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0KCNH5_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameKCNH5
DescriptionPotassium voltage-gated channel subfamily h member 5 (voltage-gated potassium channel subunit kv10.2) (ether-a-go-go potassium channel 2) (heag2).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GON/A
Domain Architecture (Details)
InterPro domains assigned to SynO:
Potassium channels are the most diverse group of the ion channel family. They are important in shaping the action potential.nd in neuronal excitability and plasticity . The potassium channel family iscomposed of several functionally distinct isoforms.hich can be broadlyseparated into 2 groups : the practically non-inactivating delayed group and the rapidly inactivating transient group.These are all highly similar proteins.ith only small amino acidchanges causing the diversity of the voltage-dependent gating mechanism.hannel 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.ogether with intracellular kinases; and others are regulated by GTP-binding proteins orother second messengers . In eukaryotic cells.+ channelsare involved in neural signalling and generation of the cardiac rhythm.ct 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.hey play a role in themaintenance of ionic homeostasis . All K+ channels discovered so far possess a core of alpha subunits.ach comprising either one or two copies of a highly conserved pore loop domain (P-domain). The P-domain contains the sequence (T/SxxTxGxG).hich hasbeen termed the K+ selectivity sequence.In families that contain one P-domain.our subunits assemble to form a selective pathway for K+ across the membrane.However.t 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.K and SK). The 2TM domain family comprises inward-rectifying K+ channels. In addition.here are K+ channel alpha-subunits that possess two P-domains. These are usually highly regulated K+ selective leak channels.The first EAG K+ channel was identified in Drosophila melanogaster.ollowing a screen for mutations giving rise to behavioural abnormalities. Disruption of the Eag gene caused an ether-induced.eg-shaking behaviour. Subsequent studies have revealed a conserved multi-gene family of EAG-like K+ channels.hich are present in human and many other species. Based on the varying functional properties of the channels.he family has been divided into 3 subfamilies: EAG.LK and ERG. Interestingly.aenorhabditis elegans appears to lack the ELK type .
  IPR003938:EAG/ELK/ERG potassium channel
InterPro domains unassigned to SynO:
This group of proteins is found in sodium.otassium.nd calcium ion channels proteins. The proteins have 6 transmembrane helices in which the last two helices flank a loop which determines ion selectivity. In some Na channels proteins the domain is repeated four times.hereas in others (e.g. K channels) the protein forms a tetramer in the membrane. A bacterial structure of the protein is known for the last two helices but is not included in the Pfam family due to it lacking the first four helices.
  IPR005821:Ion transport
Proteins that bind cyclic nucleotides (cAMP or cGMP) share a structural domain of about 120 residues . The best studied of these proteins is the prokaryotic catabolite gene activator (alsoknown as the cAMP receptor protein) (gene crp) where such a domain is known to be composed of three alpha-helices anda distinctive eight-stranded.ntiparallel beta-barrel structure. There are six invariant amino acids in this domain.hree of which are glycine residues that are thought to be essential for maintenance of the structural integrity ofthe beta-barrel. cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) contain two tandem copies of the cyclicnucleotide-binding domain. The cAPKs are composed of two different subunits. catalytic chain and a regulatory chain.hich contains both copies of the domain. The cGPKs are single chain enzymes that include the two copies of the domainin their N-terminal section. Vertebrate cyclic nucleotide-gated ion-channels also contain this domain. Two suchcations channels have been fully characterized.ne is found in rod cells where it plays a role in visual signaltransduction.
  IPR000595:Cyclic nucleotide-binding
PAC motifs occur C-terminal to a subset of all known PAS motifs (see ). It is proposed to contribute to the PAS domain fold .
  IPR001610:PAC motif
PAS domains are involved in many signalling proteins where theyare used as a signal sensor domain. PAS domains appear in archaea.acteria and eukaryotes. Several PAS-domain proteins are known todetect their signal by way of an associated cofactor. Haeme.lavin.nd a 4-hydroxycinnamyl chromophore are used in differentproteins. The PAS domain was named after three proteins that itoccurs in: Per- period circadian proteinArnt- Ah receptor nuclear translocator proteinSim- single-minded protein.PAS domains are often associated withPAC domains . It appears that these domains are directly linked.nd that together they form the conserved 3D PAS fold. The division between the PAS and PAC domains is caused by major differences in sequences in the region connecting these two motifs . In human PAS kinase.his region has been shown to be very flexible.nd adopts different conformations depending on the bound ligand .Probably the most surprising identification of a PAS domain was that inEAG-like K+-channels .
  IPR013767:PAS fold
Potassium channels are the most diverse group of the ion channel family. They are important in shaping the action potential.nd in neuronal excitability and plasticity . The potassium channel family iscomposed of several functionally distinct isoforms.hich can be broadlyseparated into 2 groups : the practically non-inactivating delayed group and the rapidly inactivating transient group.These are all highly similar proteins.ith only small amino acidchanges causing the diversity of the voltage-dependent gating mechanism.hannel 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.ogether with intracellular kinases; and others are regulated by GTP-binding proteins orother second messengers . In eukaryotic cells.+ channelsare involved in neural signalling and generation of the cardiac rhythm.ct 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.hey play a role in themaintenance of ionic homeostasis . All K+ channels discovered so far possess a core of alpha subunits.ach comprising either one or two copies of a highly conserved pore loop domain (P-domain). The P-domain contains the sequence (T/SxxTxGxG).hich hasbeen termed the K+ selectivity sequence.In families that contain one P-domain.our subunits assemble to form a selective pathway for K+ across the membrane.However.t 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.K and SK). The 2TM domain family comprises inward-rectifying K+ channels. In addition.here are K+ channel alpha-subunits that possess two P-domains. These are usually highly regulated K+ selective leak channels. The first EAG K+ channel was identified in Drosophila melanogaster.ollowing a screen for mutations giving rise to behavioural abnormalities. Disruption of the Eag gene caused an ether-induced.eg-shaking behaviour. Subsequent studies have revealed a conserved multi-gene family of EAG-like K+ channels.hich are present in human and many other species. Based on the varying functional properties of the channels.he family has been divided into 3 subfamilies: EAG.LK and ERG. Interestingly.aenorhabditis elegans appears to lack the ELK type .The EAG subfamily has been expressed in heterologous systems to reveal their biophysical and pharmacological functions and to determine their currents in native tissues. All mammalian EAG subfamily K+ channels that have been identified have properties typical of delayed rectifiers.ith no measurable inactivation . Only the Drosophila melanogaster Eag channel exhibits partial inactivation.
  IPR003949:EAG potassium channel
PAS domains are involved in many signalling proteins where theyare used as a signal sensor domain. PAS domains appear in archaea.acteria and eukaryotes. Several PAS-domain proteins are known todetect their signal by way of an associated cofactor. Haeme.lavin.nd a 4-hydroxycinnamyl chromophore are used in differentproteins. The PAS domain was named after three proteins that itoccurs in: Per- period circadian proteinArnt- Ah receptor nuclear translocator proteinSim- single-minded protein.PAS domains are often associated withPAC domains . It appears that these domains are directly linked.nd that together they form the conserved 3D PAS fold. The division between the PAS and PAC domains is caused by major differences in sequences in the region connecting these two motifs . In human PAS kinase.his region has been shown to be very flexible.nd adopts different conformations depending on the bound ligand .Probably the most surprising identification of a PAS domain was that inEAG-like K+-channels .
  IPR000014:PAS
IPR005821:Ion_trans 
Evalue:-30.3979396820068 
Location:249-467IPR000595:cNMP_binding 
Evalue:-15.2596368789673 
Location:568-655IPR001610:PAC 
Evalue:-6.18045606445813 
Location:92-134IPR003949:EAGCHANNEL 
Evalue:0 
Location:186-203IPR003949:EAGCHANNEL 
Evalue:0 
Location:671-685IPR003949:EAGCHANNEL 
Evalue:0 
Location:521-533IPR003949:EAGCHANNEL 
Evalue:0 
Location:148-160IPR003949:EAGCHANNEL 
Evalue:0 
Location:703-714IPR003938:EAGCHANLFMLY 
Evalue:0 
Location:209-218IPR003949:EAGCHANNEL 
Evalue:0 
Location:17-24IPR003938:EAGCHANLFMLY 
Evalue:0 
Location:227-234IPR003938:EAGCHANLFMLY 
Evalue:0 
Location:513-520IPR000595:CNMP_BINDING_2 
Evalue:0 
Location:0-0
SequencesProtein: KCNH5_HUMAN (988 aa)
mRNA: NM_139318
Local Annotation
Synapse Ontology
A process that increases long-term neuronal synaptic plasticity, the ability of neuronal synapses to change long-term as circumstances require. Long-term neuronal synaptic plasticity generally involves increase or decrease in actual synapse numbers.
sdb:0039 positive regulation of long-term neuronal synaptic plasticity  (Evidence:keywords,domains)
this kind of receptor usually locates at the postsynaptic plasma membranous region.
sdb:0109 ionotropic receptor  (Evidence:keywords,domains)
?
sdb:0219 GPCR mediated signaling  (Evidence:keywords,domains)
LTP that is not dependent on the function of NMDA receptor.
sdb:0255 NMDA Receptor-independent LTP  (Evidence:keywords,domains)
K channel plays an important role in the course of action potential
sdb:0286 K channel  (Evidence:keywords,domains)
all kinds of ion channels that play their roles in the synaptic activity.
sdb:0308 ion channels and receptors  (Evidence:keywords,domains)
KO assignmentK04908
  Level 3 annotation:
    potassium voltage-gated channel, Eag-related subfamily H, member 5
  Level 2 annotation:
    Ion channels
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 410 residues, 62243699-62244926Exon2: 67 residues, 62316198-62316395Exon3: 86 residues, 62338799-62339052Exon4: 68 residues, 62386123-62386323Exon5: 144 residues, 62486603-62487030Exon6: 133 residues, 62517342-62517735Exon7: 40 residues, 62523542-62523658Exon8: 45 residues, 62537801-62537930Exon9: 37 residues, 62542836-62542943Exon10: 43 residues, 62553301-62553425Exon11: 43 residues, 62581584-62581708Exon12: 2 residues, -Jump to KCNH5_HUMANExon1: 410 residues, 62243699-62244926Exon2: 86 residues, 62338799-62339052Exon3: 68 residues, 62386123-62386323Exon4: 144 residues, 62486603-62487030Exon5: 133 residues, 62517342-62517735Exon6: 40 residues, 62523542-62523658Exon7: 45 residues, 62537801-62537930Exon8: 37 residues, 62542836-62542943Exon9: 43 residues, 62553301-62553425Exon10: 43 residues, 62581584-62581708Exon11: 2 residues, -Jump to Q86XI1_HUMANExon1: 160 residues, 62248710-62249187Exon2: 67 residues, 62316198-62316395Exon3: 86 residues, 62338799-62339052Exon4: 68 residues, 62386123-62386323Exon5: 144 residues, 62486603-62487030Exon6: 133 residues, 62517342-62517735Exon7: 40 residues, 62523542-62523658Exon8: 45 residues, 62537801-62537930Exon9: 37 residues, 62542836-62542943Exon10: 43 residues, 62553301-62553425Exon11: 24 residues, 62638270-62638337Exon12: 2 residues, -Jump to Q86XI1_HUMANExon1: 248 residues, 62486288-62487030Exon2: 133 residues, 62517342-62517735Exon3: 40 residues, 62523542-62523658Exon4: 45 residues, 62537801-62537930Exon5: 37 residues, 62542836-62542943Exon6: 43 residues, 62553301-62553425Exon7: 83 residues, 62638270-62638513Exon8: 2 residues, -Jump to Q86XI1_HUMAN  
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