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1.A.1.3.1
Large conductance, voltage- and Ca2+-activated K+ calcium-dependent potassium (BK) channel. Four pairs of RCK1 and RICK2 domains form the Ca2+-sensing apparatus known as the "gating ring" in Big Potassium (BK) channel proteins (Savalli et al., 2012). Gating of BK channels does not seem to require a physical gate. Instead, changes in the pore shape and surface hydrophobicity in the Ca2+-free state allow the channel to readily undergo hydrophobic dewetting transitions, giving rise to a large free energy barrier for K+ permeation (Jia et al. 2018).  Voltage-dependent dynamics of the BK channel cytosolic gating ring are coupled to the membrane-embedded voltage sensor (Miranda et al. 2018).

Accession Number:Q03720
Protein Name:Calcium-activated potassium channel slowpoke
Length:1200
Molecular Weight:133102.00
Species: [7227]
Number of TMSs:7
Location1 / Topology2 / Orientation3: Membrane1 / Multi-pass membrane protein2
Substrate K+

Cross database links:

RefSeq: NP_001014651.1    NP_001014652.1    NP_001014653.1    NP_001014654.1    NP_001014655.1    NP_001014656.1    NP_001014657.1    NP_001014658.1    NP_001014659.1    NP_001014660.1    NP_001014661.2    NP_001014662.1    NP_001014663.1    NP_001014664.1    NP_524486.2    NP_733029.1    NP_996289.1   
Entrez Gene ID: 42940   
Pfam: PF03493    PF00520   
KEGG: dme:Dmel_CG1069   

Gene Ontology

GO:0043005 C:neuron projection
GO:0043025 C:neuronal cell body
GO:0008076 C:voltage-gated potassium channel complex
GO:0015269 F:calcium-activated potassium channel activity
GO:0003824 F:catalytic activity
GO:0005515 F:protein binding
GO:0005249 F:voltage-gated potassium channel activity
GO:0048512 P:circadian behavior
GO:0045433 P:male courtship behavior, veined wing genera...
GO:0008152 P:metabolic process
GO:0006813 P:potassium ion transport
GO:0042493 P:response to drug
GO:0055085 P:transmembrane transport

References (13)

[1] “A component of calcium-activated potassium channels encoded by the Drosophila slo locus.”  Atkinson N.S.et.al.   1857984
[2] “Calcium-activated potassium channels expressed from cloned complementary DNAs.”  Adelman J.P.et.al.   1497890
[3] “The genome sequence of Drosophila melanogaster.”  Adams M.D.et.al.   10731132
[4] “Annotation of the Drosophila melanogaster euchromatic genome: a systematic review.”  Misra S.et.al.   12537572
[5] “A Drosophila full-length cDNA resource.”  Stapleton M.et.al.   12537569
[6] “Tissue-specific expression of a Ca(2+)-activated K+ channel is controlled by multiple upstream regulatory elements.”  Brenner R.et.al.   8774450
[7] “Tissue-specific expression of a Drosophila calcium-activated potassium channel.”  Becker M.N.et.al.   7666207
[8] “dSLo interacting protein 1, a novel protein that interacts with large-conductance calcium-activated potassium channels.”  Xia X.-M.et.al.   9502797
[9] “Slob, a novel protein that interacts with the Slowpoke calcium-dependent potassium channel.”  Schopperle W.M.et.al.   9539129
[10] “Simultaneous binding of two protein kinases to a calcium-dependent potassium channel.”  Wang J.et.al.   10234050
[11] “A dynamically regulated 14-3-3, Slob, and Slowpoke potassium channel complex in Drosophila presynaptic nerve terminals.”  Zhou Y.et.al.   10230800
[12] “Ca2+-binding activity of a COOH-terminal fragment of the Drosophila BK channel involved in Ca2+-dependent activation.”  Bian S.et.al.   11274367
[13] “Modulation of Drosophila slowpoke calcium-dependent potassium channel activity by bound protein kinase a catalytic subunit.”  Zhou Y.et.al.   12019304

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Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence 
1:	MASGLIDTNF SSTLANGMSG CDQSTVESLA DDPTDSPFDA DDCLKVRKYW CFLLSSIFTF 
61:	LAGLLVVLLW RAFAFVCCRK EPDLGPNDPK QKEQKASRNK QEFEGTFMTE AKDWAGELIS 
121:	GQTTTGRILV VLVFILSIAS LIIYFVDASS EEVERCQKWS NNITQQIDLA FNIFFMVYFF 
181:	IRFIAASDKL WFMLEMYSFV DYFTIPPSFV SIYLDRTWIG LRFLRALRLM TVPDILQYLN 
241:	VLKTSSSIRL AQLVSIFISV WLTAAGIIHL LENSGDPLDF NNAHRLSYWT CVYFLIVTMS 
301:	TVGYGDVYCE TVLGRTFLVF FLLVGLAMFA SSIPEIIELV GSGNKYGGEL KREHGKRHIV 
361:	VCGHITYESV SHFLKDFLHE DREDVDVEVV FLHRKPPDLE LEGLFKRHFT TVEFFQGTIM 
421:	NPIDLQRVKV HEADACLVLA NKYCQDPDAE DAANIMRVIS IKNYSDDIRV IIQLMQYHNK 
481:	AYLLNIPSWD WKQGDDVICL AELKLGFIAQ SCLAPGFSTM MANLFAMRSF KTSPDMQSWT 
541:	NDYLRGTGME MYTETLSPTF IGIPFAQATE LCFSKLKLLL LAIEIKGAEE GADSKISINP 
601:	RGAKIQANTQ GFFIAQSADE VKRAWFYCKA CHEDIKDETL IKKCKCKNLT VQPRSKFDDL 
661:	DEHHPAPTFT PPELPKRVHV RGSVSGDITR DREDTNLLNR NVRRPNGTGN GTGGMHHMNN 
721:	TAAAAAAAAA AGKQVNKVKP TVNVSRQVEG QVISPSQYNR PTSRSSGTGT QNQNGGVSLP 
781:	AGIADDQSKD FDFEKTEMKY DSTGMFHWSP AKSLEDCILD RNQAAMTVLN GHVVVCLFAD 
841:	PDSPLIGLRN LVMPLRASNF HYHELKHVVI VGSVDYIRRE WKMLQNLPKI SVLNGSPLSR 
901:	ADLRAVNVNL CDMCCILSAK VPSNDDPTLA DKEAILASLN IKAMTFDDTI GVLSQRGPEF 
961:	DNLSATAGSP IVLQRRGSVY GANVPMITEL VNDSNVQFLD QDDDDDPDTE LYLTQPFACG 
1021:	TAFAVSVLDS LMSTTYFNQN ALTLIRSLIT GGATPELELI LAEGAGLRGG YSTVESLSNR 
1081:	DRCRVGQISL YDGPLAQFGE CGKYGDLFVA ALKSYGMLCI GLYRFRDTSS SCDASSKRYV 
1141:	ITNPPDDFSL LPTDQVFVLM QFDPGLEYKP PAVRAPAGGR GTNTQGSGVG GGGSNKDDNS