Target Information

General Information of This Target
Target ID
BTDT00153
Target Name
Calcium-activated potassium channel subunit alpha-1 (Kcnma1)
Target Bioclass
Transporter and channel
Uniprot ID
Q62976
3D Structure
Download
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
83731
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
MANGGGGGGGGSSGSSGGGGGGGGGETALRMSSNIHANHLSLDASSSSSSSSSSSSSSSS
SVHEPKMDALIIPVTMEVPCDSRGQRMWWAFLASSMVTFFGGLFIILLWRTLKYLWTVCC
HCGGKTKEAQKINNGSSQADGTLKPVDEKEEVVAAEVGWMTSVKDWAGVMISAQTLTGRV
LVVLVFALSIGALVIYFIDSSNPIESCQNFYKDFTLQIDMAFNVFFLLYFGLRFIAANDK
LWFWLEVNSVVDFFTVPPVFVSVYLNRSWLGLRFLRALRLIQFSEILQFLNILKTSNSIK
LVNLLSIFISTWLTAAGFIHLVENSGDPWENFQNNQALTYWECVYLLMVTMSTVGYGDVY
AKTTLGRLFMVFFILGGLAMFASYVPEIIELIGNRKKYGGSYSAVSGRKHIVVCGHITLE
SVSNFLKDFLHKDRDDVNVEIVFLHNISPNLELEALFKRHFTQVEFYQGSVLNPHDLARV
KIESADACLILANKYCADPDAEDASNIMRVISIKNYHPKIRIITQMLQYHNKAHLLNIPS
WNWKEGDDAICLAELKLGFIAQSCLAQGLSTMLANLFSMRSFIKIEEDTWQKYYLEGVSN
EMYTEYLSSAFVGLSFPTVCELCFVKLKLLMIAIEYKSANRESRSRKRILINPGNHLKIQ
EGTLGFFIASDAKEVKRAFFYCKACHDDVTDPKRIKKCGCRRLEDEQPPTLSPKKKQRNG
GMRNSPNTSPKLMRHDPLLIPGNDQIDNMDSNVKKYDSTGMFHWCAPKEIEKVILTRSEA
AMTVLSGHVVVCIFGDVSSALIGLRNLVMPLRASNFHYHELKHIVFVGSIEYLKREWETL
HNFPKVSILPGTPLSRADLRAVNINLCDMCVILSANQNNIDDTSLQDKECILASLNIKSM
QFDDSIGVLQANSQGFTPPGMDRSSPDNSPVHGMLRQPSITTGVNIPIITELAKPGKLPL
VSVNQEKNSGTHILMITELVNDTNVQFLDQDDDDDPDTELYLTQPFACGTAFAVSVLDSL
MSATYFNDNILTLIRTLVTGGATPELEALIAEENALRGGYSTPQTLANRDRCRVAQLALL
DGPFADLGDGGCYGDLFCKALKTYNMLCFGIYRLRDAHLSTPSQCTKRYVITNPPYEFEL
VPTDLIFCLMQFDHNAGQSRASLSHSSHSSQSSSKKSSSVHSIPSTANRPNRPKSRESRD
KQKKEMVYR

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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
10116
TCDB ID
1.A.1.3.2
        Click to Show/Hide the Complete Species Lineage
Kingdom: Metazoa
Phylum: Chordata
Class: Mammalia
Order: Rodentia
Family: Muridae
Genus: Rattus
Species: Rattus norvegicus
Toxin Information Related to This Target
                           Toxin Name Activity Data Type Activity Data Reference
 Toxin Info    ChTX (T9V) Dissociation constant
2 nM
 [1]
 Toxin Info    ChTX (T8S) Dissociation constant
3.1 nM
 [1]
 Toxin Info    ChTX (T8S,T9V) Dissociation constant
4.8 nM
 [1]
 Toxin Info    ChTX (S6D) Dissociation constant
5.3 nM
 [1]
 Toxin Info    ChTX (N4D) Dissociation constant
7.4 nM
 [1]
 Toxin Info    ChTX (N22K) Dissociation constant
11 nM
 [1]
 Toxin Info    ChTX (Q18K) Dissociation constant
11 nM
 [1]
 Toxin Info    ChTX (R19Q) Dissociation constant
13.8 nM
 [2]
 Toxin Info    ChTX (S24D) Dissociation constant
14 nM
 [1]
 Toxin Info    ChTX (Y36F) Dissociation constant
15 nM
 [1]
 Toxin Info    ChTX (V5E) Dissociation constant
17 nM
 [1]
 Toxin Info    ChTX (T3S) Dissociation constant
18 nM
 [1]
 Toxin Info    ChTX (V16E) Dissociation constant
18 nM
 [1]
 Toxin Info    ChTX (R19Q,K32Q) Dissociation constant
20 nM
 [2]
 Toxin Info    ChTX (R19Y,Y36F) Dissociation constant
20 nM
 [1]
 Toxin Info    ChTX (S10T) Dissociation constant
22 nM
 [1]
 Toxin Info    ChTX (S15Y) Dissociation constant
22 nM
 [1]
 Toxin Info    ChTX (K32Q) Dissociation constant
27 nM
 [2]
 Toxin Info    ChTX (L20N) Dissociation constant
27 nM
 [1]
 Toxin Info    ChTX (T8S,T9G) Dissociation constant
28 nM
 [1]
 Toxin Info    ChTX (S37Q) Dissociation constant
30 nM
 [1]
 Toxin Info    ChTX (K11N,E12Q) Dissociation constant
37 nM
 [2]
 Toxin Info    Potassium channel toxin alpha-KTx 1.2 Dissociation constant
43 nM
 [3], [4], [5]
 Toxin Info    ChTX (F2A) Dissociation constant
55 nM
 [1]
 Toxin Info    ChTX (K27R) Dissociation constant
55 nM
 [6]
 Toxin Info    ChTX (K11Q) Dissociation constant
56 nM
 [2]
 Toxin Info    ChTX (K31Q) Dissociation constant
60 nM
 [2]
 Toxin Info    ChTX (H21Q) Dissociation constant
71 nM
 [2]
 Toxin Info    ChTX (T3L) Dissociation constant
71 nM
 [1]
 Toxin Info    ChTX (K27N) Dissociation constant
79 nM
 [6]
 Toxin Info    ChTX (C13[Abu],C33[Abu]) Dissociation constant
80 nM
 [7]
 Toxin Info    ChTX (F2W) Dissociation constant
120 nM
 [1]
 Toxin Info    ChTX (S10A) Dissociation constant
120 nM
 [1]
 Toxin Info    ChTX (S37X) Dissociation constant
150 nM
 [1]
 Toxin Info    ChTX (N30Q) Dissociation constant
200 nM
 [1]
 Toxin Info    ChTX (Y36N) Dissociation constant
260 nM
 [1]
 Toxin Info    ChTX (R34Q) Dissociation constant
330 nM
 [2]
 Toxin Info    ChTX (W14A) Dissociation constant
330 nM
 [1]
 Toxin Info    ChTX (W14Y) Dissociation constant
370 nM
 [1]
 Toxin Info    Kunitz-type serine protease inhibitor homolog delta-dendrotoxin Dissociation constant
390 nM
 [8], [9]
 Toxin Info    ChTX (W14F) Dissociation constant
410 nM
 [1]
 Toxin Info    ChTX (W14Q) Dissociation constant
430 nM
 [1]
 Toxin Info    Potassium channel toxin alpha-KTx 2.1 Dissociation constant
450 nM
 [10- 24]
 Toxin Info    ChTX (R25Q) Dissociation constant
610 nM
 [2]
 Toxin Info    ChTX (W14M) Dissociation constant
700 nM
 [1]
 Toxin Info    Venom basic protease inhibitor K (L9V,I11Y,R16K,K17A) Dissociation constant
1.075 μM
 [25]
 Toxin Info    Venom basic protease inhibitor K (K6A,L9V,I11Y,R16K) Dissociation constant
1.14 μM
 [25]
 Toxin Info    Venom basic protease inhibitor K (L9V,I11Y,R16K,R53A) Dissociation constant
1.14 μM
 [25]
 Toxin Info    Venom basic protease inhibitor K (K16A) Dissociation constant
1.15 μM
 [25]
 Toxin Info    Venom basic protease inhibitor K (R44A) Dissociation constant
1.5 μM
 [25]
 Toxin Info    ChTX (C7[Abu],C28[Abu]) Dissociation constant
1.5 μM
 [7]
 Toxin Info    ChTX (M29L) Dissociation constant
1.6 μM
 [1]
 Toxin Info    Venom basic protease inhibitor K (R10A) Dissociation constant
1.7 μM
 [25]
 Toxin Info    ChTX (T23D) Dissociation constant
2 μM
 [1]
 Toxin Info    ChTX (C17[Abu],C35[Abu]) Dissociation constant
4.9 μM
 [7]
 Toxin Info    ChTX (Y36L) Dissociation constant
7 μM
 [1]
 Toxin Info    ChTX (K27Q) Dissociation constant
7.5 μM
 [6]
 Toxin Info    ChTX (M29I) Dissociation constant
9.1 μM
 [1]
 Toxin Info    ChTX (Y36A) Dissociation constant
9.4 μM
 [1]
 Toxin Info    ChTX (S10Q) Dissociation constant
13 μM
 [1]
 Toxin Info    ChTX (M29K) Dissociation constant
15 μM
 [1]
 Toxin Info    ChTX (Y36H) Dissociation constant
19 μM
 [1]
 Toxin Info    ChTX (K27M) Dissociation constant
24 μM
 [6]
 Toxin Info    ChTX (Y36P) Dissociation constant
94 μM
 [1]
 Toxin Info    Conotoxin im23a Effect . [26]
 Toxin Info    Kappa-conotoxin BtX Effective concentration 50
0.7 nM
 [27]
 Toxin Info    Potassium channel toxin alpha-KTx 16.2 IC50
21 nM
 [28- 33]
References
Ref 1 Intimations of K+ channel structure from a complete functional map of the molecular surface of charybdotoxin. Biochemistry. 1994 Jan 18;33(2):443-50. doi: 10.1021/bi00168a008.
Ref 2 Mapping function to structure in a channel-blocking peptide: electrostatic mutants of charybdotoxin. Biochemistry. 1992 Sep 1;31(34):7749-55. doi: 10.1021/bi00149a002.
Ref 3 Dynamic diversification from a putative common ancestor of scorpion toxins affecting sodium, potassium, and chloride channels. J Mol Evol. 1999 Feb;48(2):187-96. doi: 10.1007/pl00006457.
Ref 4 Analysis of the blocking activity of charybdotoxin homologs and iodinated derivatives against Ca2+-activated K+ channels. J Membr Biol. 1989 Aug;109(3):269-81. doi: 10.1007/BF01870284.
Ref 5 Neuromuscular effects of some potassium channel blocking toxins from the venom of the scorpion Leiurus quinquestriatus hebreus. Toxicon. 1994 Nov;32(11):1433-43. doi: 10.1016/0041-0101(94)90415-4.
Ref 6 Interaction of charybdotoxin with permeant ions inside the pore of a K+ channel. Neuron. 1992 Aug;9(2):307-13. doi: 10.1016/0896-6273(92)90169-e.
Ref 7 Consequence of the removal of evolutionary conserved disulfide bridges on the structure and function of charybdotoxin and evidence that particular cysteine spacings govern specific disulfide bond formation. Biochemistry. 1998 Feb 3;37(5):1292-301. doi: 10.1021/bi9721086.
Ref 8 Snake venoms. The amino acid sequences of two proteinase inhibitor homologues from Dendroaspis angusticeps venom. Hoppe Seylers Z Physiol Chem. 1980 May;361(5):661-74. doi: 10.1515/bchm2.1980.361.1.661.
Ref 9 Energetic and structural interactions between delta-dendrotoxin and a voltage-gated potassium channel. J Mol Biol. 2000 Mar 10;296(5):1283-94. doi: 10.1006/jmbi.2000.3522.
Ref 10 Charybdotoxin and noxiustoxin, two homologous peptide inhibitors of the K+ (Ca2+) channel. FEBS Lett. 1988 Jan 4;226(2):280-4. doi: 10.1016/0014-5793(88)81439-x.
Ref 11 Synthetic peptides corresponding to the sequence of noxiustoxin indicate that the active site of this K+ channel blocker is located on its amino-terminal portion. J Neural Transm. 1989;77(1):11-20. doi: 10.1007/BF01255815.
Ref 12 Determination of the three-dimensional solution structure of noxiustoxin: analysis of structural differences with related short-chain scorpion toxins. Biochemistry. 1995 Dec 26;34(51):16563-73. doi: 10.1021/bi00051a004.
Ref 13 Synthesis of Novel cis-2-Azetidinones from imines and aclychloride using triethylamine. Acta Chim Slov. 2023 Dec 4;70(4):628-633. doi: 10.17344/acsi.2023.8451.
Ref 14 Backward-Eulerian Footprint Modelling Based on the Adjoint Equation for Atmospheric and Urban-Terrain Dispersion. Boundary Layer Meteorol. 2023;188(1):159-183. doi: 10.1007/s10546-023-00807-z. Epub 2023 Apr 17.
Ref 15 Leaf spot on Alocasia macrorrhizos caused by Fusarium asiaticum in Sichuan, China. Plant Dis. 2022 Sep 11. doi: 10.1094/PDIS-04-22-0844-PDN. Online ahead of print.
Ref 16 Incidence and predictors of chronic kidney disease in type-II diabetes mellitus patients attending at the Amhara region referral hospitals, Ethiopia: A follow-up study. PLoS One. 2022 Jan 26;17(1):e0263138. doi: 10.1371/journal.pone.0263138. eCollection 2022.
Ref 17 A Method for More Accurate Determination of Resonance Frequency of the Cardiovascular System, and Evaluation of a Program to Perform It. Appl Psychophysiol Biofeedback. 2022 Mar;47(1):17-26. doi: 10.1007/s10484-021-09524-0. Epub 2021 Oct 16.
Ref 18 First Report of Fusarium wilt of Coleus forskohlii Caused by Fusarium oxysporum in China. Plant Dis. 2021 Jan 26. doi: 10.1094/PDIS-11-20-2489-PDN. Online ahead of print.
Ref 19 Shock waves from the inhomogeneous Boltzmann equation. Phys Rev E. 2019 Dec;100(6-1):062120. doi: 10.1103/PhysRevE.100.062120.
Ref 20 Classifying Changes to Preventive Interventions: Applying Adaptation Taxonomies. J Prim Prev. 2019 Feb;40(1):89-109. doi: 10.1007/s10935-018-00531-2.
Ref 21 Quantification of the passive and active biaxial mechanical behaviour and microstructural organization of rat thoracic ducts. J R Soc Interface. 2015 Jul 6;12(108):20150280. doi: 10.1098/rsif.2015.0280.
Ref 22 A model of mechanical interactions between heart and lungs. Philos Trans A Math Phys Eng Sci. 2009 Dec 13;367(1908):4741-57. doi: 10.1098/rsta.2009.0137.
Ref 23 Experimental test of nonlocal realistic theories without the rotational symmetry assumption. Phys Rev Lett. 2007 Nov 23;99(21):210406. doi: 10.1103/PhysRevLett.99.210406. Epub 2007 Nov 21.
Ref 24 Structures and phase transitions of the A7PSe6 (A = ag, Cu) argyrodite-type ionic conductors. III. alpha-Cu7PSe6. Acta Crystallogr B. 2000 Dec;56 (Pt 6):972-9. doi: 10.1107/s0108768100010260.
Ref 25 Interaction of the BKCa channel gating ring with dendrotoxins. Channels (Austin). 2014;8(5):421-32. doi: 10.4161/19336950.2014.949186.
Ref 26 A helical conotoxin from Conus imperialis has a novel cysteine framework and defines a new superfamily. J Biol Chem. 2012 Apr 27;287(18):14973-83. doi: 10.1074/jbc.M111.334615. Epub 2012 Mar 7.
Ref 27 A novel conotoxin from Conus betulinus, kappa-BtX, unique in cysteine pattern and in function as a specific BK channel modulator. J Biol Chem. 2003 Apr 11;278(15):12624-33. doi: 10.1074/jbc.M210200200. Epub 2003 Jan 23.
Ref 28 Martentoxin, a novel K+-channel-blocking peptide: purification, cDNA and genomic cloning, and electrophysiological and pharmacological characterization. J Neurochem. 2003 Jan;84(2):325-35. doi: 10.1046/j.1471-4159.2003.01516.x.
Ref 29 Molecular divergence of two orthologous scorpion toxins affecting potassium channels. Comp Biochem Physiol A Mol Integr Physiol. 2011 Jul;159(3):313-21. doi: 10.1016/j.cbpa.2011.03.027. Epub 2011 Apr 3.
Ref 30 Purification, characterization of two peptides from Buthus martensi Karch. J Pept Res. 2003 Dec;62(6):252-9. doi: 10.1046/j.1399-3011.2003.00095.x.
Ref 31 Short-chain peptides identification of scorpion Buthus martensi Karsch venom by employing high orthogonal 2D-HPLC system and tandem mass spectrometry. Proteomics. 2012 Oct;12(19-20):3076-84. doi: 10.1002/pmic.201200224. Epub 2012 Sep 19.
Ref 32 Inhibition of martentoxin on neuronal BK channel subtype (alpha+beta4): implications for a novel interaction model. Biophys J. 2008 May 1;94(9):3706-13. doi: 10.1529/biophysj.107.122150. Epub 2008 Jan 16.
Ref 33 The solution structure of BmTx3B, a member of the scorpion toxin subfamily alpha-KTx 16. Proteins. 2005 Feb 1;58(2):489-97. doi: 10.1002/prot.20322.
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