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Protein

Potassium voltage-gated channel subfamily D member 2

Gene

Kcnd2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Voltage-gated potassium channel that mediates transmembrane potassium transport in excitable membranes, primarily in the brain, but also in rodent heart (PubMed:1840649, PubMed:1722463, PubMed:9093524, PubMed:9058605, PubMed:10676964, PubMed:12592409, PubMed:12754210, PubMed:16207878, PubMed:16123112, PubMed:19279261, PubMed:25352783, PubMed:14980206). Mediates the major part of the dendritic A-type current I(SA) in brain neurons (PubMed:16207878, PubMed:17026528). This current is activated at membrane potentials that are below the threshold for action potentials. It regulates neuronal excitability, prolongs the latency before the first spike in a series of action potentials, regulates the frequency of repetitive action potential firing, shortens the duration of action potentials and regulates the back-propagation of action potentials from the neuronal cell body to the dendrites. Contributes to the regulation of the circadian rhytm of action potential firing in suprachiasmatic nucleus neurons, which regulates the circadian rhythm of locomotor activity (By similarity). Functions downstream of the metabotropic glutamate receptor GRM5 and plays a role in neuronal excitability and in nociception mediated by activation of GRM5 (By similarity). Mediates the transient outward current I(to) in rodent heart left ventricle apex cells, but not in human heart, where this current is mediated by another family member (PubMed:9093524, PubMed:9058605). 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:1840649, PubMed:1722463, PubMed:9093524, PubMed:10676964, PubMed:12451113, PubMed:12592409, PubMed:12754210, PubMed:15452711, PubMed:16207878, PubMed:16820361, PubMed:25352783, PubMed:14980206). Can form functional homotetrameric channels and heterotetrameric channels that contain variable proportions of KCND2 and KCND3; channel properties depend on the type of pore-forming alpha subunits that are part of the channel (PubMed:25352783). In vivo, membranes probably contain a mixture of heteromeric potassium channel complexes (PubMed:12451113, PubMed:16123112). Interaction with specific isoforms of the regulatory subunits KCNIP1, KCNIP2, KCNIP3 or KCNIP4 strongly increases expression at the cell surface and thereby increases channel activity; it modulates the kinetics of channel activation and inactivation, shifts the threshold for channel activation to more negative voltage values, shifts the threshold for inactivation to less negative voltages and accelerates recovery after inactivation (PubMed:12451113, PubMed:15452711, PubMed:16123112, PubMed:16820361, PubMed:20045463, PubMed:14980206). Likewise, interaction with DPP6 or DPP10 promotes expression at the cell membrane and regulates both channel characteristics and activity (PubMed:15671030, PubMed:16123112, PubMed:19441798, PubMed:19901547, PubMed:19279261).By similarityCurated22 Publications

Enzyme regulationi

Inhibited by 5 mM 4-aminopyridine (4-AP) (PubMed:1840649, PubMed:1722463, PubMed:9093524). Not inhibited by dendrotoxins and by tetraethylammonium (TEA) (PubMed:1722463). Inhibited by 10 mM flecainide and 20 mM quinidine (PubMed:9093524). Inhibited by the heteropodatoxins HpTx1, HpTx2, and HpTx3 (PubMed:9058605).4 Publications

Kineticsi

Homotetrameric channels activate rapidly, i.e within a few msec (PubMed:1722463, PubMed:9093524). After that, they inactivate rapidly, i.e within about 50-100 msec (PubMed:1722463, PubMed:9093524). 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 (PubMed:19901547, PubMed:19279261). Homotetrameric channels have a unitary conductance of about 4 pS when expressed in a heterologous system (PubMed:19279261). For the activation of homotetrameric channels expressed in xenopus oocytes, the voltage at half-maximal amplitude is about -10 mV (PubMed:12451113). The time constant for inactivation is about 20 msec (PubMed:12451113). For inactivation, the voltage at half-maximal amplitude is -62 mV (PubMed:12451113). The time constant for recovery after inactivation is about 70 msec (PubMed:12451113).1 Publication

5 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi105 – 1051Zinc; via pros nitrogenCombined sources
    Metal bindingi132 – 1321ZincCombined sources
    Metal bindingi133 – 1331ZincCombined sources

    GO - Molecular functioni

    1. A-type (transient outward) potassium channel activity Source: UniProtKB
    2. ion channel activity Source: RGD
    3. metal ion binding Source: UniProtKB-KW
    4. potassium channel activity Source: RGD
    5. protein heterodimerization activity Source: RGD
    6. voltage-gated potassium channel activity Source: UniProtKB

    GO - Biological processi

    1. action potential Source: RGD
    2. cardiac muscle cell action potential Source: UniProtKB
    3. cellular response to drug Source: RGD
    4. cellular response to mechanical stimulus Source: RGD
    5. potassium ion transmembrane transport Source: UniProtKB
    6. potassium ion transport Source: RGD
    7. protein heterooligomerization Source: RGD
    8. protein homooligomerization Source: InterPro
    Complete GO annotation...

    Keywords - Molecular functioni

    Ion channel, Potassium channel, Voltage-gated channel

    Keywords - Biological processi

    Ion transport, Potassium transport, Transport

    Keywords - Ligandi

    Metal-binding, Potassium, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Potassium voltage-gated channel subfamily D member 2
    Alternative name(s):
    RK52 Publications
    Shal11 Publication
    Voltage-gated potassium channel subunit Kv4.21 Publication
    Gene namesi
    Name:Kcnd2
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi68393. Kcnd2.

    Subcellular locationi

    Cell membrane 27 Publications; Multi-pass membrane protein Curated. Cell projectiondendrite 12 Publications. Cell junctionsynapse 4 Publications. Perikaryon 6 Publications. Cell junctionsynapsepostsynaptic cell membrane 2 Publications. Cell projectiondendritic spine 5 Publications. Cell membranesarcolemma 1 Publication. Cell junction 1 Publication. Membranecaveola 1 Publication
    Note: In neurons, primarily detected on dendrites, dendritic spines and on the neuron cell body, but not on axons (PubMed:9070739, PubMed:17582333, PubMed:16207878, PubMed:22098631). Localized preferentially at the dendrites of pyramidal cells in the hippocampus CA1 layer (PubMed:22098631). Detected at GABAergic synapses (By similarity). Detected at cell junctions that are distinct from synaptic cell contacts (PubMed:18371079). Detected in lipid rafts (PubMed:14559911, PubMed:20224290, PubMed:24793047). Detected primarily at the endoplasmic reticulum or Golgi when expressed by itself (PubMed:12829703, PubMed:12754210, PubMed:16820361, PubMed:19441798, PubMed:14980206). Interaction with KCNIP1, KCNIP2, KCNIP3 or KCNIP4 promotes expression at the cell membrane (PubMed:12829703, PubMed:15485870, PubMed:20045463, PubMed:14980206). Interaction with DPP6 or DPP10 promotes expression at the cell membrane (PubMed:19441798). 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 (PubMed:17582333, PubMed:18650329). Redistributed from dendritic spines to the main dendritic shaft in response to activation of AMPA-selective glutamate receptors and activation of PKA (PubMed:17582333, PubMed:18650329).By similarityCurated14 Publications

    Topology

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 182182CytoplasmicBy similarityAdd
    BLAST
    Transmembranei183 – 20422Helical; Name=Segment S1By similarityAdd
    BLAST
    Topological domaini205 – 22824ExtracellularBy similarityAdd
    BLAST
    Transmembranei229 – 25022Helical; Name=Segment S2By similarityAdd
    BLAST
    Topological domaini251 – 26111CytoplasmicBy similarityAdd
    BLAST
    Transmembranei262 – 27918Helical; Name=Segment S3By similarityAdd
    BLAST
    Topological domaini280 – 2867ExtracellularBy similarity
    Transmembranei287 – 30620Helical; Voltage-sensor; Name=Segment S4By similarityAdd
    BLAST
    Topological domaini307 – 32115CytoplasmicBy similarityAdd
    BLAST
    Transmembranei322 – 34322Helical; Name=Segment S5By similarityAdd
    BLAST
    Topological domaini344 – 35714ExtracellularBy similarityAdd
    BLAST
    Intramembranei358 – 36912Helical; Name=Pore helixBy similarityAdd
    BLAST
    Intramembranei370 – 3778By similarity
    Topological domaini378 – 3847ExtracellularBy similarity
    Transmembranei385 – 41329Helical; Name=Segment S6By similarityAdd
    BLAST
    Topological domaini414 – 630217CytoplasmicBy similarityAdd
    BLAST

    GO - Cellular componenti

    1. dendrite Source: RGD
    2. dendritic spine Source: UniProtKB
    3. integral component of plasma membrane Source: UniProtKB
    4. neuronal cell body Source: RGD
    5. neuronal cell body membrane Source: UniProtKB
    6. neuron projection Source: RGD
    7. perinuclear endoplasmic reticulum Source: RGD
    8. plasma membrane Source: RGD
    9. plasma membrane raft Source: UniProtKB
    10. postsynaptic density Source: RGD
    11. postsynaptic membrane Source: UniProtKB
    12. potassium channel complex Source: RGD
    13. sarcolemma Source: UniProtKB
    14. T-tubule Source: UniProtKB
    15. voltage-gated potassium channel complex Source: RGD
    Complete GO annotation...

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Cell projection, Membrane, Postsynaptic cell membrane, Synapse

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi7 – 115Missing : Greatly reduces interaction with KCNIP1. 1 Publication
    Mutagenesisi8 – 81W → A: Abolishes interaction with KCNP1; when associated with A-11. 1 Publication
    Mutagenesisi11 – 111F → A: Abolishes interaction with KCNP1; when associated with A-8. 1 Publication
    Mutagenesisi66 – 661L → R: Abolishes expression. 1 Publication
    Mutagenesisi71 – 711E → K: Abolishes interaction with KCNIP1. 1 Publication
    Mutagenesisi73 – 731D → M: Abolishes interaction with KCNIP1. 1 Publication
    Mutagenesisi74 – 741F → R: Abolishes interaction with KCNIP1. 1 Publication
    Mutagenesisi79 – 791E → L or R: Abolishes interaction with KCNIP1. 1 Publication
    Mutagenesisi93 – 931R → A: Greatly reduces expression and changes multimerization. 1 Publication
    Mutagenesisi105 – 1051H → A: Abolishes tetramerization and assembly of a functional channel. 1 Publication
    Mutagenesisi111 – 1111C → A: Abolishes tetramerization and assembly of a functional channel; when associated with A-105; A-132 and A-133. 1 Publication
    Mutagenesisi132 – 1321C → A: Abolishes tetramerization and assembly of a functional channel; when associated with A-105; A-111 and A-133. 1 Publication
    Mutagenesisi133 – 1331C → A: Abolishes tetramerization and assembly of a functional channel; when associated with A-105; A-111 and A-132. 1 Publication
    Mutagenesisi481 – 4822Missing : Loss of dendritic targeted expression. 1 Publication
    Mutagenesisi552 – 5521S → A: Abolishes PKA-mediated modulation of cell surface expression and channel activity. 2 Publications
    Mutagenesisi627 – 6304Missing : Abolishes interaction with DLG4. 2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 630630Potassium voltage-gated channel subfamily D member 2PRO_0000054067Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei38 – 381Phosphothreonine1 Publication
    Modified residuei438 – 4381Phosphoserine1 Publication
    Modified residuei548 – 5481Phosphoserine1 Publication
    Modified residuei552 – 5521Phosphoserine5 Publications
    Modified residuei572 – 5721Phosphoserine1 Publication
    Modified residuei575 – 5751Phosphoserine1 Publication
    Modified residuei602 – 6021Phosphothreonine1 Publication
    Modified residuei607 – 6071Phosphothreonine1 Publication
    Modified residuei616 – 6161Phosphoserine1 Publication

    Post-translational modificationi

    Phosphorylation at Ser-438 in response to MAPK activation is increased in stimulated dendrites (PubMed:24404150). Interaction with KCNIP2 and DPP6 propomtes phosphorylation by PKA at Ser-552 (PubMed:19441798). Phosphorylation at Ser-552 has no effect on interaction with KCNIP3, but is required for the regulation of channel activity by KCNIP3 (PubMed:12451113). Phosphorylation at Ser-552 leads to KCND2 internalization (PubMed:17582333). 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).By similarity4 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiQ63881.
    PRIDEiQ63881.

    PTM databases

    PhosphoSiteiQ63881.

    Expressioni

    Tissue specificityi

    Detected in brain cortex, hippocampus, dentate gyrus, thalamus and cerebellum (PubMed:16123112). Detected in neurons from the primary visual cortex (PubMed:16207878). Detected in the supraoptic nucleus in hypothalamus, in hippocampus and the habenular nucleus of the thalamus (PubMed:9070739). Detected in the bed nucleus of the stria terminalis (PubMed:24037673). Detected in dendritic fields in the hippocampus CA1 layer, in stratum radiatum, stratum oriens, stratum lacunosum-moleculare and stratum pyramidale (PubMed:10676964, PubMed:22098631). Detected in dendritic fields in the hippocampus CA3 layer and in dentate gyrus (PubMed:10676964). Detected in the cerebellum granule cell layer, where it localizes at synapses (PubMed:11102480, PubMed:10676964, PubMed:15736227). Detected in the main olfactory bulb, especially in the granule cell layer and the external plexiform layer, but also the mitral layer (PubMed:18371079). Detected in heart atrium and ventricle (PubMed:10860776). Detected in heart left ventricle (at protein level) (PubMed:24793047). Highly expressed in heart and throughout the brain, with similar levels in cortex and hypothalamus, and much higher levels in hippocampus, dentate gyrus and the habenular nucleus of the thalamus. Detected in brain, and at lower levels in heart atrium and ventricle (PubMed:1705709). Detected in neurons from the bed nucleus of the stria terminalis (PubMed:24037673). Detected in aorta, cardiac and smooth muscle.11 Publications

    Inductioni

    Down-regulated in response to hypoxia lasting about 15 min, a treatment that leads to spontaneous convulsive seizures in these pups.1 Publication

    Gene expression databases

    GenevestigatoriQ63881.

    Interactioni

    Subunit structurei

    Homotetramer or heterotetramer with KCND1 or KCND3 (PubMed:12754210, PubMed:15485870, PubMed:20224290, PubMed:25352783). Associates with the regulatory subunits KCNIP1, KCNIP2, KCNIP3 and KCNIP4 (PubMed:10676964, PubMed:12451113, PubMed:11847232, PubMed:11805342, PubMed:15485870, PubMed:15356203, PubMed:15452711, PubMed:16820361, PubMed:20045463, PubMed:24811166, PubMed:14980206). Interacts with DPP6, DPP10, DLG4 and DLG1 (PubMed:11923279, PubMed:12575952, PubMed:14559911, PubMed:15671030, PubMed:19213956). In vivo, probably exists as heteromeric complex containing variable proportions of KCND1, KCND2, KCND3, KCNIP1, KCNIP2, KCNIP3, KCNIP4, DPP6 and DPP10 (PubMed:16123112, PubMed:19901547). The tetrameric channel can associate with up to four regulatory subunits, such as KCNIP2 or KCNIP4 (By similarity). Interaction with KCNIP3 promotes tetramerization and formation of a functional potassium channel (PubMed:15485870). Interaction with four KCNIP4 chains does not reduce interaction with DPP10 (By similarity). Probably part of a complex consisting of KCNIP1, KCNIP2 isoform 3 and KCND2 (By similarity). Interacts with FLNA and FLNC (PubMed:11102480). Interacts with NCS1/FREQ (By similarity). Identified in a complex with cAMP-dependent protein kinase (PKA), CAV3, AKAP6 and KCND3 in cardiac myocytes (PubMed:20224290).By similarity2 Publications22 Publications

    Protein-protein interaction databases

    BioGridi249292. 2 interactions.
    IntActiQ63881. 3 interactions.
    MINTiMINT-104113.
    STRINGi10116.ENSRNOP00000039227.

    Structurei

    Secondary structure

    630
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi1 – 66Combined sources
    Helixi9 – 179Combined sources
    Beta strandi43 – 475Combined sources
    Beta strandi50 – 545Combined sources
    Helixi56 – 605Combined sources
    Beta strandi64 – 663Combined sources
    Helixi70 – 756Combined sources
    Helixi78 – 803Combined sources
    Beta strandi81 – 855Combined sources
    Turni89 – 913Combined sources
    Helixi92 – 10110Combined sources
    Helixi112 – 12211Combined sources
    Helixi131 – 14515Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1NN7X-ray2.10A42-146[»]
    1S6CX-ray2.00B1-30[»]
    ProteinModelPortaliQ63881.
    SMRiQ63881. Positions 3-146.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ63881.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2 – 2019Interaction with KCNIP1, KCNIP2, and other family members2 PublicationsAdd
    BLAST
    Regioni71 – 9020Interaction with KCNIP11 PublicationAdd
    BLAST
    Regioni308 – 32114S4-S5 linkerBy similarityAdd
    BLAST
    Regioni474 – 630157Important for normal channel activation and inactivation, for interaction with KCNIP2, and probably other family members as well1 PublicationAdd
    BLAST
    Regioni474 – 48916Required for dendritic targeting1 PublicationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi370 – 3756Selectivity filterBy similarity
    Motifi627 – 6304PDZ-binding2 Publications

    Domaini

    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.By similarity
    The N-terminal cytoplasmic region can mediate N-type inactivation by physically blocking the channel (PubMed:15452711). This probably does not happen in vivo, where the N-terminal region mediates interaction with regulatory subunits, such as KCNIP1 and KCNIP2 (PubMed:16820361, PubMed:18357523, PubMed:14980206). The zinc binding sites in the N-terminal domain are important for tetramerization and assembly of a functional channel complex (PubMed:12754210). Most likely, the channel undergoes closed-state inactivation, where a subtle conformation change would render the protein less sensitive to activation.By similarity3 Publications2 Publications
    The C-terminal cytoplasmic region is important for normal expression at the cell membrane and modulates the voltage-dependence of channel activation and inactivation. It is required for interaction with KCNIP2, and probably other family members as well.1 Publication

    Sequence similaritiesi

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG1226.
    HOGENOMiHOG000231013.
    HOVERGENiHBG106687.
    InParanoidiQ63881.
    KOiK04892.
    PhylomeDBiQ63881.

    Family and domain databases

    Gene3Di1.20.120.350. 1 hit.
    InterProiIPR000210. BTB/POZ-like.
    IPR011333. BTB/POZ_fold.
    IPR027359. Channel_four-helix_dom.
    IPR005821. Ion_trans_dom.
    IPR003091. K_chnl.
    IPR003968. K_chnl_volt-dep_Kv.
    IPR003975. K_chnl_volt-dep_Kv4.
    IPR004055. K_chnl_volt-dep_Kv4.2.
    IPR024587. K_chnl_volt-dep_Kv4_C.
    IPR021645. Shal-type.
    IPR003131. T1-type_BTB.
    IPR028325. VG_K_chnl.
    [Graphical view]
    PANTHERiPTHR11537. PTHR11537. 1 hit.
    PfamiPF02214. BTB_2. 1 hit.
    PF11879. DUF3399. 1 hit.
    PF00520. Ion_trans. 1 hit.
    PF11601. Shal-type. 1 hit.
    [Graphical view]
    PRINTSiPR00169. KCHANNEL.
    PR01517. KV42CHANNEL.
    PR01491. KVCHANNEL.
    PR01497. SHALCHANNEL.
    SMARTiSM00225. BTB. 1 hit.
    [Graphical view]
    SUPFAMiSSF54695. SSF54695. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q63881-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MAAGVAAWLP FARAAAIGWM PVASGPMPAP PRQERKRTQD ALIVLNVSGT
    60 70 80 90 100
    RFQTWQDTLE RYPDTLLGSS ERDFFYHPET QQYFFDRDPD IFRHILNFYR
    110 120 130 140 150
    TGKLHYPRHE CISAYDEELA FFGLIPEIIG DCCYEEYKDR RRENAERLQD
    160 170 180 190 200
    DADTDNTGES ALPTMTARQR VWRAFENPHT STMALVFYYV TGFFIAVSVI
    210 220 230 240 250
    ANVVETVPCG SSPGHIKELP CGERYAVAFF CLDTACVMIF TVEYLLRLAA
    260 270 280 290 300
    APSRYRFVRS VMSIIDVVAI LPYYIGLVMT DNEDVSGAFV TLRVFRVFRI
    310 320 330 340 350
    FKFSRHSQGL RILGYTLKSC ASELGFLLFS LTMAIIIFAT VMFYAEKGSS
    360 370 380 390 400
    ASKFTSIPAA FWYTIVTMTT LGYGDMVPKT IAGKIFGSIC SLSGVLVIAL
    410 420 430 440 450
    PVPVIVSNFS RIYHQNQRAD KRRAQKKARL ARIRAAKSGS ANAYMQSKRN
    460 470 480 490 500
    GLLSNQLQSS EDEPAFVSKS GSSFETQHHH LLHCLEKTTN HEFVDEQVFE
    510 520 530 540 550
    ESCMEVATVN RPSSHSPSLS SQQGVTSTCC SRRHKKSFRI PNANVSGSHR
    560 570 580 590 600
    GSVQELSTIQ IRCVERTPLS NSRSSLNAKM EECVKLNCEQ PYVTTAIISI
    610 620 630
    PTPPVTTPEG DDRPESPEYS GGNIVRVSAL
    Length:630
    Mass (Da):70,549
    Last modified:November 1, 1996 - v1
    Checksum:iFDE57E8A5113BABF
    GO

    Sequence cautioni

    The sequence AAA40929.1 differs from that shown. Reason: Frameshift at position 477. Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    S64320 mRNA. Translation: AAB19939.1.
    M59980 mRNA. Translation: AAA40929.1. Frameshift.
    PIRiI57681.
    JU0271.
    RefSeqiNP_113918.2. NM_031730.2.
    UniGeneiRn.87841.

    Genome annotation databases

    GeneIDi65180.
    KEGGirno:65180.
    UCSCiRGD:68393. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    S64320 mRNA. Translation: AAB19939.1.
    M59980 mRNA. Translation: AAA40929.1. Frameshift.
    PIRiI57681.
    JU0271.
    RefSeqiNP_113918.2. NM_031730.2.
    UniGeneiRn.87841.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1NN7X-ray2.10A42-146[»]
    1S6CX-ray2.00B1-30[»]
    ProteinModelPortaliQ63881.
    SMRiQ63881. Positions 3-146.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi249292. 2 interactions.
    IntActiQ63881. 3 interactions.
    MINTiMINT-104113.
    STRINGi10116.ENSRNOP00000039227.

    Chemistry

    BindingDBiQ63881.
    ChEMBLiCHEMBL1075227.
    GuidetoPHARMACOLOGYi553.

    PTM databases

    PhosphoSiteiQ63881.

    Proteomic databases

    PaxDbiQ63881.
    PRIDEiQ63881.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    GeneIDi65180.
    KEGGirno:65180.
    UCSCiRGD:68393. rat.

    Organism-specific databases

    CTDi3751.
    RGDi68393. Kcnd2.

    Phylogenomic databases

    eggNOGiCOG1226.
    HOGENOMiHOG000231013.
    HOVERGENiHBG106687.
    InParanoidiQ63881.
    KOiK04892.
    PhylomeDBiQ63881.

    Miscellaneous databases

    EvolutionaryTraceiQ63881.
    NextBioi614080.
    PROiQ63881.

    Gene expression databases

    GenevestigatoriQ63881.

    Family and domain databases

    Gene3Di1.20.120.350. 1 hit.
    InterProiIPR000210. BTB/POZ-like.
    IPR011333. BTB/POZ_fold.
    IPR027359. Channel_four-helix_dom.
    IPR005821. Ion_trans_dom.
    IPR003091. K_chnl.
    IPR003968. K_chnl_volt-dep_Kv.
    IPR003975. K_chnl_volt-dep_Kv4.
    IPR004055. K_chnl_volt-dep_Kv4.2.
    IPR024587. K_chnl_volt-dep_Kv4_C.
    IPR021645. Shal-type.
    IPR003131. T1-type_BTB.
    IPR028325. VG_K_chnl.
    [Graphical view]
    PANTHERiPTHR11537. PTHR11537. 1 hit.
    PfamiPF02214. BTB_2. 1 hit.
    PF11879. DUF3399. 1 hit.
    PF00520. Ion_trans. 1 hit.
    PF11601. Shal-type. 1 hit.
    [Graphical view]
    PRINTSiPR00169. KCHANNEL.
    PR01517. KV42CHANNEL.
    PR01491. KVCHANNEL.
    PR01497. SHALCHANNEL.
    SMARTiSM00225. BTB. 1 hit.
    [Graphical view]
    SUPFAMiSSF54695. SSF54695. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    1. "Characterization of a mammalian cDNA for an inactivating voltage-sensitive K+ channel."
      Baldwin T.J., Tsaur M.-L., Lopez G.A., Jan Y.N., Jan L.Y.
      Neuron 7:471-483(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ENZYME REGULATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      Tissue: Hippocampus.
    2. "Cloning and tissue-specific expression of five voltage-gated potassium channel cDNAs expressed in rat heart."
      Roberds S.L., Tamkun M.M.
      Proc. Natl. Acad. Sci. U.S.A. 88:1798-1802(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
      Strain: Sprague-Dawley.
      Tissue: Heart.
    3. "Functional characterization of RK5, a voltage-gated K+ channel cloned from the rat cardiovascular system."
      Blair T.A., Roberds S.L., Tamkun M.M., Hartshorne R.P.
      FEBS Lett. 295:211-213(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ENZYME REGULATION, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES.
    4. "Electrophysiological and pharmacological correspondence between Kv4.2 current and rat cardiac transient outward current."
      Yeola S.W., Snyders D.J.
      Cardiovasc. Res. 33:540-547(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ENZYME REGULATION, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES.
    5. "Heteropodatoxins: peptides isolated from spider venom that block Kv4.2 potassium channels."
      Sanguinetti M.C., Johnson J.H., Hammerland L.G., Kelbaugh P.R., Volkmann R.A., Saccomano N.A., Mueller A.L.
      Mol. Pharmacol. 51:491-498(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ENZYME REGULATION, SUBCELLULAR LOCATION.
    6. "Clustering of KV4.2 potassium channels in postsynaptic membrane of rat supraoptic neurons: an ultrastructural study."
      Alonso G., Widmer H.
      Neuroscience 77:617-621(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    7. "Kv4.2 phosphorylation by cyclic AMP-dependent protein kinase."
      Anderson A.E., Adams J.P., Qian Y., Cook R.G., Pfaffinger P.J., Sweatt J.D.
      J. Biol. Chem. 275:5337-5346(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-38 AND SER-552 BY PKACA.
    8. "Voltage-gated K(+)Channel, Kv4.2, localizes predominantly to the transverse-axial tubular system of the rat myocyte."
      Takeuchi S., Takagishi Y., Yasui K., Murata Y., Toyama J., Kodama I.
      J. Mol. Cell. Cardiol. 32:1361-1369(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    9. "The A-type potassium channel Kv4.2 is a substrate for the mitogen-activated protein kinase ERK."
      Adams J.P., Anderson A.E., Varga A.W., Dineley K.T., Cook R.G., Pfaffinger P.J., Sweatt J.D.
      J. Neurochem. 75:2277-2287(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-602; THR-607 AND SER-616.
    10. "Localization and enhanced current density of the Kv4.2 potassium channel by interaction with the actin-binding protein filamin."
      Petrecca K., Miller D.M., Shrier A.
      J. Neurosci. 20:8736-8744(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH FILAMIN.
    11. Cited for: INTERACTION WITH KCNIP1; KCNIP2 AND KCNIP3, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    12. "PKA modulation of Kv4.2-encoded A-type potassium channels requires formation of a supramolecular complex."
      Schrader L.A., Anderson A.E., Mayne A., Pfaffinger P.J., Sweatt J.D.
      J. Neurosci. 22:10123-10133(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH KCNIP3, FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-552, PHOSPHORYLATION AT SER-552, BIOPHYSICOCHEMICAL PROPERTIES.
    13. "Molecular cloning and characterization of CALP/KChIP4, a novel EF-hand protein interacting with presenilin 2 and voltage-gated potassium channel subunit Kv4."
      Morohashi Y., Hatano N., Ohya S., Takikawa R., Watabiki T., Takasugi N., Imaizumi Y., Tomita T., Iwatsubo T.
      J. Biol. Chem. 277:14965-14975(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH KCNIP4, FUNCTION, SUBCELLULAR LOCATION.
    14. "Cell surface targeting and clustering interactions between heterologously expressed PSD-95 and the Shal voltage-gated potassium channel, Kv4.2."
      Wong W., Newell E.W., Jugloff D.G.M., Jones O.T., Schlichter L.C.
      J. Biol. Chem. 277:20423-20430(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF 627-VAL--LEU-630, INTERACTION WITH DLG4, SUBCELLULAR LOCATION.
    15. Cited for: INTERACTION WITH KCNIP4.
    16. "A fundamental role for KChIPs in determining the molecular properties and trafficking of Kv4.2 potassium channels."
      Shibata R., Misonou H., Campomanes C.R., Anderson A.E., Schrader L.A., Doliveira L.C., Carroll K.I., Sweatt J.D., Rhodes K.J., Trimmer J.S.
      J. Biol. Chem. 278:36445-36454(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-552, SUBCELLULAR LOCATION.
    17. "An evolutionarily conserved dileucine motif in Shal K+ channels mediates dendritic targeting."
      Rivera J.F., Ahmad S., Quick M.W., Liman E.R., Arnold D.B.
      Nat. Neurosci. 6:243-250(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, DENDRITIC TARGETING REGION, MUTAGENESIS OF 481-LEU--LEU-482, FUNCTION.
    18. "The CD26-related dipeptidyl aminopeptidase-like protein DPPX is a critical component of neuronal A-type K+ channels."
      Nadal M.S., Ozaita A., Amarillo Y., Vega-Saenz de Miera E., Ma Y., Mo W., Goldberg E.M., Misumi Y., Ikehara Y., Neubert T.A., Rudy B.
      Neuron 37:449-461(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DPP6.
    19. "The role of Zn2+ in Shal voltage-gated potassium channel formation."
      Strang C., Kunjilwar K., DeRubeis D., Peterson D., Pfaffinger P.J.
      J. Biol. Chem. 278:31361-31371(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT, ZINC-BINDING, SUBCELLULAR LOCATION, FUNCTION, MUTAGENESIS OF HIS-105; CYS-111; CYS-132 AND CYS-133.
    20. "Differential recruitment of Kv1.4 and Kv4.2 to lipid rafts by PSD-95."
      Wong W., Schlichter L.C.
      J. Biol. Chem. 279:444-452(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF 627-VAL--LEU-630, INTERACTION WITH DLG4, SUBCELLULAR LOCATION.
    21. "KChIP3 rescues the functional expression of Shal channel tetramerization mutants."
      Kunjilwar K., Strang C., DeRubeis D., Pfaffinger P.J.
      J. Biol. Chem. 279:54542-54551(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH KCNIP3, SUBCELLULAR LOCATION.
    22. "KChIPs and Kv4 alpha subunits as integral components of A-type potassium channels in mammalian brain."
      Rhodes K.J., Carroll K.I., Sung M.A., Doliveira L.C., Monaghan M.M., Burke S.L., Strassle B.W., Buchwalder L., Menegola M., Cao J., An W.F., Trimmer J.S.
      J. Neurosci. 24:7903-7915(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH KCNIP1 AND KCNIP3.
    23. Cited for: INTERACTION WITH KCNIP1, MUTAGENESIS OF 7-ALA--PHE-11; GLU-71; ASP-73; PHE-74 AND GLU-79.
    24. "The Kv4.2 N-terminal restores fast inactivation and confers KChlP2 modulatory effects on N-terminal-deleted Kv1.4 channels."
      Pourrier M., Herrera D., Caballero R., Schram G., Wang Z., Nattel S.
      Pflugers Arch. 449:235-247(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: DOMAIN, FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH KCNIP2.
    25. "Molecular determinants of voltage-gated potassium currents in vascular smooth muscle."
      Cox R.H.
      Cell Biochem. Biophys. 42:167-195(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    26. Cited for: INTERACTION WITH DPP6 AND DPP10, FUNCTION, SUBCELLULAR LOCATION.
    27. "Light and electron microscopic analysis of KChIP and Kv4 localization in rat cerebellar granule cells."
      Strassle B.W., Menegola M., Rhodes K.J., Trimmer J.S.
      J. Comp. Neurol. 484:144-155(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    28. "Functional role of the fast transient outward K+ current IA in pyramidal neurons in (rat) primary visual cortex."
      Yuan W., Burkhalter A., Nerbonne J.M.
      J. Neurosci. 25:9185-9194(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    29. "Multiprotein assembly of Kv4.2, KChIP3 and DPP10 produces ternary channel complexes with ISA-like properties."
      Jerng H.H., Kunjilwar K., Pfaffinger P.J.
      J. Physiol. (Lond.) 568:767-788(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, TISSUE SPECIFICITY.
    30. "C-terminal domain of Kv4.2 and associated KChIP2 interactions regulate functional expression and gating of Kv4.2."
      Han W., Nattel S., Noguchi T., Shrier A.
      J. Biol. Chem. 281:27134-27144(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH KCNIP2, DOMAIN.
    31. "Manipulating Kv4.2 identifies a specific component of hippocampal pyramidal neuron A-current that depends upon Kv4.2 expression."
      Lauver A., Yuan L.L., Jeromin A., Nadin B.M., Rodriguez J.J., Davies H.A., Stewart M.G., Wu G.Y., Pfaffinger P.J.
      J. Neurochem. 99:1207-1223(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    32. "Ionic channel function in action potential generation: current perspective."
      Baranauskas G.
      Mol. Neurobiol. 35:129-150(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    33. "Regulation of dendritic excitability by activity-dependent trafficking of the A-type K+ channel subunit Kv4.2 in hippocampal neurons."
      Kim J., Jung S.C., Clemens A.M., Petralia R.S., Hoffman D.A.
      Neuron 54:933-947(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    34. "Unique clustering of A-type potassium channels on different cell types of the main olfactory bulb."
      Kollo M., Holderith N., Antal M., Nusser Z.
      Eur. J. Neurosci. 27:1686-1699(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    35. "Protein kinase A mediates activity-dependent Kv4.2 channel trafficking."
      Hammond R.S., Lin L., Sidorov M.S., Wikenheiser A.M., Hoffman D.A.
      J. Neurosci. 28:7513-7519(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-552, MUTAGENESIS OF SER-552.
    36. "Ternary Kv4.2 channels recapitulate voltage-dependent inactivation kinetics of A-type K+ channels in cerebellar granule neurons."
      Amarillo Y., De Santiago-Castillo J.A., Dougherty K., Maffie J., Kwon E., Covarrubias M., Rudy B.
      J. Physiol. (Lond.) 586:2093-2106(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, MISCELLANEOUS.
    37. Cited for: REVIEW.
    38. "Convergent modulation of Kv4.2 channel alpha subunits by structurally distinct DPPX and KChIP auxiliary subunits."
      Seikel E., Trimmer J.S.
      Biochemistry 48:5721-5730(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH DPP6 AND KCNIP2, PHOSPHORYLATION AT SER-548; SER-552; SER-572 AND SER-575, IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF SER-552.
    39. "A novel N-terminal motif of dipeptidyl peptidase-like proteins produces rapid inactivation of KV4.2 channels by a pore-blocking mechanism."
      Jerng H.H., Dougherty K., Covarrubias M., Pfaffinger P.J.
      Channels 3:448-461(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES.
    40. "Kv4 potassium channels form a tripartite complex with the anchoring protein SAP97 and CaMKII in cardiac myocytes."
      El-Haou S., Balse E., Neyroud N., Dilanian G., Gavillet B., Abriel H., Coulombe A., Jeromin A., Hatem S.N.
      Circ. Res. 104:758-769(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DLG1.
    41. "The dipeptidyl-peptidase-like protein DPP6 determines the unitary conductance of neuronal Kv4.2 channels."
      Kaulin Y.A., De Santiago-Castillo J.A., Rocha C.A., Nadal M.S., Rudy B., Covarrubias M.
      J. Neurosci. 29:3242-3251(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
    42. "Alpha1-adrenoceptors regulate only the caveolae-located subpopulation of cardiac K(V)4 channels."
      Alday A., Urrutia J., Gallego M., Casis O.
      Channels 4:168-178(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, SUBUNIT, INTERACTION WITH PKA; CAV3; AKAP6 AND KCND3, TISSUE SPECIFICITY.
    43. "KChIP4a regulates Kv4.2 channel trafficking through PKA phosphorylation."
      Lin L., Sun W., Wikenheiser A.M., Kung F., Hoffman D.A.
      Mol. Cell. Neurosci. 43:315-325(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, SUBUNIT.
    44. "Unique somato-dendritic distribution pattern of Kv4.2 channels on hippocampal CA1 pyramidal cells."
      Kerti K., Lorincz A., Nusser Z.
      Eur. J. Neurosci. 35:66-75(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    45. "Regulation of Kv4.2 A-type potassium channels in HEK-293 cells by hypoxia."
      Liu Y.Q., Huang W.X., Sanchez R.M., Min J.W., Hu J.J., He X.H., Peng B.W.
      Front. Cell. Neurosci. 8:329-329(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION BY HYPOXIA, FUNCTION, SUBCELLULAR LOCATION, SUBUNIT.
    46. "Distribution and functional expression of Kv4 family alpha subunits and associated KChIP beta subunits in the bed nucleus of the stria terminalis."
      Rainnie D.G., Hazra R., Dabrowska J., Guo J.D., Li C.C., Dewitt S., Muly E.C.
      J. Comp. Neurol. 522:609-625(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    47. "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."
      Kitazawa M., Kubo Y., Nakajo K.
      J. Biol. Chem. 289:17597-17609(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH KCNIP4.
    48. "Localization of Kv4.2 and KChIP2 in lipid rafts and modulation of outward K(+) currents by membrane cholesterol content in rat left ventricular myocytes."
      Rudakova E., Wagner M., Frank M., Volk T.
      Pflugers Arch. 0:0-0(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    49. "Local plasticity of dendritic excitability can be autonomous of synaptic plasticity and regulated by activity-based phosphorylation of Kv4.2."
      Labno A., Warrier A., Wang S., Zhang X.
      PLoS ONE 9:E84086-E84086(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PHOSPHORYLATION AT SER-438, SUBCELLULAR LOCATION.
    50. "Determining the basis of channel-tetramerization specificity by X-ray crystallography and a sequence-comparison algorithm: family values (FamVal)."
      Nanao M.H., Zhou W., Pfaffinger P.J., Choe S.
      Proc. Natl. Acad. Sci. U.S.A. 100:8670-8675(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 42-146 IN COMPLEX WITH ZINC IONS, MUTAGENESIS OF LEU-66 AND ARG-93.
    51. "Structural insights into the functional interaction of KChIP1 with Shal-type K(+) channels."
      Zhou W., Qian Y., Kunjilwar K., Pfaffinger P.J., Choe S.
      Neuron 41:573-586(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-30, FUNCTION, INTERACTION WITH KCNIP1; KCNIP2 AND KCNIP3, SUBUNIT, SUBCELLULAR LOCATION, MUTAGENESIS OF TRP-8 AND PHE-11, DOMAIN.

    Entry informationi

    Entry nameiKCND2_RAT
    AccessioniPrimary (citable) accession number: Q63881
    Secondary accession number(s): Q00090, Q99249
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 7, 2003
    Last sequence update: November 1, 1996
    Last modified: March 4, 2015
    This is version 134 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    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.2 Publications1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.