Family Search for PF11879 (DUF3399)

PF11879 hits 24 sequences in PaperBLAST's database above the trusted cutoff. Showing hits to curated sequences only. Or see all hits or try another family.

KCND2_HUMAN / Q9NZV8 A-type voltage-gated potassium channel KCND2; Potassium voltage-gated channel subfamily D member 2; Voltage-gated potassium channel subunit Kv4.2 from Homo sapiens (Human) (see 23 papers)
Aligns to 470:546 / 630 (12.2%), covers 97.4% of PF11879, 126.7 bits

• function: Voltage-gated potassium channel that mediates transmembrane potassium transport in excitable membranes, primarily in the brain. Mediates the major part of the dendritic A-type current I(SA) in brain neurons (By similarity). This current is activated at membrane potentials that are below the threshold for action potentials. It regulates neuronal excitability, prolongs the latency before the first spike in a series of action potentials, regulates the frequency of repetitive action potential firing, shortens the duration of action potentials and regulates the back-propagation of action potentials from the neuronal cell body to the dendrites. Contributes to the regulation of the circadian rhythm of action potential firing in suprachiasmatic nucleus neurons, which regulates the circadian rhythm of locomotor activity (By similarity). Functions downstream of the metabotropic glutamate receptor GRM5 and plays a role in neuronal excitability and in nociception mediated by activation of GRM5 (By similarity). Mediates the transient outward current I(to) in rodent heart left ventricle apex cells, but not in human heart, where this current is mediated by another family member. Forms tetrameric potassium-selective channels through which potassium ions pass in accordance with their electrochemical gradient (PubMed:10551270, PubMed:11507158, PubMed:14623880, PubMed:14695263, PubMed:14980201, PubMed:15454437, PubMed:16934482, PubMed:19171772, PubMed:24501278, PubMed:24811166, PubMed:34552243, PubMed:35597238). The channel alternates between opened and closed conformations in response to the voltage difference across the membrane (PubMed:11507158). Can form functional homotetrameric channels and heterotetrameric channels that contain variable proportions of KCND2 and KCND3; channel properties depend on the type of pore-forming alpha subunits that are part of the channel. In vivo, membranes probably contain a mixture of heteromeric potassium channel complexes. Interaction with specific isoforms of the regulatory subunits KCNIP1, KCNIP2, KCNIP3 or KCNIP4 strongly increases expression at the cell surface and thereby increases channel activity; it modulates the kinetics of channel activation and inactivation, shifts the threshold for channel activation to more negative voltage values, shifts the threshold for inactivation to less negative voltages and accelerates recovery after inactivation (PubMed:14623880, PubMed:14980201, PubMed:15454437, PubMed:19171772, PubMed:24501278, PubMed:24811166). Likewise, interaction with DPP6 or DPP10 promotes expression at the cell membrane and regulates both channel characteristics and activity (By similarity). Upon depolarization, the channel goes from a resting closed state (C state) to an activated but non-conducting state (C* state), from there, the channel may either inactivate (I state) or open (O state) (PubMed:35597238).
  catalytic activity: K(+)(in) = K(+)(out) (RHEA:29463)
  subunit: Homotetramer or heterotetramer with KCND1 or KCND3 (PubMed:14980201, PubMed:16934482, PubMed:24811166, PubMed:34552243, PubMed:35597238). Associates with the regulatory subunits KCNIP2, KCNIP3 and KCNIP4 (PubMed:11287421, PubMed:11847232, PubMed:12451113, PubMed:14623880, PubMed:14980201, PubMed:15358149, PubMed:24811166, PubMed:35597238). Interacts with the regulatory subunit KCNIP1; this interaction mediates the capture of both the N- and C-terminus of KCND2, preventing N-type inactivation and stabilizing the S6 conformation, thereby accelerating closed state inactivation and recovery (PubMed:10676964, PubMed:14980207, PubMed:15358149, PubMed:34552243). In vivo, probably exists as heteromeric complex containing variable proportions of KCND1, KCND2, KCND3, KCNIP1, KCNIP2, KCNIP3, KCNIP4, DPP6 and DPP10 (PubMed:19171772). The tetrameric channel can associate with up to four regulatory subunits, such as KCNIP2 or KCNIP4 (PubMed:14623880, PubMed:14980201, PubMed:24811166). Interaction with four KCNIP4 chains does not reduce interaction with DPP10 (PubMed:24811166). Interacts with DLG4 and NCS1/FREQ (By similarity). Interacts with DLG1 (PubMed:19213956). Probably part of a complex consisting of KCNIP1, KCNIP2 isoform 3 and KCND2 (PubMed:15358149). Interacts with FLNA, FLNC and DPP10 (PubMed:11102480, PubMed:15454437). Interacts (via S1 and S2 helices) with DPP6; this interaction stabilizes the conformation of the S1-S2 helices and facilitates S4 conformational change, including S4 sliding up and down, thereby accelerating activation, inactivation, and recovery (PubMed:15454437, PubMed:34552243, PubMed:35597238).

KCND2_RABIT / P59995 A-type voltage-gated potassium channel KCND2; Potassium voltage-gated channel subfamily D member 2; Voltage-gated potassium channel subunit Kv4.2 from Oryctolagus cuniculus (Rabbit) (see paper)
Aligns to 470:546 / 630 (12.2%), covers 97.4% of PF11879, 126.7 bits

• function: Voltage-gated potassium channel that mediates transmembrane potassium transport in excitable membranes, primarily in the brain. Mediates the major part of the dendritic A-type current I(SA) in brain neurons (By similarity). This current is activated at membrane potentials that are below the threshold for action potentials. It regulates neuronal excitability, prolongs the latency before the first spike in a series of action potentials, regulates the frequency of repetitive action potential firing, shortens the duration of action potentials and regulates the back-propagation of action potentials from the neuronal cell body to the dendrites. Contributes to the regulation of the circadian rhythm of action potential firing in suprachiasmatic nucleus neurons, which regulates the circadian rhythm of locomotor activity (By similarity). Functions downstream of the metabotropic glutamate receptor GRM5 and plays a role in neuronal excitability and in nociception mediated by activation of GRM5 (By similarity). Mediates the transient outward current I(to) in rodent heart left ventricle apex cells, but not in human heart, where this current is mediated by another family member. Forms tetrameric potassium-selective channels through which potassium ions pass in accordance with their electrochemical gradient (By similarity). The channel alternates between opened and closed conformations in response to the voltage difference across the membrane. Can form functional homotetrameric channels and heterotetrameric channels that contain variable proportions of KCND2 and KCND3; channel properties depend on the type of pore-forming alpha subunits that are part of the channel. In vivo, membranes probably contain a mixture of heteromeric potassium channel complexes. Interaction with specific isoforms of the regulatory subunits KCNIP1, KCNIP2, KCNIP3 or KCNIP4 strongly increases expression at the cell surface and thereby increases channel activity; it modulates the kinetics of channel activation and inactivation, shifts the threshold for channel activation to more negative voltage values, shifts the threshold for inactivation to less negative voltages and accelerates recovery after inactivation (By similarity). Likewise, interaction with DPP6 or DPP10 promotes expression at the cell membrane and regulates both channel characteristics and activity (By similarity). Upon depolarization, the channel goes from a resting closed state (C state) to an activated but non-conducting state (C* state), from there, the channel may either inactivate (I state) or open (O state) (By similarity).
  catalytic activity: K(+)(in) = K(+)(out) (RHEA:29463)
  subunit: Homotetramer or heterotetramer with KCND1 or KCND3. Associates with the regulatory subunits KCNIP1, KCNIP2, KCNIP3 and KCNIP4. Interacts with DPP6, DPP10, DLG4 and DLG1. In vivo, probably exists as heteromeric complex containing variable proportions of KCND1, KCND2, KCND3, KCNIP1, KCNIP2, KCNIP3, KCNIP4, DPP6 and DPP10 (By similarity). The tetrameric channel can associate with up to four regulatory subunits, such as KCNIP2 or KCNIP4 (By similarity). Interaction with KCNIP3 promotes tetramerization and formation of a functional potassium channel (By similarity). Interaction with four KCNIP4 chains does not reduce interaction with DPP10 (By similarity). Probably part of a complex consisting of KCNIP1, KCNIP2 isoform 3 and KCND2 (By similarity). Interacts with FLNA and FLNC (By similarity). Interacts with NCS1/FREQ (By similarity). Identified in a complex with cAMP- dependent protein kinase (PKA), CAV3, AKAP6 and KCND3 in cardiac myocytes (By similarity). Interacts (via S1 and S2 helices) with DPP6; this interaction stabilizes the conformation of the S1-S2 helices and facilitates S4 conformational change, including S4 sliding up and down, thereby accelerating activation, inactivation, and recovery (By similarity).

KCND2_RAT / Q63881 A-type voltage-gated potassium channel KCND2; Potassium voltage-gated channel subfamily D member 2; RK5; Shal1; Voltage-gated potassium channel subunit Kv4.2 from Rattus norvegicus (Rat) (see 46 papers)
Aligns to 470:546 / 630 (12.2%), covers 97.4% of PF11879, 126.7 bits

• function: Voltage-gated potassium channel that mediates transmembrane potassium transport in excitable membranes, primarily in the brain, but also in rodent heart (PubMed:10676964, PubMed:12592409, PubMed:12754210, PubMed:14980206, PubMed:16123112, PubMed:16207878, PubMed:1722463, PubMed:1840649, PubMed:19279261, PubMed:25352783, PubMed:9058605, PubMed:9093524). Mediates the major part of the dendritic A-type current I(SA) in brain neurons (PubMed:16207878, PubMed:17026528). This current is activated at membrane potentials that are below the threshold for action potentials. It regulates neuronal excitability, prolongs the latency before the first spike in a series of action potentials, regulates the frequency of repetitive action potential firing, shortens the duration of action potentials and regulates the back-propagation of action potentials from the neuronal cell body to the dendrites. Contributes to the regulation of the circadian rhythm of action potential firing in suprachiasmatic nucleus neurons, which regulates the circadian rhythm of locomotor activity (By similarity). Functions downstream of the metabotropic glutamate receptor GRM5 and plays a role in neuronal excitability and in nociception mediated by activation of GRM5 (By similarity). Mediates the transient outward current I(to) in rodent heart left ventricle apex cells, but not in human heart, where this current is mediated by another family member (PubMed:9058605, PubMed:9093524). Forms tetrameric potassium-selective channels through which potassium ions pass in accordance with their electrochemical gradient. The channel alternates between opened and closed conformations in response to the voltage difference across the membrane (PubMed:10676964, PubMed:12451113, PubMed:12592409, PubMed:12754210, PubMed:14980206, PubMed:15452711, PubMed:16207878, PubMed:16820361, PubMed:1722463, PubMed:1840649, PubMed:25352783, PubMed:9093524). Can form functional homotetrameric channels and heterotetrameric channels that contain variable proportions of KCND2 and KCND3; channel properties depend on the type of pore-forming alpha subunits that are part of the channel (PubMed:25352783). In vivo, membranes probably contain a mixture of heteromeric potassium channel complexes (PubMed:12451113, PubMed:16123112). Interaction with specific isoforms of the regulatory subunits KCNIP1, KCNIP2, KCNIP3 or KCNIP4 strongly increases expression at the cell surface and thereby increases channel activity; it modulates the kinetics of channel activation and inactivation, shifts the threshold for channel activation to more negative voltage values, shifts the threshold for inactivation to less negative voltages and accelerates recovery after inactivation (PubMed:12451113, PubMed:14980206, PubMed:15452711, PubMed:16123112, PubMed:16820361, PubMed:20045463). Likewise, interaction with DPP6 or DPP10 promotes expression at the cell membrane and regulates both channel characteristics and activity (PubMed:15671030, PubMed:16123112, PubMed:19279261, PubMed:19441798, PubMed:19901547). Upon depolarization, the channel goes from a resting closed state (C state) to an activated but non-conducting state (C* state), from there, the channel may either inactivate (I state) or open (O state) (By similarity).
  catalytic activity: K(+)(in) = K(+)(out) (RHEA:29463)
  subunit: Homotetramer or heterotetramer with KCND1 or KCND3 (PubMed:12754210, PubMed:15485870, PubMed:20224290, PubMed:25352783). Associates with the regulatory subunits KCNIP2, KCNIP3 and KCNIP4 (PubMed:10676964, PubMed:11805342, PubMed:11847232, PubMed:12451113, PubMed:14980206, PubMed:15356203, PubMed:15452711, PubMed:15485870, PubMed:16820361, PubMed:20045463, PubMed:24811166). Interacts with the regulatory subunit KCNIP1; this interaction mediates the capture of both the N- and C-terminus of KCND2, preventing N-type inactivation and stabilizing the S6 conformation, thereby accelerating closed state inactivation and recovery (PubMed:14980206, PubMed:14980207, PubMed:15356203). Interacts with DPP10, DLG4 and DLG1 (PubMed:11923279, PubMed:14559911, PubMed:15671030, PubMed:19213956). In vivo, probably exists as heteromeric complex containing variable proportions of KCND1, KCND2, KCND3, KCNIP1, KCNIP2, KCNIP3, KCNIP4, DPP6 and DPP10 (PubMed:16123112, PubMed:19901547). The tetrameric channel can associate with up to four regulatory subunits, such as KCNIP2 or KCNIP4 (By similarity). Interaction with KCNIP3 promotes tetramerization and formation of a functional potassium channel (PubMed:15485870). Interaction with four KCNIP4 chains does not reduce interaction with DPP10 (By similarity). Probably part of a complex consisting of KCNIP1, KCNIP2 isoform 3 and KCND2 (By similarity). Interacts with FLNA and FLNC (PubMed:11102480). Interacts with NCS1/FREQ (By similarity). Identified in a complex with cAMP-dependent protein kinase (PKA), CAV3, AKAP6 and KCND3 in cardiac myocytes (PubMed:20224290). Interacts (via S1 and S2 helices) with DPP6; this interaction stabilizes the conformation of the S1-S2 helices and facilitates S4 conformational change, including S4 sliding up and down, thereby accelerating activation, inactivation, and recovery (PubMed:12575952, PubMed:15671030).

KCND2_MOUSE / Q9Z0V2 A-type voltage-gated potassium channel KCND2; Potassium voltage-gated channel subfamily D member 2; Voltage-gated potassium channel subunit Kv4.2 from Mus musculus (Mouse) (see 22 papers)
Aligns to 470:546 / 630 (12.2%), covers 97.4% of PF11879, 126.6 bits

• function: Voltage-gated potassium channel that mediates transmembrane potassium transport in excitable membranes, primarily in the brain, but also in rodent heart. Mediates the major part of the dendritic A-type current I(SA) in brain neurons (PubMed:10818150, PubMed:17122039, PubMed:18045912, PubMed:18187474, PubMed:20371829, PubMed:22815518). This current is activated at membrane potentials that are below the threshold for action potentials. It regulates neuronal excitability, prolongs the latency before the first spike in a series of action potentials, regulates the frequency of repetitive action potential firing, shortens the duration of action potentials and regulates the back-propagation of action potentials from the neuronal cell body to the dendrites (PubMed:10818150, PubMed:17122039, PubMed:22815518). Contributes to the regulation of the circadian rhythm of action potential firing in suprachiasmatic nucleus neurons, which regulates the circadian rhythm of locomotor activity (PubMed:22815518). Functions downstream of the metabotropic glutamate receptor GRM5 and plays a role in neuronal excitability and in nociception mediated by activation of GRM5 (PubMed:18045912). Mediates the transient outward current I(to) in rodent heart left ventricle apex cells, but not in human heart, where this current is mediated by another family member (PubMed:10601491, PubMed:11909823, PubMed:23713033, PubMed:9734479). Forms tetrameric potassium-selective channels through which potassium ions pass in accordance with their electrochemical gradient. The channel alternates between opened and closed conformations in response to the voltage difference across the membrane (PubMed:22311982, PubMed:9734479). Can form functional homotetrameric channels and heterotetrameric channels that contain variable proportions of KCND2 and KCND3; channel properties depend on the type of pore-forming alpha subunits that are part of the channel (PubMed:11909823). In vivo, membranes probably contain a mixture of heteromeric potassium channel complexes (PubMed:11909823). Interaction with specific isoforms of the regulatory subunits KCNIP1, KCNIP2, KCNIP3 or KCNIP4 strongly increases expression at the cell surface and thereby increases channel activity; it modulates the kinetics of channel activation and inactivation, shifts the threshold for channel activation to more negative voltage values, shifts the threshold for inactivation to less negative voltages and accelerates recovery after inactivation (By similarity). Likewise, interaction with DPP6 or DPP10 promotes expression at the cell membrane and regulates both channel characteristics and activity (PubMed:22311982). Upon depolarization, the channel goes from a resting closed state (C state) to an activated but non-conducting state (C* state), from there, the channel may either inactivate (I state) or open (O state) (By similarity).
  catalytic activity: K(+)(in) = K(+)(out) (RHEA:29463)
  subunit: Homotetramer or heterotetramer with KCND3 or KCND1 (PubMed:11909823, PubMed:19713751, PubMed:20943905, PubMed:9734479). Associates with the regulatory subunits KCNIP2, KCNIP3 and KCNIP4 (PubMed:11909823, PubMed:19713751, PubMed:20943905). Interacts with the regulatory subunit KCNIP1; this interaction mediates the capture of both the N- and C-terminus of KCND2, preventing N-type inactivation and stabilizing the S6 conformation, thereby accelerating closed state inactivation and recovery (By similarity). In vivo, probably exists as heteromeric complex containing variable proportions of KCND1, KCND2, KCND3, KCNIP1, KCNIP2, KCNIP3, KCNIP4, DPP6 and DPP10 (PubMed:19713751). The tetrameric channel can associate with up to four regulatory subunits, such as KCNIP2 or KCNIP4 (By similarity). Interaction with four KCNIP4 chains does not reduce interaction with DPP10 (By similarity). Interacts with DLG1 (By similarity). Interacts with DLG4 (By similarity). Interacts with NCS1/FREQ (PubMed:11606724). Probably part of a complex consisting of KCNIP1, KCNIP2 isoform 3 and KCND2 (By similarity). Interacts with FLNA and FLNC (By similarity). Interacts with DPP10 (PubMed:22311982). Identified in a complex with cAMP-dependent protein kinase (PKA), CAV3, AKAP6 and KCND3 in cardiac myocytes (By similarity). Interacts (via S1 and S2 helices) with DPP6; this interaction stabilizes the conformation of the S1-S2 helices and facilitates S4 conformational change, including S4 sliding up and down, thereby accelerating activation, inactivation, and recovery (PubMed:22311982).
  disruption phenotype: Mice are viable, fertile and appear to be in good health (PubMed:16293790, PubMed:22738428). The loss of KCND2 has only minor functional consequences, probably due to an increase of the activity of other potassium channels, even though there is no visible change of their expression levels (PubMed:20371829). Mutant mice show no sign of heart dysfunction, but the fast component of the rapidly inactivating and rapidly recovering potassium current I(to) is lost in their ventricular myocytes (PubMed:16293790). Instead, a slowly inactivating current is expressed that is not observed in wild-type (PubMed:16293790). Electrocardiograms of mutant hearts display no significant differences relative to wild-type regarding their QT, PR, QRS and RR intervals (PubMed:16293790). The neuronal A-type current is reduced by about 80% in brain cortex and hippocampus CA1 pyramidal neurons, by about 50% in suprachiasmatic nucleus neurons and by about 60% in dorsal horn neurons (PubMed:17122039, PubMed:18045912, PubMed:18187474, PubMed:20371829, PubMed:22815518). The dendritic A- type current is abolished in pyramidal neurons from the hippocampus CA1 layer (PubMed:17122039). Concomitantly, the back-propagation of action potential in dendrites is increased (PubMed:17122039). This may lower the treshold for neuronal long-term potentiation (LTP) (PubMed:17122039). Loss of KCND2 does not influence the levels of KCND3 or KCNA4, but leads to reduced KCNIP1, KCNIP2 and KCNIP3 protein levels (PubMed:17122039, PubMed:18187474, PubMed:22612819). Mutant mice show only minor differences in their behavior when compared to wild-type; they display hyperactivity to some, but not all, novel stimuli (PubMed:22738428). Mutant mice show subtle spatial learning deficits (PubMed:20857488). Mutant mice display shorter periods of locomotor activity that wild-type littermates, due to a corresponding change in the circadian rhythm of repetitive firing in suprachiasmatic nucleus neurons (PubMed:22815518). Mutant mice display loss of spontaneous nociceptive behavior that is caused by the activation of GRM5 (PubMed:18045912).

KCND3_MOUSE / Q9Z0V1 A-type voltage-gated potassium channel KCND3; Potassium voltage-gated channel subfamily D member 3; Voltage-gated potassium channel subunit Kv4.3 from Mus musculus (Mouse) (see 3 papers)
Aligns to 468:563 / 655 (14.7%), covers 97.4% of PF11879, 122.2 bits

• function: Pore-forming (alpha) subunit of voltage-gated A-type potassium channels that mediates transmembrane potassium transport in excitable membranes, in brain and heart (By similarity). In cardiomyocytes, may generate the transient outward potassium current I(To). In neurons, may conduct the transient subthreshold somatodendritic A-type potassium current (ISA) (By similarity). Kinetics properties are characterized by fast activation at subthreshold membrane potentials, rapid inactivation, and quick recovery from inactivation. Channel properties are modulated by interactions with regulatory subunits. Interaction with the regulatory subunits KCNIP1 or KCNIP2 modulates the channel gating kinetics namely channel activation and inactivation kinetics and rate of recovery from inactivation. Likewise, interaction with DPP6 modulates the channel gating kinetics namely channel activation and inactivation kinetics (By similarity).
  catalytic activity: K(+)(in) = K(+)(out) (RHEA:29463)
  subunit: Homotetramer (By similarity). Heterotetramer with KCND2 (PubMed:11909823). Associates with the regulatory subunit KCNIP3 (PubMed:11598014). Associates with the regulatory subunit KCNIP4 (By similarity). Interacts with KCNE1, KCNE2, SCN1B and KCNAB1 and DLG1 (By similarity). Component of heteromultimeric potassium channels (PubMed:19713751). Identified in potassium channel complexes containing KCND1, KCND2, KCND3, KCNIP1, KCNIP2, KCNIP3, KCNIP4, DPP6 and DPP10 (PubMed:19713751). Interacts with KCNIP1; each KCNIP1 monomer interacts with two adjacent KCND3 subunits, through both the N-terminal inactivation ball of a KCND3 subunit and a C-terminal helix from the adjacent KCND3 subunit, clamping them together; this interaction stabilizes the tetrameric form and modulates the channel gating kinetics namely channel activation and inactivation kinetics and rate of recovery from inactivation. Interacts with DPP6; this interaction modulates the channel gating kinetics namely channel activation and inactivation kinetics and rate of recovery from inactivation (By similarity). Interacts with KCNIP2; each KCNIP2 monomer interacts with two adjacent KCND3 subunits, through both the N-terminal inactivation ball of a KCND3 subunit and a C-terminal helix from the adjacent KCND3 subunit, clamping them together; this interaction modulates the channel gating kinetics (PubMed:11909823).

KCND3_RAT / Q62897 A-type voltage-gated potassium channel KCND3; Potassium voltage-gated channel subfamily D member 3; Voltage-gated potassium channel subunit Kv4.3 from Rattus norvegicus (Rat) (see 10 papers)
Aligns to 468:563 / 655 (14.7%), covers 97.4% of PF11879, 122.2 bits

• function: Pore-forming (alpha) subunit of voltage-gated A-type potassium channels that mediates transmembrane potassium transport in excitable membranes, in brain and heart (PubMed:17057713, PubMed:8734615, PubMed:8831489, PubMed:9001401, PubMed:9450548). In cardiomyocytes, may generate the transient outward potassium current I(To) (Probable). In neurons, may conduct the transient subthreshold somatodendritic A-type potassium current (ISA) (Probable). Kinetics properties are characterized by fast activation at subthreshold membrane potentials, rapid inactivation, and quick recovery from inactivation (PubMed:17057713, PubMed:8734615, PubMed:8831489, PubMed:9001401, PubMed:9450548). Channel properties are modulated by interactions with regulatory subunits (PubMed:10676964, PubMed:17057713). Interaction with the regulatory subunits KCNIP1 or KCNIP2 modulates the channel gating kinetics namely channel activation and inactivation kinetics and rate of recovery from inactivation (PubMed:10676964, PubMed:17057713). Likewise, interaction with DPP6 modulates the channel gating kinetics namely channel activation and inactivation kinetics (By similarity).
  catalytic activity: K(+)(in) = K(+)(out) (RHEA:29463)
  subunit: Homotetramer (By similarity). Heterotetramer with KCND2 (By similarity). Associates with the regulatory subunits KCNIP3 and KCNIP4 (PubMed:10676964, PubMed:11805342). Interacts with KCNE1, KCNE2, SCN1B and KCNAB1 and DLG1 (By similarity). Component of heteromultimeric potassium channels. Identified in potassium channel complexes containing KCND1, KCND2, KCND3, KCNIP1, KCNIP2, KCNIP3, KCNIP4, DPP6 and DPP10 (By similarity). Interacts with KCNIP1; each KCNIP1 monomer interacts with two adjacent KCND3 subunits, through both the N-terminal inactivation ball of a KCND3 subunit and a C-terminal helix from the adjacent KCND3 subunit, clamping them together; this interaction stabilizes the tetrameric form and modulates the channel gating kinetics namely channel activation and inactivation kinetics and rate of recovery from inactivation (PubMed:10676964, PubMed:17057713). Interacts with DPP6; this interaction modulates the channel gating kinetics namely channel activation and inactivation kinetics and rate of recovery from inactivation (By similarity). Interacts with KCNIP2; each KCNIP2 monomer interacts with two adjacent KCND3 subunits, through both the N-terminal inactivation ball of a KCND3 subunit and a C- terminal helix from the adjacent KCND3 subunit, clamping them together; this interaction modulates the channel gating kinetics (PubMed:10676964).

KCND3_RABIT / Q9TTT5 A-type voltage-gated potassium channel KCND3; Potassium voltage-gated channel subfamily D member 3; Voltage-gated potassium channel subunit Kv4.3 from Oryctolagus cuniculus (Rabbit) (see paper)
Aligns to 468:563 / 655 (14.7%), covers 97.4% of PF11879, 122.0 bits

• function: Pore-forming (alpha) subunit of voltage-gated A-type potassium channels that mediates transmembrane potassium transport in excitable membranes, in brain and heart (PubMed:12122138). In cardiomyocytes, may generate the transient outward potassium current I(To). In neurons, may conduct the transient subthreshold somatodendritic A-type potassium current (ISA) (By similarity). Kinetics properties are characterized by fast activation at subthreshold membrane potentials, rapid inactivation, and quick recovery from inactivation. Channel properties are modulated by interactions with regulatory subunits. Interaction with the regulatory subunits KCNIP1 or KCNIP2 modulates the channel gating kinetics namely channel activation and inactivation kinetics and rate of recovery from inactivation. Likewise, interaction with DPP6 modulates the channel gating kinetics namely channel activation and inactivation kinetics (By similarity).
  catalytic activity: K(+)(in) = K(+)(out) (RHEA:29463)
  subunit: Homotetramer (By similarity). Heterotetramer with KCND2 (By similarity). Associates with the regulatory subunits KCNIP3 and KCNIP4 (By similarity). Interacts with KCNE1, KCNE2, SCN1B and KCNAB1 and DLG1 (By similarity). Component of heteromultimeric potassium channels. Identified in potassium channel complexes containing KCND1, KCND2, KCND3, KCNIP1, KCNIP2, KCNIP3, KCNIP4, DPP6 and DPP10 (By similarity). Interacts with KCNIP1; each KCNIP1 monomer interacts with two adjacent KCND3 subunits, through both the N-terminal inactivation ball of a KCND3 subunit and a C-terminal helix from the adjacent KCND3 subunit, clamping them together; this interaction stabilizes the tetrameric form and modulates the channel gating kinetics namely channel activation and inactivation kinetics and rate of recovery from inactivation. Interacts with DPP6; this interaction modulates the channel gating kinetics namely channel activation and inactivation kinetics and rate of recovery from inactivation. Interacts with KCNIP2; each KCNIP2 monomer interacts with two adjacent KCND3 subunits, through both the N-terminal inactivation ball of a KCND3 subunit and a C-terminal helix from the adjacent KCND3 subunit, clamping them together; this interaction modulates the channel gating kinetics (By similarity).

KCND3_HUMAN / Q9UK17 A-type voltage-gated potassium channel KCND3; Potassium voltage-gated channel subfamily D member 3; Voltage-gated potassium channel subunit Kv4.3 from Homo sapiens (Human) (see 13 papers)
Aligns to 468:563 / 655 (14.7%), covers 97.4% of PF11879, 121.9 bits

• function: Pore-forming (alpha) subunit of voltage-gated A-type potassium channels that mediates transmembrane potassium transport in excitable membranes, in brain and heart (PubMed:10200233, PubMed:17187064, PubMed:21349352, PubMed:22457051, PubMed:23280837, PubMed:23280838, PubMed:34997220, PubMed:9843794). In cardiomyocytes, may generate the transient outward potassium current I(To) (By similarity). In neurons, may conduct the transient subthreshold somatodendritic A-type potassium current (ISA) (By similarity). Kinetics properties are characterized by fast activation at subthreshold membrane potentials, rapid inactivation, and quick recovery from inactivation (PubMed:10200233, PubMed:17187064, PubMed:21349352, PubMed:22457051, PubMed:23280837, PubMed:23280838, PubMed:34997220, PubMed:9843794). Channel properties are modulated by interactions with regulatory subunits (PubMed:17187064, PubMed:34997220). Interaction with the regulatory subunits KCNIP1 or KCNIP2 modulates the channel gating kinetics namely channel activation and inactivation kinetics and rate of recovery from inactivation (PubMed:17187064, PubMed:34997220). Likewise, interaction with DPP6 modulates the channel gating kinetics namely channel activation and inactivation kinetics (PubMed:34997220).
  catalytic activity: K(+)(in) = K(+)(out) (RHEA:29463)
  subunit: Homotetramer (PubMed:17187064, PubMed:34997220). Heterotetramer with KCND2 (By similarity). Associates with the regulatory subunits KCNIP3 and KCNIP4 (By similarity). Interacts with KCNE1, KCNE2, SCN1B and KCNAB1 and DLG1 (PubMed:12297301, PubMed:19213956). Component of heteromultimeric potassium channels. Identified in potassium channel complexes containing KCND1, KCND2, KCND3, KCNIP1, KCNIP2, KCNIP3, KCNIP4, DPP6 and DPP10 (By similarity). Interacts with KCNIP1; each KCNIP1 monomer interacts with two adjacent KCND3 subunits, through both the N-terminal inactivation ball of a KCND3 subunit and a C-terminal helix from the adjacent KCND3 subunit, clamping them together; this interaction stabilizes the tetrameric form and modulates the channel gating kinetics namely channel activation and inactivation kinetics and rate of recovery from inactivation (PubMed:14980207, PubMed:17187064, PubMed:34997220). Interacts with DPP6; this interaction modulates the channel gating kinetics namely channel activation and inactivation kinetics and rate of recovery from inactivation (PubMed:34997220). Interacts with KCNIP2; each KCNIP2 monomer interacts with two adjacent KCND3 subunits, through both the N- terminal inactivation ball of a KCND3 subunit and a C-terminal helix from the adjacent KCND3 subunit, clamping them together; this interaction modulates the channel gating kinetics (PubMed:12297301, PubMed:34997220).

KCND1_RABIT / P59994 A-type voltage-gated potassium channel KCND1; Potassium voltage-gated channel subfamily D member 1; Voltage-gated potassium channel subunit Kv4.1 from Oryctolagus cuniculus (Rabbit) (see paper)
Aligns to 470:550 / 647 (12.5%), covers 97.4% of PF11879, 109.1 bits

• function: A-type voltage-gated potassium channel that mediates transmembrane potassium transport in excitable membranes in the brain. Mediates A-type current I(SA) in suprachiasmatic nucleus (SCN) neurons. Exhibits a low-threshold A-type current with a hyperpolarized steady- state inactivation midpoint and the recovery process was steeply voltage-dependent, with recovery being markedly faster at more negative potentials. May regulates repetitive firing rates in the suprachiasmatic nucleus (SCN) neurons and circadian rhythms in neuronal excitability and behavior. Contributes to the regulation of the circadian rhythm of action potential firing in suprachiasmatic nucleus neurons, which regulates the circadian rhythm of locomotor activity. The regulatory subunit KCNIP1 modulates the kinetics of channel inactivation, increases the current amplitudes and accelerates recovery from inactivation, shifts activation in a depolarizing direction (By similarity). The regulatory subunit DPP10 decreases the voltage sensitivity of the inactivation channel gating (By similarity).
  catalytic activity: K(+)(in) = K(+)(out) (RHEA:29463)
  subunit: Component of heteromultimeric potassium channels. Identified in potassium channel complexes containing KCND1, KCND2, KCND3, KCNIP1, KCNIP2, KCNIP3, KCNIP4, DPP6 and DPP10.

KCND1_HUMAN / Q9NSA2 A-type voltage-gated potassium channel KCND1; Potassium voltage-gated channel subfamily D member 1; Shal-type potassium channel KCND1; Voltage-gated potassium channel subunit Kv4.1 from Homo sapiens (Human) (see 2 papers)
Aligns to 470:550 / 647 (12.5%), covers 97.4% of PF11879, 107.3 bits

• function: A-type voltage-gated potassium channel that mediates transmembrane potassium transport in excitable membranes in the brain (PubMed:15454437). Mediates A-type current I(SA) in suprachiasmatic nucleus (SCN) neurons. Exhibits a low-threshold A-type current with a hyperpolarized steady-state inactivation midpoint and the recovery process was steeply voltage-dependent, with recovery being markedly faster at more negative potentials. May regulates repetitive firing rates in the suprachiasmatic nucleus (SCN) neurons and circadian rhythms in neuronal excitability and behavior. Contributes to the regulation of the circadian rhythm of action potential firing in suprachiasmatic nucleus neurons, which regulates the circadian rhythm of locomotor activity. The regulatory subunit KCNIP1 modulates the kinetics of channel inactivation, increases the current amplitudes and accelerates recovery from inactivation, shifts activation in a depolarizing direction (By similarity). The regulatory subunit DPP10 decreases the voltage sensitivity of the inactivation channel gating (PubMed:15454437).
  catalytic activity: K(+)(in) = K(+)(out) (RHEA:29463)
  subunit: Component of heteromultimeric potassium channels. Identified in potassium channel complexes containing KCND1, KCND2, KCND3, KCNIP1, KCNIP2, KCNIP3, KCNIP4, DPP6 and DPP10.

KCND1_MOUSE / Q03719 A-type voltage-gated potassium channel KCND1; Potassium voltage-gated channel subfamily D member 1; Voltage-gated potassium channel subunit Kv4.1; mShal from Mus musculus (Mouse) (see 4 papers)
Aligns to 470:550 / 651 (12.4%), covers 97.4% of PF11879, 105.4 bits

• function: A-type voltage-gated potassium channel that mediates transmembrane potassium transport in excitable membranes in the brain (PubMed:28560311). Mediates A-type current I(SA) in suprachiasmatic nucleus (SCN) neurons (PubMed:28560311). Exhibits a low-threshold A- type current with a hyperpolarized steady-state inactivation midpoint and the recovery process was steeply voltage-dependent, with recovery being markedly faster at more negative potentials (PubMed:2034678). May regulates repetitive firing rates in the suprachiasmatic nucleus (SCN) neurons and circadian rhythms in neuronal excitability and behavior (PubMed:28560311). Contributes to the regulation of the circadian rhythm of action potential firing in suprachiasmatic nucleus neurons, which regulates the circadian rhythm of locomotor activity (PubMed:28560311). The regulatory subunit KCNIP1 modulates the kinetics of channel inactivation, increases the current amplitudes and accelerates recovery from inactivation, shifts activation in a depolarizing direction (PubMed:11423117). The regulatory subunit DPP10 decreases the voltage sensitivity of the inactivation channel gating (By similarity).
  catalytic activity: K(+)(in) = K(+)(out) (RHEA:29463)
  subunit: Component of heteromultimeric potassium channels (PubMed:19713751). Identified in potassium channel complexes containing KCND1, KCND2, KCND3, KCNIP1, KCNIP2, KCNIP3, KCNIP4, DPP6 and DPP10 (PubMed:19713751).

KCNAL_DROME / P17971 Potassium voltage-gated channel protein Shal; Shaker cognate l; Shal2 from Drosophila melanogaster (Fruit fly) (see paper)
Aligns to 470:546 / 571 (13.5%), covers 86.8% of PF11879, 65.5 bits

• function: Mediates the voltage-dependent potassium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a potassium-selective channel through which potassium ions may pass in accordance with their electrochemical gradient. May play a role in the nervous system and in the regulation of beating frequency in pacemaker cells
  subunit: Heterotetramer of potassium channel proteins (By similarity). Interacts (via C-terminal dendritic targeting motif) with SIDL.

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