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potassium voltage-gated channel, shaker-related subfamily, member 1
Synonyms: Kv1.1 kcna1 kcpvd. Symbol: Kcna1


The α-subunit of the Kv1 family are mammalian homologous of the Shaker subunits originally described in Drosophila[1348]. Multiple members of the Kv1(Kv1.1-1.6) subfamily have been found in the CNS. Kv1.1 is a shaker voltage-gated potassium channel encoded by the KCNA1 gene [252]. Kv1.1 and Kv1.2 are low-voltage activated (LVA) channels that open with small depolarizations at or below rest- ing potential [1590] Kcna1 gene is conserved in human, chimpanzee, dog, cow, mouse, chicken and zebra fish. The α-subunit of Kv1 are known to form heteromultimers [734]. In the nervous system Kv1.1 appears to be widely distributed; it is highly expressed in the juxtaparanodal regions of myelinated axons. However, the channel is also expressed in unmyelinated axons, cell somas, axon terminals, and in some dendrites [734]. Disruption of the Kcna1 gene in mice has displayed frequent spontaneous seizures. [1345].


The Kcna1 gene is conserved in human, chimpanzee, dog, cow, mouse, chicken and zebrafish. It contains only one exon hence no splicing event possible.

Kcna1 KO model

Mice lacking Kcna1-gene-encoded Kv1.1 shaker-like potassium channels exhibit severe seizures and die prematurely[346].

Kcna1 : potassium voltage-gated channel, shaker-related subfamily, member 1

RGD ID Chromosome Position Species
2949 4 163011777-163013522 Rat
1552897 6 126586481-126595819 Mouse
1346938 12 5019073-5027422 Human



Kv1.l Phylogeny


No splicing variants known. Kcna1 mRNA is subjected to RNA editing[371].

Acc No Sequence Length Source
NM_173095 NCBI
NM_010595 NCBI
NM_000217 NCBI


Accession Name Definition Evidence
GO:0016021 integral to membrane Penetrating at least one phospholipid bilayer of a membrane. May also refer to the state of being buried in the bilayer with no exposure outside the bilayer. When used to describe a protein, indicates that all or part of the peptide sequence is embedded in the membrane. IEA
GO:0008076 voltage-gated potassium channel complex A protein complex that forms a transmembrane channel through which potassium ions may cross a cell membrane in response to changes in membrane potential. IEA
GO:0016020 membrane Double layer of lipid molecules that encloses all cells, and, in eukaryotes, many organelles; may be a single or double lipid bilayer; also includes associated proteins. IEA
GO:0016324 apical plasma membrane The region of the plasma membrane located at the apical end of the cell. IMP
GO:0044224 juxtaparanode region of axon A region of an axon near a node of Ranvier that is between the paranode and internode regions. IEA


Amitriptyline and Retigabine

Amitriptyline inhibited Kv1.1 and Kv7.2/7.3 channels in a concentration-dependent and reversible manner. The IC50-value was 22 +/- 3 microM (n = 33) and 10 +/- 1 microM (n = 40), respectively. Since amitriptyline inhibited Kv1.1 and Kv7.2/7.3 channels only at toxicologically relevant plasma concentrations, our results suggest a role for these channels in the neuroexcitatory side effects of amitriptyline. As the inhibitory effects of amitriptyline were reversed by retigabine, a combination of amitriptyline and retigabine could be of additional benefit in the therapy of neuropathic pain [1707]

Kv Family

Studies have demonstrated that in the nervous system Kv1.1 can combine with KV1.2, 1.4 or Kv1.6 [432]. However homomers of Kv1.1 have not been detected in the nervous system[432].

Syntaxin 1A

Single Kv1.1 channels interact with syntaxin 1A in the following way: Syntaxin decreases the unitary conductance of all conductance states (two subconductances and a full conductance) and decreases their open probabilities by prolongation of mean closed dwell-times at depolarized potentials. Syntaxin 1A increases the probabilities of the subconductance states at subthreshold potentials. This leads to decrease of the macroscopic conductance at potentials above threshold and increase of it at threshold potentials. [1]

Fatty acid ethyl esters

Kv1.1 structure

fatty acid ethyl esters, dramatically accelerate the kinetics of the voltage-induced activation of the human brain delayed rectifier potassium channel, Kv1.1. Specifically, the external application of ethyl oleate (20 μM) to Sf9 cells expressing the recombinant Kv1.1 channel resulted in a decrease in the rise times of the macroscopic current [1591]

Kvbeta1 and Kvbeta2 beta-subunits with Kv1

A much larger portion of the total brain pool of Kv1-containing channel complexes was found associated with Kvbeta2 than with Kvbeta1. Single- and multiple-label immunohistochemical staining indicated that Kvbeta1 codistributes extensively with Kv1.1 and Kv1.4 in cortical interneurons, in the hippocampal perforant path and mossy fiber pathways, and in the globus pallidus and substantia nigra. This suggests Kvbeta1 and Kvbeta2 associate and colocalize with Kv1 alpha-subunits in native tissues and provide a biochemical and neuroanatomical basis for the differential contribution of Kv1 alpha- and beta-subunits to electrophysiologically diverse neuronal K+ currents [1593]


α-dendrotoxin can influence spike latency in Kv1.1 channels. Application of DTX slightly shifted the AP threshold to more hyperpolarized potentials [1595]Dendrotoxin-κ (DTX-κ)a Kv1.1 specific channel blocker was shown to inhibit proliferation of gefitinib-resistant H460 non-small cell lung cancer (NSCLC) cells in vitro and in vivo in a nude mice model[1890]

General anaesthetics

In heterologous expression systems, sevoflurane, isoflurane, and desflurane at subsurgical concentrations potentiated delayed rectifier Kv1 channels at low depolarizing potentials. In mouse thalamic brain slices, sevoflurane inhibited firing frequency and delayed the onset of action potentials in CMT neurons, and ShK-186, a Kv1.3-selective inhibitor, prevented these effects. Our findings demonstrate the exquisite sensitivity of delayed rectifier Kv1 channels to modulation by volatile anesthetics and highlight an arousal suppressing role of Kv1 channels in CMT neurons during the process of anesthesia [1597]


Ankyrin-3 (ANK3) was identified as a binding partner of Kv1.1 and was enriched in isolated distal convoluted tubules as compared to whole kidney. Electrophysiology studies performed in HEK293 cells expressing Kv1.1 showed that ANK3 significantly inhibited Kv1.1-mediated currents (267 compared to 125 pA/pF) for control and ANK3, respectively [1763]


Scorpion peptide venom urotoxin binds with high affinity to hKv1.2 (IC50 of 160 pM),hKv1.1 and hKv1.3 channels (IC50 = 253 nM and 91 nM respectively)[1889]


Non-peptidic snail toxin 6-bromo-2-mercaptotryptamine dimer (BrMT)2 and its derivatives were reported to slow Kv1.1 channel activation [1896]


Nociceptive processing in trigeminal ganglion (TG) neurons involves endogenous H2S generating enzyme (CBS) co-localization with Kv1.1 and Kv1.4. Application of NaHS, an H2S donor, supresses IK density with impact on neuronal excitability[1893]

Sensitisation to cytotoxins

Tumour cells expressing Kv1.1 or Kv1.3 are more sensitive to cytotoxins (staurosporine, C2-ceramide, cisplatin and clofazimine)[1899]

Phosphatidylinositol-4,5-bisphosphate (PIP2)

Kv1.1/Kv1.2 heteromeric channels in spiral ganglion neurons are positively regulated by phosphatidylinositol-4,5-bisphosphate (PIP2), a possible intrinsic control of rapid spike adaption in the auditory nerve [1914]



Crystal Structure

Kv1.1 structure Kv1.1 structureThe protein is believed to have six domains (S1-S6) with the loop between S5 and S6 forming the channel pore. In general the functional K+ channels is a tetramer, typically of four identical subunits folded around a central pore. Since the P-loop region of various K+ channels consists of the turret, the pore helix, the selectivity filter, and share strong sequence similarity suggests that it may be possible to generate homology models by using KcsA [1346] as a template[1347]. The functional channel is claimed to be heteromeric. The N-terminus of the protein associates with β subunits. These subunits regulate channel inactivation as well as it's expression. The C-terminus is associated with a PDZ domain protein which is involved in channel targeting. Recent experiments show that homomeric Kv1.1 channels are retained in the endoplasmic reticulum [453], which support the hypothesis of heteromeric assembly [329].

Pharmacological Characteristics

Pharmacological characteristics of Kv1.1- and Kv1.2-containing channels are influenced by the stoichiometry and positioning of their α subunits.The findings of the present study support the possibility of α subunits being precisely arranged in Kv1 channels, rather than being randomly assembled. This is important in designing drugs with abilities to inhibit particular oligomeric Kv1 subtypes, with the goal of elevating neuronal excitability and improving neurotransmission in certain diseases [1603]



Assembly of Kv1.1 with Kv1.4 prevents axonal localization but not surface expression, while inclusion of Kv1.2 imparts clustering at presynaptic sites and decreases channel mobility within the axon [1350].


When exogenously expressed in neurons, Kv1 proteins are detected in both dendrites and axons. However, detection of surface-expressed channels has revealed that Kv1 channels are only expressed in the axonal membrane. This has led to the speculation that Kv1 may be localized to the axonal surface through compartment-specific endocytosis or compartment-specific vesicle fusion. Conversely, recent studies have indicated that axonal targeting of Kv1 channels is mediated by selective transport to the axon. [1351]


Highly dense clusters of Kv1.1 and Kv1.2 are found in the juxtaparanodal (JPX) region next to the nodes of Ranvier (NORs), at axonal initial segments (AIS), and in the pinceau region terminals of cerebellar basket cells. Hippocampal expression of Kv1.1, Kv1.2, and Kv1.4 channels occurs in the middle molecular layer of the dentate gyrus, where the channels are highly expressed in the axons and terminals of the medial perforate path [1590]

Kv1.1 and Kv1.2 subunits show identical distribution along the AIS of neurons from the forebrain and cerebellum of adult male Wistar rats when both are present together, which may mean that they share the same anchoring machinery and may form heteromeric channels. A couple of anchoring proteins including Caspr2 [441] and PSD-93 [427] were implicated in clustering Kv1 channels in the AIS. Recent experiments show that homomeric Kv1.1 channels are retained in the endoplasmic reticulum [453], which support the hypothesis of heteromeric assembly [329].

Expression of Kv1.1

Both endogenous Kv1.1 mRNA and newly synthesized Kv1.1 protein were found prominently in dendrites associated with translational “hotspots.” A unique aspect of local mRNA translation in dendrites is the selective localization of protein synthesis machinery at or near synaptic sites and an accumulation of mRNAs near synaptic sites that have recently experienced strong activity, a form of synaptic tagging. That Kv1.1 mRNA was found at such sites prompted Rabb-Graham et al. to test whether translation of this component subunit of the Kv1 channels, critical to regulating dendritic excitability, could be regulated by neuronal activity, as has been shown for a subset of other dendritic proteins [1770]

RNA editing and trafficking

RNA editing of a single amino acid (I400V)located in the inner pore cavity of Kv1.1 was shown to reduce surface expression of Kv1.1 and whole-cell currents. Kv1.4 expression was not subject to this trafficking regulation [1898]


Mammalian Brain

Kv1.1 is widely expressed in mammalian brain but rare in mouse myocardium.[346]


Although broadly expressed throughout many regions of the central nervous system—including hippocampus, cerebellum, and brainstem nuclei—differential expression of Kv channels facilitates the organization and transfer of neuronal information [1590]


Hippocampal expression of Kv1.1, Kv1.2, and Kv1.4 channels occurs in the middle molecular layer of the den- tate gyrus, where the channels are highly expressed in the axons and terminals of the medial perforant path. Localization to subpopulations of interneurons was found in hilus and CA1 [1590]


Renal expression of Kv1.1 was attested for cells of the distal convoluted tubule and associated with Mg2+ re-absorbation [1885]


Kv1.1 expression in human atria suggests a cardiac role. Kv1.1 deficiency may elicit a higher susceptibility to atrial fibrillation (AF)[1920]


Neuronal Control

A fast delayed rectifying K+ channel in heterologous expression systems is encoded by Kv1.1. Neuronal deficiency or blockade of Kv1.1 influenced learning negatively or increased transmitter release, respectively, which implies the role of Kv1.1 in repolarizing the membrane in axons and at synaptic terminals and impulse conduction. [329] [1592]

Kv1.1-containing channels are critical for temporal precision during spike initiation [1772]

Mice lacking Kcna1-gene-encoded Kv1.1 shaker-like potassium channels exhibit severe seizures and die prematurely. [346] Recordings from neurons in Kcna1-null animals demonstrated that less current was required to produce AP firing and that these Kv1.1-null neurons typically fired many APs compared with the single AP observed in wildtype mice [1349]. These results indicate that Kv1.1 plays a critical role in setting both the point at which a neuron generates an AP and for a given stimulus whether the cell fires single or multiple APs.

Kv1 channels have a defined task in shaping the AP of presynaptic compartments in the sub millisecond range [1595]

In DRG neurons the inhibition of Kv1.1 produces a nearly twofold increase in the number of APs evoked by a ramp of depolarizing current. Associated with the increased AP firing were reductions in both the firing threshold and the rheobase[252].

Deminished expression of the Kv1.1 channel subunit in parvalbumin-positive, fast-spiking interneurons (FSI) coincides with their reduced first-spike latency. This dysfunction, reported after transient disruption of NMDA signaling during neonatal development, likely contributes to the pathophysiology of Schizophrenia [1900]

Axonal Kv1.1 channels in CA3 neurons determine glutamate release in a time-dependent manner through the control of the presynaptic spike waveform [1911]

Small pyramidal neurons in layer 2 of the rodent granular retrosplenial cortex (GRS), associated with head-direction cells, exhibit a late-spiking (LS) firing property as a consequence of delayed rectifier and A-type potassium channels (Kv1.1, Kv1.4 and Kv4.3)[1891]

Kv1.1 channels shape the firing characteristics of single-spiking Mauthner cells, which are reticulospinal neurons (RSNs) in the hindbrain of embryonal zebrafish involved in escape behaviour[1892] The aquisition of these unique firing properties requires the coexpression of Kvβ2 subunits along with Kv1.1 channels [1902]


Experiments found that in cells where the Kv1.1 and Kv1.2 subunits are coexpressed with the Nav1.6 subunit, their subcellular distributions are correlated. For instance, in AISs where the Nav1.6 subunit distribution shows a strong gradient, the Kv1.1/Kv1.2 subunits also increase in density toward the distal part of the AIS [329].

The presence of Kv1 channels at the AIS has been demonstrated in a variety of cell types, where they have been shown to play important roles in regulating the timing of AP initiation and AP firing patterns [1590]

Input deprivation switched Kv channel expression at the AIS from Kv1.1 to Kv7.2 enhancing neuronal excitability [1910]

The transmembrane disintegrin ADAM11 is essential for the localization of Kv1.1 and Kv1.2 subunit complexes to the specialized axonal ending of the basket cell (pinceau) encapsulating the Purkinje AIS. Absence of Kv1 channels at the Baskets cells distal terminal due to Adam11 mutation eliminates the ultrarapid ephaptic inhibitory synchronization of Purkinje cell firing [1915]

Seizure, Epilepsy and Ataxia

Kcna1 and Kcna2, is associated with neu- rologic pathologies including epilepsy and ataxia in humans and in rodent models. Kv1.1 and Kv1.2 knockout mice both have seizures beginning early in development; however, each express a different seizure type (pathway) [1590] Characterization of the Kv1.1 I262T and S342I mutations associated with episodic ataxia 1 with distinct phenotypes [1767]Episodic ataxia associated mutations alter subunit surface expression of Kv1 heteromers [1886]

Seizure onset in KCNA1 null mice was affected by circadian rythmicity as demonstrated by epidural EEG [1917]

In a cohort study of 39 participants with clinical phenotype of AE1 10 different pathogenic point mutations in KCNA1 were identified accounting for 85% of the subjects [1907] A point mutation of Kv1.1(I262M) causing phenotypic EA1 was shown to lead to a defective channel in HEK cell expression system [1908]

The combination of copy number variants (CNVs) of KCNA1 and single nucleotide polymorphisms (SNPs) of SCN1A may constitute a principal risk factor for sudden unexpected death in epilepsy (SUDEP)[1906] Physiological examination of KCNA -/- mice suggests a role for the vagus nerve in mediating seizure related bradycardy and SUDEP [1909] Spreading depolarization in the brainstem of KCNA -/- mouse may cause sudden cardiorespiratory arrest[1913]

RNA editing of the Kv1.1 mRNA at the functionally relevant I/V site was found to be inversely correlated to the duration of epileptic seizures in patients [1895]

Spontaneous seizures in Kcna1-null mice activate select limbic circuits, as revealed by C-Fos immunohistochemistry, suggesting the recruitment of extrahippocampal networks in particular the amygdala and hilus during epilepsy[1921]

Hearing impairment

A study of the genetic basis of episodic ataxia type 1 in 15 individuals of four families_reports new mutations that all caused a loss of K(v)1.1 channel function. 4 cases of deafness in this group suggest a possible link between Kv1.1 dysfunction and hearing impairment [1897]

Behavioral effect of Kv1.1 deletion impedes primarily binaural integration and mimics monaural hearing [1919]

Pain Sensation

Finally, mice lacking Kv1.1 channels exhibit signs of neuronal hyperexcitability such as spontaneous seizures and enhanced pain sensation [1592] Kv1.1 channels act as mechanical brake in the senses of touch and pain [1765]


Potassium channel KCNA1 modulates oncogene-induced senescence and transformation [1764]


Functional analysis of the Kv1.1 N255D mutation associated with autosomal dominant hypomagnesemia [1769] N255D mutation of KCNA1 results in a nonfunctional channel compromising Mg2+ re-absorption in cells of the kidneys distal convoluted tubule [1885]

Hyperthermia, Migraine

A single nucleotide change in KCNA1 (c.555C>G) changes a highly conserved residue (p.C185W) of Kv1.1 and may cause a dominant-negative phenotype including hyperthermia and severe migraine [1918]

Neuronal Activity and Cell Volume

Kv1.1 blockade may target neurons and astrocytes, and modulate neuronal activity and neural cell volume, which may partly account for the attenuation of the neurological deficits. We propose that Kv1.1 blockade has a broad therapeutic potential in neuroinflammatory diseases (multiple sclerosis, stroke, and trauma).

Ketogenic diet (KD)attenuates CA3-generated pathologic oscillations presumably by dampening hyperactive mossy fiber in Kv1.1 alpha KO mice [1888]

Knock Out

Loss of the Kv1.1 potassium channel promotes pathologic sharp waves and high frequency oscillations in in vitro hippocampal slices [1766]

Kcna1 gene deletion lowers the behavioral sensitivity of mice to small changes in sound location and increases asynchronous brainstem auditory evoked potentials but does not affect hearing threshold [1768]

KCNA1 null mice also displayed vagus nerve related bradycardie [1909]


Mutation of position F184 of the Shaker channel shows that F184 interacts with the gating charges of S4 subunit and creates a functional link to the selectivity filter of the neighboring subunit.[1884]

Tetraethylammonium (TEA)inhibits Kv1.1 by binding Tyr379 in the pore region. Mutagenesis of Kv1.2 to resemble Kv1.1 and the ratio of subunit assembly of Kv1.1 and Kv1.2 were shown to alter TAE susceptiblity [1603]

In rats carrying a missence mutation in the S4 voltage-sensor domain of KCNA1 myokymia,neuromyotonia and generalized tonic–clonic seizures are the dominant phenotypes displayed [1887]

A C-terminus-truncated mutant of Kv1.1 is associated with severe drug-resistant episodic ataxia type 1. Cultured rat hippocampal neurons expressing this mutant displayed increased excitability and neurotransmitter release probability compared to those trancduced with the wild type gene coding for Kv1.1 [1903]

Transcriptional Regulation

Evidence for combinatorial regulation of gene expression of the Drosophila Shaker channel homolog of Kv1.1 by Isl and Lim3 has come from experiments using DNA adenine methyltransferase identification (DamID)[1901]

miRNA repression

Kv1.1 mRNA translation is repressed by miR-129 in the presence of mTORC1 kinase activity. RNA-binding protein HuD promotes Kv1.1 mRNA translation in the absence of mTORC1 activity [1894] Post status epilepticus Kv1.1 was proposed to be repressed in two phases; an initial mTOR-dependent repression sensitive to rapamycin and after 21 days through persistent inhibition by miR-129-5p [1905]


Calcium-dependend binding of calmodulin to Kvβ1.1 decelerates the Kvβ1.1 induced inactivation of Kv1.1 and Kv1.4 channels [1916]


SIngle channel current in CHO

Kv1.1 Recordings were performed at potentials ranging from −50 to +70 mV with 20 mV increments [1]. For single channel currents in CHO cells [1773]

Rat Kv1.1 in CHO Cells

Kv1.1 The effect of glycosylation on Kv1.1 potassium channel function was investigated in mammalian cells stably transfected with Kv1.1 or Kv1.1N207Q. Macroscopic current analysis showed that both channels were expressed but Kv1.1N207Q, which was not glycosylated, displayed functional differences compared with wild-type, including slowed activation kinetics, a positively shifted VÎ, a shallower slope for the conductance versus voltage relationship, slowed C-type inactivation kinetics, and a reduced extent of and recovery from C-type inactivation. Kv1.1N207Q activation properties were also less sensitive to divalent cations compared with those of Kv1.1 [1835]

Kv1.1 kinetics

Kv1.1 These currents exhibited the rapid activation and little time-dependent inactivation that is characteristic of delayed rectifier potassium currents (IK) [252]

Kinetics of mKv1.1 in X. oocytes

Kv1.1 structure Corroboration of steady-state activation and kinetic behavior in single channel patches of Kv1.1. Because current amplitudes were variable among different macro-patch recordings (due to different distribution of the channels on the cell surface), the analyzed amplitudes were normalized to the maximal amplitude observed in the measured range in each group. [1]

Kv1.1/Kv1.4 channels and mutants recorded in Xenopus oocytes

In Kv1.1/Kv1.4 channels, the Kv1.4 subunits refer rapid inactivation properties to otherwise noninactivating Kv1.1 channels via their N-terminal inactivation domains. Normalized whole cell currents were recorded at +60 mV from X. laevis oocytes coexpressing Kv1.4WT and Kv1.1EA1 mutants and compared to WT control traces. The results showed that the N-type inactivation rates of Kv1.1/Kv1.4 channels is faster in I177N and E325D mutations and slower in channels with the V404I and V408A mutations.[1886]

hKv1.1 currents in CHO cells and inhibition by urotoxin

Whole-cell hKv1.1 currents were measured in Chinese hamster ovary (CHO) cells during a voltage pulse to +60 mV for 300 ms, and a repolarizing step to 250 mV for 100 milliseconds at intervals of 2.7 seconds. hKv1.1 currents were fast and reversibly inhibited in the presence of 1 mM urotoxin.[1889]

Kv1.1 currents in HEK cells and effect of EA1-associated mutation

HEK293 cells were transiently transfected with Kv1.1 channels and mutant variants. Currents were elicited by application of square voltage steps from -80 mV to +50 mV in 200 ms intervals from a holding voltage of -80 mV. Tail currents were evoked by extracellularly added potassium. In WT Kv1.1-expressing cells fast delayed rectifying currents were recorded at depolarizing potentials and density currents of 186 +- 42 pA/pF were measured. In Kv1.1 I262M-mutant expressing cells currents were significantly (P < 0.05) reduced with recorded density currents of 14 +- 3 pA/pF. The mutated variant elicits a dominant negative effect when co-expressed with WT Kv1.1.[1908]

Comparison of Kv1.1 Wt and Kv1.1 F184C currents in Xenopus oocytes

The Mutation F184C in Kv1.1 associated with of episodic ataxia type I (EA1) impaires fast and slow inactivation of Kv1.1.[1884]

rKv1.1 currents in Xenopus oocytes and effects of scorpion venom K blockers

Rat Kv1.1 currents were measured in Xenopus oocytes. Further, the effects on the rKv1.1 by potassium channel-blocking toxins from the Mesobuthus eupeus scorpion venom were measured in Xenopus oocytes. Using the two-electrode voltage clamp technique eight high affinity Kv1.1 channel blockers were identified.[2062]


Markov Model

Kv1.1 A model simulating Kv1.1 behavior in the presence and absence„ of syx, based on a Hidden Markov Model (HMM) [1]

Hodgkin and Huxley type model

Kv1.1 Kv1.1 [1594]

[1] Kv1.1 (Model ID = 18)

Model was built from [252]

Animalrat 80
CellType Oocyte
Age 0 Days
Reversal -65.0 mV
Ion K +
Ligand ion
Reference M J Christie et. al; Science 1989 Apr 14
mpower 1.0
mInf 1.0000/(1+ exp((v - -30.5000)/-11.3943))
mTau 30.0000/(1+ exp((v - -76.5600)/26.1479))
hpower 2.0
hInf 1.0000/(1+ exp((v - -30.0000)/27.3943))
hTau 15000.0000/(1+ exp((v - -160.5600)/-100.0000))

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