Kcna2
entrez
16490
canonical
uniprot
P63141
canonical
ensembl
ENSMUSG00000040724
resolver
ensp
ENSMUSP00000041702
resolver
ensp
ENSMUSP00000142873
resolver
ensp
ENSMUSP00000143798
resolver
ensp
ENSMUSP00000246244
resolver
ensp
ENSMUSP00000246245
resolver
ensp
ENSMUSP00000246247
resolver
enst
ENSMUST00000038695
resolver
enst
ENSMUST00000196403
resolver
enst
ENSMUST00000197470
resolver
genesymbol
Kcna2
resolver
uniprot
B2RS05
resolver
uniprot
P15386
resolver
uniprot
Q02010
resolver
uniprot
Q8C8W4
resolver
uniprot_entry
KCNA2_MOUSE
resolver
uniprot_sec
B2RS05
resolver
uniprot_sec
P15386
resolver
uniprot_sec
Q02010
resolver
uniprot_sec
Q8C8W4
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by 4-aminopyridine (4-AP), dendrotoxin (DTX) and charybdotoxin (CTX), but not by tetraethylammonium (TEA) (By similarity). Inhibited by tityustoxin-K alpha (TsTX-Kalpha), a toxin that is highly specific for KCNA2 (By similarity). Inhibited by maurotoxin (PubMed:12527813). Inhibited by kappaM conotoxins kappaM-RIIIJ and kappaM-RIIIK (By similarity). {ECO:0000250|UniProtKB:P16389, ECO:0000250|UniProtKB:P63142, ECO:0000269|PubMed:12527813}.
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:12527813, PubMed:21233214). 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:20696761). 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 (By similarity). In vivo, membranes probably contain a mixture of heteromeric potassium channel complexes, making it difficult to assign currents observed in intact tissues to any 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:23864368). In contrast, a heteromultimer formed by KCNA2 and KCNA4 shows rapid inactivation (PubMed:23864368). Contributes to the regulation of action potentials in neurons (PubMed:12527813, PubMed:17925011). KCNA2-containing channels play a presynaptic role and prevent hyperexcitability and aberrant action potential firing (PubMed:17634333, PubMed:17925011). 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 (By similarity). 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 (By similarity). KCNA2-containing channels play a role in GABAergic transmission from basket cells to Purkinje cells in the cerebellum, and thereby play an import role in motor coordination (PubMed:20696761). Plays a role in the induction of long-term potentiation of neuron excitability in the CA3 layer of the hippocampus (PubMed:23981714). May function as down-stream effector for G protein-coupled receptors and inhibit GABAergic inputs to basolateral amygdala neurons (By similarity). May contribute to the regulation of neurotransmitter release, such as gamma-aminobutyric acid (GABA) (By similarity). Contributes to the regulation of the axonal release of the neurotransmitter dopamine (PubMed:21233214). Reduced KCNA2 expression plays a role in the perception of neuropathic pain after peripheral nerve injury, but not acute pain (By similarity). Plays a role in the regulation of the time spent in non-rapid eye movement (NREM) sleep (PubMed:17925011). {ECO:0000250, ECO:0000269|PubMed:12527813, ECO:0000269|PubMed:17634333, ECO:0000269|PubMed:17925011, ECO:0000269|PubMed:20696761, ECO:0000269|PubMed:21233214, ECO:0000269|PubMed:23864368, ECO:0000269|PubMed:23981714, ECO:0000269|PubMed:9635436, ECO:0000305}.
uniprot
proteins
mass_dalton
56701
uniprot
proteins
mutagenesis
MUTAGEN 402; /note="I->T: In Pgu; chronic motor incoordination; decreases the number of functional channels at the cell surface."; /evidence="ECO:0000269|PubMed:20696761
uniprot
proteins
post_translational_modification
PTM: Phosphorylated on tyrosine residues; phosphorylation increases in response to ischemia (By similarity). Phosphorylated on tyrosine residues by activated PTK2B/PYK2 (By similarity). Phosphorylation on tyrosine residues suppresses ion channel activity (By similarity). Phosphorylated on tyrosine residues in response to CHRM1 activation; this abolishes interaction with CTTN. This is probably due to endocytosis of the phosphorylated channel subunits (By similarity). Phosphorylated on serine residues in response to increased cAMP levels; phosphorylation is apparently not catalyzed by PKA (By similarity). {ECO:0000250|UniProtKB:P63142}.; PTM: N-glycosylated, with complex, sialylated N-glycans. {ECO:0000250|UniProtKB:P63142}.
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
12527813
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
1691985
uniprot
proteins
pubmed
17634333
uniprot
proteins
pubmed
17917103
uniprot
proteins
pubmed
17925011
uniprot
proteins
pubmed
18034455
uniprot
proteins
pubmed
18509034
uniprot
proteins
pubmed
18760366
uniprot
proteins
pubmed
20696761
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
21233214
uniprot
proteins
pubmed
22649228
uniprot
proteins
pubmed
2305265
uniprot
proteins
pubmed
23332758
uniprot
proteins
pubmed
23864368
uniprot
proteins
pubmed
23981714
uniprot
proteins
pubmed
25378149
uniprot
proteins
pubmed
26269648
uniprot
proteins
pubmed
8046438
uniprot
proteins
pubmed
8361541
uniprot
proteins
pubmed
9635436
uniprot
proteins
pubmed
9852577
uniprot
proteins
sequence_length
499
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12527813, ECO:0000269|PubMed:18509034, ECO:0000269|PubMed:20696761, ECO:0000269|PubMed:23332758, ECO:0000269|PubMed:23864368}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P63142}. Membrane {ECO:0000269|PubMed:23332758, ECO:0000269|PubMed:8361541, ECO:0000269|PubMed:9852577}. Cell projection, axon {ECO:0000269|PubMed:18509034, ECO:0000269|PubMed:21233214, ECO:0000269|PubMed:26269648, ECO:0000269|PubMed:8046438, ECO:0000269|PubMed:8361541}. Synapse {ECO:0000250|UniProtKB:P63142}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P63142}. Cell projection, lamellipodium membrane {ECO:0000250|UniProtKB:P63142}. Synapse, synaptosome {ECO:0000269|PubMed:21233214}. Presynaptic cell membrane {ECO:0000269|PubMed:21233214}. Cell projection, dendrite {ECO:0000269|PubMed:8046438}. Perikaryon {ECO:0000269|PubMed:26269648, ECO:0000269|PubMed:8046438}. Cell junction, paranodal septate junction {ECO:0000269|PubMed:25378149}. 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. Coexpression with KCNA1 inhibits cell surface expression (By similarity). Cocaine-induced interaction with SIGMAR1 increases expression at the cell surface (PubMed:23332758). In myelinated peripheral axons, clustered in the juxtaparadonal region and at an internodal line located along the mesaxon and below the Schmidt-Lanterman incisures (PubMed:25378149). {ECO:0000250|UniProtKB:P63142, ECO:0000269|PubMed:23332758, ECO:0000269|PubMed:25378149}.
uniprot
proteins
transmembrane_region
TRANSMEM 161..182; /note="Helical; Name=Segment S1"; /evidence="ECO:0000250|UniProtKB:P63142"; TRANSMEM 222..243; /note="Helical; Name=Segment S2"; /evidence="ECO:0000250|UniProtKB:P63142"; TRANSMEM 255..275; /note="Helical; Name=Segment S3"; /evidence="ECO:0000250|UniProtKB:P63142"; TRANSMEM 290..310; /note="Helical; Voltage-sensor; Name=Segment S4"; /evidence="ECO:0000250|UniProtKB:P63142"; TRANSMEM 326..347; /note="Helical; Name=Segment S5"; /evidence="ECO:0000250|UniProtKB:P63142"; TRANSMEM 389..417; /note="Helical; Name=Segment S6"; /evidence="ECO:0000250|UniProtKB:P63142
uniprot
proteins