Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Potassium voltage-gated channel subfamily A member 2 (MK2) (Voltage-gated potassium channel subunit Kv1.2)

 KCNA2_MOUSE             Reviewed;         499 AA.
P63141; B2RS05; P15386; Q02010; Q8C8W4;
13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
13-SEP-2004, sequence version 1.
20-JUN-2018, entry version 149.
RecName: Full=Potassium voltage-gated channel subfamily A member 2;
AltName: Full=MK2 {ECO:0000303|PubMed:16141072};
AltName: Full=Voltage-gated potassium channel subunit Kv1.2;
Name=Kcna2;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2305265; DOI=10.1126/science.2305265;
Chandy K.G., Williams C.B., Spencer R.H., Aguilar B.A., Ghanshani S.,
Tempel B.L., Gutman G.A.;
"A family of three mouse potassium channel genes with intronless
coding regions.";
Science 247:973-975(1990).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Retina;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain {ECO:0000312|EMBL:AAI38651.1};
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 338-394.
PubMed=1691985; DOI=10.1016/0014-5793(90)80719-Y;
Betsholtz C., Baumann A., Kenna S., Ashcroft F.M., Ashcroft S.J.H.,
Berggren P.-O., Grupe A., Pongs O., Rorsman P., Sandblom J., Welsh M.;
"Expression of voltage-gated K+ channels in insulin-producing cells.
Analysis by polymerase chain reaction.";
FEBS Lett. 263:121-126(1990).
[6]
SUBUNIT, INTERACTION WITH KCNA1, TISSUE SPECIFICITY, AND SUBCELLULAR
LOCATION.
PubMed=8361541; DOI=10.1038/365075a0;
Wang H., Kunkel D.D., Martin T.M., Schwartzkroin P.A., Tempel B.L.;
"Heteromultimeric K+ channels in terminal and juxtaparanodal regions
of neurons.";
Nature 365:75-79(1993).
[7]
TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
PubMed=8046438;
Wang H., Kunkel D.D., Schwartzkroin P.A., Tempel B.L.;
"Localization of Kv1.1 and Kv1.2, two K channel proteins, to synaptic
terminals, somata, and dendrites in the mouse brain.";
J. Neurosci. 14:4588-4599(1994).
[8]
FUNCTION, AND INTERACTION WITH RHOA.
PubMed=9635436; DOI=10.1016/S0092-8674(00)81212-X;
Cachero T.G., Morielli A.D., Peralta E.G.;
"The small GTP-binding protein RhoA regulates a delayed rectifier
potassium channel.";
Cell 93:1077-1085(1998).
[9]
INTERACTION WITH KCNA5, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=9852577;
Sobko A., Peretz A., Shirihai O., Etkin S., Cherepanova V., Dagan D.,
Attali B.;
"Heteromultimeric delayed-rectifier K+ channels in Schwann cells:
developmental expression and role in cell proliferation.";
J. Neurosci. 18:10398-10408(1998).
[10]
FUNCTION, SUBCELLULAR LOCATION, AND ENZYME REGULATION.
PubMed=12527813; DOI=10.1124/mol.63.2.409;
Castle N.A., London D.O., Creech C., Fajloun Z., Stocker J.W.,
Sabatier J.-M.;
"Maurotoxin: a potent inhibitor of intermediate conductance Ca2+-
activated potassium channels.";
Mol. Pharmacol. 63:409-418(2003).
[11]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=17925011; DOI=10.1186/1741-7007-5-42;
Douglas C.L., Vyazovskiy V., Southard T., Chiu S.-Y., Messing A.,
Tononi G., Cirelli C.;
"Sleep in Kcna2 knockout mice.";
BMC Biol. 5:42-42(2007).
[12]
DISRUPTION PHENOTYPE, FUNCTION, DEVELOPMENTAL STAGE, AND TISSUE
SPECIFICITY.
PubMed=17634333; DOI=10.1152/jn.00640.2006;
Brew H.M., Gittelman J.X., Silverstein R.S., Hanks T.D., Demas V.P.,
Robinson L.C., Robbins C.A., McKee-Johnson J., Chiu S.Y., Messing A.,
Tempel B.L.;
"Seizures and reduced life span in mice lacking the potassium channel
subunit Kv1.2, but hypoexcitability and enlarged Kv1 currents in
auditory neurons.";
J. Neurophysiol. 98:1501-1525(2007).
[13]
REVIEW.
PubMed=17917103; DOI=10.1007/s12035-007-8001-0;
Baranauskas G.;
"Ionic channel function in action potential generation: current
perspective.";
Mol. Neurobiol. 35:129-150(2007).
[14]
SUBCELLULAR LOCATION.
PubMed=18509034; DOI=10.1523/JNEUROSCI.4431-07.2008;
Ogawa Y., Horresh I., Trimmer J.S., Bredt D.S., Peles E.,
Rasband M.N.;
"Postsynaptic density-93 clusters Kv1 channels at axon initial
segments independently of Caspr2.";
J. Neurosci. 28:5731-5739(2008).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-429, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=18034455; DOI=10.1021/pr0701254;
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
"Large-scale identification and evolution indexing of tyrosine
phosphorylation sites from murine brain.";
J. Proteome Res. 7:311-318(2008).
[16]
TISSUE SPECIFICITY.
PubMed=18760366; DOI=10.1016/j.mcn.2008.07.025;
Savvaki M., Panagiotaropoulos T., Stamatakis A., Sargiannidou I.,
Karatzioula P., Watanabe K., Stylianopoulou F., Karagogeos D.,
Kleopa K.A.;
"Impairment of learning and memory in TAG-1 deficient mice associated
with shorter CNS internodes and disrupted juxtaparanodes.";
Mol. Cell. Neurosci. 39:478-490(2008).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-434; SER-440 AND
SER-468, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Brain;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[18]
FUNCTION, MUTAGENESIS OF ILE-402, SUBCELLULAR LOCATION, MISCELLANEOUS,
TISSUE SPECIFICITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=20696761; DOI=10.1074/jbc.M110.153676;
Xie G., Harrison J., Clapcote S.J., Huang Y., Zhang J.Y., Wang L.Y.,
Roder J.C.;
"A new Kv1.2 channelopathy underlying cerebellar ataxia.";
J. Biol. Chem. 285:32160-32173(2010).
[19]
FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND INTERACTION
WITH DRD2.
PubMed=21233214; DOI=10.1074/jbc.M110.153262;
Fulton S., Thibault D., Mendez J.A., Lahaie N., Tirotta E.,
Borrelli E., Bouvier M., Tempel B.L., Trudeau L.E.;
"Contribution of Kv1.2 voltage-gated potassium channel to D2
autoreceptor regulation of axonal dopamine overflow.";
J. Biol. Chem. 286:9360-9372(2011).
[20]
TISSUE SPECIFICITY.
PubMed=22649228; DOI=10.1523/JNEUROSCI.0719-12.2012;
Zenker J., Poirot O., de Preux Charles A.S., Arnaud E., Medard J.J.,
Lacroix C., Kuntzer T., Chrast R.;
"Altered distribution of juxtaparanodal kv1.2 subunits mediates
peripheral nerve hyperexcitability in type 2 diabetes mellitus.";
J. Neurosci. 32:7493-7498(2012).
[21]
INTERACTION WITH SIGMAR1, AND SUBCELLULAR LOCATION.
PubMed=23332758; DOI=10.1016/j.cell.2012.12.004;
Kourrich S., Hayashi T., Chuang J.Y., Tsai S.Y., Su T.P., Bonci A.;
"Dynamic interaction between sigma-1 receptor and Kv1.2 shapes
neuronal and behavioral responses to cocaine.";
Cell 152:236-247(2013).
[22]
DISRUPTION PHENOTYPE, FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND
TISSUE SPECIFICITY.
PubMed=23864368; DOI=10.1152/jn.00290.2013;
Wang W., Kim H.J., Lv P., Tempel B., Yamoah E.N.;
"Association of the Kv1 family of K+ channels and their functional
blueprint in the properties of auditory neurons as revealed by genetic
and functional analyses.";
J. Neurophysiol. 110:1751-1764(2013).
[23]
FUNCTION.
PubMed=23981714; DOI=10.1113/jphysiol.2013.259002;
Hyun J.H., Eom K., Lee K.H., Ho W.K., Lee S.H.;
"Activity-dependent downregulation of D-type K+ channel subunit Kv1.2
in rat hippocampal CA3 pyramidal neurons.";
J. Physiol. (Lond.) 591:5525-5540(2013).
[24]
SUBCELLULAR LOCATION.
PubMed=25378149; DOI=10.1523/JNEUROSCI.3369-14.2014;
Gordon A., Adamsky K., Vainshtein A., Frechter S., Dupree J.L.,
Rosenbluth J., Peles E.;
"Caspr and caspr2 are required for both radial and longitudinal
organization of myelinated axons.";
J. Neurosci. 34:14820-14826(2014).
-!- 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:0000305}.
-!- ENZYME 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}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
Note=Homotetrameric channels activate rapidly, i.e within a few
msec, but inactivation is very slow, with only a marginal
decrease in conductance over several seconds. The voltage-
dependence of activation and inactivation and other channel
characteristics vary depending on the experimental conditions,
the expression system, post-translational modifications and the
presence or absence of ancillary subunits. For the activation of
homotetrameric channels expressed in Chinese hamster ovary (CHO)
cells, the voltage at half-maximal amplitude is about -37 mV.
{ECO:0000269|PubMed:20696761};
-!- SUBUNIT: Homotetramer and heterotetramer with other channel-
forming alpha subunits, such as KCNA1, KCNA4, KCNA5, KCNA6 and
KCNA7 (PubMed:8361541, PubMed:9852577, PubMed:23864368). Channel
activity is regulated by interaction with beta subunits, including
KCNAB1 and KCNAB2 (By similarity). Identified in a complex with
KCNA1 and KCNAB2 (By similarity). Identified in a complex with
KCNA5 and KCNAB1 (By similarity). Identified in a complex with
KCNA4 and FYN (By similarity). Interacts with PTK2B (By
similarity). Interacts (via C-terminus) with CTTN (By similarity).
Interacts with ADAM22 (By similarity). Interacts with CNTNAP2 (By
similarity). Interacts (via C-terminus) with the PDZ domains of
DLG1, DLG2 and DLG4 (By similarity). Interacts (via N-terminal
cytoplasmic domain) with RHOA (GTP-bound form); this regulates
channel activity by reducing location at the cell surface in
response to CHRM1 activation (PubMed:9635436). Interacts with DRD2
(PubMed:21233214). Interacts with SIGMAR1; cocaine consumption
leads to increased interaction (PubMed:23332758).
{ECO:0000250|UniProtKB:P16389, ECO:0000250|UniProtKB:P63142,
ECO:0000250|UniProtKB:Q09081, ECO:0000269|PubMed:17634333,
ECO:0000269|PubMed:21233214, ECO:0000269|PubMed:23332758,
ECO:0000269|PubMed:8361541, ECO:0000269|PubMed:9635436,
ECO:0000269|PubMed:9852577, ECO:0000305,
ECO:0000305|PubMed:23864368}.
-!- INTERACTION:
Q60598:Cttn; NbExp=3; IntAct=EBI-644033, EBI-397955;
O55242:Sigmar1; NbExp=3; IntAct=EBI-644033, EBI-1557700;
Q9R0C9:Sigmar1 (xeno); NbExp=3; IntAct=EBI-644033, EBI-1557826;
-!- 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:8046438, ECO:0000269|PubMed:8361541}. Cell
junction, synapse {ECO:0000250|UniProtKB:P63142}. Endoplasmic
reticulum membrane {ECO:0000250|UniProtKB:P63142}. Cell
projection, lamellipodium membrane {ECO:0000250|UniProtKB:P63142}.
Cell junction, synapse, synaptosome {ECO:0000269|PubMed:21233214}.
Cell junction, synapse, presynaptic cell membrane
{ECO:0000269|PubMed:21233214}. Cell projection, dendrite
{ECO:0000269|PubMed:8046438}. Perikaryon
{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}.
-!- TISSUE SPECIFICITY: Detected in brain (PubMed:17634333). Detected
in cerebellum (PubMed:20696761). Detected in mitral cells in the
olfactory bulb (PubMed:8046438). Detected in cochlea
(PubMed:23864368). Detected in cerebellum, particularly in the
basket cell axon plexus and in the terminal regions around
Purkinje cells (PubMed:8361541, PubMed:8046438, PubMed:18760366).
Detected in juxtaparanodal regions in sciatic nerve
(PubMed:22649228). Detected in Schwann cells from sciatic nerve
(PubMed:9852577). Detected in dopamine neurons in substantia nigra
(PubMed:21233214). Detected in large myelinated fibers in
juxtaparanodes in the CA3 and CA1 areas of the hippocampus
(PubMed:8046438, PubMed:18760366). Detected in brain, in punctae
on fiber tracts in brain stem and spinal cord, and on axons in the
juxtaparanodal regions of the node of Ranvier (at protein level)
(PubMed:8361541). Detected in dopamine neurons in the midbrain
(PubMed:21233214). {ECO:0000269|PubMed:17634333,
ECO:0000269|PubMed:18760366, ECO:0000269|PubMed:20696761,
ECO:0000269|PubMed:22649228, ECO:0000269|PubMed:23864368,
ECO:0000269|PubMed:8046438, ECO:0000269|PubMed:8361541,
ECO:0000269|PubMed:9852577}.
-!- DEVELOPMENTAL STAGE: Detected at low levels in brainstem from
neonates; increases tenfold during the first 29 days after birth.
{ECO:0000269|PubMed:17634333}.
-!- DOMAIN: The cytoplasmic N-terminus is important for
tetramerization. Interactions between the different subunits
modulate the gating characteristics (By similarity). Besides, the
cytoplasmic N-terminal domain mediates interaction with RHOA and
thus is required for RHOA-mediated endocytosis (By similarity).
{ECO:0000250|UniProtKB:P63142}.
-!- DOMAIN: The transmembrane segment S4 functions as voltage-sensor
and is characterized by a series of positively charged amino acids
at every third position. Channel opening and closing is effected
by a conformation change that affects the position and orientation
of the voltage-sensor paddle formed by S3 and S4 within the
membrane. A transmembrane electric field that is positive inside
would push the positively charged S4 segment outwards, thereby
opening the pore, while a field that is negative inside would pull
the S4 segment inwards and close the pore. Changes in the position
and orientation of S4 are then transmitted to the activation gate
formed by the inner helix bundle via the S4-S5 linker region.
{ECO:0000250|UniProtKB:P63142}.
-!- 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}.
-!- DISRUPTION PHENOTYPE: Pups are born at the expected Mendelian rate
and appear normal during the first 14 days after birth. Starting
at 14 to 17 days after birth, mice exhibit susceptibility to
generalized seizures, followed by full tonic extension, which in
mice often results in fatal apne. The average lifespan is 17 days;
none survive more than 28 days (PubMed:17925011, PubMed:17634333).
At P17 seizures are very rare and abnormal electroencephalograph
activity is only present during the seizure. P17 pups have
significantly less non-rapid eye movement (NREM) sleep (-23%) and
significantly more waking (+21%) than wild-type siblings with no
change in rapid eye movement (REM) sleep time. The decrease in
NREM sleep is due to an increase in the number of waking episodes,
with no change in number or duration of sleep episodes
(PubMed:17925011). Auditory neurons from the medial nucleus of the
trapezoid body in brain stem are hypoexcitable and fire fewer
action potentials than wild-type neurons with significantly
smaller threshold current amplitudes (PubMed:17634333). In the
inner ear, spiral ganglion neurons display a hyperpolarized
resting membrane potential, increased excitability and increased
outward potassium currents; this might be because normally
channels there are heterotetramers formed by KCNA2 and KCNA4, so
the loss of KCNA2 changes channel characteristics
(PubMed:23864368). {ECO:0000269|PubMed:17634333,
ECO:0000269|PubMed:17925011, ECO:0000269|PubMed:23864368}.
-!- MISCELLANEOUS: Mutagenesis with N-ethyl-N-nitrosourea (ENU) lead
to the discovery of the Pingu (Pgu) phenotype. At P21,
heterozygous mice are clearly smaller than wild-type and have
abnormal gait with a higher stance and splayed hind limbs.
Homozygous mice are even smaller, and about half of them die
between P15 and P35. Mutant mice have difficulty staing on a
rotating rod and perform poorly in a beam-walking test, where they
display flattened posture, severe tremors, myoclonic jerks and
ataxic movement. These symptoms are alleviated by a drug used to
treat cerebellar ataxia. Measurements with Purkinje cells from
cerebellar brain slices show increased frequency and amplitude of
spontaneous inhibitory postsynaptic currents.
{ECO:0000269|PubMed:20696761}.
-!- MISCELLANEOUS: The delay or D-type current observed in hippocampus
pyramidal neurons is probably mediated by potassium channels
containing KCNA2 plus KCNA1 or other family members. It is
activated at about -50 mV, i.e. below the action potential
threshold, and is characterized by slow inactivation, extremely
slow recovery from inactivation, sensitivity to dendrotoxin (DTX)
and to 4-aminopyridine (4-AP). {ECO:0000305|PubMed:17917103}.
-!- SIMILARITY: Belongs to the potassium channel family. A (Shaker)
(TC 1.A.1.2) subfamily. Kv1.2/KCNA2 sub-subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; M30440; AAA39713.1; -; Genomic_DNA.
EMBL; AK044342; BAC31877.1; -; mRNA.
EMBL; CH466607; EDL01892.1; -; Genomic_DNA.
EMBL; BC138650; AAI38651.1; -; mRNA.
EMBL; BC138651; AAI38652.1; -; mRNA.
CCDS; CCDS17733.1; -.
PIR; B40090; I84204.
RefSeq; NP_032443.3; NM_008417.5.
RefSeq; XP_006501111.1; XM_006501048.3.
RefSeq; XP_006501112.1; XM_006501049.3.
RefSeq; XP_006501113.1; XM_006501050.3.
RefSeq; XP_006501114.1; XM_006501051.3.
RefSeq; XP_006501115.1; XM_006501052.3.
RefSeq; XP_006501116.1; XM_006501053.3.
RefSeq; XP_006501117.1; XM_006501054.3.
RefSeq; XP_006501118.1; XM_006501055.3.
UniGene; Mm.39285; -.
PDB; 5WIE; X-ray; 3.30 A; B/H=266-279.
PDBsum; 5WIE; -.
ProteinModelPortal; P63141; -.
SMR; P63141; -.
BioGrid; 200877; 5.
DIP; DIP-32239N; -.
IntAct; P63141; 7.
STRING; 10090.ENSMUSP00000041702; -.
iPTMnet; P63141; -.
PhosphoSitePlus; P63141; -.
MaxQB; P63141; -.
PaxDb; P63141; -.
PeptideAtlas; P63141; -.
PRIDE; P63141; -.
Ensembl; ENSMUST00000038695; ENSMUSP00000041702; ENSMUSG00000040724.
Ensembl; ENSMUST00000196403; ENSMUSP00000142873; ENSMUSG00000040724.
Ensembl; ENSMUST00000197470; ENSMUSP00000143798; ENSMUSG00000040724.
GeneID; 16490; -.
KEGG; mmu:16490; -.
UCSC; uc008qws.2; mouse.
CTD; 3737; -.
MGI; MGI:96659; Kcna2.
eggNOG; KOG1545; Eukaryota.
eggNOG; COG1226; LUCA.
GeneTree; ENSGT00760000118846; -.
HOGENOM; HOG000231015; -.
HOVERGEN; HBG052230; -.
InParanoid; P63141; -.
KO; K04875; -.
OMA; PEPDHEC; -.
OrthoDB; EOG091G10NU; -.
PhylomeDB; P63141; -.
TreeFam; TF313103; -.
Reactome; R-MMU-1296072; Voltage gated Potassium channels.
ChiTaRS; Kcna2; mouse.
PRO; PR:P63141; -.
Proteomes; UP000000589; Chromosome 3.
Bgee; ENSMUSG00000040724; -.
Genevisible; P63141; MM.
GO; GO:0030424; C:axon; IDA:UniProtKB.
GO; GO:0043679; C:axon terminus; IDA:UniProtKB.
GO; GO:0030425; C:dendrite; IDA:UniProtKB.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0005887; C:integral component of plasma membrane; IMP:UniProtKB.
GO; GO:0044224; C:juxtaparanode region of axon; IDA:UniProtKB.
GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
GO; GO:0031258; C:lamellipodium membrane; IEA:UniProtKB-SubCell.
GO; GO:0032809; C:neuronal cell body membrane; IDA:UniProtKB.
GO; GO:0033010; C:paranodal junction; IEA:UniProtKB-SubCell.
GO; GO:0043204; C:perikaryon; IDA:UniProtKB.
GO; GO:0034705; C:potassium channel complex; ISO:MGI.
GO; GO:0042734; C:presynaptic membrane; IEA:UniProtKB-SubCell.
GO; GO:0008076; C:voltage-gated potassium channel complex; IDA:BHF-UCL.
GO; GO:0005251; F:delayed rectifier potassium channel activity; ISS:UniProtKB.
GO; GO:0019894; F:kinesin binding; ISO:MGI.
GO; GO:0015271; F:outward rectifier potassium channel activity; ISO:MGI.
GO; GO:0005249; F:voltage-gated potassium channel activity; IDA:UniProtKB.
GO; GO:0019228; P:neuronal action potential; ISS:UniProtKB.
GO; GO:0021633; P:optic nerve structural organization; IMP:MGI.
GO; GO:0071805; P:potassium ion transmembrane transport; IDA:UniProtKB.
GO; GO:0051259; P:protein complex oligomerization; ISO:MGI.
GO; GO:0051260; P:protein homooligomerization; IEA:InterPro.
GO; GO:0045188; P:regulation of circadian sleep/wake cycle, non-REM sleep; IMP:UniProtKB.
GO; GO:0014059; P:regulation of dopamine secretion; IMP:UniProtKB.
GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
GO; GO:0019233; P:sensory perception of pain; ISS:UniProtKB.
Gene3D; 1.20.120.350; -; 1.
InterPro; IPR000210; BTB/POZ_dom.
InterPro; IPR005821; Ion_trans_dom.
InterPro; IPR003968; K_chnl_volt-dep_Kv.
InterPro; IPR003972; K_chnl_volt-dep_Kv1.
InterPro; IPR004049; K_chnl_volt-dep_Kv1.2.
InterPro; IPR011333; SKP1/BTB/POZ_sf.
InterPro; IPR003131; T1-type_BTB.
InterPro; IPR028325; VG_K_chnl.
InterPro; IPR027359; Volt_channel_dom_sf.
PANTHER; PTHR11537; PTHR11537; 1.
PANTHER; PTHR11537:SF23; PTHR11537:SF23; 1.
Pfam; PF02214; BTB_2; 1.
Pfam; PF00520; Ion_trans; 1.
PRINTS; PR00169; KCHANNEL.
PRINTS; PR01509; KV12CHANNEL.
PRINTS; PR01491; KVCHANNEL.
PRINTS; PR01496; SHAKERCHANEL.
SMART; SM00225; BTB; 1.
SUPFAM; SSF54695; SSF54695; 1.
1: Evidence at protein level;
3D-structure; Cell junction; Cell membrane; Cell projection;
Complete proteome; Endoplasmic reticulum; Glycoprotein; Ion channel;
Ion transport; Lipoprotein; Membrane; Palmitate; Phosphoprotein;
Potassium; Potassium channel; Potassium transport; Reference proteome;
Synapse; Synaptosome; Transmembrane; Transmembrane helix; Transport;
Voltage-gated channel.
CHAIN 1 499 Potassium voltage-gated channel subfamily
A member 2.
/FTId=PRO_0000053973.
TOPO_DOM 1 160 Cytoplasmic.
{ECO:0000250|UniProtKB:P63142}.
TRANSMEM 161 182 Helical; Name=Segment S1.
{ECO:0000250|UniProtKB:P63142}.
TOPO_DOM 183 221 Extracellular.
{ECO:0000250|UniProtKB:P63142}.
TRANSMEM 222 243 Helical; Name=Segment S2.
{ECO:0000250|UniProtKB:P63142}.
TOPO_DOM 244 254 Cytoplasmic.
{ECO:0000250|UniProtKB:P63142}.
TRANSMEM 255 275 Helical; Name=Segment S3.
{ECO:0000250|UniProtKB:P63142}.
TOPO_DOM 276 289 Extracellular.
{ECO:0000250|UniProtKB:P63142}.
TRANSMEM 290 310 Helical; Voltage-sensor; Name=Segment S4.
{ECO:0000250|UniProtKB:P63142}.
TOPO_DOM 311 325 Cytoplasmic.
{ECO:0000250|UniProtKB:P63142}.
TRANSMEM 326 347 Helical; Name=Segment S5.
{ECO:0000250|UniProtKB:P63142}.
TOPO_DOM 348 361 Extracellular.
{ECO:0000250|UniProtKB:P63142}.
INTRAMEM 362 373 Helical; Name=Pore helix.
{ECO:0000250|UniProtKB:P63142}.
INTRAMEM 374 381 {ECO:0000250|UniProtKB:P63142}.
TOPO_DOM 382 388 Extracellular.
{ECO:0000250|UniProtKB:P63142}.
TRANSMEM 389 417 Helical; Name=Segment S6.
{ECO:0000250|UniProtKB:P63142}.
TOPO_DOM 418 499 Cytoplasmic.
{ECO:0000250|UniProtKB:P63142}.
REGION 1 125 Tetramerization domain.
{ECO:0000250|UniProtKB:P63142}.
REGION 312 325 S4-S5 linker.
{ECO:0000250|UniProtKB:P63142}.
MOTIF 374 379 Selectivity filter.
{ECO:0000250|UniProtKB:P63142}.
MOTIF 497 499 PDZ-binding.
{ECO:0000250|UniProtKB:P63142}.
SITE 252 252 Important for normal, slow channel
gating. {ECO:0000250|UniProtKB:P63142}.
SITE 381 381 Important for binding with the scorpion
mesomartoxin; when the scorpion
mesomartoxin-rKv1.2/KCNA2 interaction is
modeled, this residue is close to the 'Y-
57' residue of the toxin.
{ECO:0000250|UniProtKB:P63142}.
MOD_RES 429 429 Phosphotyrosine.
{ECO:0000244|PubMed:18034455}.
MOD_RES 434 434 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 440 440 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 441 441 Phosphoserine.
{ECO:0000250|UniProtKB:Q09081}.
MOD_RES 449 449 Phosphoserine.
{ECO:0000250|UniProtKB:Q09081}.
MOD_RES 458 458 Phosphotyrosine.
{ECO:0000250|UniProtKB:P63142}.
MOD_RES 468 468 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
LIPID 244 244 S-palmitoyl cysteine. {ECO:0000255}.
CARBOHYD 207 207 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
MUTAGEN 402 402 I->T: In Pgu; chronic motor
incoordination; decreases the number of
functional channels at the cell surface.
{ECO:0000269|PubMed:20696761}.
CONFLICT 33 33 E -> G (in Ref. 2; BAC31877).
{ECO:0000305}.
SEQUENCE 499 AA; 56701 MW; A8FEA6F3F59AF42A CRC64;
MTVATGDPVD EAAALPGHPQ DTYDPEADHE CCERVVINIS GLRFETQLKT LAQFPETLLG
DPKKRMRYFD PLRNEYFFDR NRPSFDAILY YYQSGGRLRR PVNVPLDIFS EEIRFYELGE
EAMEMFREDE GYIKEEERPL PENEFQRQVW LLFEYPESSG PARIIAIVSV MVILISIVSF
CLETLPIFRD ENEDMHGGGV TFHTYSNSTI GYQQSTSFTD PFFIVETLCI IWFSFEFLVR
FFACPSKAGF FTNIMNIIDI VAIIPYFITL GTELAEKPED AQQGQQAMSL AILRVIRLVR
VFRIFKLSRH SKGLQILGQT LKASMRELGL LIFFLFIGVI LFSSAVYFAE ADERDSQFPS
IPDAFWWAVV SMTTVGYGDM VPTTIGGKIV GSLCAIAGVL TIALPVPVIV SNFNYFYHRE
TEGEEQAQYL QVTSCPKIPS SPDLKKSRSA STISKSDYME IQEGVNNSNE DFREENLKTA
NCTLANTNYV NITKMLTDV


Related products :

Catalog number Product name Quantity
18-003-42663 Potassium voltage-gated channel subfamily KQT member 2 - Voltage-gated potassium channel subunit Kv7.2; Neuroblastoma-specific potassium channel subunit alpha KvLQT2; KQT-like 2 Polyclonal 0.05 mg Aff Pur
18-003-42664 Potassium voltage-gated channel subfamily KQT member 2 - Voltage-gated potassium channel subunit Kv7.2; Neuroblastoma-specific potassium channel subunit alpha KvLQT2; KQT-like 2 Polyclonal 0.1 mg Protein A
28-297 This gene encodes a member of the potassium channel, voltage-gated, subfamily H. This member is a pore-forming (alpha) subunit of a voltage-gated non-inactivating delayed rectifier potassium channel. 0.1 mg
18-662-20074 Potassium voltage-gated channel subfamily C member 1 - Voltage-gated potassium channel subunit Kv3.1; Kv4; NGK2; RAW2 Polyclonal 0.1 ml
18-662-20009 Potassium voltage-gated channel subfamily B member 2 - Voltage-gated potassium channel subunit Kv2.2; CDRK Polyclonal 0.1 ml
18-003-42629 Potassium voltage-gated channel subfamily D member 3 - Voltage-gated potassium channel subunit Kv4.3 Polyclonal 0.1 mg Protein A
18-003-43133 Potassium voltage-gated channel subfamily G member 1 - Voltage-gated potassium channel subunit Kv6.1; kH2 Polyclonal 0.05 mg Aff Pur
18-003-42631 Cyclic GMP gated potassium channel - Potassium voltage-gated channel. shaker-related subfamily. member 10 Polyclonal 0.1 mg Protein A
E0614m Rat ELISA Kit FOR Potassium voltage-gated channel subfamily KQT member 2 96T
E15045p Pig ELISA Kit FOR Potassium voltage-gated channel subfamily H member 2 96T
KCNG3_RAT Rat ELISA Kit FOR Potassium voltage-gated channel subfamily G member 3 96T
KCNA5_RAT Rat ELISA Kit FOR Potassium voltage-gated channel subfamily A member 5 96T
KCNQ1_PIG Pig ELISA Kit FOR Potassium voltage-gated channel subfamily KQT member 1 96T
EH2214 Potassium voltage-gated channel subfamily B member 2 Elisa Kit 96T
E0522m Rat ELISA Kit FOR Potassium voltage-gated channel subfamily KQT member 1 96T
E13768r Rat ELISA Kit FOR Potassium voltage-gated channel subfamily KQT member 4 96T
KCNH4_RAT Rat ELISA Kit FOR Potassium voltage-gated channel subfamily H member 4 96T
PPAC_MOUSE Rat ELISA Kit FOR Potassium voltage-gated channel subfamily KQT member 1 96T
WDR64_MOUSE Rat ELISA Kit FOR Potassium voltage-gated channel subfamily KQT member 2 96T
E1366h Rat ELISA Kit FOR Potassium voltage-gated channel subfamily H member 1 96T
KCNH2_RAT Rat ELISA Kit FOR Potassium voltage-gated channel subfamily H member 2 96T
CSB-EL012097RA Rat Potassium voltage-gated channel subfamily S member 3(KCNS3) ELISA kit 96T
CSB-EL012096RA Rat Potassium voltage-gated channel subfamily S member 2(KCNS2) ELISA kit 96T
CSB-EL012095RA Rat Potassium voltage-gated channel subfamily S member 1(KCNS1) ELISA kit 96T
CSB-EL012090RA Rat Potassium voltage-gated channel subfamily KQT member 2(KCNQ2) ELISA kit 96T


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur