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Protein

Potassium voltage-gated channel subfamily A member 2

Gene

Kcna2

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 and the central nervous system, but also in the cardiovascular system. Prevents aberrant action potential firing and regulates neuronal output. Forms tetrameric potassium-selective channels through which potassium ions pass in accordance with their electrochemical gradient. The channel alternates between opened and closed conformations in response to the voltage difference across the membrane (PubMed:12151401, PubMed:21602278, PubMed:24472174). Can form functional homotetrameric channels and heterotetrameric channels that contain variable proportions of KCNA1, KCNA2, KCNA4, KCNA5, KCNA6, KCNA7, and possibly other family members as well; channel properties depend on the type of alpha subunits that are part of the channel (PubMed:8495559, PubMed:15618540, PubMed:20805574, PubMed:23725331). Channel properties are modulated by cytoplasmic beta subunits that regulate the subcellular location of the alpha subunits and promote rapid inactivation of delayed rectifier potassium channels (PubMed:18003609, PubMed:19713757). In vivo, membranes probably contain a mixture of heteromeric potassium channel complexes, making it difficult to assign currents observed in intact tissues to a particular potassium channel family member. Homotetrameric KCNA2 forms a delayed-rectifier potassium channel that opens in response to membrane depolarization, followed by slow spontaneous channel closure (PubMed:1715584, PubMed:16770729, PubMed:17766348, PubMed:18003609, PubMed:18638484, PubMed:19713757, PubMed:20089912). In contrast, a heteromultimer formed by KCNA2 and KCNA4 shows rapid inactivation (PubMed:8495559). Response to toxins that are selective for KCNA1, respectively for KCNA2, suggests that heteromeric potassium channels composed of both KCNA1 and KCNA2 play a role in pacemaking and regulate the output of deep cerebellar nuclear neurons (PubMed:23318870). KCNA2-containing channels play a presynaptic role and prevent hyperexcitability and aberrant action potential firing (PubMed:12777451). Response to toxins that are selective for KCNA2-containing potassium channels suggests that in Purkinje cells, dendritic subthreshold KCNA2-containing potassium channels prevent random spontaneous calcium spikes, suppressing dendritic hyperexcitability without hindering the generation of somatic action potentials, and thereby play an important role in motor coordination (PubMed:16210348). Plays a role in the induction of long-term potentiation of neuron excitability in the CA3 layer of the hippocampus (By similarity). May function as down-stream effector for G protein-coupled receptors and inhibit GABAergic inputs to basolateral amygdala neurons (PubMed:16306173). May contribute to the regulation of neurotransmitter release, such as gamma-aminobutyric acid (GABA) (PubMed:17869444). Contributes to the regulation of the axonal release of the neurotransmitter dopamine (PubMed:21647367). Reduced KCNA2 expression plays a role in the perception of neuropathic pain after peripheral nerve injury, but not acute pain (PubMed:24472174). Plays a role in the regulation of the time spent in non-rapid eye movement (NREM) sleep (By similarity).By similarityCurated20 Publications

Enzyme regulationi

Inhibited by 4-aminopyridine (4-AP), dendrotoxin (DTX) and charybdotoxin (CTX), but not by tetraethylammonium (TEA) (PubMed:2555158, PubMed:8495559, PubMed:18638484). Inhibited by tityustoxin-K alpha (TsTX-Kalpha), a toxin that is highly specific for KCNA2 (PubMed:8355670). Inhibited by maurotoxin (PubMed:24472174). Inhibited by kappaM conotoxins kappaM-RIIIJ and kappaM-RIIIK (By similarity).By similarity6 Publications

Kineticsi

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 xenopus oocytes, the voltage at half-maximal amplitude is about -34 mV (PubMed:2555158). Unit channel conductance is about 10 pS (PubMed:2555158). For the activation of homotetrameric channels expressed in Chinese hamster ovary (CHO) cells, the voltage at half-maximal amplitude is about -10 mV (PubMed:17324383).2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei252 – 2521Important for normal, slow channel gating1 Publication

    GO - Molecular functioni

    1. delayed rectifier potassium channel activity Source: UniProtKB
    2. outward rectifier potassium channel activity Source: RGD
    3. voltage-gated potassium channel activity Source: UniProtKB

    GO - Biological processi

    1. neuronal action potential Source: UniProtKB
    2. optic nerve structural organization Source: Ensembl
    3. potassium ion transmembrane transport Source: UniProtKB
    4. protein homooligomerization Source: InterPro
    5. protein oligomerization Source: RGD
    6. regulation of dopamine secretion Source: UniProtKB
    7. sensory perception of pain Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Ion channel, Potassium channel, Voltage-gated channel

    Keywords - Biological processi

    Ion transport, Potassium transport, Transport

    Keywords - Ligandi

    Potassium

    Enzyme and pathway databases

    ReactomeiREACT_352543. Voltage gated Potassium channels.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Potassium voltage-gated channel subfamily A member 2
    Alternative name(s):
    RAK
    RBK21 Publication
    RCK51 Publication
    Voltage-gated potassium channel subunit Kv1.2
    Gene namesi
    Name:Kcna2
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494 Componenti: Chromosome 2

    Organism-specific databases

    RGDi2950. Kcna2.

    Subcellular locationi

    Cell membrane 1 Publication17 Publications; Multi-pass membrane protein Curated6 Publications. Membrane 9 Publications. Cell projectionaxon 6 Publications. Cell junctionsynapse 1 Publication. Cell junctionsynapsesynaptosome By similarity. Cell junctionsynapsepresynaptic cell membrane By similarity. Cell projectiondendrite By similarity. Endoplasmic reticulum membrane 1 Publication. Cell projectionlamellipodium membrane 1 Publication. Endosome 1 Publication. Perikaryon 1 Publication
    Note: KCNA2 by itself is detected both at the endoplasmic reticulum and at the cell membrane. Coexpression with KCNA4 or with beta subunits promotes expression at the cell membrane (PubMed:10896669, PubMed:16770729, PubMed:18003609). Coexpression with KCNA1 inhibits cell surface expression (PubMed:10896669). Surface levels are regulated both by steady-state and stimulus-induced clathrin-dependent endocytosis (PubMed:19403695). Expression at the cell surface is down-regulated in response to CHRM1 activation (PubMed:9635436). Expression at the cell surface is increased in response to the activation of beta-adrenergic receptors and increased cAMP levels (PubMed:18003609). Detected on presynaptic and postsynaptic axon segments (PubMed:12777451).6 Publications

    Topology

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 160160Cytoplasmic3 PublicationsAdd
    BLAST
    Transmembranei161 – 18222Helical; Name=Segment S13 PublicationsAdd
    BLAST
    Topological domaini183 – 22139Extracellular1 Publication3 PublicationsAdd
    BLAST
    Transmembranei222 – 24322Helical; Name=Segment S23 PublicationsAdd
    BLAST
    Topological domaini244 – 25411Cytoplasmic3 PublicationsAdd
    BLAST
    Transmembranei255 – 27521Helical; Name=Segment S32 PublicationsAdd
    BLAST
    Topological domaini276 – 28914Extracellular3 PublicationsAdd
    BLAST
    Transmembranei290 – 31021Helical; Voltage-sensor; Name=Segment S42 PublicationsAdd
    BLAST
    Topological domaini311 – 32515Cytoplasmic3 PublicationsAdd
    BLAST
    Transmembranei326 – 34722Helical; Name=Segment S53 PublicationsAdd
    BLAST
    Topological domaini348 – 36114Extracellular3 PublicationsAdd
    BLAST
    Intramembranei362 – 37312Helical; Name=Pore helix3 PublicationsAdd
    BLAST
    Intramembranei374 – 38183 Publications
    Topological domaini382 – 3887Extracellular3 Publications
    Transmembranei389 – 41729Helical; Name=Segment S63 PublicationsAdd
    BLAST
    Topological domaini418 – 49982CytoplasmicCurated1 PublicationAdd
    BLAST

    GO - Cellular componenti

    1. axon terminus Source: UniProtKB
    2. cell junction Source: UniProtKB-KW
    3. dendrite Source: UniProtKB
    4. endoplasmic reticulum membrane Source: UniProtKB-SubCell
    5. endosome Source: UniProtKB-SubCell
    6. integral component of membrane Source: GO_Central
    7. integral component of plasma membrane Source: UniProtKB
    8. juxtaparanode region of axon Source: UniProtKB
    9. lamellipodium Source: UniProtKB
    10. lamellipodium membrane Source: UniProtKB-SubCell
    11. neuronal cell body membrane Source: UniProtKB
    12. perikaryon Source: UniProtKB
    13. potassium channel complex Source: UniProtKB
    14. presynaptic membrane Source: UniProtKB-SubCell
    15. voltage-gated potassium channel complex Source: UniProtKB
    Complete GO annotation...

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Cell projection, Endoplasmic reticulum, Endosome, Membrane, Synapse, Synaptosome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi34 – 341R → L: No effect on channel opening. 1 Publication
    Mutagenesisi38 – 381N → A: Alters voltage-sensitive channel opening. 1 Publication
    Mutagenesisi40 – 401S → A: No effect on channel opening. 1 Publication
    Mutagenesisi41 – 411G → A: Loss of channel activity. 1 Publication
    Mutagenesisi42 – 421L → A: No effect on channel opening. 1 Publication
    Mutagenesisi43 – 431R → L: No effect on channel opening. 1 Publication
    Mutagenesisi44 – 441F → A: Alters voltage-sensitive channel opening. 1 Publication
    Mutagenesisi45 – 451E → A: Loss of channel activity. 1 Publication
    Mutagenesisi46 – 461T → D: Impairs protein folding. Loss of tetramerization. 1 Publication
    Mutagenesisi46 – 461T → V or A: No effect on tetramerization. Alters voltage-sensitive channel opening. 1 Publication
    Mutagenesisi46 – 461T → V: Abolishes interaction with KCNAB2 and strongly reduces cell surface expression. No effect phosphorylation in response to increased cAMP levels. 1 Publication
    Mutagenesisi47 – 471Q → A: No effect on channel opening. 1 Publication
    Mutagenesisi50 – 501T → A: Alters voltage-sensitive channel opening. 1 Publication
    Mutagenesisi70 – 701D → A: No effect on channel opening. 1 Publication
    Mutagenesisi73 – 731R → A: No effect on channel opening. 1 Publication
    Mutagenesisi75 – 751E → A: No effect on channel opening. 1 Publication
    Mutagenesisi77 – 771F → W: Alters voltage-sensitive channel opening. 1 Publication
    Mutagenesisi79 – 791D → N: Alters voltage-sensitive channel opening. 1 Publication
    Mutagenesisi81 – 811N → A: No effect on channel opening. 1 Publication
    Mutagenesisi82 – 821R → A: Loss of channel activity. 1 Publication
    Mutagenesisi86 – 861D → A: Alters voltage-sensitive channel opening. 1 Publication
    Mutagenesisi89 – 891L → A: No effect on channel opening. 1 Publication
    Mutagenesisi90 – 901Y → A: No effect on channel opening. 1 Publication
    Mutagenesisi93 – 931Q → A: Loss of channel activity. 1 Publication
    Mutagenesisi97 – 971R → A: No effect on channel opening. 1 Publication
    Mutagenesisi99 – 991R → A: No effect on channel opening. 1 Publication
    Mutagenesisi102 – 1021V → T: Alters voltage-sensitive channel opening. 1 Publication
    Mutagenesisi103 – 1031N → A: No effect on channel opening. 1 Publication
    Mutagenesisi105 – 1051P → A: No effect on channel opening. 1 Publication
    Mutagenesisi107 – 1071D → A: Alters voltage-sensitive channel opening. 1 Publication
    Mutagenesisi108 – 1081I → A: No effect on channel opening. 1 Publication
    Mutagenesisi111 – 1111E → A: Alters voltage-sensitive channel opening. 1 Publication
    Mutagenesisi207 – 2071N → Q: Loss of glycosylation site. 1 Publication
    Mutagenesisi252 – 2521T → R: Changes channel gating from a predominantly slow mode to a much more rapid mode. 1 Publication
    Mutagenesisi267 – 30236FITLG…LVRVF → YVTIFLTESNKSVLQFQNVR RVVQIFRIM in paddle chimera; changes channel activation to less negative voltage values and renders the channel susceptible to inhibition by the spider toxin VsTx1. 1 PublicationAdd
    BLAST
    Mutagenesisi356 – 3561S → A: Impairs N-glycosylation and abolishes expression at the cell surface. 1 Publication
    Mutagenesisi360 – 3601S → A: No effect on N-glycosylation. Abolishes channel activity of the homotetramer, but retains channel activity in the presence of a beta subunit. 1 Publication
    Mutagenesisi381 – 3811V → Y: Confers sensitivity to inhibition by tetraethylammonium (TEA). 1 Publication
    Mutagenesisi383 – 3831T → A: Impairs N-glycosylation and abolishes expression at the cell surface. 1 Publication
    Mutagenesisi415 – 4151Y → F: Nearly abolishes interaction with CTTN; when associated with F-417. 1 Publication
    Mutagenesisi417 – 4171Y → F: Nearly abolishes interaction with CTTN; when associated with F-415. Strongly reduces channel activity. 1 Publication
    Mutagenesisi440 – 4401S → A: Strongly reduces cell surface expression. Abolishes phosphorylation in response to increased cAMP levels. 1 Publication
    Mutagenesisi449 – 4491S → A: Strongly reduces cell surface expression. Abolishes phosphorylation in response to increased cAMP levels. 1 Publication
    Mutagenesisi458 – 4581Y → A: Impairs clustering on axon membranes. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 499499Potassium voltage-gated channel subfamily A member 2PRO_0000053975Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi207 – 2071N-linked (GlcNAc...)Sequence Analysis1 Publication
    Lipidationi244 – 2441S-palmitoyl cysteineSequence Analysis
    Modified residuei429 – 4291PhosphotyrosineBy similarity
    Modified residuei440 – 4401Phosphoserine1 Publication
    Modified residuei441 – 4411PhosphoserineBy similarity
    Modified residuei449 – 4491Phosphoserine2 Publications
    Modified residuei458 – 4581Phosphotyrosine1 Publication

    Post-translational modificationi

    Phosphorylated on tyrosine residues; phosphorylation increases in response to ischemia (PubMed:14713306). Phosphorylated on tyrosine residues by activated PTK2B/PYK2 (PubMed:7544443). Phosphorylation on tyrosine residues suppresses ion channel activity (PubMed:7544443). Phosphorylated on tyrosine residues in response to CHRM1 activation; this abolishes interaction with CTTN (PubMed:12151401). This is probably due to endocytosis of the phosphorylated channnel subunits. Phosphorylated on serine residues in response to increased cAMP levels; phosphorylation is apparently not catalyzed by PKA (PubMed:18003609).4 Publications
    N-glycosylated, with complex, sialylated N-glycans.2 Publications

    Keywords - PTMi

    Glycoprotein, Lipoprotein, Palmitate, Phosphoprotein

    Proteomic databases

    PaxDbiP63142.
    PRIDEiP63142.

    PTM databases

    PhosphoSiteiP63142.

    Expressioni

    Tissue specificityi

    Detected in neurons in dorsal root ganglion (PubMed:24472174). Detected in hippocampus neurons (PubMed:21602278). Detected on neurons of the anteroventral cochlear nucleus (PubMed:12777451). Detected in renal arteries (PubMed:12632190). Detected in neurons of the medial nucleus of the trapezoid body (PubMed:12177193). Detected in neurons in the brain cortex (PubMed:14713306). Detected in axon tracts of the corpus callosum, specific terminal fields of the brain cortex neuropil, neurons in the medial entorhinal cortex, and in puncta representing mossy fiber terminals in the hippocampus mossy fiber tract; these puncta correspond to synapses made by dentate granule cells (PubMed:8361540). Detected in paranodal and juxtanodal zones in the central nervous system, including myelinated spinal cord (PubMed:11086297, PubMed:20089912). Detected in the juxtaparanodal region in optic nerve (PubMed:10624965). Detected at nerve terminal plexuses of basket cells in the cerebellum (at protein level) (PubMed:7477295, PubMed:20089912). Detected in brain (PubMed:2722779). Detected in heart atrium and ventricle (PubMed:1715584). Detected in renal arteries (PubMed:12632190).12 Publications

    Inductioni

    Up-regulated in brain cortex in response to ischemia (at protein level) (PubMed:14713306). Down-regulated in dorsal root ganglion neurons after peripheral nerve injury (at protein level) (PubMed:24472174). Down-regulated in pulmonary artery myocytes in response to chronic moderate hypoxia.3 Publications

    Gene expression databases

    GenevestigatoriP63142.

    Interactioni

    Subunit structurei

    Homotetramer and heterotetramer with other channel-forming alpha subunits, such as KCNA1, KCNA4, KCNA5, KCNA6 and KCNA7 (PubMed:8495559, PubMed:8361540, PubMed:10896669, PubMed:12777451, PubMed:12632190, PubMed:15618540, PubMed:11007484, PubMed:16002581, PubMed:18004376, PubMed:20534430). Channel activity is regulated by interaction with beta subunits, including KCNAB1 and KCNAB2 (PubMed:18003609, PubMed:19713757, PubMed:16002581, PubMed:18004376, PubMed:20534430, PubMed:20360102, PubMed:23705070). Identified in a complex with KCNA1 and KCNAB2 (PubMed:11086297, PubMed:23318870). Identified in a complex with KCNA5 and KCNAB1 (By similarity). Identified in a complex with KCNA4 and FYN (By similarity). Interacts (via C-terminus) with the PDZ domains of DLG1 and DLG2 (PubMed:7477295). Interacts with DLG4 (via PDZ domain) (PubMed:7477295, PubMed:20089912). Interacts with PTK2B (PubMed:11739373). Interacts (via C-terminus) with CTTN (PubMed:12151401). 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 (By similarity). Interacts with SIGMAR1; cocaine consumption leads to increased interaction (By similarity). Interacts with CNTNAP2 (PubMed:10624965). Interacts with ADAM22 (PubMed:20089912).By similarityCurated20 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    DLG4P783522EBI-631446,EBI-80389From a different organism.

    Protein-protein interaction databases

    BioGridi247501. 5 interactions.
    IntActiP63142. 1 interaction.
    STRINGi10116.ENSRNOP00000042653.

    Structurei

    Secondary structure

    1
    499
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi34 – 396Combined sources
    Beta strandi42 – 476Combined sources
    Helixi48 – 525Combined sources
    Turni58 – 603Combined sources
    Helixi62 – 665Combined sources
    Turni71 – 744Combined sources
    Beta strandi75 – 784Combined sources
    Turni82 – 843Combined sources
    Helixi85 – 939Combined sources
    Helixi106 – 11611Combined sources
    Helixi120 – 13011Combined sources
    Turni143 – 1453Combined sources
    Helixi146 – 1494Combined sources
    Turni150 – 1545Combined sources
    Beta strandi156 – 1583Combined sources
    Helixi160 – 18223Combined sources
    Helixi186 – 1894Combined sources
    Beta strandi190 – 1923Combined sources
    Turni193 – 1964Combined sources
    Helixi202 – 2109Combined sources
    Helixi225 – 24218Combined sources
    Beta strandi243 – 2453Combined sources
    Turni249 – 2524Combined sources
    Helixi254 – 2607Combined sources
    Turni261 – 2633Combined sources
    Helixi279 – 2824Combined sources
    Helixi291 – 2999Combined sources
    Helixi301 – 3099Combined sources
    Helixi312 – 32312Combined sources
    Helixi325 – 35127Combined sources
    Helixi361 – 37212Combined sources
    Beta strandi378 – 3803Combined sources
    Helixi385 – 40319Combined sources
    Helixi406 – 41813Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1DSXX-ray1.60A/B/C/D/E/F/G/H33-119[»]
    1QDVX-ray1.60A/B/C/D33-131[»]
    1QDWX-ray2.10A/B/C/D/E/F/G/H33-119[»]
    2A79X-ray2.90B1-499[»]
    2R9RX-ray2.40B/H1-499[»]
    3LNMX-ray2.90B/D1-266[»]
    B/D303-499[»]
    3LUTX-ray2.90B1-499[»]
    4JTAX-ray2.50B/Q1-266[»]
    B/Q304-499[»]
    4JTCX-ray2.56B/H1-266[»]
    B/H304-499[»]
    4JTDX-ray2.54B/H1-266[»]
    B/H304-499[»]
    SMRiP63142. Positions 3-421.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP63142.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 125125Tetramerization domain1 PublicationAdd
    BLAST
    Regioni312 – 32514S4-S5 linker1 PublicationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi374 – 3796Selectivity filterCurated
    Motifi497 – 4993PDZ-binding1 Publication

    Domaini

    The cytoplasmic N-terminus is important for tetramerization. Interactions between the different subunits modulate the gating characteristics (PubMed:11007484). Besides, the cytoplasmic N-terminal domain mediates interaction with RHOA and thus is required for RHOA-mediated endocytosis (PubMed:9635436).3 Publications
    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.2 Publications

    Sequence similaritiesi

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG1226.
    GeneTreeiENSGT00760000118846.
    HOGENOMiHOG000231015.
    HOVERGENiHBG052230.
    InParanoidiP63142.
    KOiK04875.
    OMAiMTFHTYS.
    OrthoDBiEOG7M0NRD.
    PhylomeDBiP63142.
    TreeFamiTF313103.

    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.
    IPR003972. K_chnl_volt-dep_Kv1.
    IPR004049. K_chnl_volt-dep_Kv1.2.
    IPR003131. T1-type_BTB.
    IPR028325. VG_K_chnl.
    [Graphical view]
    PANTHERiPTHR11537. PTHR11537. 1 hit.
    PfamiPF02214. BTB_2. 1 hit.
    PF00520. Ion_trans. 1 hit.
    [Graphical view]
    PRINTSiPR00169. KCHANNEL.
    PR01509. KV12CHANNEL.
    PR01491. KVCHANNEL.
    PR01496. SHAKERCHANEL.
    SMARTiSM00225. BTB. 1 hit.
    [Graphical view]
    SUPFAMiSSF54695. SSF54695. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P63142-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MTVATGDPVD EAAALPGHPQ DTYDPEADHE CCERVVINIS GLRFETQLKT
    60 70 80 90 100
    LAQFPETLLG DPKKRMRYFD PLRNEYFFDR NRPSFDAILY YYQSGGRLRR
    110 120 130 140 150
    PVNVPLDIFS EEIRFYELGE EAMEMFREDE GYIKEEERPL PENEFQRQVW
    160 170 180 190 200
    LLFEYPESSG PARIIAIVSV MVILISIVSF CLETLPIFRD ENEDMHGGGV
    210 220 230 240 250
    TFHTYSNSTI GYQQSTSFTD PFFIVETLCI IWFSFEFLVR FFACPSKAGF
    260 270 280 290 300
    FTNIMNIIDI VAIIPYFITL GTELAEKPED AQQGQQAMSL AILRVIRLVR
    310 320 330 340 350
    VFRIFKLSRH SKGLQILGQT LKASMRELGL LIFFLFIGVI LFSSAVYFAE
    360 370 380 390 400
    ADERDSQFPS IPDAFWWAVV SMTTVGYGDM VPTTIGGKIV GSLCAIAGVL
    410 420 430 440 450
    TIALPVPVIV SNFNYFYHRE TEGEEQAQYL QVTSCPKIPS SPDLKKSRSA
    460 470 480 490
    STISKSDYME IQEGVNNSNE DFREENLKTA NCTLANTNYV NITKMLTDV
    Length:499
    Mass (Da):56,701
    Last modified:September 13, 2004 - v1
    Checksum:iA8FEA6F3F59AF42A
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti411 – 4111S → F in AAA19867 (PubMed:1715584).Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    J04731 mRNA. Translation: AAA40819.1.
    X16003 mRNA. Translation: CAA34134.1.
    M74449 mRNA. Translation: AAA19867.1.
    PIRiA33814.
    RefSeqiNP_037102.1. NM_012970.3.
    XP_006233194.1. XM_006233132.2.
    XP_006233195.1. XM_006233133.2.
    XP_006233196.1. XM_006233134.2.
    XP_006233197.1. XM_006233135.2.
    XP_008759593.1. XM_008761371.1.
    UniGeneiRn.10298.
    Rn.40779.

    Genome annotation databases

    EnsembliENSRNOT00000050149; ENSRNOP00000042653; ENSRNOG00000018285.
    GeneIDi25468.
    KEGGirno:25468.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    J04731 mRNA. Translation: AAA40819.1.
    X16003 mRNA. Translation: CAA34134.1.
    M74449 mRNA. Translation: AAA19867.1.
    PIRiA33814.
    RefSeqiNP_037102.1. NM_012970.3.
    XP_006233194.1. XM_006233132.2.
    XP_006233195.1. XM_006233133.2.
    XP_006233196.1. XM_006233134.2.
    XP_006233197.1. XM_006233135.2.
    XP_008759593.1. XM_008761371.1.
    UniGeneiRn.10298.
    Rn.40779.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1DSXX-ray1.60A/B/C/D/E/F/G/H33-119[»]
    1QDVX-ray1.60A/B/C/D33-131[»]
    1QDWX-ray2.10A/B/C/D/E/F/G/H33-119[»]
    2A79X-ray2.90B1-499[»]
    2R9RX-ray2.40B/H1-499[»]
    3LNMX-ray2.90B/D1-266[»]
    B/D303-499[»]
    3LUTX-ray2.90B1-499[»]
    4JTAX-ray2.50B/Q1-266[»]
    B/Q304-499[»]
    4JTCX-ray2.56B/H1-266[»]
    B/H304-499[»]
    4JTDX-ray2.54B/H1-266[»]
    B/H304-499[»]
    SMRiP63142. Positions 3-421.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi247501. 5 interactions.
    IntActiP63142. 1 interaction.
    STRINGi10116.ENSRNOP00000042653.

    Chemistry

    GuidetoPHARMACOLOGYi539.

    PTM databases

    PhosphoSiteiP63142.

    Proteomic databases

    PaxDbiP63142.
    PRIDEiP63142.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENSRNOT00000050149; ENSRNOP00000042653; ENSRNOG00000018285.
    GeneIDi25468.
    KEGGirno:25468.

    Organism-specific databases

    CTDi3737.
    RGDi2950. Kcna2.

    Phylogenomic databases

    eggNOGiCOG1226.
    GeneTreeiENSGT00760000118846.
    HOGENOMiHOG000231015.
    HOVERGENiHBG052230.
    InParanoidiP63142.
    KOiK04875.
    OMAiMTFHTYS.
    OrthoDBiEOG7M0NRD.
    PhylomeDBiP63142.
    TreeFamiTF313103.

    Enzyme and pathway databases

    ReactomeiREACT_352543. Voltage gated Potassium channels.

    Miscellaneous databases

    EvolutionaryTraceiP63142.
    NextBioi289787.
    PROiP63142.

    Gene expression databases

    GenevestigatoriP63142.

    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.
    IPR003972. K_chnl_volt-dep_Kv1.
    IPR004049. K_chnl_volt-dep_Kv1.2.
    IPR003131. T1-type_BTB.
    IPR028325. VG_K_chnl.
    [Graphical view]
    PANTHERiPTHR11537. PTHR11537. 1 hit.
    PfamiPF02214. BTB_2. 1 hit.
    PF00520. Ion_trans. 1 hit.
    [Graphical view]
    PRINTSiPR00169. KCHANNEL.
    PR01509. KV12CHANNEL.
    PR01491. KVCHANNEL.
    PR01496. SHAKERCHANEL.
    SMARTiSM00225. BTB. 1 hit.
    [Graphical view]
    SUPFAMiSSF54695. SSF54695. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    1. "Isolation of a cDNA clone coding for a putative second potassium channel indicates the existence of a gene family."
      McKinnon D.
      J. Biol. Chem. 264:8230-8236(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    2. "Molecular basis of functional diversity of voltage-gated potassium channels in mammalian brain."
      Stuehmer W., Ruppersberg J.P., Schroerter K.H., Sakmann B., Stocker M., Giese K.P., Perschke A., Baumann A., Pongs O.
      EMBO J. 8:3235-3244(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
      Tissue: Brain.
    3. Ludwig J.
      Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    4. Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      Tissue: Heart atrium.
    5. "Heteromultimeric assembly of human potassium channels. Molecular basis of a transient outward current?"
      Po S., Roberds S., Snyders D.J., Tamkun M.M., Bennett P.B.
      Circ. Res. 72:1326-1336(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, INTERACTION WITH KCNA4, ENZYME REGULATION.
    6. "Tityustoxin-K alpha, a structurally novel and highly potent K+ channel peptide toxin, interacts with the alpha-dendrotoxin binding site on the cloned Kv1.2 K+ channel."
      Werkman T.R., Gustafson T.A., Rogowski R.S., Blaustein M.P., Rogawski M.A.
      Mol. Pharmacol. 44:430-436(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION.
    7. "Presynaptic A-current based on heteromultimeric K+ channels detected in vivo."
      Sheng M., Liao Y.J., Jan Y.N., Jan L.Y.
      Nature 365:72-75(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT, INTERACTION WITH KCNA4, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    8. "Clustering of Shaker-type K+ channels by interaction with a family of membrane-associated guanylate kinases."
      Kim E., Niethammer M., Rothschild A., Jan Y.N., Sheng M.
      Nature 378:85-88(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DLG1; DLG2 AND DLG4, TISSUE SPECIFICITY.
    9. "Protein tyrosine kinase PYK2 involved in Ca(2+)-induced regulation of ion channel and MAP kinase functions."
      Lev S., Moreno H., Martinez R., Canoll P., Peles E., Musacchio J.M., Plowman G.D., Rudy B., Schlessinger J.
      Nature 376:737-745(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION.
      Tissue: Brain.
    10. "The small GTP-binding protein RhoA regulates a delayed rectifier potassium channel."
      Cachero T.G., Morielli A.D., Peralta E.G.
      Cell 93:1077-1085(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH RHOA.
    11. "Caspr2, a new member of the neurexin superfamily, is localized at the juxtaparanodes of myelinated axons and associates with K+ channels."
      Poliak S., Gollan L., Martinez R., Custer A., Einheber S., Salzer J.L., Trimmer J.S., Shrager P., Peles E.
      Neuron 24:1037-1047(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CNTNAP2, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    12. "Subunit composition determines Kv1 potassium channel surface expression."
      Manganas L.N., Trimmer J.S.
      J. Biol. Chem. 275:29685-29693(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, SUBUNIT, INTERACTION WITH KCNAB2; KCNA1 AND KCNA4, GLYCOSYLATION.
    13. "Subunit composition and novel localization of K+ channels in spinal cord."
      Rasband M.N., Trimmer J.S.
      J. Comp. Neurol. 429:166-176(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH KCNA1 AND KCNAB2, SUBUNIT, TISSUE SPECIFICITY.
    14. "Signal transduction of physiological concentrations of vasopressin in A7r5 vascular smooth muscle cells. A role for PYK2 and tyrosine phosphorylation of K+ channels in the stimulation of Ca2+ spiking."
      Byron K.L., Lucchesi P.A.
      J. Biol. Chem. 277:7298-7307(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PTK2B, PHOSPHORYLATION.
    15. "Tyrosine phosphorylation of Kv1.2 modulates its interaction with the actin-binding protein cortactin."
      Hattan D., Nesti E., Cachero T.G., Morielli A.D.
      J. Biol. Chem. 277:38596-38606(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PHOSPHORYLATION, INTERACTION WITH CTTN, SUBCELLULAR LOCATION, TOPOLOGY, MUTAGENESIS OF TYR-415 AND TYR-417.
    16. "Two heteromeric Kv1 potassium channels differentially regulate action potential firing."
      Dodson P.D., Barker M.C., Forsythe I.D.
      J. Neurosci. 22:6953-6961(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, SUBUNIT.
    17. "Enhancement of ischemia-induced tyrosine phosphorylation of Kv1.2 by vascular endothelial growth factor via activation of phosphatidylinositol 3-kinase."
      Qiu M.H., Zhang R., Sun F.Y.
      J. Neurochem. 87:1509-1517(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION BY HYPOXIA, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, PHOSPHORYLATION.
    18. "Presynaptic rat Kv1.2 channels suppress synaptic terminal hyperexcitability following action potential invasion."
      Dodson P.D., Billups B., Rusznak Z., Szucs G., Barker M.C., Forsythe I.D.
      J. Physiol. (Lond.) 550:27-33(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    19. "Kv channel subunits that contribute to voltage-gated K+ current in renal vascular smooth muscle."
      Fergus D.J., Martens J.R., England S.K.
      Pflugers Arch. 445:697-704(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT, INTERACTION WITH KCNA4, TISSUE SPECIFICITY.
    20. "Subacute hypoxia decreases voltage-activated potassium channel expression and function in pulmonary artery myocytes."
      Hong Z., Weir E.K., Nelson D.P., Olschewski A.
      Am. J. Respir. Cell Mol. Biol. 31:337-343(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION BY HYPOXIA.
    21. "Heteromultimeric Kv1 channels contribute to myogenic control of arterial diameter."
      Plane F., Johnson R., Kerr P., Wiehler W., Thorneloe K., Ishii K., Chen T., Cole W.
      Circ. Res. 96:216-224(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, SUBUNIT.
    22. "Kv1 channels selectively prevent dendritic hyperexcitability in rat Purkinje cells."
      Khavandgar S., Walter J.T., Sageser K., Khodakhah K.
      J. Physiol. (Lond.) 569:545-557(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    23. "Mu opioid receptor activation inhibits GABAergic inputs to basolateral amygdala neurons through Kv1.1/1.2 channels."
      Finnegan T.F., Chen S.R., Pan H.L.
      J. Neurophysiol. 95:2032-2041(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    24. "Glycosylation and cell surface expression of Kv1.2 potassium channel are regulated by determinants in the pore region."
      Fujita T., Utsunomiya I., Ren J., Matsushita Y., Kawai M., Sasaki S., Hoshi K., Miyatake T., Taguchi K.
      Neurochem. Res. 31:589-596(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, GLYCOSYLATION AT ASN-207, MUTAGENESIS OF ASN-207; SER-356; SER-360 AND THR-383.
    25. "The glycosylation state of Kv1.2 potassium channels affects trafficking, gating, and simulated action potentials."
      Watanabe I., Zhu J., Sutachan J.J., Gottschalk A., Recio-Pinto E., Thornhill W.B.
      Brain Res. 1144:1-18(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, GLYCOSYLATION, BIOPHYSICOCHEMICAL PROPERTIES.
    26. "An activation gating switch in Kv1.2 is localized to a threonine residue in the S2-S3 linker."
      Rezazadeh S., Kurata H.T., Claydon T.W., Kehl S.J., Fedida D.
      Biophys. J. 93:4173-4186(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF THR-252.
    27. "Ionic channel function in action potential generation: current perspective."
      Baranauskas G.
      Mol. Neurobiol. 35:129-150(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    28. "Kv1.1/1.2 channels are downstream effectors of nitric oxide on synaptic GABA release to preautonomic neurons in the paraventricular nucleus."
      Yang Q., Chen S.R., Li D.P., Pan H.L.
      Neuroscience 149:315-327(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    29. "Homeostatic regulation of Kv1.2 potassium channel trafficking by cyclic AMP."
      Connors E.C., Ballif B.A., Morielli A.D.
      J. Biol. Chem. 283:3445-3453(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-440 AND SER-449, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH KCNAB2, MUTAGENESIS OF THR-46; SER-440 AND SER-449.
    30. "Functional analysis of Kv1.2 and paddle chimera Kv channels in planar lipid bilayers."
      Tao X., MacKinnon R.
      J. Mol. Biol. 382:24-33(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF 267-PHE--PHE-302.
    31. "The molecular basis for the actions of Kvbeta1.2 on the opening and closing of the Kv1.2 delayed rectifier channel."
      Peters C.J., Vaid M., Horne A.J., Fedida D., Accili E.A.
      Channels 3:314-322(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT, INTERACTION WITH KCNAB1.
    32. "Dual roles for RHOA/RHO-kinase in the regulated trafficking of a voltage-sensitive potassium channel."
      Stirling L., Williams M.R., Morielli A.D.
      Mol. Biol. Cell 20:2991-3002(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    33. Cited for: FUNCTION, SUBCELLULAR LOCATION, ENZYME REGULATION.
    34. "ADAM22, a Kv1 channel-interacting protein, recruits membrane-associated guanylate kinases to juxtaparanodes of myelinated axons."
      Ogawa Y., Oses-Prieto J., Kim M.Y., Horresh I., Peles E., Burlingame A.L., Trimmer J.S., Meijer D., Rasband M.N.
      J. Neurosci. 30:1038-1048(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH ADAM22 AND DLG4, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, TISSUE SPECIFICITY.
    35. "Clustering and activity tuning of Kv1 channels in myelinated hippocampal axons."
      Gu C., Gu Y.
      J. Biol. Chem. 286:25835-25847(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, PHOSPHORYLATION AT TYR-458, MUTAGENESIS OF TYR-458.
    36. "Role of Kv1 potassium channels in regulating dopamine release and presynaptic D2 receptor function."
      Martel P., Leo D., Fulton S., Berard M., Trudeau L.E.
      PLoS ONE 6:E20402-E20402(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    37. "Pharmacological characteristics of Kv1.1- and Kv1.2-containing channels are influenced by the stoichiometry and positioning of their alpha subunits."
      Al-Sabi A., Kaza S.K., Dolly J.O., Wang J.
      Biochem. J. 454:101-108(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF VAL-381.
    38. "A defined heteromeric KV1 channel stabilizes the intrinsic pacemaking and regulates the output of deep cerebellar nuclear neurons to thalamic targets."
      Ovsepian S.V., Steuber V., Le Berre M., O'Hara L., O'Leary V.B., Dolly J.O.
      J. Physiol. (Lond.) 591:1771-1791(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, IDENTIFICATION IN A COMPLEX WITH KCNA1 AND KCNAB2.
    39. "Impaired neuropathic pain and preserved acute pain in rats overexpressing voltage-gated potassium channel subunit Kv1.2 in primary afferent neurons."
      Fan L., Guan X., Wang W., Zhao J.Y., Zhang H., Tiwari V., Hoffman P.N., Li M., Tao Y.X.
      Mol. Pain 10:8-8(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION.
    40. "The polar T1 interface is linked to conformational changes that open the voltage-gated potassium channel."
      Minor D.L. Jr., Lin Y.-F., Mobley B.C., Avelar A., Jan Y.N., Jan L.Y., Berger J.M.
      Cell 102:657-670(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 33-119 OF WILD-TYPE AND MUTANT VAL-46, FUNCTION, SUBUNIT, REGION, DOMAIN, MUTAGENESIS OF ARG-34; ASN-38; SER-40; GLY-41; LEU-42; ARG-43; PHE-44; GLU-45; THR-46; GLN-47; THR-50; ASP-70; ARG-73; GLU-75; PHE-77; ASP-79; ASN-81; ARG-82; ASP-86; LEU-89; TYR-90; GLN-93; ARG-97; ARG-99; VAL-102; ASN-103; PRO-105; ASP-107; ILE-108 AND GLU-111.
    41. "Crystal structure of a mammalian voltage-dependent Shaker family K+ channel."
      Long S.B., Campbell E.B., Mackinnon R.
      Science 309:897-903(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) IN COMPLEX WITH KCNAB2, SUBCELLULAR LOCATION, TOPOLOGY, SUBUNIT, INTERACTION WITH KCNAB2.
    42. "Voltage sensor of Kv1.2: structural basis of electromechanical coupling."
      Long S.B., Campbell E.B., Mackinnon R.
      Science 309:903-908(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) IN COMPLEX WITH KCNAB2, DOMAIN.
    43. "Atomic structure of a voltage-dependent K+ channel in a lipid membrane-like environment."
      Long S.B., Tao X., Campbell E.B., MacKinnon R.
      Nature 450:376-382(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF PADDLE CHIMERA MUTANT IN COMPLEX WITH KCNAB2, FUNCTION, SUBUNIT, INTERACTION WITH KCNAB2, SUBCELLULAR LOCATION, TOPOLOGY.
    44. "Structure of the full-length Shaker potassium channel Kv1.2 by normal-mode-based X-ray crystallographic refinement."
      Chen X., Wang Q., Ni F., Ma J.
      Proc. Natl. Acad. Sci. U.S.A. 107:11352-11357(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) IN COMPLEX WITH KCNAB2, INTERACTION WITH KCNAB2, SUBUNIT, SUBCELLULAR LOCATION, TOPOLOGY.
    45. "A gating charge transfer center in voltage sensors."
      Tao X., Lee A., Limapichat W., Dougherty D.A., MacKinnon R.
      Science 328:67-73(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 1-266 AND 303-499 IN COMPLEX WITH KCNAB2, SUBUNIT, INTERACTION WITH KCNAB2, SUBCELLULAR LOCATION, TOPOLOGY.
    46. "Structure of a pore-blocking toxin in complex with a eukaryotic voltage-dependent K(+) channel."
      Banerjee A., Lee A., Campbell E., Mackinnon R.
      Elife 2:E00594-E00594(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF PADDLE CHIMERA MUTANT IN COMPLEX WITH KCNAB2 AND CHARYBDOTOXIN, INTERACTION WITH KCNAB2, SUBUNIT, SUBCELLULAR LOCATION, TOPOLOGY.

    Entry informationi

    Entry nameiKCNA2_RAT
    AccessioniPrimary (citable) accession number: P63142
    Secondary accession number(s): P15386, Q02010
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 13, 2004
    Last sequence update: September 13, 2004
    Last modified: April 1, 2015
    This is version 108 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    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).1 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.