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Protein

Potassium voltage-gated channel subfamily A member 1

Gene

Kcna1

Organism
Mus musculus (Mouse)
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 kidney. Contributes to the regulation of the membrane potential and nerve signaling, and prevents neuronal hyperexcitability (PubMed:9736643, PubMed:9581771 PubMed:10191303, PubMed:12611922, PubMed:21966978, PubMed:22158511, PubMed:23473320). 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:15361858). 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. 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:15361858). In vivo, membranes probably contain a mixture of heteromeric potassium channel complexes, making it difficult to assign currents observed in intact tissues to any particular potassium channel family member. Homotetrameric KCNA1 forms a delayed-rectifier potassium channel that opens in response to membrane depolarization, followed by slow spontaneous channel closure (PubMed:7517498, PubMed:15361858). In contrast, a heterotetrameric channel formed by KCNA1 and KCNA4 shows rapid inactivation (By similarity). Regulates neuronal excitability in hippocampus, especially in mossy fibers and medial perforant path axons, preventing neuronal hyperexcitability (PubMed:23466697). May function as down-stream effector for G protein-coupled receptors and inhibit GABAergic inputs to basolateral amygdala neurons (By similarity). May contribute to the regulation of neurotransmitter release, such as gamma-aminobutyric acid (GABA) release (By similarity). Plays a role in regulating the generation of action potentials and preventing hyperexcitability in myelinated axons of the vagus nerve, and thereby contributes to the regulation of heart contraction (PubMed:20392939, PubMed:22641786, PubMed:25377007). Required for normal neuromuscular responses (PubMed:9736643). Regulates the frequency of neuronal action potential firing in response to mechanical stimuli, and plays a role in the perception of pain caused by mechanical stimuli, but does not play a role in the perception of pain due to heat stimuli (PubMed:23473320). Required for normal responses to auditory stimuli and precise location of sound sources, but not for sound perception (PubMed:21966978, PubMed:22396426). The use of toxins that block specific channels suggest that it contributes to the regulation of the axonal release of the neurotransmitter dopamine (PubMed:21233214). Required for normal postnatal brain development and normal proliferation of neuronal precursor cells in the brain (PubMed:8995755, PubMed:17250763, PubMed:17315199, PubMed:22411008). Plays a role in the reabsorption of Mg2+ in the distal convoluted tubules in the kidney and in magnesium ion homeostasis, probably via its effect on the membrane potential (By similarity).By similarity19 Publications

Enzyme regulationi

Inhibited by 4-aminopyridine (4-AP), tetraethylammonium (TEA) and dendrotoxin (DTX), but not by charybdotoxin (CTX).1 Publication

GO - Molecular functioni

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

GO - Biological processi

  1. brain development Source: UniProtKB
  2. cellular response to magnesium ion Source: UniProtKB
  3. detection of mechanical stimulus involved in sensory perception of pain Source: UniProtKB
  4. detection of mechanical stimulus involved in sensory perception of touch Source: UniProtKB
  5. hippocampus development Source: UniProtKB
  6. magnesium ion homeostasis Source: UniProtKB
  7. neuroblast proliferation Source: UniProtKB
  8. neuromuscular process Source: UniProtKB
  9. neuronal action potential Source: UniProtKB
  10. potassium ion transmembrane transport Source: UniProtKB
  11. protein homooligomerization Source: InterPro
  12. regulation of membrane potential Source: UniProtKB
  13. startle response 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_199077. Voltage gated Potassium channels.

Names & Taxonomyi

Protein namesi
Recommended name:
Potassium voltage-gated channel subfamily A member 1
Alternative name(s):
MBK11 Publication
MKI
Voltage-gated potassium channel subunit Kv1.1
Gene namesi
Name:Kcna1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 6

Organism-specific databases

MGIiMGI:96654. Kcna1.

Subcellular locationi

Cell membrane 2 Publications; Multi-pass membrane protein Curated. Cell projectionaxon 6 Publications. Membrane 1 Publication. Perikaryon 2 Publications. Cell projectiondendrite 1 Publication. Cell junction 1 Publication. Cell junctionsynapse 1 Publication. Cytoplasmic vesicle 1 Publication. Endoplasmic reticulum By similarity. Cell junctionsynapsepresynaptic cell membrane By similarity
Note: Homotetrameric KCNA1 is primarily located in the endoplasmic reticulum. Interaction with KCNA2 and KCNAB2 or with KCNA4 and KCNAB2 promotes expression at the cell membrane (By similarity). Detected at axon terminals (PubMed:21233214).By similarity1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 164164CytoplasmicBy similarityAdd
BLAST
Transmembranei165 – 18622Helical; Name=Segment S1By similarityAdd
BLAST
Topological domaini187 – 22034ExtracellularBy similarityAdd
BLAST
Transmembranei221 – 24222Helical; Name=Segment S2By similarityAdd
BLAST
Topological domaini243 – 25311CytoplasmicBy similarityAdd
BLAST
Transmembranei254 – 27421Helical; Name=Segment S3By similarityAdd
BLAST
Topological domaini275 – 28713ExtracellularBy similarityAdd
BLAST
Transmembranei288 – 30821Helical; Voltage-sensor; Name=Segment S4By similarityAdd
BLAST
Topological domaini309 – 32315CytoplasmicBy similarityAdd
BLAST
Transmembranei324 – 34522Helical; Name=Segment S5By similarityAdd
BLAST
Topological domaini346 – 35914ExtracellularBy similarityAdd
BLAST
Intramembranei360 – 37112Helical; Name=Pore helixBy similarityAdd
BLAST
Intramembranei372 – 3798By similarity
Topological domaini380 – 3867ExtracellularBy similarity
Transmembranei387 – 41529Helical; Name=Segment S6By similarityAdd
BLAST
Topological domaini416 – 49580CytoplasmicBy similarityAdd
BLAST

GO - Cellular componenti

  1. apical plasma membrane Source: Ensembl
  2. axon Source: UniProtKB
  3. axon terminus Source: UniProtKB
  4. cell junction Source: UniProtKB
  5. cell surface Source: MGI
  6. dendrite Source: UniProtKB
  7. integral component of membrane Source: GO_Central
  8. integral component of plasma membrane Source: UniProtKB
  9. juxtaparanode region of axon Source: UniProtKB
  10. neuronal cell body Source: UniProtKB
  11. paranode region of axon Source: UniProtKB
  12. synapse Source: UniProtKB
  13. voltage-gated potassium channel complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Cytoplasmic vesicle, Endoplasmic reticulum, Membrane, Synapse

Pathology & Biotechi

Involvement in diseasei

A spontaneous mutation leading to a frameshift and truncation of Kcna2 causes megencephaly with a 25% increase of brain weight relative to wild-type. Especially the hippocampus shows increased proliferation of neurons and astrocytes, leading to increased brain volume (PubMed:17315199). Mutant mice appear normal at birth. After 3-4 weeks, they display low body weight, a subtle shakiness in their gait, a preference for a strange sitting position that is maintained for periods ranging from 30 seconds to several minutes, excessive lacrimation and acoustic startle hypersensitivity (PubMed:8995755, PubMed:21966978). The increase in the acoustic startle response is down-regulated by treatment with the anti-epileptic drug valproate (PubMed:21966978). Mutant mice display an abnormal electro-encephalogram with single spikes and waves, when anesthesized (PubMed:21966978). The electric activity of mossy cells from the dentate hilus region is altered and shows increased firing of action potentials, probably due to the absence of functional Kcna1 channels (PubMed:14686897). Heterozygotes show mechanical allodynia, but no increased sensitivity to heat (PubMed:23473320). Homozygotes show no alteration of the islet of Langerhans structure, of the basal levels of insulin secretion and blood glucose levels (PubMed:21483673). Compared to wild-type, they display moderately increased insulin secretion in response to a glucose stimulus (PubMed:21483673). Besides, the frequency of beta cell action potentials is increased (PubMed:21483673).

Disruption phenotypei

Mice are born at the expected Mendelian rate. After three weeks, mice begin to display episodic eye blinking, twitching of whiskers, forlimb padding, arrested motion and a hyperstartle response. About 50% of the homozygotes die between the third and the fifth week after birth. Surviving mice continue to display spontaneous seizures occurring once or twice every hour throughout adult life (PubMed:9581771). The fecundity of homozygotes is extremely low (PubMed:9581771). Mutant mice display interictal cardiac abnormalities, including a fivefold increase in atrioventricular conduction blocks, brachycardia and premature ventricular contractions; this may lead to sudden unexplained death in epilepsy (PubMed:20392939). Mutant mice have slightly elevated heart rates; they all have a reduced livespan and are subject to sudden death after presumed seizure activity and sinus bradycardia (PubMed:25377007). About 70% of the mutant mice have an enlarged hippocampus and ventral brain cortex (PubMed:17250763). Mutant mice show a temperature-sensitive alteration in neuromuscular transmission, causing nerve hyperexcitability when exposed to cold and delayed repetitive discharge after a single nerve stimulation (PubMed:9736643). After 2 minutes of swimming in cold water, mutant mice have impaired motor control; they fall over when placed on dry ground and exhibit severe neuromyotonia with violent tremors that decrease with time, leading to full recovery after twenty minutes (PubMed:9736643). Mutant mice have an increased frequency of spontaneous postsynaptic currents in Purkinje cells, impaired ability to maintain their balance on a thin stationary rod, but perform as well as wild-type on a rotarod (PubMed:10191303). Mutant mice have a normal hearing threshold, but altered brainstem responses to auditory stimuli and reduced sensitivity to small changes in sound location (PubMed:22396426). Mutant mice display no alteration of the islet of Langerhans, but have reduced blood glucose levels and increased insulin secretion in response to a glucose stimulus (PubMed:21483673).8 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 495495Potassium voltage-gated channel subfamily A member 1PRO_0000053969Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi207 – 2071N-linked (GlcNAc...)Sequence Analysis
Lipidationi243 – 2431S-palmitoyl cysteineBy similarity
Modified residuei322 – 3221Phosphoserine; by PKASequence Analysis
Modified residuei446 – 4461Phosphoserine; by PKABy similarity

Post-translational modificationi

N-glycosylated.By similarity
Palmitoylated on Cys-243; which may be required for membrane targeting.By similarity
Phosphorylated on tyrosine residues. Phosphorylation increases in response to NRG1; this inhibits channel activity (PubMed:22158511). Phosphorylation at Ser-446 regulates channel activity by down-regulating expression at the cell membrane (By similarity).By similarity1 Publication

Keywords - PTMi

Glycoprotein, Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

MaxQBiP16388.
PaxDbiP16388.
PRIDEiP16388.

PTM databases

PhosphoSiteiP16388.

Expressioni

Tissue specificityi

Detected in brain (PubMed:21483673, PubMed:22158511). Detected in the juxtaparanodal regions of the nodes of Ranvier in myelinated axons (PubMed:8361541, PubMed:8046438). Detected in the paranodal region in sciatic nerve (PubMed:9736643). Detected on cell bodies in cerebellum, dorsal and ventral cochlear nucleus, pontine reticular nucleus, mesencephalic trigeminal nucleus, motor trigeminal nucleus and the pricipal sensory trigeminal nucleus (PubMed:8046438). Detected in terminal fields of basket cells in the cerebellum corpus medullare (PubMed:8361541, PubMed:8046438, PubMed:9581771). Detected in hippocampus CA3 pyramidal neurons and in the hilus and stratum moleculare of the dentate gyrus (PubMed:8046438, PubMed:9581771, PubMed:14686897). Detected in the central nucleus and the external nucleus of the inferior colliculus (PubMed:8046438, PubMed:21966978). Detected in fiber tracts in the optic tract, external medullary lamina, stria terminalis, medulla, ventral pallidum and substantia nigra (PubMed:8046438). Detected in neurons from dorsal root ganglion (PubMed:23473320). Detected in neurons in the medial nucleus of the trapezoid body (PubMed:12611922). Detected in midbrain dopamine neuron axon terminals (PubMed:21233214). Detected in brain cortex (PubMed:8046438, PubMed:14686897). Detected in brainstem (PubMed:8361541). Detected in juxtaparanodal regions of the nodes of Ranvier in the vagus nerve, but only at very low levels in the heart (PubMed:20392939, PubMed:22641786). Detected in the islet of Langerhans (PubMed:21483673). Detected at the luminal membrane in distal convoluted tubules in the kidney (at protein level) (PubMed:19307729). Detected in brain (PubMed:2451788, PubMed:9581771). Detected in hippocampus, thalamus, neocortex and ventral brain cortex, including the piriform and entorhinal cortex and the amygdala (PubMed:14686897). Detected in midbrain dopamine neurons (PubMed:21233214). Detected in heart atrium, ventricule, sinoatrial node and atrioventricular node (PubMed:20392939). Detected in the islet of Langerhans (PubMed:21483673).15 Publications

Inductioni

Down-regulated by high dietary Mg2+ levels.1 Publication

Gene expression databases

BgeeiP16388.
ExpressionAtlasiP16388. baseline and differential.
GenevestigatoriP16388.

Interactioni

Subunit structurei

Homotetramer and heterotetramer with other channel-forming alpha subunits, such as KCNA2, KCNA4, KCNA5, KCNA6 and KCNA7 (PubMed:8361541). Channel activity is regulated by interaction with the beta subunits KCNAB1 and KCNAB2 (PubMed:15361858). Identified in a complex with KCNA2 and KCNAB2. Interacts (via C-terminus) with the PDZ domains of DLG1, DLG2 and DLG4 (By similarity). Interacts with LGI1 within a complex containing LGI1, KCNA4 and KCNAB1 (By similarity). Interacts (via N-terminus) with STX1A; this promotes channel inactivation (By similarity). Interacts (via N-terminus) with the heterodimer formed by GNB1 and GNG2; this promotes channel inactivation (By similarity). Can interact simultaneously with STX1A and the heterodimer formed by GNB1 and GNG2 (By similarity). Interacts (via cytoplasmic N-terminal domain) with KCNRG; this inhibits channel activity (By similarity). Interacts with ANK3; this inhibits channel activity (PubMed:23903368).By similarity3 PublicationsCurated

Protein-protein interaction databases

BioGridi200876. 1 interaction.
IntActiP16388. 2 interactions.
MINTiMINT-4099639.

Structurei

3D structure databases

ProteinModelPortaliP16388.
SMRiP16388. Positions 36-419.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 128128Tetramerization domainBy similarityAdd
BLAST
Regioni310 – 32314S4-S5 linkerBy similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi372 – 3776Selectivity filterBy similarity
Motifi493 – 4953PDZ-bindingBy similarity

Domaini

The cytoplasmic N-terminus is important for tetramerization and for interaction with the beta subunits that promote rapid channel closure.By similarity
The transmembrane segment S4 functions as voltage-sensor and is characterized by a series of positively charged amino acids at every third position. Channel opening and closing is effected by a conformation change that affects the position and orientation of the voltage-sensor paddle formed by S3 and S4 within the membrane. A transmembrane electric field that is positive inside would push the positively charged S4 segment outwards, thereby opening the pore, while a field that is negative inside would pull the S4 segment inwards and close the pore. Changes in the position and orientation of S4 are then transmitted to the activation gate formed by the inner helix bundle via the S4-S5 linker region.By similarity

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1226.
GeneTreeiENSGT00760000118846.
HOGENOMiHOG000231015.
HOVERGENiHBG052230.
InParanoidiP16388.
KOiK04874.
OMAiIHRIDNT.
OrthoDBiEOG7M0NRD.
PhylomeDBiP16388.
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.
IPR004048. K_chnl_volt-dep_Kv1.1.
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.
PR01508. KV11CHANNEL.
PR01491. KVCHANNEL.
PR01496. SHAKERCHANEL.
SMARTiSM00225. BTB. 1 hit.
[Graphical view]
SUPFAMiSSF54695. SSF54695. 1 hit.

Sequencei

Sequence statusi: Complete.

P16388-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTVMSGENAD EASTAPGHPQ DGSYPRQADH DDHECCERVV INISGLRFET
60 70 80 90 100
QLKTLAQFPN TLLGNPKKRM RYFDPLRNEY FFDRNRPSFD AILYYYQSGG
110 120 130 140 150
RLRRPVNVPL DMFSEEIKFY ELGEEAMEKF REDEGFIKEE ERPLPEKEYQ
160 170 180 190 200
RQVWLLFEYP ESSGPARVIA IVSVMVILIS IVIFCLETLP ELKDDKDFTG
210 220 230 240 250
TIHRIDNTTV IYTSNIFTDP FFIVETLCII WFSFELVVRF FACPSKTDFF
260 270 280 290 300
KNIMNFIDIV AIIPYFITLG TEIAEQEGNQ KGEQATSLAI LRVIRLVRVF
310 320 330 340 350
RIFKLSRHSK GLQILGQTLK ASMRELGLLI FFLFIGVILF SSAVYFAEAE
360 370 380 390 400
EAESHFSSIP DAFWWAVVSM TTVGYGDMYP VTIGGKIVGS LCAIAGVLTI
410 420 430 440 450
ALPVPVIVSN FNYFYHRETE GEEQAQLLHV SSPNLASDSD LSRRSSSTIS
460 470 480 490
KSEYMEIEED MNNSIAHYRQ ANIRTGNCTT ADQNCVNKSK LLTDV
Length:495
Mass (Da):56,409
Last modified:August 1, 1990 - v1
Checksum:iC9249F130E943D3D
GO

RNA editingi

Partially edited. RNA editing varies from 35% in the frontal cortex to 75% in the spinal chord.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti400 – 4001I → V in RNA edited version.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M30439 Genomic DNA. Translation: AAA39711.1.
Y00305 mRNA. Translation: CAA68408.1.
CCDSiCCDS20555.1.
PIRiA40090.
S09042.
RefSeqiNP_034725.3. NM_010595.3.
UniGeneiMm.40424.

Genome annotation databases

EnsembliENSMUST00000055168; ENSMUSP00000055225; ENSMUSG00000047976.
GeneIDi16485.
KEGGimmu:16485.
UCSCiuc009dvb.1. mouse.

Keywords - Coding sequence diversityi

RNA editing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M30439 Genomic DNA. Translation: AAA39711.1.
Y00305 mRNA. Translation: CAA68408.1.
CCDSiCCDS20555.1.
PIRiA40090.
S09042.
RefSeqiNP_034725.3. NM_010595.3.
UniGeneiMm.40424.

3D structure databases

ProteinModelPortaliP16388.
SMRiP16388. Positions 36-419.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi200876. 1 interaction.
IntActiP16388. 2 interactions.
MINTiMINT-4099639.

Chemistry

ChEMBLiCHEMBL2429705.
GuidetoPHARMACOLOGYi538.

PTM databases

PhosphoSiteiP16388.

Proteomic databases

MaxQBiP16388.
PaxDbiP16388.
PRIDEiP16388.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000055168; ENSMUSP00000055225; ENSMUSG00000047976.
GeneIDi16485.
KEGGimmu:16485.
UCSCiuc009dvb.1. mouse.

Organism-specific databases

CTDi3736.
MGIiMGI:96654. Kcna1.

Phylogenomic databases

eggNOGiCOG1226.
GeneTreeiENSGT00760000118846.
HOGENOMiHOG000231015.
HOVERGENiHBG052230.
InParanoidiP16388.
KOiK04874.
OMAiIHRIDNT.
OrthoDBiEOG7M0NRD.
PhylomeDBiP16388.
TreeFamiTF313103.

Enzyme and pathway databases

ReactomeiREACT_199077. Voltage gated Potassium channels.

Miscellaneous databases

NextBioi289783.
PROiP16388.
SOURCEiSearch...

Gene expression databases

BgeeiP16388.
ExpressionAtlasiP16388. baseline and differential.
GenevestigatoriP16388.

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.
IPR004048. K_chnl_volt-dep_Kv1.1.
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.
PR01508. KV11CHANNEL.
PR01491. KVCHANNEL.
PR01496. SHAKERCHANEL.
SMARTiSM00225. BTB. 1 hit.
[Graphical view]
SUPFAMiSSF54695. SSF54695. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A family of three mouse potassium channel genes with intronless coding regions."
    Chandy K.G., Williams C.B., Spencer R.H., Aguilar B.A., Ghanshani S., Tempel B.L., Gutman G.A.
    Science 247:973-975(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Cloning of a probable potassium channel gene from mouse brain."
    Tempel B.L., Jan Y.N., Jan L.Y.
    Nature 332:837-839(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Tissue: Brain.
  3. "Heteromultimeric K+ channels in terminal and juxtaparanodal regions of neurons."
    Wang H., Kunkel D.D., Martin T.M., Schwartzkroin P.A., Tempel B.L.
    Nature 365:75-79(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, INTERACTION WITH KCNA2, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  4. "Localization of Kv1.1 and Kv1.2, two K channel proteins, to synaptic terminals, somata, and dendrites in the mouse brain."
    Wang H., Kunkel D.D., Schwartzkroin P.A., Tempel B.L.
    J. Neurosci. 14:4588-4599(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
  5. "Pharmacological characterization of five cloned voltage-gated K+ channels, types Kv1.1, 1.2, 1.3, 1.5, and 3.1, stably expressed in mammalian cell lines."
    Grissmer S., Nguyen A.N., Aiyar J., Hanson D.C., Mather R.J., Gutman G.A., Karmilowicz M.J., Auperin D.D., Chandy K.G.
    Mol. Pharmacol. 45:1227-1234(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, ENZYME REGULATION.
  6. "Megencephaly: a new mouse mutation on chromosome 6 that causes hypertrophy of the brain."
    Donahue L.R., Cook S.A., Johnson K.R., Bronson R.T., Davisson M.T.
    Mamm. Genome 7:871-876(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISEASE, FUNCTION.
  7. "Temperature-sensitive neuromuscular transmission in Kv1.1 null mice: role of potassium channels under the myelin sheath in young nerves."
    Zhou L., Zhang C.L., Messing A., Chiu S.Y.
    J. Neurosci. 18:7200-7215(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
  8. Cited for: DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
  9. "Specific alteration of spontaneous GABAergic inhibition in cerebellar Purkinje cells in mice lacking the potassium channel Kv1. 1."
    Zhang C.L., Messing A., Chiu S.Y.
    J. Neurosci. 19:2852-2864(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION.
  10. "Truncation of the Shaker-like voltage-gated potassium channel, Kv1.1, causes megencephaly."
    Petersson S., Persson A.S., Johansen J.E., Ingvar M., Nilsson J., Klement G., Arhem P., Schalling M., Lavebratt C.
    Eur. J. Neurosci. 18:3231-3240(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISEASE, FUNCTION, TISSUE SPECIFICITY.
  11. "Hyperexcitability and reduced low threshold potassium currents in auditory neurons of mice lacking the channel subunit Kv1.1."
    Brew H.M., Hallows J.L., Tempel B.L.
    J. Physiol. (Lond.) 548:1-20(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  12. "Nervous system targets of RNA editing identified by comparative genomics."
    Hoopengardner B., Bhalla T., Staber C., Reenan R.
    Science 301:832-836(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: RNA EDITING OF POSITION 400.
  13. "Control of human potassium channel inactivation by editing of a small mRNA hairpin."
    Bhalla T., Rosenthal J.J., Holmgren M., Reenan R.
    Nat. Struct. Mol. Biol. 11:950-956(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, INTERACTION WITH KCNAB1.
  14. "Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
    Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
    Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  15. "Kv1.1 null mice have enlarged hippocampus and ventral cortex."
    Persson A.S., Westman E., Wang F.H., Khan F.H., Spenger C., Lavebratt C.
    BMC Neurosci. 8:10-10(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION.
  16. "Lack of potassium channel induces proliferation and survival causing increased neurogenesis and two-fold hippocampus enlargement."
    Almgren M., Persson A.S., Fenghua C., Witgen B.M., Schalling M., Nyengaard J.R., Lavebratt C.
    Hippocampus 17:292-304(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISEASE, FUNCTION.
  17. "A missense mutation in the Kv1.1 voltage-gated potassium channel-encoding gene KCNA1 is linked to human autosomal dominant hypomagnesemia."
    Glaudemans B., van der Wijst J., Scola R.H., Lorenzoni P.J., Heister A., van der Kemp A.W., Knoers N.V., Hoenderop J.G., Bindels R.J.
    J. Clin. Invest. 119:936-942(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  18. "Kv1.1 potassium channel deficiency reveals brain-driven cardiac dysfunction as a candidate mechanism for sudden unexplained death in epilepsy."
    Glasscock E., Yoo J.W., Chen T.T., Klassen T.L., Noebels J.L.
    J. Neurosci. 30:5167-5175(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  19. "Acoustic startle hypersensitivity in Mceph mice and its effect on hippocampal excitability."
    Fisahn A., Lavebratt C., Canlon B.
    Eur. J. Neurosci. 34:1121-1130(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISEASE, FUNCTION, TISSUE SPECIFICITY.
  20. "Contribution of Kv1.2 voltage-gated potassium channel to D2 autoreceptor regulation of axonal dopamine overflow."
    Fulton S., Thibault D., Mendez J.A., Lahaie N., Tirotta E., Borrelli E., Bouvier M., Tempel B.L., Trudeau L.E.
    J. Biol. Chem. 286:9360-9372(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  21. "Evidence for presence and functional effects of Kv1.1 channels in beta-cells: general survey and results from mceph/mceph mice."
    Ma Z., Lavebratt C., Almgren M., Portwood N., Forsberg L.E., Branstrom R., Berglund E., Falkmer S., Sundler F., Wierup N., Bjorklund A.
    PLoS ONE 6:E18213-E18213(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, DISEASE, DISRUPTION PHENOTYPE.
  22. "Kcna1 gene deletion lowers the behavioral sensitivity of mice to small changes in sound location and increases asynchronous brainstem auditory evoked potentials but does not affect hearing thresholds."
    Allen P.D., Ison J.R.
    J. Neurosci. 32:2538-2543(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION.
  23. "Kv1.1-dependent control of hippocampal neuron number as revealed by mosaic analysis with double markers."
    Yang S.B., Mclemore K.D., Tasic B., Luo L., Jan Y.N., Jan L.Y.
    J. Physiol. (Lond.) 590:2645-2658(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  24. "Transcompartmental reversal of single fibre hyperexcitability in juxtaparanodal Kv1.1-deficient vagus nerve axons by activation of nodal KCNQ channels."
    Glasscock E., Qian J., Kole M.J., Noebels J.L.
    J. Physiol. (Lond.) 590:3913-3926(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY.
  25. "Neuregulin 1 regulates excitability of fast-spiking neurons through Kv1.1 and acts in epilepsy."
    Li K.X., Lu Y.M., Xu Z.H., Zhang J., Zhu J.M., Zhang J.M., Cao S.X., Chen X.J., Chen Z., Luo J.H., Duan S., Li X.M.
    Nat. Neurosci. 15:267-273(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  26. "Loss of the Kv1.1 potassium channel promotes pathologic sharp waves and high frequency oscillations in in vitro hippocampal slices."
    Simeone T.A., Simeone K.A., Samson K.K., Kim D.Y., Rho J.M.
    Neurobiol. Dis. 54:68-81(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  27. "Kv1.1 channels act as mechanical brake in the senses of touch and pain."
    Hao J., Padilla F., Dandonneau M., Lavebratt C., Lesage F., Noel J., Delmas P.
    Neuron 77:899-914(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISEASE, TISSUE SPECIFICITY.
  28. "The Kv1.1 null mouse, a model of sudden unexpected death in epilepsy (SUDEP)."
    Moore B.M., Jerry Jou C., Tatalovic M., Kaufman E.S., Kline D.D., Kunze D.L.
    Epilepsia 55:1808-1816(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION.
  29. "Ankyrin-3 is a novel binding partner of the voltage-gated potassium channel Kv1.1 implicated in renal magnesium handling."
    San-Cristobal P., Lainez S., Dimke H., de Graaf M.J., Hoenderop J.G., Bindels R.J.
    Kidney Int. 85:94-102(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ANK3, INDUCTION BY MAGNESIUM.

Entry informationi

Entry nameiKCNA1_MOUSE
AccessioniPrimary (citable) accession number: P16388
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: February 4, 2015
This is version 138 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  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.