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Protein

Potassium voltage-gated channel subfamily A member 1

Gene

Kcna1

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 kidney. Contributes to the regulation of the membrane potential and nerve signaling, and prevents neuronal hyperexcitability (PubMed:12177193, PubMed:17855588, PubMed:22206926). Forms tetrameric potassium-selective channels through which potassium ions pass in accordance with their electrochemical gradient (PubMed:23725331). The channel alternates between opened and closed conformations in response to the voltage difference across the membrane (PubMed:2539643). 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:2348860, PubMed:12177193, PubMed:10896669, 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:10896669, PubMed:12114518). 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:2348860, PubMed:8038169, PubMed:12681381, PubMed:22206926, PubMed:23725331). In contrast, a heterotetrameric channel formed by KCNA1 and KCNA4 shows rapid inactivation (PubMed:2348860). Regulates neuronal excitability in hippocampus, especially in mossy fibers and medial perforant path axons, preventing neuronal hyperexcitability. 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:12177193, PubMed:23318870). 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) release (PubMed:17869444). 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 (By similarity). Required for normal neuromuscular responses (PubMed:22206926). 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 (By similarity). Required for normal responses to auditory stimuli and precise location of sound sources, but not for sound perception (By similarity). The use of toxins that block specific channels suggest that it contributes to the regulation of the axonal release of the neurotransmitter dopamine (By similarity). Required for normal postnatal brain development and normal proliferation of neuronal precursor cells in the brain (By similarity). 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 similarity1 Publication12 Publications

Enzyme regulationi

Inhibited by 4-aminopyridine (4-AP) and by tetraethylammonium (TEA) (PubMed:2539643). Inhibited by kaliotoxin (KTX) (PubMed:23725331).3 Publications

GO - Molecular functioni

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

GO - Biological processi

  1. cell communication by electrical coupling Source: UniProtKB
  2. cellular protein localization Source: UniProtKB
  3. cellular response to magnesium ion Source: UniProtKB
  4. detection of mechanical stimulus involved in sensory perception of pain Source: UniProtKB
  5. detection of mechanical stimulus involved in sensory perception of touch Source: UniProtKB
  6. magnesium ion homeostasis Source: UniProtKB
  7. neuromuscular process Source: UniProtKB
  8. neuronal action potential Source: UniProtKB
  9. neuronal signal transduction Source: UniProtKB
  10. potassium ion transmembrane transport Source: UniProtKB
  11. protein homooligomerization Source: InterPro
  12. regulation of membrane potential Source: UniProtKB
  13. regulation of muscle contraction Source: UniProtKB
  14. 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_352543. Voltage gated Potassium channels.

Names & Taxonomyi

Protein namesi
Recommended name:
Potassium voltage-gated channel subfamily A member 1
Alternative name(s):
RBKI1 Publication
RCK12 Publications
Voltage-gated potassium channel subunit Kv1.1
Gene namesi
Name:Kcna1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Chromosome 4

Organism-specific databases

RGDi2949. Kcna1.

Subcellular locationi

Cell membrane 8 Publications; Multi-pass membrane protein Curated. Membrane 2 Publications. Cell projectionaxon 3 Publications. Cytoplasmic vesicle 2 Publications. Perikaryon 1 Publication. Endoplasmic reticulum 2 Publications. Cell projectiondendrite By similarity. Cell junction By similarity. Cell junctionsynapse By similarity. Cell junctionsynapsepresynaptic cell membrane 1 Publication
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 (PubMed:10896669). Detected at axon terminals (By similarity).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: RGD
  2. axon terminus Source: UniProtKB
  3. cell junction Source: UniProtKB
  4. cell surface Source: Ensembl
  5. cytoplasmic membrane-bounded vesicle Source: UniProtKB-SubCell
  6. cytosol Source: UniProtKB
  7. dendrite Source: BHF-UCL
  8. endoplasmic reticulum Source: UniProtKB
  9. integral component of membrane Source: GO_Central
  10. integral component of plasma membrane Source: UniProtKB
  11. juxtaparanode region of axon Source: UniProtKB
  12. neuronal cell body Source: UniProtKB
  13. paranode region of axon Source: UniProtKB
  14. perikaryon Source: UniProtKB-SubCell
  15. potassium channel complex Source: UniProtKB
  16. presynaptic membrane Source: UniProtKB
  17. synapse Source: UniProtKB
  18. 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

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi309 – 3091S → T in ADMS: Dominant negative mutation that abolishes channel activity; leads to myokymia, neuromyotonia, spontaneous epileptic seizures and premature death. 1 Publication
Mutagenesisi443 – 4431R → C: Abolishes phosphorylation by PKA; when associated with A-446.
Mutagenesisi446 – 4461S → A: Abolishes phosphorylation by PKA; when associated with C-443.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 495495Potassium voltage-gated channel subfamily A member 1PRO_0000053970Add
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 PKA1 Publication

Post-translational modificationi

Palmitoylated on Cys-243; which may be required for membrane targeting.By similarity
N-glycosylated.2 Publications
Phosphorylated on tyrosine residues. Phosphorylation increases in response to NRG1; this inhibits channel activity (By similarity). Phosphorylated by PKA (PubMed:8038169, PubMed:12681381). Phosphorylation at Ser-446 regulates channel activity by down-regulating expression at the cell membrane (By similarity).By similarity2 Publications

Keywords - PTMi

Glycoprotein, Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

PaxDbiP10499.
PRIDEiP10499.

PTM databases

PhosphoSiteiP10499.

Expressioni

Tissue specificityi

Detected in hippocampus, in the middle third of the molecular layer of the dentate gyrus and in stratum radiatum and stratum oriens (PubMed:9334400). Detected in the mossy fiber zone in the hippocampus CA3 region, at or near axon terminals (PubMed:9334400). Detected in brain cortex, at basket cell terminals (PubMed:9334400). Detected adjacent to nodes of Ranvier in juxtaparanodal zones in spinal cord nerve fibers, but also in paranodal regions in some myelinated spinal cord axons (PubMed:11086297). Detected in juxtaparanodal regions adjacent to the nodes of Ranvier in myelinated axons in cerebellar white matter (PubMed:9334400). Detected in sensory neurons (PubMed:17855588). Detected in neurons from the medial nucleus of the trapezoid body (PubMed:12177193). Detected in basolateral amygdala (PubMed:16306173). Detected in the paraventricular nucleus of the hypothalamus (PubMed:17869444). Detected in the islet of Langerhans (at protein level) (PubMed:21483673). Detected in the islet of Langerhans (PubMed:21483673).6 Publications

Gene expression databases

GenevestigatoriP10499.

Interactioni

Subunit structurei

Homotetramer and heterotetramer with other channel-forming alpha subunits, such as KCNA2, KCNA4, KCNA5, KCNA6 and KCNA7 (PubMed:10896669, PubMed:10884227). Channel activity is regulated by interaction with the beta subunits KCNAB1 and KCNAB2 (PubMed:9334400, PubMed:12114518). Identified in a complex with KCNA2 and KCNAB2 (PubMed:10896669, PubMed:11086297, PubMed:23318870, PubMed:10884227). Interacts (via C-terminus) with the PDZ domains of DLG1, DLG2 and DLG4. Interacts with LGI1 within a complex containing LGI1, KCNA4 and KCNAB1. Interacts (via cytoplasmic N-terminal domain) with KCNRG; this inhibits channel activity (By similarity). Interacts with ANK3; this inhibits channel activity (By similarity). Interacts (via N-terminus) with STX1A; this promotes channel inactivation (PubMed:12114518). Interacts (via N-terminus) with the heterodimer formed by GNB1 and GNG2; this promotes channel inactivation (PubMed:12114518). Can interact simultaneously with STX1A and the heterodimer formed by GNB1 and GNG2 (PubMed:12114518).By similarity8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
DLG4P783522EBI-631463,EBI-80389From a different organism.

Protein-protein interaction databases

BioGridi246675. 2 interactions.
IntActiP10499. 2 interactions.
MINTiMINT-138588.
STRINGi10116.ENSRNOP00000026731.

Structurei

Secondary structure

1
495
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi38 – 436Combined sources
Beta strandi46 – 516Combined sources
Helixi52 – 565Combined sources
Turni62 – 643Combined sources
Helixi66 – 694Combined sources
Helixi70 – 723Combined sources
Turni75 – 784Combined sources
Beta strandi79 – 824Combined sources
Helixi86 – 9712Combined sources
Helixi110 – 11910Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EXBX-ray2.10E27-129[»]
ProteinModelPortaliP10499.
SMRiP10499. Positions 36-419.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP10499.

Family & Domainsi

Region

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

Motif

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

Domaini

The cytoplasmic N-terminus is important for tetramerization and for interaction with the beta subunits that promote rapid channel closure.1 Publication
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.
InParanoidiP10499.
KOiK04874.
OMAiIHRIDNT.
OrthoDBiEOG7M0NRD.
PhylomeDBiP10499.
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.

P10499-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTVMSGENAD EASAAPGHPQ 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 ANIRTGNCTA TDQNCVNKSK LLTDV
Length:495
Mass (Da):56,379
Last modified:March 31, 1990 - v1
Checksum:i29804463133F5D31
GO

RNA editingi

Edited at position 400.1 Publication
Partially edited. RNA editing is at an average of 50% in the whole brain.

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
X12589 mRNA. Translation: CAA31102.1.
M26161 mRNA. Translation: AAA41982.1.
PIRiB39113.
RefSeqiNP_775118.1. NM_173095.3.
UniGeneiRn.9769.

Genome annotation databases

EnsembliENSRNOT00000026731; ENSRNOP00000026731; ENSRNOG00000019750.
GeneIDi24520.
KEGGirno:24520.
UCSCiRGD:2949. rat.

Keywords - Coding sequence diversityi

RNA editing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X12589 mRNA. Translation: CAA31102.1.
M26161 mRNA. Translation: AAA41982.1.
PIRiB39113.
RefSeqiNP_775118.1. NM_173095.3.
UniGeneiRn.9769.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EXBX-ray2.10E27-129[»]
ProteinModelPortaliP10499.
SMRiP10499. Positions 36-419.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi246675. 2 interactions.
IntActiP10499. 2 interactions.
MINTiMINT-138588.
STRINGi10116.ENSRNOP00000026731.

Chemistry

ChEMBLiCHEMBL5190.
GuidetoPHARMACOLOGYi538.

PTM databases

PhosphoSiteiP10499.

Proteomic databases

PaxDbiP10499.
PRIDEiP10499.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000026731; ENSRNOP00000026731; ENSRNOG00000019750.
GeneIDi24520.
KEGGirno:24520.
UCSCiRGD:2949. rat.

Organism-specific databases

CTDi3736.
RGDi2949. Kcna1.

Phylogenomic databases

eggNOGiCOG1226.
GeneTreeiENSGT00760000118846.
HOGENOMiHOG000231015.
HOVERGENiHBG052230.
InParanoidiP10499.
KOiK04874.
OMAiIHRIDNT.
OrthoDBiEOG7M0NRD.
PhylomeDBiP10499.
TreeFamiTF313103.

Enzyme and pathway databases

ReactomeiREACT_352543. Voltage gated Potassium channels.

Miscellaneous databases

EvolutionaryTraceiP10499.
NextBioi603561.
PROiP10499.

Gene expression databases

GenevestigatoriP10499.

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

  1. "Structure of the voltage-dependent potassium channel is highly conserved from Drosophila to vertebrate central nervous systems."
    Baumann A., Grupe A., Ackermann A., Pongs O.
    EMBO J. 7:2457-2463(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  2. "Expression of a cloned rat brain potassium channel in Xenopus oocytes."
    Christie M.J., Adelman J.P., Douglass J., North R.A.
    Science 244:221-224(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, ENZYME REGULATION.
    Tissue: Brain.
  3. "Heteromultimeric channels formed by rat brain potassium-channel proteins."
    Ruppersberg J.P., Schroeter K.H., Sakmann B., Stocker M., Sewing S., Pongs O.
    Nature 345:535-537(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, ENZYME REGULATION.
  4. "Phosphorylation by protein kinase A of RCK1 K+ channels expressed in Xenopus oocytes."
    Ivanina T., Perets T., Thornhill W.B., Levin G., Dascal N., Lotan I.
    Biochemistry 33:8786-8792(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, GLYCOSYLATION, PHOSPHORYLATION AT SER-446, MUTAGENESIS OF ARG-443 AND SER-446.
  5. "Nervous system targets of RNA editing identified by comparative genomics."
    Hoopengardner B., Bhalla T., Staber C., Reenan R.
    Science 301:832-836(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: RNA EDITING OF POSITION 400.
  6. "Association and colocalization of the Kvbeta1 and Kvbeta2 beta-subunits with Kv1 alpha-subunits in mammalian brain K+ channel complexes."
    Rhodes K.J., Strassle B.W., Monaghan M.M., Bekele-Arcuri Z., Matos M.F., Trimmer J.S.
    J. Neurosci. 17:8246-8258(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH KCNAB1 AND KCNAB2, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  7. "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: SUBUNIT, INTERACTION WITH KCNA2 AND KCNA4, SUBCELLULAR LOCATION, GLYCOSYLATION.
  8. "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: INTERACTION WITH KCNA2 AND KCNA4, SUBUNIT, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
  9. "Modulation of a brain voltage-gated K+ channel by syntaxin 1A requires the physical interaction of Gbetagamma with the channel."
    Michaelevski I., Chikvashvili D., Tsuk S., Fili O., Lohse M.J., Singer-Lahat D., Lotan I.
    J. Biol. Chem. 277:34909-34917(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH STX1A; GNB1 AND GNG2, FUNCTION, SUBCELLULAR LOCATION.
  10. "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, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  11. "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.
  12. Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION.
  13. "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.
  14. "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, TISSUE SPECIFICITY.
  15. "The epilepsy-linked Lgi1 protein assembles into presynaptic Kv1 channels and inhibits inactivation by Kvbeta1."
    Schulte U., Thumfart J.-O., Kloecker N., Sailer C.A., Bildl W., Biniossek M., Dehn D., Deller T., Eble S., Abbass K., Wangler T., Knaus H.-G., Fakler B.
    Neuron 49:697-706(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH LGI1; KCNA4 AND KCNAB1.
  16. "Manipulation of the potassium channel Kv1.1 and its effect on neuronal excitability in rat sensory neurons."
    Chi X.X., Nicol G.D.
    J. Neurophysiol. 98:2683-2692(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  17. "Ionic channel function in action potential generation: current perspective."
    Baranauskas G.
    Mol. Neurobiol. 35:129-150(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  18. "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, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  19. Cited for: FUNCTION, SUBCELLULAR LOCATION, ENZYME REGULATION.
  20. "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(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  21. "Kcna1-mutant rats dominantly display myokymia, neuromyotonia and spontaneous epileptic seizures."
    Ishida S., Sakamoto Y., Nishio T., Baulac S., Kuwamura M., Ohno Y., Takizawa A., Kaneko S., Serikawa T., Mashimo T.
    Brain Res. 1435:154-166(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF SER-309, SUBCELLULAR LOCATION, MISCELLANEOUS.
  22. "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, ENZYME REGULATION.
  23. "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 KCNA2 AND KCNAB2.
  24. "Structure of the cytoplasmic beta subunit-T1 assembly of voltage-dependent K+ channels."
    Gulbis J.M., Zhou M., Mann S., MacKinnon R.
    Science 289:123-127(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 29-128, INTERACTION WITH KCNAB2, TETRAMERIZATION, SUBUNIT, DOMAIN.

Entry informationi

Entry nameiKCNA1_RAT
AccessioniPrimary (citable) accession number: P10499
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 31, 1990
Last sequence update: March 31, 1990
Last modified: March 31, 2015
This is version 143 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

A missense mutation at Ser-309 is the cause of the autosomal dominant myokymia and seizures (ADMS) phenotype. Homozygous and heterozygous rats are born at the expected Mendelian rate. After 6 weeks, heterozygous rats begin to display muscle twitching, startle responses and spontaneous convulsive seizures; over 80% of the animals are dead after 30 weeks. After 16 weeks, they display lower body weight compared to wild-type. The rats exhibit severe periodic seizures with characteristic alterations in their cortical and hippocampal electroencephalogram, similar to rodent models of temporal lobe epilepsy. Homozygous rats display impaired development starting 14 days after birth, with reduced body weight, tremors, motor incoordination, spontaneous convulsive seizures; none survive past 18 days after birth.1 Publication
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.