Target Information

General Information of This Target
Target ID
BTDT00130
Target Name
Calcium-activated potassium channel subunit alpha-1 (Kcnma1)
Target Bioclass
Transporter and channel
Uniprot ID
Q08460
3D Structure
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2D Sequence
3D Structure
Source
Predict by Alphafold2
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Alphafold Parameters: msa_mode: mmseqs2_uniref_env model_type: auto num_recycles: auto
Gene Name
Kcnma1
Gene ID
16531
Synonym
Kcnma; BK channel; BKCA alpha; Calcium-activated potassium channel, subfamily M subunit alpha-1; K(VCA)alpha; KCa1.1; Maxi K channel; Slo-alpha; Slo1; Slowpoke homolog
Sequence
MANGGGGGGGSSGGGGGGGGGSGLRMSSNIHANNLSLDASSSSSSSSSSSSSSSSSSSSS
VHEPKMDALIIPVTMEVPCDSRGQRMWWAFLASSMVTFFGGLFIILLWRTLKYLWTVCCH
CGGKTKEAQKINNGSSQADGTLKPVDEKEEVVAAEVGWMTSVKDWAGVMISAQTLTGRVL
VVLVFALSIGALVIYFIDSSNPIESCQNFYKDFTLQIDMAFNVFFLLYFGLRFIAANDKL
WFWLEVNSVVDFFTVPPVFVSVYLNRSWLGLRFLRALRLIQFSEILQFLNILKTSNSIKL
VNLLSIFISTWLTAAGFIHLVENSGDPWENFQNNQALTYWECVYLLMVTMSTVGYGDVYA
KTTLGRLFMVFFILGGLAMFASYVPEIIELIGNRKKYGGSYSAVSGRKHIVVCGHITLES
VSNFLKDFLHKDRDDVNVEIVFLHNISPNLELEALFKRHFTQVEFYQGSVLNPHDLARVK
IESADACLILANKYCADPDAEDASNIMRVISIKNYHPKIRIITQMLQYHNKAHLLNIPSW
NWKEGDDAICLAELKLGFIAQSCLAQGLSTMLANLFSMRSFIKIEEDTWQKYYLEGVSNE
MYTEYLSSAFVGLSFPTVCELCFVKLKLLMIAIEYKSANRESRSRKRILINPGNHLKIQE
GTLGFFIASDAKEVKRAFFYCKACHDDVTDPKRIKKCGCRRLEDEQPPTLSPKKKQRNGG
MRNSPNTSPKLMRHDPLLIPGNDQIDNMDSNVKKYDSTGMFHWCAPKEIEKVILTRSEAA
MTVLSGHVVVCIFGDVSSALIGLRNLVMPLRASNFHYHELKHIVFVGSIEYLKREWETLH
NFPKVSILPGTPLSRADLRAVNINLCDMCVILSANQNNIDDTSLQDKECILASLNIKSMQ
FDDSIGVLQANSQGFTPPGMDRSSPDNSPVHGMLRQPSITTGVNIPIITELAKPGKLPLV
SVNQEKNSGTHILMITELVNDTNVQFLDQDDDDDPDTELYLTQPFACGTAFAVSVLDSLM
SATYFNDNILTLIRTLVTGGATPELEALIAEENALRGGYSTPQTLANRDRCRVAQLALLD
GPFADLGDGGCYGDLFCKALKTYNMLCFGIYRLRDAHLSTPSQCTKRYVITNPPYEFELV
PTDLIFCLMQFDHNAGQSRASLSHSSHSSQSSSKKSSSVHSIPSTANRPNRPKSRESRDK
QNRKEMVYR

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Family
the potassium channel family
Function
Potassium channel activated by both membrane depolarization or increase in cytosolic Ca(2+) that mediates export of K(+). It is also activated by the concentration of cytosolic Mg(2+). Its activation dampens the excitatory events that elevate the cytosolic Ca(2+) concentration and/or depolarize the cell membrane. It therefore contributes to repolarization of the membrane potential. Plays a key role in controlling excitability in a number of systems, such as regulation of the contraction of smooth muscle, the tuning of hair cells in the cochlea, regulation of transmitter release, and innate immunity. In smooth muscles, its activation by high level of Ca(2+), caused by ryanodine receptors in the sarcoplasmic reticulum, regulates the membrane potential. In cochlea cells, its number and kinetic properties partly determine the characteristic frequency of each hair cell and thereby helps to establish a tonotopic map. Kinetics of KCNMA1 channels are determined by alternative splicing, phosphorylation status and its combination with modulating beta subunits. Highly sensitive to both iberiotoxin (IbTx) and charybdotoxin (CTX).

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Taxonomy ID
10090
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Kingdom: Metazoa
Phylum: Chordata
Class: Mammalia
Order: Rodentia
Family: Muridae
Genus: Mus
Species: Mus musculus
Toxin Information Related to This Target
                           Toxin Name Activity Data Type Activity Data Reference
 Toxin Info    Potassium channel toxin alpha-KTx 1.1 Dissociation constant
3.5 nM
 [1]
 Toxin Info    Potassium channel toxin alpha-KTx 3.1 Dissociation constant
1.56 μM
 [1]
 Toxin Info    Neurotoxin HsTX1 (R14A) Inhibition rate . [2]
 Toxin Info    Kappa-scoloptoxin(03)-Ssd1a Inhibition rate . [3], [4]
 Toxin Info    Kunitz-type conkunitzin-S1 Inhibition rate . [5], [6], [7]
 Toxin Info    Potassium channel toxin alpha-KTx 4.8 Inhibition rate . [8]
 Toxin Info    Toxin KTx8 Inhibition rate . [9]
 Toxin Info    Potassium channel toxin alpha-KTx 32.1 Inhibition rate . [10]
 Toxin Info    Kunitz-type serine protease inhibitor Hg1 Inhibition rate . [11]
 Toxin Info    Potassium channel toxin kappa-KTx 2.8 Inhibition rate
15 %
 [12]
 Toxin Info    Cysteine-rich venom protein natrin-1 IC50
34.4 nM
 [13- 18]
 Toxin Info    Lambda-hexatoxin-Hv1c IC50
9.776 μM
 [19]
References
Ref 1 A designer ligand specific for Kv1.3 channels from a scorpion neurotoxin-based library. Proc Natl Acad Sci U S A. 2009 Dec 29;106(52):22211-6. doi: 10.1073/pnas.0910123106. Epub 2009 Dec 10.
Ref 2 A Fluorescent Peptide Toxin for Selective Visualization of the Voltage-Gated Potassium Channel K(V)1.3. Bioconjug Chem. 2022 Nov 16;33(11):2197-2212. doi: 10.1021/acs.bioconjchem.2c00436. Epub 2022 Nov 4.
Ref 3 Venomic and transcriptomic analysis of centipede Scolopendra subspinipes dehaani. J Proteome Res. 2012 Dec 7;11(12):6197-212. doi: 10.1021/pr300881d. Epub 2012 Nov 29.
Ref 4 A distinct three-helix centipede toxin SSD609 inhibits I(ks) channels by interacting with the KCNE1 auxiliary subunit. Sci Rep. 2015 Aug 26;5:13399. doi: 10.1038/srep13399.
Ref 5 Production of recombinant Conkunitzin-S1 in Escherichia coli. Protein Expr Purif. 2006 Jun;47(2):640-4. doi: 10.1016/j.pep.2006.01.019. Epub 2006 Feb 20.
Ref 6 Conkunitzin-S1 is the first member of a new Kunitz-type neurotoxin family. Structural and functional characterization. J Biol Chem. 2005 Jun 24;280(25):23766-70. doi: 10.1074/jbc.C500064200. Epub 2005 Apr 15.
Ref 7 Structure of conkunitzin-S1, a neurotoxin and Kunitz-fold disulfide variant from cone snail. Acta Crystallogr D Biol Crystallogr. 2006 Sep;62(Pt 9):980-90. doi: 10.1107/S0907444906021123. Epub 2006 Aug 19.
Ref 8 Characterization and Chemical Synthesis of Cm39 (-KTx 4.8): A Scorpion Toxin That Inhibits Voltage-Gated K(+) Channel K(V)1.2 and Small- and Intermediate-Conductance Ca(2+)-Activated K(+) Channels K(Ca)2.2 and K(Ca)3.1. Toxins (Basel). 2023 Jan 5;15(1):41. doi: 10.3390/toxins15010041.
Ref 9 Molecular cloning and electrophysiological studies on the first K(+) channel toxin (LmKTx8) derived from scorpion Lychas mucronatus. Peptides. 2007 Dec;28(12):2306-12. doi: 10.1016/j.peptides.2007.10.009. Epub 2007 Oct 22.
Ref 10 Cm28, a scorpion toxin having a unique primary structure, inhibits KV1.2 and KV1.3 with high affinity. J Gen Physiol. 2022 Aug 1;154(8):e202213146. doi: 10.1085/jgp.202213146. Epub 2022 Jun 14.
Ref 11 Hg1, novel peptide inhibitor specific for Kv1.3 channels from first scorpion Kunitz-type potassium channel toxin family. J Biol Chem. 2012 Apr 20;287(17):13813-21. doi: 10.1074/jbc.M112.343996. Epub 2012 Feb 21.
Ref 12 Structural and functional diversity of acidic scorpion potassium channel toxins. PLoS One. 2012;7(4):e35154. doi: 10.1371/journal.pone.0035154. Epub 2012 Apr 12.
Ref 13 Purification and cloning of cysteine-rich proteins from Trimeresurus jerdonii and Naja atra venoms. Toxicon. 2003 Oct;42(5):539-47. doi: 10.1016/s0041-0101(03)00234-4.
Ref 14 Purification and characterization of Taiwan cobra venom proteins with weak toxicity. Toxicon. 2005 Jan;45(1):21-5. doi: 10.1016/j.toxicon.2004.09.002.
Ref 15 Structural and functional analysis of natrin, a venom protein that targets various ion channels. Biochem Biophys Res Commun. 2006 Dec 15;351(2):443-8. doi: 10.1016/j.bbrc.2006.10.067. Epub 2006 Oct 20.
Ref 16 Structural and functional characterization of ryanodine receptor-natrin toxin interaction. Biophys J. 2008 Nov 1;95(9):4289-99. doi: 10.1529/biophysj.108.137224. Epub 2008 Jul 25.
Ref 17 Purification, crystallization and preliminary X-ray crystallographic analysis of a cysteine-rich secretory protein (CRISP) from Naja atra venom. Acta Crystallogr D Biol Crystallogr. 2004 Oct;60(Pt 10):1912-5. doi: 10.1107/S0907444904019766. Epub 2004 Sep 23.
Ref 18 Blocking effect and crystal structure of natrin toxin, a cysteine-rich secretory protein from Naja atra venom that targets the BKCa channel. Biochemistry. 2005 Aug 2;44(30):10145-52. doi: 10.1021/bi050614m.
Ref 19 The Janus-faced atracotoxins are specific blockers of invertebrate K(Ca) channels. FEBS J. 2008 Aug;275(16):4045-59. doi: 10.1111/j.1742-4658.2008.06545.x. Epub 2008 Jul 9.
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