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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

      • delayed rectifier potassium channel activity Source: UniProtKB
      • outward rectifier potassium channel activity Source: RGD
      • voltage-gated potassium channel activity Source: UniProtKB

      GO - Biological processi

      • neuronal action potential Source: UniProtKB
      • optic nerve structural organization Source: Ensembl
      • potassium ion transmembrane transport Source: UniProtKB
      • protein homooligomerization Source: InterPro
      • protein oligomerization Source: RGD
      • regulation of circadian sleep/wake cycle, non-REM sleep Source: Ensembl
      • regulation of dopamine secretion Source: UniProtKB
      • 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

      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

      • axon terminus Source: UniProtKB
      • cell junction Source: UniProtKB-KW
      • dendrite Source: UniProtKB
      • endoplasmic reticulum membrane Source: UniProtKB-SubCell
      • endosome Source: UniProtKB-SubCell
      • integral component of plasma membrane Source: UniProtKB
      • juxtaparanode region of axon Source: UniProtKB
      • lamellipodium Source: UniProtKB
      • lamellipodium membrane Source: UniProtKB-SubCell
      • neuronal cell body membrane Source: UniProtKB
      • perikaryon Source: UniProtKB
      • potassium channel complex Source: UniProtKB
      • presynaptic membrane Source: UniProtKB-SubCell
      • 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

      GenevisibleiP63142. RN.

      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. 3 interactions.
      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
      Helixi221 – 24121Combined sources
      Turni249 – 2524Combined sources
      Helixi254 – 2618Combined sources
      Helixi279 – 2824Combined sources
      Helixi291 – 2999Combined sources
      Helixi304 – 3096Combined 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[»]
      ProteinModelPortaliP63142.
      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[»]
      ProteinModelPortaliP63142.
      SMRiP63142. Positions 3-421.
      ModBaseiSearch...
      MobiDBiSearch...

      Protein-protein interaction databases

      BioGridi247501. 5 interactions.
      IntActiP63142. 3 interactions.
      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.
      NextBioi606761.
      PROiP63142.

      Gene expression databases

      GenevisibleiP63142. RN.

      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(1989) [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(1989) [PubMed] [Europe PMC] [Abstract]
        Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
        Tissue: Brain.
      3. Ludwig J.
        Submitted (MAR-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(1993) [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(1993) [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(1993) [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(1995) [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(1995) [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(1998) [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(1999) [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(2000) [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(2001) [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(2002) [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(2002) [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(2002) [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(2003) [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(2003) [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(2003) [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(2004) [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(2005) [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(2005) [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(2006) [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(2006) [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(2007) [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(2007) [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(2007) [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(2007) [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(2008) [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(2008) [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(2009) [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(2009) [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(2010) [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(2011) [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(2011) [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(2013) [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(2013) [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(2014) [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(2000) [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(2005) [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(2005) [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(2007) [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(2010) [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(2010) [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(2013) [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: July 22, 2015
      This is version 112 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.