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Potassium voltage-gated channel subfamily D member 2 (Voltage-gated potassium channel subunit Kv4.2)

 KCND2_HUMAN             Reviewed;         630 AA.
Q9NZV8; O95012; O95021; Q2TBD3; Q9UBY7; Q9UN98; Q9UNH9;
07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
07-NOV-2003, sequence version 2.
23-MAY-2018, entry version 165.
RecName: Full=Potassium voltage-gated channel subfamily D member 2;
AltName: Full=Voltage-gated potassium channel subunit Kv4.2;
Name=KCND2; Synonyms=KIAA1044;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
PubMed=9843794;
Kong W., Po S., Yamagishi T., Ashen M.D., Stetten G., Tomaselli G.F.;
"Isolation and characterization of the human gene encoding Ito:
further diversity by alternative mRNA splicing.";
Am. J. Physiol. 275:H1963-H1970(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=10470851; DOI=10.1093/dnares/6.3.197;
Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N.,
Tanaka A., Kotani H., Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XIV.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro.";
DNA Res. 6:197-205(1999).
[3]
NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND FUNCTION.
PubMed=10551270;
Zhu X.-R., Wulf A., Schwarz M., Isbrandt D., Pongs O.;
"Characterization of human Kv4.2 mediating a rapidly-inactivating
transient voltage-sensitive K+ current.";
Recept. Channels 6:387-400(1999).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
TISSUE=Brain cortex;
PubMed=10729221; DOI=10.1006/geno.2000.6117;
Isbrandt D., Leicher T., Waldschuetz R., Zhu X.-R., Luhmann U.,
Michel U., Sauter K., Pongs O.;
"Gene structures and expression profiles of three human KCND (Kv4)
potassium channels mediating A-type currents I(TO) and I(SA).";
Genomics 64:144-154(2000).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12853948; DOI=10.1038/nature01782;
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
Waterston R.H., Wilson R.K.;
"The DNA sequence of human chromosome 7.";
Nature 424:157-164(2003).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
[7]
MUTAGENESIS OF 601-PRO--PRO-604, SUBCELLULAR LOCATION, AND INTERACTION
WITH FLNA AND FLNC.
PubMed=11102480;
Petrecca K., Miller D.M., Shrier A.;
"Localization and enhanced current density of the Kv4.2 potassium
channel by interaction with the actin-binding protein filamin.";
J. Neurosci. 20:8736-8744(2000).
[8]
INTERACTION WITH KCNIP1.
PubMed=10676964; DOI=10.1038/35000592;
An W.F., Bowlby M.R., Betty M., Cao J., Ling H.-P., Mendoza G.,
Hinson J.W., Mattsson K.I., Strassle B.W., Trimmer J.S., Rhodes K.J.;
"Modulation of A-type potassium channels by a family of calcium
sensors.";
Nature 403:553-556(2000).
[9]
INTERACTION WITH KCNIP2.
PubMed=11287421; DOI=10.1074/jbc.M101320200;
Baehring R., Dannenberg J., Peters H.C., Leicher T., Pongs O.,
Isbrandt D.;
"Conserved Kv4 N-terminal domain critical for effects of Kv channel-
interacting protein 2.2 on channel expression and gating.";
J. Biol. Chem. 276:23888-23894(2001).
[10]
FUNCTION, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES, AND
DOMAIN.
PubMed=11507158; DOI=10.1111/j.1469-7793.2001.00065.x;
Baehring R., Boland L.M., Varghese A., Gebauer M., Pongs O.;
"Kinetic analysis of open- and closed-state inactivation transitions
in human Kv4.2 A-type potassium channels.";
J. Physiol. (Lond.) 535:65-81(2001).
[11]
TISSUE SPECIFICITY.
PubMed=12395204; DOI=10.1007/s00395-002-0377-4;
Bertaso F., Sharpe C.C., Hendry B.M., James A.F.;
"Expression of voltage-gated K+ channels in human atrium.";
Basic Res. Cardiol. 97:424-433(2002).
[12]
INTERACTION WITH KCNIP4.
PubMed=11847232; DOI=10.1074/jbc.M200897200;
Morohashi Y., Hatano N., Ohya S., Takikawa R., Watabiki T.,
Takasugi N., Imaizumi Y., Tomita T., Iwatsubo T.;
"Molecular cloning and characterization of CALP/KChIP4, a novel EF-
hand protein interacting with presenilin 2 and voltage-gated potassium
channel subunit Kv4.";
J. Biol. Chem. 277:14965-14975(2002).
[13]
INTERACTION WITH KCNIP3.
PubMed=12451113;
Schrader L.A., Anderson A.E., Mayne A., Pfaffinger P.J., Sweatt J.D.;
"PKA modulation of Kv4.2-encoded A-type potassium channels requires
formation of a supramolecular complex.";
J. Neurosci. 22:10123-10133(2002).
[14]
FUNCTION, SUBCELLULAR LOCATION, AND DOMAIN.
PubMed=14695263; DOI=10.1016/S0006-3495(04)74097-7;
Gebauer M., Isbrandt D., Sauter K., Callsen B., Nolting A., Pongs O.,
Baehring R.;
"N-type inactivation features of Kv4.2 channel gating.";
Biophys. J. 86:210-223(2004).
[15]
FUNCTION, INTERACTION WITH DPP10 AND DPP6, AND SUBCELLULAR LOCATION.
PubMed=15454437; DOI=10.1529/biophysj.104.042358;
Jerng H.H., Qian Y., Pfaffinger P.J.;
"Modulation of Kv4.2 channel expression and gating by dipeptidyl
peptidase 10 (DPP10).";
Biophys. J. 87:2380-2396(2004).
[16]
INTERACTION WITH KCNIP1 AND KCNIP2, SUBUNIT, AND DOMAIN.
PubMed=15358149; DOI=10.1016/j.bbrc.2004.07.006;
Lin Y.-L., Chen C.Y., Cheng C.P., Chang L.S.;
"Protein-protein interactions of KChIP proteins and Kv4.2.";
Biochem. Biophys. Res. Commun. 321:606-610(2004).
[17]
FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, DOMAIN, AND ROLE IN DISEASE.
PubMed=16934482; DOI=10.1016/j.nbd.2006.07.001;
Singh B., Ogiwara I., Kaneda M., Tokonami N., Mazaki E., Baba K.,
Matsuda K., Inoue Y., Yamakawa K.;
"A Kv4.2 truncation mutation in a patient with temporal lobe
epilepsy.";
Neurobiol. Dis. 24:245-253(2006).
[18]
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).
[19]
REVIEW.
PubMed=18357523; DOI=10.1007/s11064-008-9650-8;
Covarrubias M., Bhattacharji A., De Santiago-Castillo J.A.,
Dougherty K., Kaulin Y.A., Na-Phuket T.R., Wang G.;
"The neuronal Kv4 channel complex.";
Neurochem. Res. 33:1558-1567(2008).
[20]
FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND MUTAGENESIS OF GLY-309;
ARG-311; ILE-312; LEU-313; GLY-314; TYR-315; THR-316; LEU-317;
LYS-318; SER-319; CYS-320; SER-322; GLU-323; LEU-324; LEU-327;
LEU-328; VAL-397; ILE-398; ALA-399; PRO-401; 402-VAL--VAL-404;
PRO-403; ILE-405; VAL-406; SER-407; ASN-408 AND PHE-409.
PubMed=19171772; DOI=10.1085/jgp.200810073;
Barghaan J., Baehring R.;
"Dynamic coupling of voltage sensor and gate involved in closed-state
inactivation of Kv4.2 channels.";
J. Gen. Physiol. 133:205-224(2009).
[21]
FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND INTERACTION WITH KCNIP4.
PubMed=24811166; DOI=10.1074/jbc.M114.563452;
Kitazawa M., Kubo Y., Nakajo K.;
"The stoichiometry and biophysical properties of the Kv4 potassium
channel complex with K+ channel-interacting protein (KChIP) subunits
are variable, depending on the relative expression level.";
J. Biol. Chem. 289:17597-17609(2014).
[22]
STRUCTURE BY ELECTRON MICROSCOPY (21 ANGSTROMS) OF THE KCND2-KCNIP2
COMPLEX, FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
PubMed=14980201; DOI=10.1016/S0896-6273(04)00050-9;
Kim L.A., Furst J., Gutierrez D., Butler M.H., Xu S., Goldstein S.A.,
Grigorieff N.;
"Three-dimensional structure of I(to); Kv4.2-KChIP2 ion channels by
electron microscopy at 21 Angstrom resolution.";
Neuron 41:513-519(2004).
[23]
INTERACTION WITH KCNIP2, FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
PubMed=14623880; DOI=10.1074/jbc.M311332200;
Kim L.A., Furst J., Butler M.H., Xu S., Grigorieff N., Goldstein S.A.;
"Ito channels are octameric complexes with four subunits of each Kv4.2
and K+ channel-interacting protein 2.";
J. Biol. Chem. 279:5549-5554(2004).
[24]
TISSUE SPECIFICITY.
PubMed=15991246; DOI=10.1002/jcp.20453;
Kunz L., Ramsch R., Krieger A., Young K.A., Dissen G.A.,
Stouffer R.L., Ojeda S.R., Mayerhofer A.;
"Voltage-dependent K+ channel acts as sex steroid sensor in endocrine
cells of the human ovary.";
J. Cell. Physiol. 206:167-174(2006).
[25]
INTERACTION WITH KCNIP1.
PubMed=14980207; DOI=10.1016/S0896-6273(04)00049-2;
Scannevin R.H., Wang K., Jow F., Megules J., Kopsco D.C., Edris W.,
Carroll K.C., Lu Q., Xu W., Xu Z., Katz A.H., Olland S., Lin L.,
Taylor M., Stahl M., Malakian K., Somers W., Mosyak L., Bowlby M.R.,
Chanda P., Rhodes K.J.;
"Two N-terminal domains of Kv4 K(+) channels regulate binding to and
modulation by KChIP1.";
Neuron 41:587-598(2004).
[26]
INTERACTION WITH DLG1.
PubMed=19213956; DOI=10.1161/CIRCRESAHA.108.191007;
El-Haou S., Balse E., Neyroud N., Dilanian G., Gavillet B., Abriel H.,
Coulombe A., Jeromin A., Hatem S.N.;
"Kv4 potassium channels form a tripartite complex with the anchoring
protein SAP97 and CaMKII in cardiac myocytes.";
Circ. Res. 104:758-769(2009).
[27]
VARIANT MET-404, CHARACTERIZATION OF VARIANT MET-404, FUNCTION, AND
SUBCELLULAR LOCATION.
PubMed=24501278; DOI=10.1093/hmg/ddu056;
Lee H., Lin M.C., Kornblum H.I., Papazian D.M., Nelson S.F.;
"Exome sequencing identifies de novo gain of function missense
mutation in KCND2 in identical twins with autism and seizures that
slows potassium channel inactivation.";
Hum. Mol. Genet. 23:3481-3489(2014).
-!- 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:15454437, PubMed:14695263,
PubMed:14623880, PubMed:14980201, PubMed:16934482,
PubMed:24811166, PubMed:24501278). 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:15454437,
PubMed:14623880, PubMed:14980201, 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).
{ECO:0000250|UniProtKB:Q63881, ECO:0000250|UniProtKB:Q9Z0V2,
ECO:0000269|PubMed:10551270, ECO:0000269|PubMed:10729221,
ECO:0000269|PubMed:11507158, ECO:0000269|PubMed:14623880,
ECO:0000269|PubMed:14695263, ECO:0000269|PubMed:14980201,
ECO:0000269|PubMed:15454437, ECO:0000269|PubMed:16934482,
ECO:0000269|PubMed:19171772, ECO:0000269|PubMed:24501278,
ECO:0000269|PubMed:24811166}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
Note=Homotetrameric channels activate rapidly, i.e within a few
msec. After that, they inactivate rapidly, i.e within about 50-
100 msec. The voltage-dependence of activation and inactivation
and other channel characteristics vary depending on the
experimental conditions, the expression system and the presence
or absence of ancillary subunits. Homotetrameric channels have a
unitary conductance of about 4 pS when expressed in a
heterologous system. For the activation of homotetrameric
channels expressed in xenopus oocytes, the voltage at half-
maximal amplitude is about -10 mV. The time constant for
inactivation is about 20 msec. For inactivation, the voltage at
half-maximal amplitude is -62 mV. The time constant for recovery
after inactivation is about 70 msec.
{ECO:0000305|PubMed:11507158, ECO:0000305|PubMed:17917103};
-!- SUBUNIT: Homotetramer or heterotetramer with KCND1 or KCND3
(PubMed:14980201, PubMed:16934482, PubMed:24811166). Associates
with the regulatory subunits KCNIP1, KCNIP2, KCNIP3 and KCNIP4
(PubMed:10676964, PubMed:11287421, PubMed:11847232,
PubMed:12451113, PubMed:15358149, PubMed:14623880,
PubMed:14980201, PubMed:14980207, PubMed:24811166). 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, DPP6 and DPP10
(PubMed:11102480, PubMed:15454437, PubMed:24811166).
{ECO:0000250|UniProtKB:Q63881, ECO:0000250|UniProtKB:Q9Z0V2,
ECO:0000269|PubMed:10676964, ECO:0000269|PubMed:11102480,
ECO:0000269|PubMed:11287421, ECO:0000269|PubMed:11847232,
ECO:0000269|PubMed:12451113, ECO:0000269|PubMed:14623880,
ECO:0000269|PubMed:14980201, ECO:0000269|PubMed:14980207,
ECO:0000269|PubMed:15358149, ECO:0000269|PubMed:15454437,
ECO:0000269|PubMed:16934482, ECO:0000269|PubMed:19213956,
ECO:0000269|PubMed:24811166, ECO:0000305|PubMed:19171772}.
-!- INTERACTION:
Q9NZI2:KCNIP1; NbExp=4; IntAct=EBI-1646745, EBI-2120635;
Q9NS61:KCNIP2; NbExp=3; IntAct=EBI-1646745, EBI-1052975;
Q9NS61-3:KCNIP2; NbExp=3; IntAct=EBI-1646745, EBI-1053010;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11102480,
ECO:0000269|PubMed:11507158, ECO:0000269|PubMed:14623880,
ECO:0000269|PubMed:14695263, ECO:0000269|PubMed:14980201,
ECO:0000269|PubMed:15454437, ECO:0000269|PubMed:16934482,
ECO:0000269|PubMed:19171772, ECO:0000269|PubMed:24501278,
ECO:0000269|PubMed:24811166}; Multi-pass membrane protein
{ECO:0000269|PubMed:11102480, ECO:0000269|PubMed:14980201,
ECO:0000305}. Cell projection, dendrite
{ECO:0000269|PubMed:11102480}. Cell junction, synapse
{ECO:0000250|UniProtKB:Q63881}. Perikaryon
{ECO:0000250|UniProtKB:Q63881}. Cell junction, synapse,
postsynaptic cell membrane {ECO:0000250|UniProtKB:Q63881}. Cell
projection, dendritic spine {ECO:0000250|UniProtKB:Q63881}. Cell
junction {ECO:0000250|UniProtKB:Q63881}. Note=In neurons,
primarily detected on dendrites, dendritic spines and on the
neuron cell body, but not on axons. Localized preferentially at
the dendrites of pyramidal cells in the hippocampus CA1 layer.
Detected at GABAergic synapses. Detected at cell junctions that
are distinct from synaptic cell contacts. Detected in lipid rafts.
Detected primarily at the endoplasmic reticulum or Golgi when
expressed by itself (PubMed:15454437). Interaction with KCNIP1,
KCNIP2, KCNIP3 or KCNIP4 promotes expression at the cell membrane
(PubMed:15454437, PubMed:24811166). Interaction with DPP6 or DPP10
promotes expression at the cell membrane (By similarity).
Internalized from the cell membrane by clathrin-dependent
endocytosis in response to activation of AMPA-selective glutamate
receptors and PKA-mediated phosphorylation at Ser-552.
Redistributed from dendritic spines to the main dendritic shaft in
response to activation of AMPA-selective glutamate receptors and
activation of PKA (By similarity). {ECO:0000250|UniProtKB:Q63881,
ECO:0000250|UniProtKB:Q9Z0V2, ECO:0000269|PubMed:15454437,
ECO:0000269|PubMed:24811166}.
-!- TISSUE SPECIFICITY: Detected in ovary, in corpus luteum and in
granulosa and theca cells in the follicle (at protein level)
(PubMed:15991246). Highly expressed throughout the brain
(PubMed:10551270, PubMed:10729221). Detected in amygdala, caudate
nucleus, cerebellum, hippocampus, substantia nigra and thalamus
(PubMed:10551270, PubMed:10729221). Expression is not detectable
or very low in heart, kidney, liver, lung, pancreas and skeletal
muscle (PubMed:10551270, PubMed:10729221). Not detectable in human
heart atrium (PubMed:12395204). {ECO:0000269|PubMed:10551270,
ECO:0000269|PubMed:10729221, ECO:0000269|PubMed:12395204,
ECO:0000269|PubMed:15991246}.
-!- 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}.
-!- DOMAIN: The N-terminal cytoplasmic region can mediate N-type
inactivation by physically blocking the channel (PubMed:14695263).
This probably does not happen in vivo, where the N-terminal region
mediates interaction with regulatory subunits, such as KCNIP1 and
KCNIP2 (PubMed:15358149). The zinc binding sites in the N-terminal
domain are important for tetramerization and assembly of a
functional channel complex (By similarity). Most likely, the
channel undergoes closed-state inactivation, where a subtle
conformation change would render the protein less sensitive to
activation. {ECO:0000250|UniProtKB:Q63881,
ECO:0000305|PubMed:11507158, ECO:0000305|PubMed:14695263,
ECO:0000305|PubMed:15358149, ECO:0000305|PubMed:18357523}.
-!- DOMAIN: The C-terminal cytoplasmic region is important for normal
expression at the cell membrane and modulates the voltage-
dependence of channel activation and inactivation
(PubMed:16934482). It is required for interaction with KCNIP2, and
probably other family members as well (By similarity).
{ECO:0000250|UniProtKB:Q63881, ECO:0000269|PubMed:16934482}.
-!- PTM: Phosphorylation at Ser-438 in response to MAPK activation is
increased in stimulated dendrites. Interaction with KCNIP2 and
DPP6 propomtes phosphorylation by PKA at Ser-552. Phosphorylation
at Ser-552 has no effect on interaction with KCNIP3, but is
required for the regulation of channel activity by KCNIP3.
Phosphorylation at Ser-552 leads to KCND2 internalization (By
similarity). Phosphorylated by MAPK in response to signaling via
the metabotropic glutamate receptor GRM5 (By similarity).
Phosphorylation at Ser-616 is required for the down-regulation of
neuronal A-type currents in response to signaling via GRM5 (By
similarity). {ECO:0000250|UniProtKB:Q63881,
ECO:0000250|UniProtKB:Q9Z0V2}.
-!- DISEASE: Note=KNCD2 mutations have been found in a family with
autism and epilepsy and may play a role in disease pathogenesis.
Autism is a complex multifactorial, pervasive developmental
disorder characterized by impairments in reciprocal social
interaction and communication, restricted and stereotyped patterns
of interests and activities, and the presence of developmental
abnormalities by 3 years of age. Epilepsy is characterized by
paroxysmal transient disturbances of the electrical activity of
the brain that may be manifested as episodic impairment or loss of
consciousness, abnormal motor phenomena, psychic or sensory
disturbances, or perturbation of the autonomic nervous system.
{ECO:0000269|PubMed:24501278}.
-!- DISEASE: Note=A KCND2 mutation leading to the production of a C-
terminally truncated protein has been identified in a patient with
epilepsy. Epilepsy is characterized by paroxysmal transient
disturbances of the electrical activity of the brain that may be
manifested as episodic impairment or loss of consciousness,
abnormal motor phenomena, psychic or sensory disturbances, or
perturbation of the autonomic nervous system.
{ECO:0000269|PubMed:16934482}.
-!- MISCELLANEOUS: The transient neuronal A-type potassium current
called I(SA) is triggered at membrane potentials that are below
the threshold for action potentials. It inactivates rapidly and
recovers rapidly from inactivation. It regulates the firing of
action potentials and plays a role in synaptic integration and
plasticity. Potassium channels containing KCND2 account for about
80% of the neuronal A-type potassium current. In contrast, the
potassium channel responsible for the cardiac I(to) current
differs between species; it is mediated by KCND2 in rodents. In
human and other non-rodents KCND3 may play an equivalent role.
{ECO:0000269|PubMed:10551270, ECO:0000305|PubMed:17917103,
ECO:0000305|PubMed:18357523}.
-!- MISCELLANEOUS: Is specifically and reversibly inhibited by the
scorpion toxin Ts8 (AC P69940). {ECO:0000250|UniProtKB:Q63881}.
-!- SIMILARITY: Belongs to the potassium channel family. D (Shal) (TC
1.A.1.2) subfamily. Kv4.2/KCND2 sub-subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA82996.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF121104; AAD22053.1; -; mRNA.
EMBL; AB028967; BAA82996.2; ALT_INIT; mRNA.
EMBL; AJ010969; CAB56841.1; -; mRNA.
EMBL; AF166008; AAF65618.1; -; Genomic_DNA.
EMBL; AF166007; AAF65618.1; JOINED; Genomic_DNA.
EMBL; AC004888; AAC83405.1; -; Genomic_DNA.
EMBL; AC004946; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AF142568; AAD52159.1; -; Genomic_DNA.
EMBL; BC110449; AAI10450.1; -; mRNA.
EMBL; BC110450; AAI10451.1; -; mRNA.
CCDS; CCDS5776.1; -.
RefSeq; NP_036413.1; NM_012281.2.
UniGene; Hs.654739; -.
ProteinModelPortal; Q9NZV8; -.
SMR; Q9NZV8; -.
BioGrid; 109953; 18.
CORUM; Q9NZV8; -.
IntAct; Q9NZV8; 2.
STRING; 9606.ENSP00000333496; -.
ChEMBL; CHEMBL5885; -.
DrugBank; DB00321; Amitriptyline.
DrugBank; DB06637; Dalfampridine.
DrugBank; DB00280; Disopyramide.
DrugBank; DB00458; Imipramine.
TCDB; 1.A.1.2.5; the voltage-gated ion channel (vic) superfamily.
iPTMnet; Q9NZV8; -.
PhosphoSitePlus; Q9NZV8; -.
BioMuta; KCND2; -.
DMDM; 38258257; -.
EPD; Q9NZV8; -.
PaxDb; Q9NZV8; -.
PeptideAtlas; Q9NZV8; -.
PRIDE; Q9NZV8; -.
Ensembl; ENST00000331113; ENSP00000333496; ENSG00000184408.
GeneID; 3751; -.
KEGG; hsa:3751; -.
UCSC; uc003vjj.2; human.
CTD; 3751; -.
DisGeNET; 3751; -.
EuPathDB; HostDB:ENSG00000184408.9; -.
GeneCards; KCND2; -.
HGNC; HGNC:6238; KCND2.
HPA; HPA029068; -.
MIM; 605410; gene.
neXtProt; NX_Q9NZV8; -.
OpenTargets; ENSG00000184408; -.
PharmGKB; PA30030; -.
eggNOG; KOG4390; Eukaryota.
eggNOG; COG1226; LUCA.
GeneTree; ENSGT00760000118846; -.
HOVERGEN; HBG106687; -.
InParanoid; Q9NZV8; -.
KO; K04892; -.
OMA; GIQFQTW; -.
OrthoDB; EOG091G18X0; -.
PhylomeDB; Q9NZV8; -.
TreeFam; TF313103; -.
Reactome; R-HSA-1296072; Voltage gated Potassium channels.
Reactome; R-HSA-5576894; Phase 1 - inactivation of fast Na+ channels.
ChiTaRS; KCND2; human.
GeneWiki; KCND2; -.
GenomeRNAi; 3751; -.
PRO; PR:Q9NZV8; -.
Proteomes; UP000005640; Chromosome 7.
Bgee; ENSG00000184408; -.
CleanEx; HS_KCND2; -.
ExpressionAtlas; Q9NZV8; baseline and differential.
Genevisible; Q9NZV8; HS.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-SubCell.
GO; GO:0043197; C:dendritic spine; ISS:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
GO; GO:0031226; C:intrinsic component of plasma membrane; IMP:UniProtKB.
GO; GO:0032809; C:neuronal cell body membrane; ISS:UniProtKB.
GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0044853; C:plasma membrane raft; ISS:UniProtKB.
GO; GO:0045211; C:postsynaptic membrane; ISS:UniProtKB.
GO; GO:0008076; C:voltage-gated potassium channel complex; IDA:UniProtKB.
GO; GO:0005250; F:A-type (transient outward) potassium channel activity; IMP:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0005249; F:voltage-gated potassium channel activity; IDA:UniProtKB.
GO; GO:0001508; P:action potential; TAS:UniProtKB.
GO; GO:0071456; P:cellular response to hypoxia; ISS:UniProtKB.
GO; GO:0007268; P:chemical synaptic transmission; TAS:UniProtKB.
GO; GO:0045475; P:locomotor rhythm; IEA:Ensembl.
GO; GO:0019228; P:neuronal action potential; IEA:Ensembl.
GO; GO:0071805; P:potassium ion transmembrane transport; IDA:UniProtKB.
GO; GO:0051260; P:protein homooligomerization; IEA:InterPro.
GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
GO; GO:0019233; P:sensory perception of pain; IEA:Ensembl.
Gene3D; 1.20.120.350; -; 1.
InterPro; IPR000210; BTB/POZ_dom.
InterPro; IPR005821; Ion_trans_dom.
InterPro; IPR003968; K_chnl_volt-dep_Kv.
InterPro; IPR003975; K_chnl_volt-dep_Kv4.
InterPro; IPR004055; K_chnl_volt-dep_Kv4.2.
InterPro; IPR024587; K_chnl_volt-dep_Kv4_C.
InterPro; IPR021645; Shal-type_N.
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; 2.
Pfam; PF02214; BTB_2; 1.
Pfam; PF11879; DUF3399; 1.
Pfam; PF00520; Ion_trans; 1.
Pfam; PF11601; Shal-type; 1.
PRINTS; PR00169; KCHANNEL.
PRINTS; PR01517; KV42CHANNEL.
PRINTS; PR01491; KVCHANNEL.
PRINTS; PR01497; SHALCHANNEL.
SMART; SM00225; BTB; 1.
SUPFAM; SSF54695; SSF54695; 1.
1: Evidence at protein level;
Autism; Autism spectrum disorder; Cell junction; Cell membrane;
Cell projection; Complete proteome; Disease mutation; Epilepsy;
Ion channel; Ion transport; Membrane; Metal-binding; Phosphoprotein;
Postsynaptic cell membrane; Potassium; Potassium channel;
Potassium transport; Reference proteome; Synapse; Transmembrane;
Transmembrane helix; Transport; Voltage-gated channel; Zinc.
CHAIN 1 630 Potassium voltage-gated channel subfamily
D member 2.
/FTId=PRO_0000054064.
TOPO_DOM 1 182 Cytoplasmic.
{ECO:0000250|UniProtKB:P63142}.
TRANSMEM 183 204 Helical; Name=Segment S1.
{ECO:0000250|UniProtKB:P63142}.
TOPO_DOM 205 228 Extracellular.
{ECO:0000250|UniProtKB:P63142}.
TRANSMEM 229 250 Helical; Name=Segment S2.
{ECO:0000250|UniProtKB:P63142}.
TOPO_DOM 251 261 Cytoplasmic.
{ECO:0000250|UniProtKB:P63142}.
TRANSMEM 262 279 Helical; Name=Segment S3.
{ECO:0000250|UniProtKB:P63142}.
TOPO_DOM 280 286 Extracellular.
{ECO:0000250|UniProtKB:P63142}.
TRANSMEM 287 306 Helical; Voltage-sensor; Name=Segment S4.
{ECO:0000250|UniProtKB:P63142}.
TOPO_DOM 307 321 Cytoplasmic.
{ECO:0000250|UniProtKB:P63142}.
TRANSMEM 322 343 Helical; Name=Segment S5.
{ECO:0000250|UniProtKB:P63142}.
TOPO_DOM 344 357 Extracellular.
{ECO:0000250|UniProtKB:P63142}.
INTRAMEM 358 369 Helical; Name=Pore helix.
{ECO:0000250|UniProtKB:P63142}.
INTRAMEM 370 377 {ECO:0000250|UniProtKB:P63142}.
TOPO_DOM 378 384 Extracellular.
{ECO:0000250|UniProtKB:P63142}.
TRANSMEM 385 413 Helical; Name=Segment S6.
{ECO:0000250|UniProtKB:P63142}.
TOPO_DOM 414 630 Cytoplasmic.
{ECO:0000250|UniProtKB:P63142}.
REGION 2 20 Interaction with KCNIP1, KCNIP2, and
other family members.
{ECO:0000250|UniProtKB:Q63881}.
REGION 71 90 Interaction with KCNIP1.
{ECO:0000250|UniProtKB:Q63881}.
REGION 308 321 S4-S5 linker.
{ECO:0000250|UniProtKB:P63142}.
REGION 474 630 Important for normal channel activation
and inactivation, for interaction with
KCNIP2, and probably other family members
as well. {ECO:0000250|UniProtKB:Q63881,
ECO:0000305|PubMed:16934482}.
REGION 474 489 Required for dendritic targeting.
{ECO:0000250|UniProtKB:Q63881}.
MOTIF 370 375 Selectivity filter.
{ECO:0000250|UniProtKB:P63142}.
MOTIF 627 630 PDZ-binding.
{ECO:0000250|UniProtKB:Q63881}.
METAL 105 105 Zinc; via pros nitrogen.
{ECO:0000250|UniProtKB:Q63881}.
METAL 132 132 Zinc. {ECO:0000250|UniProtKB:Q63881}.
METAL 133 133 Zinc. {ECO:0000250|UniProtKB:Q63881}.
MOD_RES 38 38 Phosphothreonine.
{ECO:0000250|UniProtKB:Q63881}.
MOD_RES 438 438 Phosphoserine.
{ECO:0000250|UniProtKB:Q63881}.
MOD_RES 548 548 Phosphoserine.
{ECO:0000250|UniProtKB:Q63881}.
MOD_RES 552 552 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Z0V2}.
MOD_RES 572 572 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Z0V2}.
MOD_RES 575 575 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Z0V2}.
MOD_RES 602 602 Phosphothreonine.
{ECO:0000250|UniProtKB:Q63881}.
MOD_RES 607 607 Phosphothreonine.
{ECO:0000250|UniProtKB:Q63881}.
MOD_RES 616 616 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Z0V2}.
VARIANT 404 404 V -> M (probable disease-associated
mutation found in a family with atypical
autism and severe epilepsy; disrupts
potassium current inactivation;
dbSNP:rs587777631).
{ECO:0000269|PubMed:24501278}.
/FTId=VAR_072076.
MUTAGEN 309 309 G->A: Increases peak current amplitude
and causes a negative shift in the
voltage-dependence of activation.
{ECO:0000269|PubMed:19171772}.
MUTAGEN 311 311 R->A: No effect on peak current
amplitude, but causes a positive shift in
the voltage-dependence of activation. May
increase the affinity for the closed-
inactivated state of the channel.
{ECO:0000269|PubMed:19171772}.
MUTAGEN 312 312 I->A: Increases peak current amplitude
and causes a positive shift in the
voltage-dependence of activation.
{ECO:0000269|PubMed:19171772}.
MUTAGEN 313 313 L->A: Causes a positive shift in the
voltage-dependence of activation. May
decrease the affinity for the closed-
inactivated state of the channel.
{ECO:0000269|PubMed:19171772}.
MUTAGEN 314 314 G->A: Loss of channel activity.
{ECO:0000269|PubMed:19171772}.
MUTAGEN 315 315 Y->A: Increases peak current amplitude
but has a minor effect on the voltage-
dependence of activation.
{ECO:0000269|PubMed:19171772}.
MUTAGEN 316 316 T->A: Increases peak current amplitude
and causes a positive shift in the
voltage-dependence of activation.
{ECO:0000269|PubMed:19171772}.
MUTAGEN 317 317 L->A: Increases peak current amplitude
and causes a positive shift in the
voltage-dependence of activation.
{ECO:0000269|PubMed:19171772}.
MUTAGEN 318 318 K->A: Increases peak current amplitude
and causes a positive shift in the
voltage-dependence of activation.
{ECO:0000269|PubMed:19171772}.
MUTAGEN 319 319 S->A: May impair protein folding.
{ECO:0000269|PubMed:19171772}.
MUTAGEN 320 320 C->A: Increases peak current amplitude
and causes a positive shift in the
voltage-dependence of activation.
{ECO:0000269|PubMed:19171772}.
MUTAGEN 320 320 C->S: Increases peak current amplitude
and slows the onset of inactivation at
low voltage, but has no effect on the
voltage-dependence of activation.
{ECO:0000269|PubMed:19171772}.
MUTAGEN 322 322 S->A: Increases peak current amplitude
and causes a positive shift in the
voltage-dependence of activation. May
increase the affinity for the closed-
inactivated state of the channel.
{ECO:0000269|PubMed:19171772}.
MUTAGEN 323 323 E->A: Slightly increases peak current
amplitude and causes a negative shift in
the voltage-dependence of activation. May
decrease the affinity for the closed-
inactivated state of the channel.
{ECO:0000269|PubMed:19171772}.
MUTAGEN 324 324 L->A: May impair protein folding.
{ECO:0000269|PubMed:19171772}.
MUTAGEN 327 327 L->A: Loss of channel activity.
{ECO:0000269|PubMed:19171772}.
MUTAGEN 328 328 L->A: May impair protein folding.
{ECO:0000269|PubMed:19171772}.
MUTAGEN 329 329 F->A: Loss of channel activity.
{ECO:0000269|PubMed:19171772}.
MUTAGEN 397 397 V->A: May impair protein folding.
{ECO:0000269|PubMed:19171772}.
MUTAGEN 398 398 I->A: Loss of channel activity.
{ECO:0000269|PubMed:19171772}.
MUTAGEN 399 399 A->V: May impair protein folding.
{ECO:0000269|PubMed:19171772}.
MUTAGEN 401 401 P->A: May impair protein folding.
{ECO:0000269|PubMed:19171772}.
MUTAGEN 402 404 VPV->IPI: Increases pak current amplitude
and causes a positive shift in the
voltage-dependence of activation and
steady-state inactivation. May increase
the affinity for the closed-inactivated
state of the channel.
{ECO:0000269|PubMed:19171772}.
MUTAGEN 403 403 P->A: Loss of channel activity.
{ECO:0000269|PubMed:19171772}.
MUTAGEN 405 405 I->A: Loss of channel activity.
{ECO:0000269|PubMed:19171772}.
MUTAGEN 406 406 V->A: Loss of channel activity.
{ECO:0000269|PubMed:19171772}.
MUTAGEN 407 407 S->A: Increases peak current amplitude
but has no effect on the voltage-
dependence of activation. May increase
the affinity for the closed-inactivated
state of the channel.
{ECO:0000269|PubMed:19171772}.
MUTAGEN 408 408 N->A: Decreases peak current amplitude
and causes a positive shift in the
voltage-dependence of activation. May
increase the affinity for the closed-
inactivated state of the channel.
{ECO:0000269|PubMed:19171772}.
MUTAGEN 409 409 F->A: May impair protein folding.
{ECO:0000269|PubMed:19171772}.
MUTAGEN 601 604 PTPP->ATAA: Abolishes interaction with
FLNC. {ECO:0000269|PubMed:11102480}.
CONFLICT 450 450 N -> S (in Ref. 1; AAD22053).
{ECO:0000305}.
CONFLICT 464 464 Q -> P (in Ref. 1; AAD22053).
{ECO:0000305}.
CONFLICT 550 550 Q -> R (in Ref. 1; AAD22053).
{ECO:0000305}.
CONFLICT 553 553 I -> V (in Ref. 1; AAD22053).
{ECO:0000305}.
SEQUENCE 630 AA; 70537 MW; 0C11E62FFA220421 CRC64;
MAAGVAAWLP FARAAAIGWM PVASGPMPAP PRQERKRTQD ALIVLNVSGT RFQTWQDTLE
RYPDTLLGSS ERDFFYHPET QQYFFDRDPD IFRHILNFYR TGKLHYPRHE CISAYDEELA
FFGLIPEIIG DCCYEEYKDR RRENAERLQD DADTDTAGES ALPTMTARQR VWRAFENPHT
STMALVFYYV TGFFIAVSVI ANVVETVPCG SSPGHIKELP CGERYAVAFF CLDTACVMIF
TVEYLLRLAA APSRYRFVRS VMSIIDVVAI LPYYIGLVMT DNEDVSGAFV TLRVFRVFRI
FKFSRHSQGL RILGYTLKSC ASELGFLLFS LTMAIIIFAT VMFYAEKGSS ASKFTSIPAA
FWYTIVTMTT LGYGDMVPKT IAGKIFGSIC SLSGVLVIAL PVPVIVSNFS RIYHQNQRAD
KRRAQKKARL ARIRAAKSGS ANAYMQSKRN GLLSNQLQSS EDEQAFVSKS GSSFETQHHH
LLHCLEKTTN HEFVDEQVFE ESCMEVATVN RPSSHSPSLS SQQGVTSTCC SRRHKKTFRI
PNANVSGSHQ GSIQELSTIQ IRCVERTPLS NSRSSLNAKM EECVKLNCEQ PYVTTAIISI
PTPPVTTPEG DDRPESPEYS GGNIVRVSAL


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