference
verapamil Mm - - - 1x10-4 -80.0 2
Conc range: 1x10-4 M [2]
Holding voltage: -80.0 mV
isradipine Hs - - - 1x10-6 -90.0 – -50.0 18
Conc range: 1x10-6 M [18]
Holding voltage: -90.0 – -50.0 mV
isradipine Mm - 6.7 pIC50 - -80.0 2
pIC50 6.7 [2]
Holding voltage: -80.0 mV
nifedipine Hs - 6.0 pIC50 - -100.0 22
pIC50 6.0 [22]
Holding voltage: -100.0 mV
L-(cis)-diltiazem Mm - 4.1 pIC50 - -80.0 2
pIC50 4.1 [2]
Holding voltage: -80.0 mV
diltiazem Mm - 4.0 pIC50 - -80.0 2
pIC50 4.0 [2]
Holding voltage: -80.0 mV
View species-specific gating inhibitor tables
Gating Inhibitor Comments
The effect of (+/-)-isradipine is voltage-depepndant with 100nM producing 20-42% current block at a holding potential of -80 - -90mV and 80-90% block at -50mV [2,18]. Nifedipine also shows a mild increase in block at more positive holding voltages [22].

(+)-[3H]-isradipine does not show any high affinity binding with Cav1.4 [32].
Channel Blocker Comments
Cav1.4 is less sensitive to dihydropyridine antagonists than other members of the family.
Tissue Distribution
Lymphoid tissues, plasma, mast cells
Species:  Human
Technique:  Immunohistochemistry
References:  22
T-lymphocytes
Species:  Human
Technique:  RT-PCR, immunoprecipitation
References:  19
Retina
Species:  Human
Technique:  Northern Blot
References:  34
Retina (outer plexiform layer, inner plexiform and nuclear layer)
Species:  Human
Technique:  Immunohistochemistry
References:  22
Retina
Species:  Human
Technique:  RT-PCR
References:  3,22
T-lymphocytes
Species:  Mouse
Technique:  Western blot
References:  28
Retina (inner and outer nuclear layer, ganglion cell layer).
Species:  Mouse
Technique:  In situ hybridisation
References:  34
Dorsal root ganglia
Species:  Mouse
Technique:  RT-PCR
References:  24
Functional Assays
Electrophysiology (whole-cell voltage clamp).
Species:  Human
Tissue:  HEK-293 cells expressing Cav1.4.
Response measured:  L-type currents.
References:  18,22,31
Electrophysiology (whole-cell voltage clamp)
Species:  Mouse
Tissue:  HEK-293 cells expressing Cav1.4.
Response measured:  L-type currents
References:  2,11,35
Electrophysiology (single channel recording).
Species:  Human
Tissue:  HEK-293 cells expressing Cav1.4
Response measured:  L-type currents
References:  8
Electrophysiology (two electrode voltage clamp).
Species:  Human
Tissue:  Xenopus laevis oocytes expressing Cav1.4
Response measured:  L-type currents.
References:  14
Physiological Functions
Retinal signaling; neurotransmitter release from photoreceptors
Species:  Mouse
Tissue:  Retina
References:  7
Critical regulator of T cell receptor signaling and naive T cell homeostasis
Species:  Mouse
Tissue:  T-lymphocytes
References:  28
Physiological Consequences of Altering Gene Expression
Mouse CSNB2 mouse model (I745T): abnormal ERGs, altered retinal morphology
Species:  Mouse
Tissue:  Retina
Technique:  Homologous recombination (I745T introduced)
References:  28
Absence of post-receptoral ERG responses and the diminished photoreceptor calcium signals; abnormal dendritic sprouting of second-order neurons in the photoreceptor layer
Species:  Mouse
Tissue:  Retina
Technique:  Cacna1f-gene knockout
References:  21
An abnormal light- and dark-adapted electroretinogram and a disorganised outer plexiform layer can be seen in the nob2 mouse (partial loss-of-function mutation in Cacna1f).
Species:  Mouse
Tissue:  Retina
Technique:  Natural mutation (in-frame stop codon, partially rescued by alternative splicing)
References:  7,9
An abnormal light- and dark-adapted electroretinogram and a disorganised outer plexiform layer can be seen in the nob2 mouse (null mutation in Cacna1f ).
Species:  Mouse
Tissue:  Retina
Technique:  Natural mutation
References:  7,9
Impaired function and survival of naive CD4+ and CD8+ T cells; impaired store-operated calcium entry, T cell receptor-induced rises in cytosolic Ca2+, activation of Ras-extracellular signal-regulated kinase and NFAT pathways
Species:  Mouse
Tissue:  T-lymphocytes
Technique:  Cacna1f-gene knockout
References:  28
Phenotypes, Alleles and Disease Models Mouse data from MGI

Show »

Allele Composition & genetic background Accession Phenotype Id Phenotype Reference
Cacna1fnob2 Cacna1fnob2/Cacna1fnob2
AXB6/PgnJ
MGI:1859639  MP:0004022 abnormal cone electrophysiology PMID: 16597347 
Cacna1fnob2 Cacna1fnob2/Y
AXB6/PgnJ
MGI:1859639  MP:0004022 abnormal cone electrophysiology PMID: 16597347 
Cacna1ftm1Ntbh Cacna1ftm1Ntbh/Y
B6.129-Cacna1f
MGI:1859639  MP:0005551 abnormal eye electrophysiology PMID: 16155113 
Cacna1ftm1Ntbh Cacna1ftm1Ntbh/Cacna1ftm1Ntbh
B6.129-Cacna1f
MGI:1859639  MP:0005551 abnormal eye electrophysiology PMID: 16155113 
Cacna1ftm1Ntbh Cacna1ftm1Ntbh/Y
B6.129-Cacna1f
MGI:1859639  MP:0006068 abnormal horizontal cell morphology PMID: 16155113 
Cacna1ftm1Ntbh Cacna1ftm1Ntbh/Cacna1ftm1Ntbh
B6.129-Cacna1f
MGI:1859639  MP:0006068 abnormal horizontal cell morphology PMID: 16155113 
Cacna1fnob2 Cacna1fnob2/Cacna1fnob2
AXB6/PgnJ
MGI:1859639  MP:0006068 abnormal horizontal cell morphology PMID: 16597347 
Cacna1fnob2 Cacna1fnob2/Y
AXB6/PgnJ
MGI:1859639  MP:0006068 abnormal horizontal cell morphology PMID: 16597347 
Cacna1fnob2 Cacna1fnob2/Cacna1fnob2
AXB6/PgnJ
MGI:1859639  MP:0008056 abnormal retinal ganglion cell morphology PMID: 16597347 
Cacna1fnob2 Cacna1fnob2/Y
AXB6/PgnJ
MGI:1859639  MP:0008056 abnormal retinal ganglion cell morphology PMID: 16597347 
Cacna1ftm1Ntbh Cacna1ftm1Ntbh/Y
B6.129-Cacna1f
MGI:1859639  MP:0006069 abnormal retinal neuronal layer morphology PMID: 16155113 
Cacna1ftm1Ntbh Cacna1ftm1Ntbh/Cacna1ftm1Ntbh
B6.129-Cacna1f
MGI:1859639  MP:0006069 abnormal retinal neuronal layer morphology PMID: 16155113 
Cacna1fnob2 Cacna1fnob2/Cacna1fnob2
AXB6/PgnJ
MGI:1859639  MP:0003731 abnormal retinal outer nuclear layer morphology PMID: 16597347 
Cacna1fnob2 Cacna1fnob2/Y
AXB6/PgnJ
MGI:1859639  MP:0003731 abnormal retinal outer nuclear layer morphology PMID: 16597347 
Cacna1ftm1Ntbh Cacna1ftm1Ntbh/Y
B6.129-Cacna1f
MGI:1859639  MP:0006074 abnormal retinal rod bipolar cell morphology PMID: 16155113 
Cacna1ftm1Ntbh Cacna1ftm1Ntbh/Cacna1ftm1Ntbh
B6.129-Cacna1f
MGI:1859639  MP:0006074 abnormal retinal rod bipolar cell morphology PMID: 16155113 
Cacna1fnob2 Cacna1fnob2/Cacna1fnob2
AXB6/PgnJ
MGI:1859639  MP:0006074 abnormal retinal rod bipolar cell morphology PMID: 16597347 
Cacna1fnob2 Cacna1fnob2/Y
AXB6/PgnJ
MGI:1859639  MP:0006074 abnormal retinal rod bipolar cell morphology PMID: 16597347 
Cacna1fnob2 Cacna1fnob2/Cacna1fnob2
AXB6/PgnJ
MGI:1859639  MP:0004021 abnormal rod electrophysiology PMID: 16597347 
Cacna1fnob2 Cacna1fnob2/Y
AXB6/PgnJ
MGI:1859639  MP:0004021 abnormal rod electrophysiology PMID: 16597347 
Cacna1ftm1Ntbh Cacna1ftm1Ntbh/Y
B6.129-Cacna1f
MGI:1859639  MP:0000968 abnormal sensory neuron innervation pattern PMID: 16155113 
Cacna1ftm1Ntbh Cacna1ftm1Ntbh/Cacna1ftm1Ntbh
B6.129-Cacna1f
MGI:1859639  MP:0000968 abnormal sensory neuron innervation pattern PMID: 16155113 
Cacna1fnob2 Cacna1fnob2/Cacna1fnob2
AXB6/PgnJ
MGI:1859639  MP:0008520 disorganized retinal outer plexiform layer PMID: 16597347 
Cacna1fnob2 Cacna1fnob2/Y
AXB6/PgnJ
MGI:1859639  MP:0008520 disorganized retinal outer plexiform layer PMID: 16597347 
Cacna1ftm1Ntbh Cacna1ftm1Ntbh/Y
B6.129-Cacna1f
MGI:1859639  MP:0008519 thin retinal outer plexiform layer PMID: 16155113 
Cacna1ftm1Ntbh Cacna1ftm1Ntbh/Cacna1ftm1Ntbh
B6.129-Cacna1f
MGI:1859639  MP:0008519 thin retinal outer plexiform layer PMID: 16155113 
Clinically-Relevant Mutations and Pathophysiology
Disease:  Congenital stationary night blindness type 2 (CSNB2)
OMIM:  300071
Orphanet:  215
Role: 
Drugs: 
References:  3,7,34
Click column headers to sort
Type Species Molecular location Description Reference
Deletion Human p.F318del 4-5
Deletion Human 3720-3731 (mRNA) 34
Deletion Human c.3691del12bp
Deletion Human p.L662del/p.G1001R 36
Deletion Human p.I1003del 5
Frameshift Human c.244insG 4
Frameshift Human c.3125delG
Frameshift Human c.3166-3167insC
Frameshift Human D406delC
Frameshift Human c.5665delG
Frameshift Human c.3673delC
Frameshift Human I1224delC
Frameshift Human L1056insC 6
Frameshift Human c.904insG 26
Frameshift Human c.1218delC
Frameshift Human L991insC 3
Frameshift Human D341delC 3
Frameshift Human 213del5bp 37
Frameshift Human 5727delG 5
Frameshift Human 3735delC (mRNA) 5
Frameshift Human 3228insC (mRNA) 5
Frameshift Human 3195insC (mRNA) 34
Frameshift Human c.3471_3472delGC 38
Frameshift Human c.935delA 38
Frameshift Human c.5337_5338insG 4
Frameshift Human c.2623_2624del 4
Frameshift Human c.2246delT 4
Frameshift Human c.808delC 4
Frameshift Human c.413del 4
Frameshift Human c.151del5bp 4
Frameshift Human c.281dup 4
Frameshift Human 3187delG 5
Frameshift Human 1280delC (mRNA) 5
Frameshift Human I1159insC 3
Insertion/deletion Human c.271del4/ins34 (ins net 30 bp) 5,26
Missense Human P1489R 37
Missense Human L1497P 37
Missense Human C1488R 37
Missense Human L1364H 14,34
Missense Human L1068P 13,37
Missense Human R1049W 34
Missense Human G1007R 37
Missense Human L849P 37
Missense Human F742C 37
Missense Human R508Q 14,34
Missense Human p.A928D 5,22
Missense Human p.G369D 13,22,34
Missense Human p.G674D 5,22,26
Missense Human p.G261R 37
Missense Human p.S229P 13,37
Missense Human p.L1508P
Missense Human p.P1500R
Missense Human p.C1499R
Missense Human p.L1375H
Missense Human p.L1079P
Missense Human p.R1060W
Missense Human p.G1018R 4
Missense Human p.L860P
Missense Human p.F753C
Missense Human p.R519Q
Missense Human p.C74R 4
Missense Human p.R70W 4
Missense Human p.G359R
Missense Human p.S1265I 39
Missense Human p.G927A 4
Missense Human p.E278X 40
Missense Human p.D944Y 38
Missense Human p.E1145K 38
Missense Human p.L1486P 38
Missense Human p.1492A 38
Missense Human p.I756T 12
Splice site Human 2420G>C
Splice site Human 2707delCA
Splice site Human 2706 (several mutations)
Splice site Human 3975T>C or T>A
Splice site Human 4134G>C
Splice site Human intron splice site (stop in exon 42) 5
Splice site Human intron splice site (stop exon 7) 5
Truncation Human p.Q1359X
Truncation Human p.R1827X
Truncation Human p.K1602X
Truncation Human p.R625X 5
Truncation Human p.R895X 4-5,39
Truncation Human p.W1451X 4-5
Truncation Human p.R1299X 4-5
Truncation Human R50X 5
Truncation Human R82X 5,37
Truncation Human R380X 3
Truncation Human Q428X 37
Truncation Human R614X 37
Truncation Human R958X 34
Truncation Human R1234X 3
Truncation Human R1288X 37
Truncation Human W1386X 3
Truncation Human K1591X 31,34
Truncation Human R1816X 37
Truncation Human p.R1302X
Truncation Human p.Q325X 4
Truncation Human p.R978X 4,26
Truncation Human p.R969X 40
Truncation Human p.Q439X
Truncation Human p.R379X 4
Truncation Human p.R691X 4,39
Truncation Human p.S1114X 4
Disease:  Aland Island eye disease; AIED
OMIM:  300600
Orphanet:  178333
Role: 
Comments: 
References:  15
Click column headers to sort
Type Species Molecular location Description Reference
Deletion Human In frame 425 bp deletion (p.1211-1247del) 15
Disease:  Cone-rod dystrophy, X-linked, 3
OMIM:  300476
Orphanet:  1872
Role: 
Comments: 
References:  16
Click column headers to sort
Type Species Molecular location Description Reference
Deletion Human IVS28-1 GCGTC>TGG (intron 28) 16
Disease:  Night-blindness-associated transient tonic downgaze (NATTD)
References: 
Click column headers to sort
Type Species Molecular location Description Reference
Missense Human Gly359Arg 33
Missense Human Pro1489Arg 33
Missense Human Trp349stop 33
Disease:  Retinal and optic disc atrophy and a progressive decrease of visual function
References:  25
Click column headers to sort
Type Species Molecular location Description Reference
Deletion Human 4 bp deletion and 34 bp insertion in exon 4 (nucleotides 271-274) 25
Clinically-Relevant Mutations and Pathophysiology Comments
Mutations in intronic sequences of the Cav gene have also been associated with CSNB2 [5]. The electrophysiological consequences of several of these mutations have been investigated in heterologous expression systems [13-14,22,31,35]

REFERENCES

1. Ball SL, Powers PA, Shin HS, Morgans CW, Peachey NS, Gregg RG. (2002) Role of the beta(2) subunit of voltage-dependent calcium channels in the retinal outer plexiform layer. Invest. Ophthalmol. Vis. Sci.43 (5): 1595-603. [PMID:11980879]

2. Baumann L, Gerstner A, Zong X, Biel M, Wahl-Schott C. (2004) Functional characterization of the L-type Ca2+ channel Cav1.4alpha1 from mouse retina. Invest. Ophthalmol. Vis. Sci.45 (2): 708-13. [PMID:14744918]

3. Bech-Hansen NT, Naylor MJ, Maybaum TA, Pearce WG, Koop B, Fishman GA, Mets M, Musarella MA, Boycott KM. (1998) Loss-of-function mutations in a calcium-channel alpha1-subunit gene in Xp11.23 cause incomplete X-linked congenital stationary night blindness. Nat. Genet.19 (3): 264-7. [PMID:9662400]

4. Bijveld MM, Florijn RJ, Bergen AA, van den Born LI, Kamermans M, Prick L, Riemslag FC, van Schooneveld MJ, Kappers AM, van Genderen MM. (2013) Genotype and phenotype of 101 dutch patients with congenital stationary night blindness. Ophthalmology120 (10): 2072-81. [PMID:23714322]

5. Boycott KM, Maybaum TA, Naylor MJ, Weleber RG, Robitaille J, Miyake Y, Bergen AA, Pierpont ME, Pearce WG, Bech-Hansen NT. (2001) A summary of 20 CACNA1F mutations identified in 36 families with incomplete X-linked congenital stationary night blindness, and characterization of splice variants. Hum. Genet.108 (2): 91-7. [PMID:11281458]

6. Boycott KM, Pearce WG, Bech-Hansen NT. (2000) Clinical variability among patients with incomplete X-linked congenital stationary night blindness and a founder mutation in CACNA1F. Can. J. Ophthalmol.35 (4): 204-13. [PMID:10900517]

7. Chang B, Heckenlively JR, Bayley PR, Brecha NC, Davisson MT, Hawes NL, Hirano AA, Hurd RE, Ikeda A, Johnson BA, McCall MA, Morgans CW, Nusinowitz S, Peachey NS, Rice DS, Vessey KA, Gregg RG. (2006) The nob2 mouse, a null mutation in Cacna1f: anatomical and functional abnormalities in the outer retina and their consequences on ganglion cell visual responses. Vis. Neurosci.23 (1): 11-24. [PMID:16597347]

8. Doering CJ, Hamid J, Simms B, McRory JE, Zamponi GW. (2005) Cav1.4 encodes a calcium channel with low open probability and unitary conductance. Biophys. J.89 (5): 3042-8. [PMID:16085774]

9. Doering CJ, Rehak R, Bonfield S, Peloquin JB, Stell WK, Mema SC, Sauvé Y, McRory JE. (2008) Modified Ca(v)1.4 expression in the Cacna1f(nob2) mouse due to alternative splicing of an ETn inserted in exon 2. PLoS ONE3 (7): e2538. [PMID:18596967]

10. Griessmeier K, Cuny H, Rötzer K, Griesbeck O, Harz H, Biel M, Wahl-Schott C. (2009) Calmodulin is a functional regulator of Cav1.4 L-type Ca2+ channels. J. Biol. Chem.284 (43): 29809-16. [PMID:19717559]

11. Haeseleer F, Imanishi Y, Maeda T, Possin DE, Maeda A, Lee A, Rieke F, Palczewski K. (2004) Essential role of Ca2+-binding protein 4, a Cav1.4 channel regulator, in photoreceptor synaptic function. Nat. Neurosci.7 (10): 1079-87. [PMID:15452577]

12. Hemara-Wahanui A, Berjukow S, Hope CI, Dearden PK, Wu SB, Wilson-Wheeler J, Sharp DM, Lundon-Treweek P, Clover GM, Hoda JC et al.. (2005) A CACNA1F mutation identified in an X-linked retinal disorder shifts the voltage dependence of Cav1.4 channel activation. Proc. Natl. Acad. Sci. U.S.A.102 (21): 7553-8. [PMID:15897456]

13. Hoda JC, Zaghetto F, Koschak A, Striessnig J. (2005) Congenital stationary night blindness type 2 mutations S229P, G369D, L1068P, and W1440X alter channel gating or functional expression of Ca(v)1.4 L-type Ca2+ channels. J. Neurosci.25 (1): 252-9. [PMID:15634789]

14. Hoda JC, Zaghetto F, Singh A, Koschak A, Striessnig J. (2006) Effects of congenital stationary night blindness type 2 mutations R508Q and L1364H on Cav1.4 L-type Ca2+ channel function and expression. J. Neurochem.96 (6): 1648-58. [PMID:16476079]

15. Jalkanen R, Bech-Hansen NT, Tobias R, Sankila EM, Mäntyjärvi M, Forsius H, de la Chapelle A, Alitalo T. (2007) A novel CACNA1F gene mutation causes Aland Island eye disease. Invest. Ophthalmol. Vis. Sci.48 (6): 2498-502. [PMID:17525176]

16. Jalkanen R, Mäntyjärvi M, Tobias R, Isosomppi J, Sankila EM, Alitalo T, Bech-Hansen NT. (2006) X linked cone-rod dystrophy, CORDX3, is caused by a mutation in the CACNA1F gene. J. Med. Genet.43 (8): 699-704. [PMID:16505158]

17. Klugbauer N, Marais E, Hofmann F. (2003) Calcium channel alpha2delta subunits: differential expression, function, and drug binding. J. Bioenerg. Biomembr.35 (6): 639-47. [PMID:15000524]

18. Koschak A, Reimer D, Walter D, Hoda JC, Heinzle T, Grabner M, Striessnig J. (2003) Cav1.4alpha1 subunits can form slowly inactivating dihydropyridine-sensitive L-type Ca2+ channels lacking Ca2+-dependent inactivation. J. Neurosci.23 (14): 6041-9. [PMID:12853422]

19. Kotturi MF, Jefferies WA. (2005) Molecular characterization of L-type calcium channel splice variants expressed in human T lymphocytes. Mol. Immunol.42 (12): 1461-74. [PMID:15899519]

20. Liu X, Yang PS, Yang W, Yue DT. (2010) Enzyme-inhibitor-like tuning of Ca(2+) channel connectivity with calmodulin. Nature463 (7283): 968-72. [PMID:20139964]

21. Mansergh F, Orton NC, Vessey JP, Lalonde MR, Stell WK, Tremblay F, Barnes S, Rancourt DE, Bech-Hansen NT. (2005) Mutation of the calcium channel gene Cacna1f disrupts calcium signaling, synaptic transmission and cellular organization in mouse retina. Hum. Mol. Genet.14 (20): 3035-46. [PMID:16155113]

22. McRory JE, Hamid J, Doering CJ, Garcia E, Parker R, Hamming K, Chen L, Hildebrand M, Beedle AM, Feldcamp L, Zamponi GW, Snutch TP. (2004) The CACNA1F gene encodes an L-type calcium channel with unique biophysical properties and tissue distribution. J. Neurosci.24 (7): 1707-18. [PMID:14973233]

23. Morgans CW, Gaughwin P, Maleszka R. (2001) Expression of the alpha1F calcium channel subunit by photoreceptors in the rat retina. Mol. Vis.7: 202-9. [PMID:11526344]

24. Murakami M, Nakagawasai O, Fujii S, Kameyama K, Murakami S, Hozumi S, Esashi A, Taniguchi R, Yanagisawa T, Tan-no K, Tadano T, Kitamura K, Kisara K. (2001) Antinociceptive action of amlodipine blocking N-type Ca2+ channels at the primary afferent neurons in mice. Eur. J. Pharmacol.419 (2-3): 175-81. [PMID:11426839]

25. Nakamura M, Ito S, Piao CH, Terasaki H, Miyake Y. (2003) Retinal and optic disc atrophy associated with a CACNA1F mutation in a Japanese family. Arch. Ophthalmol.121 (7): 1028-33. [PMID:12860808]

26. Nakamura M, Ito S, Terasaki H, Miyake Y. (2001) Novel CACNA1F mutations in Japanese patients with incomplete congenital stationary night blindness. Invest. Ophthalmol. Vis. Sci.42 (7): 1610-6. [PMID:11381068]

27. Naylor MJ, Rancourt DE, Bech-Hansen NT. (2000) Isolation and characterization of a calcium channel gene, Cacna1f, the murine orthologue of the gene for incomplete X-linked congenital stationary night blindness. Genomics66 (3): 324-7. [PMID:10873387]

28. Omilusik K, Priatel JJ, Chen X, Wang YT, Xu H, Choi KB, Gopaul R, McIntyre-Smith A, Teh HS, Tan R et al.. (2011) The Ca(v)1.4 calcium channel is a critical regulator of T cell receptor signaling and naive T cell homeostasis. Immunity35 (3): 349-60. [PMID:21835646]

29. Qin N, Yagel S, Momplaisir ML, Codd EE, D'Andrea MR. (2002) Molecular cloning and characterization of the human voltage-gated calcium channel alpha(2)delta-4 subunit. Mol. Pharmacol.62 (3): 485-96. [PMID:12181424]

30. Shaltiel L, Paparizos C, Fenske S, Hassan S, Gruner C, Rötzer K, Biel M, Wahl-Schott CA. (2012) Complex regulation of voltage-dependent activation and inactivation properties of retinal voltage-gated Cav1.4 L-type Ca2+ channels by Ca2+-binding protein 4 (CaBP4). J. Biol. Chem.287 (43): 36312-21. [PMID:22936811]

31. Singh A, Hamedinger D, Hoda JC, Gebhart M, Koschak A, Romanin C, Striessnig J. (2006) C-terminal modulator controls Ca2+-dependent gating of Ca(v)1.4 L-type Ca2+ channels. Nat. Neurosci.9 (9): 1108-16. [PMID:16921373]

32. Sinnegger-Brauns MJ Huber IG Koschak A Wild C Obermair GJ Einzinger U Hoda JC Sartori SB Striessnig J. (2008) Expression and 1,4-dihydropyridine-binding properties of brain L-type calcium channel isoforms. Mol Pharmacol.Epub (issue number): pages. [PMID:19029287]

33. Stockner T, Koschak A. (2013) What can naturally occurring mutations tell us about Ca(v)1.x channel function?. Biochim. Biophys. Acta1828 (7): 1598-607. [PMID:23219801]

34. Strom TM, Nyakatura G, Apfelstedt-Sylla E, Hellebrand H, Lorenz B, Weber BH, Wutz K, Gutwillinger N, Rüther K, Drescher B, Sauer C, Zrenner E, Meitinger T, Rosenthal A, Meindl A. (1998) An L-type calcium-channel gene mutated in incomplete X-linked congenital stationary night blindness. Nat. Genet.19 (3): 260-3. [PMID:9662399]

35. Wahl-Schott C, Baumann L, Cuny H, Eckert C, Griessmeier K, Biel M. (2006) Switching off calcium-dependent inactivation in L-type calcium channels by an autoinhibitory domain. Proc. Natl. Acad. Sci. U.S.A.103 (42): 15657-62. [PMID:17028172]

36. Wang Q, Gao Y, Li S, Guo X, Zhang Q. (2012) Mutation screening of TRPM1, GRM6, NYX and CACNA1F genes in patients with congenital stationary night blindness. Int. J. Mol. Med.30 (3): 521-6. [PMID:22735794]

37. Wutz K, Sauer C, Zrenner E, Lorenz B, Alitalo T, Broghammer M, Hergersberg M, de la Chapelle A, Weber BH, Wissinger B, Meindl A, Pusch CM. (2002) Thirty distinct CACNA1F mutations in 33 families with incomplete type of XLCSNB and Cacna1f expression profiling in mouse retina. Eur. J. Hum. Genet.10 (8): 449-56. [PMID:12111638]

38. Zeitz C, Labs S, Lorenz B, Forster U, Uksti J, Kroes HY, De Baere E, Leroy BP, Cremers FP, Wittmer M et al.. (2009) Genotyping microarray for CSNB-associated genes. Invest. Ophthalmol. Vis. Sci.50 (12): 5919-26. [PMID:19578023]

39. Zeitz C, Minotti R, Feil S, Mátyás G, Cremers FP, Hoyng CB, Berger W. (2005) Novel mutations in CACNA1F and NYX in Dutch families with X-linked congenital stationary night blindness. Mol. Vis.11: 179-83. [PMID:15761389]

40. Zito I, Allen LE, Patel RJ, Meindl A, Bradshaw K, Yates JR, Bird AC, Erskine L, Cheetham ME, Webster AR et al.. (2003) Mutations in the CACNA1F and NYX genes in British CSNBX families. Hum. Mutat.21 (2): 169. [PMID:12552565]

To cite this database page, please use the following:

William A. Catterall, Edward Perez-Reyes, Terrance P. Snutch, Joerg Striessnig.
Voltage-gated calcium channels: Cav1.4. Last modified on 30/01/2014. Accessed on 21/04/2014. IUPHAR database (IUPHAR-DB), http://www.iuphar-db.org/DATABASE/ObjectDisplayForward?objectId=531.

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