Kcna2
entrez
25468
canonical
uniprot
P63142
canonical
ensembl
ENSRNOG00000018285
resolver
ensembl
ENSRNOG00055020280
resolver
ensembl
ENSRNOG00060029911
resolver
ensembl
ENSRNOG00065022931
resolver
ensp
ENSRNOP00000079590
resolver
ensp
ENSRNOP00000089201
resolver
ensp
ENSRNOP00000090952
resolver
ensp
ENSRNOP00055028059
resolver
ensp
ENSRNOP00055028062
resolver
ensp
ENSRNOP00055028065
resolver
ensp
ENSRNOP00055028070
resolver
ensp
ENSRNOP00060043198
resolver
ensp
ENSRNOP00060043210
resolver
ensp
ENSRNOP00060043217
resolver
ensp
ENSRNOP00060043223
resolver
ensp
ENSRNOP00065031816
resolver
ensp
ENSRNOP00065031817
resolver
ensp
ENSRNOP00065031822
resolver
ensp
ENSRNOP00065031826
resolver
enst
ENSRNOT00000100022
resolver
enst
ENSRNOT00000108979
resolver
enst
ENSRNOT00000116262
resolver
enst
ENSRNOT00055034634
resolver
enst
ENSRNOT00055034637
resolver
enst
ENSRNOT00055034641
resolver
enst
ENSRNOT00055034645
resolver
enst
ENSRNOT00060051941
resolver
enst
ENSRNOT00060051956
resolver
enst
ENSRNOT00060051963
resolver
enst
ENSRNOT00060051970
resolver
enst
ENSRNOT00065039166
resolver
enst
ENSRNOT00065039168
resolver
enst
ENSRNOT00065039175
resolver
enst
ENSRNOT00065039180
resolver
genesymbol
Kcna2
resolver
uniprot
P15386
resolver
uniprot
Q02010
resolver
uniprot_entry
KCNA2_RAT
resolver
uniprot_sec
P15386
resolver
uniprot_sec
Q02010
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by 4-aminopyridine (4-AP), dendrotoxin (DTX) and charybdotoxin (CTX), but not by tetraethylammonium (TEA) (PubMed:18638484, PubMed:2555158, PubMed:8495559). Inhibited by tityustoxin-K alpha (TsTX-Kalpha), a toxin that is highly specific for KCNA2 (PubMed:8355670). Inhibited by maurotoxin (PubMed:24472174). Inhibited by kappaM conotoxins kappaM-RIIIJ and kappaM-RIIIK (By similarity). {ECO:0000250|UniProtKB:P16389, ECO:0000269|PubMed:18638484, ECO:0000269|PubMed:20805574, ECO:0000269|PubMed:24472174, ECO:0000269|PubMed:2555158, ECO:0000269|PubMed:8355670, ECO:0000269|PubMed:8495559}.
uniprot
proteins
amino_acid_sequence
MTVATGDPVDEAAALPGHPQDTYDPEADHECCERVVINISGLRFETQLKTLAQFPETLLGDPKKRMRYFDPLRNEYFFDRNRPSFDAILYYYQSGGRLRRPVNVPLDIFSEEIRFYELGEEAMEMFREDEGYIKEEERPLPENEFQRQVWLLFEYPESSGPARIIAIVSVMVILISIVSFCLETLPIFRDENEDMHGGGVTFHTYSNSTIGYQQSTSFTDPFFIVETLCIIWFSFEFLVRFFACPSKAGFFTNIMNIIDIVAIIPYFITLGTELAEKPEDAQQGQQAMSLAILRVIRLVRVFRIFKLSRHSKGLQILGQTLKASMRELGLLIFFLFIGVILFSSAVYFAEADERDSQFPSIPDAFWWAVVSMTTVGYGDMVPTTIGGKIVGSLCAIAGVLTIALPVPVIVSNFNYFYHRETEGEEQAQYLQVTSCPKIPSSPDLKKSRSASTISKSDYMEIQEGVNNSNEDFREENLKTANCTLANTNYVNITKMLTDV
uniprot
proteins
function
FUNCTION: Voltage-gated potassium channel that mediates transmembrane potassium transport in excitable membranes, primarily in the brain and the central nervous system, but also in the cardiovascular system. Prevents aberrant action potential firing and regulates neuronal output. 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:12151401, PubMed:21602278, PubMed:24472174). Can form functional homotetrameric channels and heterotetrameric channels that contain variable proportions of KCNA1, KCNA2, KCNA4, KCNA5, KCNA6, KCNA7, and possibly other family members as well; channel properties depend on the type of alpha subunits that are part of the channel (PubMed:15618540, PubMed:20805574, PubMed:23725331, PubMed:8495559). Channel properties are modulated by cytoplasmic beta subunits that regulate the subcellular location of the alpha subunits and promote rapid inactivation of delayed rectifier potassium channels (PubMed:18003609, PubMed:19713757). In vivo, membranes probably contain a mixture of heteromeric potassium channel complexes, making it difficult to assign currents observed in intact tissues to a particular potassium channel family member. Homotetrameric KCNA2 forms a delayed-rectifier potassium channel that opens in response to membrane depolarization, followed by slow spontaneous channel closure (PubMed:16770729, PubMed:1715584, PubMed:17766348, PubMed:18003609, PubMed:18638484, PubMed:19713757, PubMed:20089912). In contrast, a heteromultimer formed by KCNA2 and KCNA4 shows rapid inactivation (PubMed:8495559). Response to toxins that are selective for KCNA1, respectively for KCNA2, suggests that heteromeric potassium channels composed of both KCNA1 and KCNA2 play a role in pacemaking and regulate the output of deep cerebellar nuclear neurons (PubMed:23318870). KCNA2-containing channels play a presynaptic role and prevent hyperexcitability and aberrant action potential firing (PubMed:12777451). Response to toxins that are selective for KCNA2-containing potassium channels suggests that in Purkinje cells, dendritic subthreshold KCNA2-containing potassium channels prevent random spontaneous calcium spikes, suppressing dendritic hyperexcitability without hindering the generation of somatic action potentials, and thereby play an important role in motor coordination (PubMed:16210348). Plays a role in the induction of long-term potentiation of neuron excitability in the CA3 layer of the hippocampus (By similarity). May function as down-stream effector for G protein-coupled receptors and inhibit GABAergic inputs to basolateral amygdala neurons (PubMed:16306173). May contribute to the regulation of neurotransmitter release, such as gamma-aminobutyric acid (GABA) (PubMed:17869444). Contributes to the regulation of the axonal release of the neurotransmitter dopamine (PubMed:21647367). Reduced KCNA2 expression plays a role in the perception of neuropathic pain after peripheral nerve injury, but not acute pain (PubMed:24472174). Plays a role in the regulation of the time spent in non-rapid eye movement (NREM) sleep (By similarity). {ECO:0000250|UniProtKB:P63141, ECO:0000269|PubMed:11007484, ECO:0000269|PubMed:12151401, ECO:0000269|PubMed:12177193, ECO:0000269|PubMed:12777451, ECO:0000269|PubMed:15618540, ECO:0000269|PubMed:16210348, ECO:0000269|PubMed:16770729, ECO:0000269|PubMed:1715584, ECO:0000269|PubMed:17766348, ECO:0000269|PubMed:18003609, ECO:0000269|PubMed:18004376, ECO:0000269|PubMed:18638484, ECO:0000269|PubMed:20089912, ECO:0000269|PubMed:20805574, ECO:0000269|PubMed:21602278, ECO:0000269|PubMed:23318870, ECO:0000269|PubMed:24472174, ECO:0000269|PubMed:2555158, ECO:0000269|PubMed:7544443, ECO:0000269|PubMed:8495559, ECO:0000305, ECO:0000305|PubMed:12177193, ECO:0000305|PubMed:16306173, ECO:0000305|PubMed:17869444, ECO:0000305|PubMed:21647367}.
uniprot
proteins
mass_dalton
56701
uniprot
proteins
mutagenesis
MUTAGEN 34; /note="R->L: No effect on channel opening."; /evidence="ECO:0000269|PubMed:11007484"; MUTAGEN 38; /note="N->A: Alters voltage-sensitive channel opening."; /evidence="ECO:0000269|PubMed:11007484"; MUTAGEN 40; /note="S->A: No effect on channel opening."; /evidence="ECO:0000269|PubMed:11007484"; MUTAGEN 41; /note="G->A: Loss of channel activity."; /evidence="ECO:0000269|PubMed:11007484"; MUTAGEN 42; /note="L->A: No effect on channel opening."; /evidence="ECO:0000269|PubMed:11007484"; MUTAGEN 43; /note="R->L: No effect on channel opening."; /evidence="ECO:0000269|PubMed:11007484"; MUTAGEN 44; /note="F->A: Alters voltage-sensitive channel opening."; /evidence="ECO:0000269|PubMed:11007484"; MUTAGEN 45; /note="E->A: Loss of channel activity."; /evidence="ECO:0000269|PubMed:11007484"; MUTAGEN 46; /note="T->D: Impairs protein folding. Loss of tetramerization."; /evidence="ECO:0000269|PubMed:11007484"; MUTAGEN 46; /note="T->V,A: No effect on tetramerization. Alters voltage-sensitive channel opening."; /evidence="ECO:0000269|PubMed:11007484"; MUTAGEN 46; /note="T->V: Abolishes interaction with KCNAB2 and strongly reduces cell surface expression. No effect phosphorylation in response to increased cAMP levels."; /evidence="ECO:0000269|PubMed:18003609"; MUTAGEN 47; /note="Q->A: No effect on channel opening."; /evidence="ECO:0000269|PubMed:11007484"; MUTAGEN 50; /note="T->A: Alters voltage-sensitive channel opening."; /evidence="ECO:0000269|PubMed:11007484"; MUTAGEN 70; /note="D->A: No effect on channel opening."; /evidence="ECO:0000269|PubMed:11007484"; MUTAGEN 73; /note="R->A: No effect on channel opening."; /evidence="ECO:0000269|PubMed:11007484"; MUTAGEN 75; /note="E->A: No effect on channel opening."; /evidence="ECO:0000269|PubMed:11007484"; MUTAGEN 77; /note="F->W: Alters voltage-sensitive channel opening."; /evidence="ECO:0000269|PubMed:11007484"; MUTAGEN 79; /note="D->N: Alters voltage-sensitive channel opening."; /evidence="ECO:0000269|PubMed:11007484"; MUTAGEN 81; /note="N->A: No effect on channel opening."; /evidence="ECO:0000269|PubMed:11007484"; MUTAGEN 82; /note="R->A: Loss of channel activity."; /evidence="ECO:0000269|PubMed:11007484"; MUTAGEN 86; /note="D->A: Alters voltage-sensitive channel opening."; /evidence="ECO:0000269|PubMed:11007484"; MUTAGEN 89; /note="L->A: No effect on channel opening."; /evidence="ECO:0000269|PubMed:11007484"; MUTAGEN 90; /note="Y->A: No effect on channel opening."; /evidence="ECO:0000269|PubMed:11007484"; MUTAGEN 93; /note="Q->A: Loss of channel activity."; /evidence="ECO:0000269|PubMed:11007484"; MUTAGEN 97; /note="R->A: No effect on channel opening."; /evidence="ECO:0000269|PubMed:11007484"; MUTAGEN 99; /note="R->A: No effect on channel opening."; /evidence="ECO:0000269|PubMed:11007484"; MUTAGEN 102; /note="V->T: Alters voltage-sensitive channel opening."; /evidence="ECO:0000269|PubMed:11007484"; MUTAGEN 103; /note="N->A: No effect on channel opening."; /evidence="ECO:0000269|PubMed:11007484"; MUTAGEN 105; /note="P->A: No effect on channel opening."; /evidence="ECO:0000269|PubMed:11007484"; MUTAGEN 107; /note="D->A: Alters voltage-sensitive channel opening."; /evidence="ECO:0000269|PubMed:11007484"; MUTAGEN 108; /note="I->A: No effect on channel opening."; /evidence="ECO:0000269|PubMed:11007484"; MUTAGEN 111; /note="E->A: Alters voltage-sensitive channel opening."; /evidence="ECO:0000269|PubMed:11007484"; MUTAGEN 207; /note="N->Q: Loss of glycosylation site."; /evidence="ECO:0000269|PubMed:16770729"; MUTAGEN 252; /note="T->R: Changes channel gating from a predominantly slow mode to a much more rapid mode."; /evidence="ECO:0000269|PubMed:17766348"; MUTAGEN 267..302; /note="FITLGTELAEKPEDAQQGQQAMSLAILRVIRLVRVF->YVTIFLTESNKSVLQFQNVRRVVQIFRIM: In paddle chimera; changes channel activation to less negative voltage values and renders the channel susceptible to inhibition by the spider toxin VsTx1."; /evidence="ECO:0000269|PubMed:18638484"; MUTAGEN 356; /note="S->A: Impairs N-glycosylation and abolishes expression at the cell surface."; /evidence="ECO:0000269|PubMed:16770729"; MUTAGEN 360; /note="S->A: No effect on N-glycosylation. Abolishes channel activity of the homotetramer, but retains channel activity in the presence of a beta subunit."; /evidence="ECO:0000269|PubMed:16770729"; MUTAGEN 381; /note="V->Y: Confers sensitivity to inhibition by tetraethylammonium (TEA)."; /evidence="ECO:0000269|PubMed:23725331"; MUTAGEN 383; /note="T->A: Impairs N-glycosylation and abolishes expression at the cell surface."; /evidence="ECO:0000269|PubMed:16770729"; MUTAGEN 415; /note="Y->F: Nearly abolishes interaction with CTTN; when associated with F-417."; /evidence="ECO:0000269|PubMed:12151401"; MUTAGEN 417; /note="Y->F: Nearly abolishes interaction with CTTN; when associated with F-415. Strongly reduces channel activity."; /evidence="ECO:0000269|PubMed:12151401"; MUTAGEN 440; /note="S->A: Strongly reduces cell surface expression. Abolishes phosphorylation in response to increased cAMP levels."; /evidence="ECO:0000269|PubMed:18003609"; MUTAGEN 449; /note="S->A: Strongly reduces cell surface expression. Abolishes phosphorylation in response to increased cAMP levels."; /evidence="ECO:0000269|PubMed:18003609"; MUTAGEN 458; /note="Y->A: Impairs clustering on axon membranes."; /evidence="ECO:0000269|PubMed:21602278
uniprot
proteins
post_translational_modification
PTM: Phosphorylated on tyrosine residues; phosphorylation increases in response to ischemia (PubMed:14713306). Phosphorylated on tyrosine residues by activated PTK2B/PYK2 (PubMed:7544443). Phosphorylation on tyrosine residues suppresses ion channel activity (PubMed:7544443). Phosphorylated on tyrosine residues in response to CHRM1 activation; this abolishes interaction with CTTN (PubMed:12151401). This is probably due to endocytosis of the phosphorylated channel subunits. Phosphorylated on serine residues in response to increased cAMP levels; phosphorylation is apparently not catalyzed by PKA (PubMed:18003609). {ECO:0000269|PubMed:12151401, ECO:0000269|PubMed:14713306, ECO:0000269|PubMed:18003609, ECO:0000269|PubMed:7544443}.; PTM: N-glycosylated, with complex, sialylated N-glycans. {ECO:0000269|PubMed:10896669, ECO:0000269|PubMed:16770729}.
uniprot
proteins
protein_family
A (Shaker) (TC 1.A.1.2) subfamily
uniprot
proteins
protein_family
Kv1.2/KCNA2 sub-subfamily
uniprot
proteins
protein_family
Potassium channel family
uniprot
proteins
pubmed
10624965
uniprot
proteins
pubmed
10896669
uniprot
proteins
pubmed
11007484
uniprot
proteins
pubmed
11086297
uniprot
proteins
pubmed
11739373
uniprot
proteins
pubmed
12151401
uniprot
proteins
pubmed
12177193
uniprot
proteins
pubmed
12632190
uniprot
proteins
pubmed
12777451
uniprot
proteins
pubmed
14713306
uniprot
proteins
pubmed
15151918
uniprot
proteins
pubmed
15618540
uniprot
proteins
pubmed
16002579
uniprot
proteins
pubmed
16002581
uniprot
proteins
pubmed
16210348
uniprot
proteins
pubmed
16306173
uniprot
proteins
pubmed
16770729
uniprot
proteins
pubmed
1715584
uniprot
proteins
pubmed
17324383
uniprot
proteins
pubmed
17766348
uniprot
proteins
pubmed
17869444
uniprot
proteins
pubmed
17917103
uniprot
proteins
pubmed
18003609
uniprot
proteins
pubmed
18004376
uniprot
proteins
pubmed
18638484
uniprot
proteins
pubmed
19403695
uniprot
proteins
pubmed
19713757
uniprot
proteins
pubmed
20089912
uniprot
proteins
pubmed
20360102
uniprot
proteins
pubmed
20534430
uniprot
proteins
pubmed
20805574
uniprot
proteins
pubmed
21602278
uniprot
proteins
pubmed
21647367
uniprot
proteins
pubmed
22673903
uniprot
proteins
pubmed
23318870
uniprot
proteins
pubmed
23705070
uniprot
proteins
pubmed
23725331
uniprot
proteins
pubmed
24472174
uniprot
proteins
pubmed
25514171
uniprot
proteins
pubmed
2555158
uniprot
proteins
pubmed
2722779
uniprot
proteins
pubmed
7477295
uniprot
proteins
pubmed
7544443
uniprot
proteins
pubmed
8355670
uniprot
proteins
pubmed
8361540
uniprot
proteins
pubmed
8495559
uniprot
proteins
pubmed
9635436
uniprot
proteins
sequence_length
499
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10896669, ECO:0000269|PubMed:12151401, ECO:0000269|PubMed:14713306, ECO:0000269|PubMed:15618540, ECO:0000269|PubMed:16770729, ECO:0000269|PubMed:1715584, ECO:0000269|PubMed:17766348, ECO:0000269|PubMed:18003609, ECO:0000269|PubMed:20089912, ECO:0000269|PubMed:20805574, ECO:0000269|PubMed:21602278, ECO:0000269|PubMed:23318870, ECO:0000269|PubMed:23725331, ECO:0000269|PubMed:24472174, ECO:0000269|PubMed:2555158, ECO:0000269|PubMed:7544443, ECO:0000269|PubMed:9635436, ECO:0000305|PubMed:11086297}; Multi-pass membrane protein {ECO:0000269|PubMed:12151401, ECO:0000269|PubMed:16002581, ECO:0000269|PubMed:18004376, ECO:0000269|PubMed:20360102, ECO:0000269|PubMed:20534430, ECO:0000269|PubMed:23705070, ECO:0000305}. Membrane {ECO:0000269|PubMed:10624965, ECO:0000269|PubMed:16002581, ECO:0000269|PubMed:18004376, ECO:0000269|PubMed:18638484, ECO:0000269|PubMed:20089912, ECO:0000269|PubMed:20360102, ECO:0000269|PubMed:20534430, ECO:0000269|PubMed:23705070, ECO:0000269|PubMed:8361540}. Cell projection, axon {ECO:0000269|PubMed:10624965, ECO:0000269|PubMed:12177193, ECO:0000269|PubMed:12777451, ECO:0000269|PubMed:20089912, ECO:0000269|PubMed:21602278, ECO:0000269|PubMed:8361540}. Synapse {ECO:0000269|PubMed:8361540}. Synapse, synaptosome {ECO:0000250|UniProtKB:P63141}. Presynaptic cell membrane {ECO:0000250|UniProtKB:P63141}. Cell projection, dendrite {ECO:0000250|UniProtKB:P63141}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:10896669}. Cell projection, lamellipodium membrane {ECO:0000269|PubMed:12151401}. Endosome {ECO:0000269|PubMed:19403695}. Perikaryon {ECO:0000269|PubMed:23318870}. Cell junction, paranodal septate junction {ECO:0000250|UniProtKB:P63141}. Note=KCNA2 by itself is detected both at the endoplasmic reticulum and at the cell membrane. Coexpression with KCNA4 or with beta subunits promotes expression at the cell membrane (PubMed:10896669, PubMed:16770729, PubMed:18003609). Coexpression with KCNA1 inhibits cell surface expression (PubMed:10896669). Surface levels are regulated both by steady-state and stimulus-induced clathrin-dependent endocytosis (PubMed:19403695). Expression at the cell surface is down-regulated in response to CHRM1 activation (PubMed:9635436). Expression at the cell surface is increased in response to the activation of beta-adrenergic receptors and increased cAMP levels (PubMed:18003609). Detected on presynaptic and postsynaptic axon segments (PubMed:12777451). In myelinated peripheral axons, clustered in the juxtaparadonal region and at an internodal line located along the mesaxon and below the Schmidt-Lanterman incisures (By similarity). {ECO:0000250|UniProtKB:P63141, ECO:0000269|PubMed:10896669, ECO:0000269|PubMed:12777451, ECO:0000269|PubMed:16770729, ECO:0000269|PubMed:18003609, ECO:0000269|PubMed:19403695, ECO:0000269|PubMed:9635436}.
uniprot
proteins
transmembrane_region
TRANSMEM 161..182; /note="Helical; Name=Segment S1"; /evidence="ECO:0000269|PubMed:18004376, ECO:0000269|PubMed:20360102, ECO:0000269|PubMed:20534430"; TRANSMEM 222..243; /note="Helical; Name=Segment S2"; /evidence="ECO:0000269|PubMed:18004376, ECO:0000269|PubMed:20360102, ECO:0000269|PubMed:20534430"; TRANSMEM 255..275; /note="Helical; Name=Segment S3"; /evidence="ECO:0000269|PubMed:18004376, ECO:0000269|PubMed:20534430"; TRANSMEM 290..310; /note="Helical; Voltage-sensor; Name=Segment S4"; /evidence="ECO:0000269|PubMed:18004376, ECO:0000269|PubMed:20534430"; TRANSMEM 326..347; /note="Helical; Name=Segment S5"; /evidence="ECO:0000269|PubMed:18004376, ECO:0000269|PubMed:20360102, ECO:0000269|PubMed:20534430"; TRANSMEM 389..417; /note="Helical; Name=Segment S6"; /evidence="ECO:0000269|PubMed:18004376, ECO:0000269|PubMed:20360102, ECO:0000269|PubMed:20534430
uniprot
proteins