Slo3
Description: potassium large conductance pH-sensitive channel, subfamily M, alpha member 3 Gene: Kcnu1 Alias: Slo3, kcnu1, Kcnma3, KCa5, Kcnma3, KCa5.1
The mouse Slo3 gene (KCNMA3) encodes a K+ channel that is regulated by changes in cytosolic pH. Like Slo1 subunits responsible for the Ca2+ and voltage-activated BK-type channel, the Slo3 α subunit contains a pore module with homology to voltage-gated K+ channels and also an extensive cytosolic C terminus thought to be responsible for ligand dependence. For the Slo3 K+ channel, increases in cytosolic pH promote channel activation, but very little is known about many fundamental properties of Slo3 currents. (Zhang [165])
Slo3 shares the most extensive sequence homology with Slo1 (Schreiber 1998 [1160]).
Transcript
Species | NCBI accession | Length (nt) | |
---|---|---|---|
Human | NM_001031836.3 | 3692 | |
Mouse | NM_008432.3 | 3548 |
Protein Isoforms
Isoforms
Post-Translational Modifications
K+ channels formed from α subunits encoded by the Slo gene family (Adelman et al., 1992 [1156]; Butler et al., 1993 [1157]) are characterized by a large cytosolic C-terminal structure that is thought to be involved in ligand-dependent regulation of the channels (Wei et al., 1994 [1158]; Schreiber and Salkoff [1159], 1997; Schreiber et al. , 1998 [1160]; Bhattacharjee et al., 2002 [1161]; Jiang et al., 2002 [625]; Shi et al., 2002 [1131]; Xia et al., 2002 [1136]; Bhattacharjee et al., 2003 [1141]; Yuan et al., 2003 [1139]; Xia et al., 2004 [164]). In fact, the hallmark for each member of the Slo family appears to be regulation by a specific cytosolic ligand: pH for Slo3 (Schreiber et al., 1998 [1160]; Xia et al., 2004 [164]).
Slo3 predicted AlphaFold size
Methodology for AlphaFold size prediction and disclaimer are available here
Slo1 and Slo3 differ in two primary ways: first, the intrinsic voltage dependence of the Slo3 closed–open equilibrium is weaker, and, second, voltage sensor movement in Slo3 is much more weakly coupled to channel opening. Both activation and deactivation are best described by two exponential components, both of which are only weakly voltage dependent. Qualitatively, the properties of the two kinetic components in the activation time course suggest that increases in pH increase the fraction of more rapidly opening channels. (Zhang [165])
In contrast to the wide distribution of channels arising from either Slo1 and Slo2.x subunits, Slo3 has a much more limited pattern of expression than the other family members, being found predominantly in mouse testis (Schreiber et al., 1998 [1160]).
In contrast to Slo1, Slo3 is insensitive to cytosolic Ca2+ and appears sensitive to cytosolic pH (Schreiber et al., 1998 [1160]; Xia et al., 2004 [164]).
References
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et al.
Bovine and mouse SLO3 K+ channels: evolutionary divergence points to an RCK1 region of critical function.
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Xia XM
et al.
Ligand-dependent activation of Slo family channels is defined by interchangeable cytosolic domains.
J. Neurosci.,
2004
Jun
16
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Zhang X
et al.
Slo3 K+ channels: voltage and pH dependence of macroscopic currents.
J. Gen. Physiol.,
2006
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Jiang Y
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Crystal structure and mechanism of a calcium-gated potassium channel.
Nature,
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Shi J
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Mechanism of magnesium activation of calcium-activated potassium channels.
Nature,
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Xia XM
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Multiple regulatory sites in large-conductance calcium-activated potassium channels.
Nature,
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Yuan A
et al.
The sodium-activated potassium channel is encoded by a member of the Slo gene family.
Neuron,
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Bhattacharjee A
et al.
Slick (Slo2.1), a rapidly-gating sodium-activated potassium channel inhibited by ATP.
J. Neurosci.,
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Adelman JP
et al.
Calcium-activated potassium channels expressed from cloned complementary DNAs.
Neuron,
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Butler A
et al.
mSlo, a complex mouse gene encoding "maxi" calcium-activated potassium channels.
Science,
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Wei A
et al.
Calcium sensitivity of BK-type KCa channels determined by a separable domain.
Neuron,
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Schreiber M
et al.
Transplantable sites confer calcium sensitivity to BK channels.
Nat. Neurosci.,
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Schreiber M
et al.
Slo3, a novel pH-sensitive K+ channel from mammalian spermatocytes.
J. Biol. Chem.,
1998
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Bhattacharjee A
et al.
Localization of the Slack potassium channel in the rat central nervous system.
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2002
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