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Search results 1 to 98 out of 98 for Kcne4

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Hits by Strain

Type Details Score
Gene
23704 | KCNE4
Type: gene
Organism: human
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Gene
100490086 | kcne4
Type: gene
Organism: frog, western clawed
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Gene
367302 | Kcne4
Type: gene
Organism: rat
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Gene
488549 | KCNE4
Type: gene
Organism: dog, domestic
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Gene
735608 | KCNE4
Type: gene
Organism: chimpanzee
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Gene
615761 | KCNE4
Type: gene
Organism: cattle
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Gene
771271 | KCNE4
Type: gene
Organism: chicken
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Gene
794240 | kcne4
Type: gene
Organism: zebrafish
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Gene
723519 | KCNE4
Type: gene
Organism: macaque, rhesus
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Protein Coding Gene
MGI:1891125 | Kcne4
Type: protein_coding_gene
Organism: mouse, laboratory
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Publication
26399785 | J:227222
First Author: Crump SM
Year: 2016
Journal: FASEB J
Title: Kcne4 deletion sex- and age-specifically impairs cardiac repolarization in mice.
Volume: 30
Issue: 1
Pages: 360-9
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Publication
19773357 | J:154629
First Author: Solé L
Year: 2009
Journal: J Cell Sci
Title: KCNE4 suppresses Kv1.3 currents by modulating trafficking, surface expression and channel gating.
Volume: 122
Issue: Pt 20
Pages: 3738-48
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Publication
27802162 | J:246816
First Author: Solé L
Year: 2016
Journal: J Cell Sci
Title: The C-terminal domain of Kv1.3 regulates functional interactions with the KCNE4 subunit.
Volume: 129
Issue: 22
Pages: 4265-4277
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Publication
29844497 | J:263713
First Author: Hu Z
Year: 2018
Journal: Sci Rep
Title: Kcne4 deletion sex-specifically predisposes to cardiac arrhythmia via testosterone-dependent impairment of RISK/SAFE pathway induction in aged mice.
Volume: 8
Issue: 1
Pages: 8258
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Publication
32370164 | J:352579
 
First Author: Solé L
Year: 2020
Journal: Cells
Title: Functional Consequences of the Variable Stoichiometry of the Kv1.3-KCNE4 Complex.
Volume: 9
Issue: 5
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Publication
10219239 | J:64949
First Author: Abbott GW
Year: 1999
Journal: Cell
Title: MiRP1 forms IKr potassium channels with HERG and is associated with cardiac arrhythmia.
Volume: 97
Issue: 2
Pages: 175-87
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Protein Coding Gene
MGP_CAROLIEiJ_G0014314 | -
Type: protein_coding_gene
Organism: Mus caroli
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Protein Coding Gene
MGP_129S1SvImJ_G0016203 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_AJ_G0016186 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_AKRJ_G0016143 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_BALBcJ_G0016141 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_C3HHeJ_G0015971 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI_C57BL6J_1891125 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_C57BL6NJ_G0016594 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_CASTEiJ_G0015556 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_CBAJ_G0015945 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_DBA2J_G0016046 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_FVBNJ_G0016049 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_LPJ_G0016118 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_NODShiLtJ_G0016069 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_NZOHlLtJ_G0016641 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_PWKPhJ_G0015342 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_WSBEiJ_G0015617 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_PahariEiJ_G0027552 | -
Type: protein_coding_gene
Organism: Mus pahari
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Protein Coding Gene
MGP_SPRETEiJ_G0015120 | -
Type: protein_coding_gene
Organism: Mus spretus
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Publication
9468318 | J:45544
First Author: Vullhorst D
Year: 1998
Journal: FEBS Lett
Title: Expression of the potassium channel KV3.4 in mouse skeletal muscle parallels fiber type maturation and depends on excitation pattern.
Volume: 421
Issue: 3
Pages: 259-62
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GXD Expression
GXD Expression
     
Probe: MGI:3707804
Assay Type: RT-PCR
Annotation Date: 2007-05-15
Strength: Present
Sex: Not Specified
Emaps: EMAPS:1733125
Stage: TS25
Assay Id: MGI:3708128
Age: embryonic day 17.5
Specimen Label: Fetus
Detected: true
Specimen Num: 1
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GXD Expression
GXD Expression
     
Probe: MGI:3707804
Assay Type: RT-PCR
Annotation Date: 2007-05-15
Strength: Present
Sex: Not Specified
Emaps: EMAPS:1733127
Stage: TS27
Assay Id: MGI:3708128
Age: postnatal day 1
Specimen Label: Neonate
Detected: true
Specimen Num: 2
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GXD Expression
GXD Expression
     
Probe: MGI:3707804
Assay Type: RT-PCR
Annotation Date: 2007-05-15
Strength: Present
Sex: Male
Emaps: EMAPS:1733128
Stage: TS28
Assay Id: MGI:3708128
Age: postnatal week 5-8
Specimen Label: Adult
Detected: true
Specimen Num: 3
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GXD Expression
GXD Expression
     
Probe: MGI:3707804
Assay Type: RT-PCR
Annotation Date: 2007-05-17
Strength: Present
Sex: Not Specified
Emaps: EMAPS:1610525
Stage: TS25
Assay Id: MGI:3709314
Age: embryonic day 17.5
Specimen Label: Fetus
Detected: true
Specimen Num: 1
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GXD Expression
GXD Expression
     
Probe: MGI:3707804
Assay Type: RT-PCR
Annotation Date: 2007-05-17
Strength: Present
Sex: Not Specified
Emaps: EMAPS:1610527
Stage: TS27
Assay Id: MGI:3709314
Age: postnatal day 1
Specimen Label: Neonate
Detected: true
Specimen Num: 2
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GXD Expression
GXD Expression
     
Probe: MGI:3707804
Assay Type: RT-PCR
Annotation Date: 2007-05-17
Strength: Present
Sex: Male
Emaps: EMAPS:1610528
Stage: TS28
Assay Id: MGI:3709314
Age: postnatal adult
Specimen Label: Adult
Detected: true
Specimen Num: 3
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Publication
11700028 | J:72903
First Author: Boettger-Tong HL
Year: 2001
Journal: Biochem Biophys Res Commun
Title: Identification and sequencing the juvenile spermatogonial depletion critical interval on mouse chromosome 1 reveals the presence of eight candidate genes.
Volume: 288
Issue: 5
Pages: 1129-35
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Publication
31907354 | J:309350
First Author: Estrada SM
Year: 2020
Journal: Cell Death Dis
Title: The orphan nuclear receptor Nr4a1 mediates perinatal neuroinflammation in a murine model of preterm labor.
Volume: 11
Issue: 1
Pages: 11
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Publication
16985003 | J:119550
First Author: Harrell MD
Year: 2007
Journal: Physiol Genomics
Title: Large-scale analysis of ion channel gene expression in the mouse heart during perinatal development.
Volume: 28
Issue: 3
Pages: 273-83
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Publication
- | J:94338
     
First Author: NIH Mouse Knockout Inventory
Year: 2004
Journal: MGI Direct Data Submission
Title: Information obtained from the NIH Mouse Knockout Inventory
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Publication
- | J:157065
     
First Author: Helmholtz Zentrum Muenchen GmbH
Year: 2010
Journal: MGI Direct Data Submission
Title: Alleles produced for the EUCOMM and EUCOMMTools projects by the Helmholtz Zentrum Muenchen GmbH (Hmgu)
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Publication
- | J:155856
       
First Author: The Gene Ontology Consortium
Year: 2014
Title: Automated transfer of experimentally-verified manual GO annotation data to mouse-rat orthologs
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Publication
- | J:72247
       
First Author: DDB, FB, MGI, GOA, ZFIN curators
Year: 2001
Title: Gene Ontology annotation through association of InterPro records with GO terms
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Publication
16141072 | J:99680
First Author: Carninci P
Year: 2005
Journal: Science
Title: The transcriptional landscape of the mammalian genome.
Volume: 309
Issue: 5740
Pages: 1559-63
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Publication
- | J:342587
       
First Author: AgBase, BHF-UCL, Parkinson's UK-UCL, dictyBase, HGNC, Roslin Institute, FlyBase and UniProtKB curators
Year: 2011
Title: Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
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Publication
- | J:60000
       
First Author: UniProt-GOA
Year: 2012
Title: Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
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Publication
- | J:342605
       
First Author: GOA curators
Year: 2016
Title: Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
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Publication
- | J:68900
     
First Author: The Jackson Laboratory Mouse Radiation Hybrid Database
Year: 2004
Journal: Database Release
Title: Mouse T31 Radiation Hybrid Data Load
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Publication
- | J:164563
       
First Author: The Gene Ontology Consortium
Year: 2010
Title: Automated transfer of experimentally-verified manual GO annotation data to mouse-human orthologs
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Publication
- | J:75000
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2002
Title: Mouse Genome Informatics Computational Sequence to Gene Associations
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Publication
- | J:157972
     
First Author: Mouse Genome Informatics Scientific Curators
Year: 2010
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Genome U74 Array Platform (A, B, C v2).
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Publication
- | J:57747
     
First Author: MGI Genome Annotation Group and UniGene Staff
Year: 2015
Journal: Database Download
Title: MGI-UniGene Interconnection Effort
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Publication
- | J:161428
       
First Author: Marc Feuermann, Huaiyu Mi, Pascale Gaudet, Dustin Ebert, Anushya Muruganujan, Paul Thomas
Year: 2010
Title: Annotation inferences using phylogenetic trees
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Publication
- | J:63103
     
First Author: Mouse Genome Database and National Center for Biotechnology Information
Year: 2000
Journal: Database Release
Title: Entrez Gene Load
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Publication
- | J:262123
     
First Author: Allen Institute for Brain Science
Year: 2004
Journal: Allen Institute
Title: Allen Brain Atlas: mouse riboprobes
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Publication
- | J:144086
     
First Author: Mouse Genome Informatics Scientific Curators
Year: 2009
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Gene 1.0 ST Array Platform
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Publication
- | J:155721
     
First Author: Mouse Genome Informatics (MGI) and The National Center for Biotechnology Information (NCBI)
Year: 2010
Journal: Database Download
Title: Consensus CDS project
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Publication
- | J:85324
     
First Author: Mouse Genome Informatics Group
Year: 2003
Journal: Database Procedure
Title: Automatic Encodes (AutoE) Reference
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Publication
- | J:53168
     
First Author: Bairoch A
Year: 1999
Journal: Database Release
Title: SWISS-PROT Annotated protein sequence database
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Publication
- | J:91388
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and Loading Genome Assembly Coordinates from Ensembl Annotations
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Publication
- | J:155221
     
First Author: Mouse Genome Informatics
Year: 2010
Journal: Database Release
Title: Protein Ontology Association Load.
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Publication
- | J:90438
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and loading genome assembly coordinates from NCBI annotations
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Publication
- | J:144087
     
First Author: Mouse Genome Informatics Scientific Curators
Year: 2009
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Genome 430 2.0 Array Platform
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Protein
Q8JZQ4
Organism: Mus musculus/domesticus
Length: 71  
Fragment?: false
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Interaction Experiment
Sole L (2016)
Description: The C-terminal domain of Kv1.3 regulates functional interactions with the KCNE4 subunit.
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Publication
12670483 | J:83146
First Author: Teng S
Year: 2003
Journal: Biochem Biophys Res Commun
Title: Novel gene hKCNE4 slows the activation of the KCNQ1 channel.
Volume: 303
Issue: 3
Pages: 808-13
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Publication
10493825 | J:57928
First Author: Piccini M
Year: 1999
Journal: Genomics
Title: KCNE1-like gene is deleted in AMME contiguous gene syndrome: identification and characterization of the human and mouse homologs.
Volume: 60
Issue: 3
Pages: 251-7
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Protein
Q9QZ26
Organism: Mus musculus/domesticus
Length: 143  
Fragment?: false
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Protein
Q9WTW3
Organism: Mus musculus/domesticus
Length: 170  
Fragment?: false
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Protein
A0A087WQK6
Organism: Mus musculus/domesticus
Length: 64  
Fragment?: false
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Protein
Q8C1K1
Organism: Mus musculus/domesticus
Length: 192  
Fragment?: false
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Publication
19219384 | -
First Author: McCrossan ZA
Year: 2009
Journal: J Membr Biol
Title: Regulation of the Kv2.1 potassium channel by MinK and MiRP1.
Volume: 228
Issue: 1
Pages: 1-14
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Publication
11207363 | -
First Author: Abbott GW
Year: 2001
Journal: Cell
Title: MiRP2 forms potassium channels in skeletal muscle with Kv3.4 and is associated with periodic paralysis.
Volume: 104
Issue: 2
Pages: 217-31
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Publication
10646604 | -
First Author: Schroeder BC
Year: 2000
Journal: Nature
Title: A constitutively open potassium channel formed by KCNQ1 and KCNE3.
Volume: 403
Issue: 6766
Pages: 196-9
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Protein Domain
IPR000369 | K_chnl_KCNE
Type: Family
Description: Two types of beta subunit (KCNE and KCNAB) are presently known to associate with voltage-gated alpha subunits (Kv, KCNQ and eag-like). However, not all combinations of alpha and beta subunits are possible. The KCNE family of K+ channel subunits are membrane glycoproteins that possess a single transmembrane (TM) domain. They share no structural relationship with the alpha subunit proteins, which possess pore forming domains. The subunits appear to have a regulatory function, modulating the kinetics and voltage dependence of the alpha subunits of voltage-dependent K+ channels. KCNE subunits are formed from short polypeptides of ~130 amino acids, and are divided into five subfamilies: KCNE1 (MinK/IsK), KCNE2 (MiRP1), KCNE3 (MiRP2), KCNE4 (MiRP3) and KCNE1L (AMMECR2). Potassium channels are the most diverse group of the ion channel family [, ]. They are important in shaping the action potential, and in neuronal excitability and plasticity []. The potassium channel family is composed of several functionally distinct isoforms, which can be broadly separated into 2 groups []: the practically non-inactivating 'delayed' group and the rapidly inactivating 'transient' group.These are all highly similar proteins, with only small amino acid changes causing the diversity of the voltage-dependent gating mechanism, channel conductance and toxin binding properties. Each type of K+channel is activated by different signals and conditions depending on their type of regulation: some open in response to depolarisation of the plasma membrane; others in response to hyperpolarisation or an increase in intracellular calcium concentration; some can be regulated by binding of a transmitter, together with intracellular kinases; while others are regulated by GTP-binding proteins or other second messengers []. In eukaryotic cells, K+channels are involved in neural signalling and generation of the cardiac rhythm, act as effectors in signal transduction pathways involving G protein-coupled receptors (GPCRs) and may have a role in target cell lysis by cytotoxic T-lymphocytes []. In prokaryotic cells, they play a role in the maintenance of ionic homeostasis [].All K+channels discovered so far possess a core of alpha subunits, each comprising either one or two copies of a highly conserved pore loop domain (P-domain). The P-domain contains the sequence (T/SxxTxGxG), which has been termed the K+selectivity sequence. In families that contain one P-domain, four subunits assemble to form a selective pathway for K+across the membrane. However, it remains unclear how the 2 P-domain subunits assemble to form a selective pore. The functional diversity of these families can arise through homo- or hetero-associations of alpha subunits or association with auxiliary cytoplasmic beta subunits. K+channel subunits containing one pore domain can be assigned into one of two superfamilies: those that possess six transmembrane (TM) domains and those that possess only two TM domains. The six TM domain superfamily can be further subdivided into conserved gene families: the voltage-gated (Kv) channels; the KCNQ channels (originally known as KvLQT channels); the EAG-like K+channels; and three types of calcium (Ca)-activated K+channels (BK, IK and SK) []. The 2TM domain family comprises inward-rectifying K+channels. In addition, there are K+channel alpha-subunits that possess two P-domains. These are usually highly regulated K+selective leak channels.
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Protein Domain
IPR005424 | KCNE1
Type: Family
Description: KCNE1 (Potassium voltage-gated channel subfamily E member 1, also known as Mink) subunits associate with KCNQ1 alpha subunits to form channels that are responsible for the IkS currents that determine the duration of the action potential in cardiac muscle []. Mutations in both of the genes encoding these subunits cause an inherited disorder that increases the risk of death from cardiac arrhythmia (long QT syndrome type 1) and Jervell and Lange-Nielsen syndrome, associated with congenital deafness [].Two types of beta subunit (KCNE and KCNAB) are presently known to associate with voltage-gated alpha subunits (Kv, KCNQ and eag-like). However, not all combinations of alpha and beta subunits are possible. The KCNE family of K+ channel subunits are membrane glycoproteins that possess a single transmembrane (TM) domain. They share no structural relationship with the alpha subunit proteins, which possess pore forming domains. The subunits appear to have a regulatory function, modulating the kinetics and voltage dependence of the alpha subunits of voltage-dependent K+ channels. KCNE subunits are formed from short polypeptides of ~130 amino acids, and are divided into five subfamilies: KCNE1 (MinK/IsK), KCNE2 (MiRP1), KCNE3 (MiRP2), KCNE4 (MiRP3) and KCNE1L (AMMECR2). Potassium channels are the most diverse group of the ion channel family [, ]. They are important in shaping the action potential, and in neuronal excitability and plasticity []. The potassium channel family is composed of several functionally distinct isoforms, which can be broadly separated into 2 groups []: the practically non-inactivating 'delayed' group and the rapidly inactivating 'transient' group.These are all highly similar proteins, with only small amino acid changes causing the diversity of the voltage-dependent gating mechanism, channel conductance and toxin binding properties. Each type of K+channel is activated by different signals and conditions depending on their type of regulation: some open in response to depolarisation of the plasma membrane; others in response to hyperpolarisation or an increase in intracellular calcium concentration; some can be regulated by binding of a transmitter, together with intracellular kinases; while others are regulated by GTP-binding proteins or other second messengers []. In eukaryotic cells, K+channels are involved in neural signalling and generation of the cardiac rhythm, act as effectors in signal transduction pathways involving G protein-coupled receptors (GPCRs) and may have a role in target cell lysis by cytotoxic T-lymphocytes []. In prokaryotic cells, they play a role in the maintenance of ionic homeostasis [].All K+channels discovered so far possess a core of alpha subunits, each comprising either one or two copies of a highly conserved pore loop domain (P-domain). The P-domain contains the sequence (T/SxxTxGxG), which has been termed the K+selectivity sequence. In families that contain one P-domain, four subunits assemble to form a selective pathway for K+across the membrane. However, it remains unclear how the 2 P-domain subunits assemble to form a selective pore. The functional diversity of these families can arise through homo- or hetero-associations of alpha subunits or association with auxiliary cytoplasmic beta subunits. K+channel subunits containing one pore domain can be assigned into one of two superfamilies: those that possess six transmembrane (TM) domains and those that possess only two TM domains. The six TM domain superfamily can be further subdivided into conserved gene families: the voltage-gated (Kv) channels; the KCNQ channels (originally known as KvLQT channels); the EAG-like K+channels; and three types of calcium (Ca)-activated K+channels (BK, IK and SK) []. The 2TM domain family comprises inward-rectifying K+channels. In addition, there are K+channel alpha-subunits that possess two P-domains. These are usually highly regulated K+selective leak channels.
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Protein Domain
IPR005425 | K_chnl_volt-dep_bsu_KCNE2
Type: Family
Description: Potassium channels are the most diverse group of the ion channel family [, ]. They are important in shaping the action potential, and in neuronal excitability and plasticity []. The potassium channel family is composed of several functionally distinct isoforms, which can be broadly separated into 2 groups []: the practically non-inactivating 'delayed' group and the rapidly inactivating 'transient' group.These are all highly similar proteins, with only small amino acid changes causing the diversity of the voltage-dependent gating mechanism, channel conductance and toxin binding properties. Each type of K+channel is activated by different signals and conditions depending on their type of regulation: some open in response to depolarisation of the plasma membrane; others in response to hyperpolarisation or an increase in intracellular calcium concentration; some can be regulated by binding of a transmitter, together with intracellular kinases; while others are regulated by GTP-binding proteins or other second messengers []. In eukaryotic cells, K+channels are involved in neural signalling and generation of the cardiac rhythm, act as effectors in signal transduction pathways involving G protein-coupled receptors (GPCRs) and may have a role in target cell lysis by cytotoxic T-lymphocytes []. In prokaryotic cells, they play a role in the maintenance of ionic homeostasis [].All K+channels discovered so far possess a core of alpha subunits, each comprising either one or two copies of a highly conserved pore loop domain (P-domain). The P-domain contains the sequence (T/SxxTxGxG), which has been termed the K+selectivity sequence. In families that contain one P-domain, four subunits assemble to form a selective pathway for K+across the membrane. However, it remains unclear how the 2 P-domain subunits assemble to form a selective pore. The functional diversity of these families can arise through homo- or hetero-associations of alpha subunits or association with auxiliary cytoplasmic beta subunits. K+channel subunits containing one pore domain can be assigned into one of two superfamilies: those that possess six transmembrane (TM) domains and those that possess only two TM domains. The six TM domain superfamily can be further subdivided into conserved gene families: the voltage-gated (Kv) channels; the KCNQ channels (originally known as KvLQT channels); the EAG-like K+channels; and three types of calcium (Ca)-activated K+channels (BK, IK and SK) []. The 2TM domain family comprises inward-rectifying K+channels. In addition, there are K+channel alpha-subunits that possess two P-domains. These are usually highly regulated K+selective leak channels.Two types of beta subunit (KCNE and KCNAB) are presently known to associate with voltage-gated alpha subunits (Kv, KCNQ and eag-like). However, not all combinations of alpha and beta subunits are possible. The KCNE family of K+ channel subunits are membrane glycoproteins that possess a single transmembrane (TM) domain. They share no structural relationship with the alpha subunit proteins, which possess pore forming domains. The subunits appear to have a regulatory function, modulating the kinetics and voltage dependence of the alpha subunits of voltage-dependent K+ channels. KCNE subunits are formed from short polypeptides of ~130 amino acids, and are divided into five subfamilies: KCNE1 (MinK/IsK), KCNE2 (MiRP1), KCNE3 (MiRP2), KCNE4 (MiRP3) and KCNE1L (AMMECR2). KCNE2 subunits associate with the eag-like HERG alpha subunits, which arethe pore-forming subunits of cardiac IKr channels. Channels formed solelyfrom HERG subunits display similar properties to native IKr channels;however, they differ in their gating and single channel conductance. Channels formed from both KCNE2 and HERG exhibit properties that are identical to those seen in native IKr channels. Three mutations in the KCNE2gene are associated with long QT syndrome and ventricular fibrillation. These mutations result in channels that open slower and close more rapidly,the net effect being a reduced K+ current [].
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Protein Domain
IPR005426 | K_chnl_volt-dep_bsu_KCNE3
Type: Family
Description: Potassium channels are the most diverse group of the ion channel family [, ]. They are important in shaping the action potential, and in neuronal excitability and plasticity []. The potassium channel family is composed of several functionally distinct isoforms, which can be broadly separated into 2 groups []: the practically non-inactivating 'delayed' group and the rapidly inactivating 'transient' group.These are all highly similar proteins, with only small amino acid changes causing the diversity of the voltage-dependent gating mechanism, channel conductance and toxin binding properties. Each type of K+channel is activated by different signals and conditions depending on their type of regulation: some open in response to depolarisation of the plasma membrane; others in response to hyperpolarisation or an increase in intracellular calcium concentration; some can be regulated by binding of a transmitter, together with intracellular kinases; while others are regulated by GTP-binding proteins or other second messengers []. In eukaryotic cells, K+channels are involved in neural signalling and generation of the cardiac rhythm, act as effectors in signal transduction pathways involving G protein-coupled receptors (GPCRs) and may have a role in target cell lysis by cytotoxic T-lymphocytes []. In prokaryotic cells, they play a role in the maintenance of ionic homeostasis [].All K+channels discovered so far possess a core of alpha subunits, each comprising either one or two copies of a highly conserved pore loop domain (P-domain). The P-domain contains the sequence (T/SxxTxGxG), which has been termed the K+selectivity sequence. In families that contain one P-domain, four subunits assemble to form a selective pathway for K+across the membrane. However, it remains unclear how the 2 P-domain subunits assemble to form a selective pore. The functional diversity of these families can arise through homo- or hetero-associations of alpha subunits or association with auxiliary cytoplasmic beta subunits. K+channel subunits containing one pore domain can be assigned into one of two superfamilies: those that possess six transmembrane (TM) domains and those that possess only two TM domains. The six TM domain superfamily can be further subdivided into conserved gene families: the voltage-gated (Kv) channels; the KCNQ channels (originally known as KvLQT channels); the EAG-like K+channels; and three types of calcium (Ca)-activated K+channels (BK, IK and SK) []. The 2TM domain family comprises inward-rectifying K+channels. In addition, there are K+channel alpha-subunits that possess two P-domains. These are usually highly regulated K+selective leak channels.Two types of beta subunit (KCNE and KCNAB) are presently known to associate with voltage-gated alpha subunits (Kv, KCNQ and eag-like). However, not all combinations of alpha and beta subunits are possible. The KCNE family of K+ channel subunits are membrane glycoproteins that possess a single transmembrane (TM) domain. They share no structural relationship with the alpha subunit proteins, which possess pore forming domains. The subunits appear to have a regulatory function, modulating the kinetics and voltage dependence of the alpha subunits of voltage-dependent K+ channels. KCNE subunits are formed from short polypeptides of ~130 amino acids, and are divided into five subfamilies: KCNE1 (MinK/IsK), KCNE2 (MiRP1), KCNE3 (MiRP2), KCNE4 (MiRP3) and KCNE1L (AMMECR2). KCNE3 is known to associate with the pore forming subunits KCNQ1, KCNQ4,HERG and Kv3.4. KCNE3 forms complexes with Kv3.4 in skeletal muscle -KCNE3 mutations have been identified in families with skeletal muscledisorders []. In the intestine, KCNE3 associates with KCNQ1 to formchannels that are stimulated by cAMP and are thought to be involved insecretory diarrhoea and cystic fibrosis [].
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Protein
Q9WTW2
Organism: Mus musculus/domesticus
Length: 103  
Fragment?: false
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Protein
P23299
Organism: Mus musculus/domesticus
Length: 129  
Fragment?: false
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Protein
Q9D808
Organism: Mus musculus/domesticus
Length: 123  
Fragment?: false
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Protein
Q545H9
Organism: Mus musculus/domesticus
Length: 103  
Fragment?: false
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Protein
Q545H6
Organism: Mus musculus/domesticus
Length: 129  
Fragment?: false
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Protein
A0A0R4J1J2
Organism: Mus musculus/domesticus
Length: 123  
Fragment?: false
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Publication
2451788 | J:9129
First Author: Tempel BL
Year: 1988
Journal: Nature
Title: Cloning of a probable potassium channel gene from mouse brain.
Volume: 332
Issue: 6167
Pages: 837-9
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Publication
1772658 | -
First Author: Perney TM
Year: 1991
Journal: Curr Opin Cell Biol
Title: The molecular biology of K+ channels.
Volume: 3
Issue: 4
Pages: 663-70
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Publication
1879548 | -
First Author: Luneau C
Year: 1991
Journal: FEBS Lett
Title: Shaw-like rat brain potassium channel cDNA's with divergent 3' ends.
Volume: 288
Issue: 1-2
Pages: 163-7
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Publication
1373731 | J:931
First Author: Attali B
Year: 1992
Journal: J Biol Chem
Title: Cloning, functional expression, and regulation of two K+ channels in human T lymphocytes.
Volume: 267
Issue: 12
Pages: 8650-7
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Publication
2448635 | -
First Author: Schwarz TL
Year: 1988
Journal: Nature
Title: Multiple potassium-channel components are produced by alternative splicing at the Shaker locus in Drosophila.
Volume: 331
Issue: 6152
Pages: 137-42
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Publication
2555158 | -
First Author: Stühmer W
Year: 1989
Journal: EMBO J
Title: Molecular basis of functional diversity of voltage-gated potassium channels in mammalian brain.
Volume: 8
Issue: 11
Pages: 3235-44
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Publication
11178249 | -
First Author: Miller C
Year: 2000
Journal: Genome Biol
Title: An overview of the potassium channel family.
Volume: 1
Issue: 4
Pages: REVIEWS0004
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Publication
15489334 | -
First Author: Gerhard DS
Year: 2004
Journal: Genome Res
Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
Volume: 14
Issue: 10B
Pages: 2121-7
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