Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-01309
Entry Name
UniProt Accession
Theoretical PI
6.66
Molecular Weight
137559.53
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Calcium-activated potassium channel subunit alpha-1
Protein Synonyms/Alias
BK channel; BKCA alpha; Calcium-activated potassium channel, subfamily M subunit alpha-1; K(VCA)alpha; KCa1.1; Maxi K channel; MaxiK; Slo-alpha; Slo1; Slowpoke homolog; Slo homolog; hSlo;
Gene Name
KCNMA1
Gene Synonyms/Alias
KCNMA; SLO;
Created Date
13-APR-2004
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
118
Canonical
LKYLWTVCCHCGGKT
[1]
S-Palmitoylation
119
Canonical
KYLWTVCCHCGGKTK
[1]
S-Palmitoylation
121
Canonical
LWTVCCHCGGKTKEA
[1]
S-Palmitoylation
710
Canonical
YKRMRRACCFDCGRS
[1]
S-Palmitoylation
711
Canonical
KRMRRACCFDCGRSE
[1]
S-Palmitoylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
Reference
[1] Shipston MJ. Regulation of large conductance calcium- and voltage-activatedpotassium (BK) channels by S-palmitoylation. Biochem Soc Trans. 2013 Feb1;41(1):67-71. doi: 10.1042/BST20120226.[PMID:23356260]
Functional Description
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).
Sequence Annotation
Topological domain: 1 86 Extracellular.
Transmembrane: 87 107 Helical; Name=Segment S0.
Topological domain: 108 178 Cytoplasmic.
Transmembrane: 179 199 Helical; Name=Segment S1.
Topological domain: 200 214 Extracellular.
Transmembrane: 215 235 Helical; Name=Segment S2.
Topological domain: 236 239 Cytoplasmic.
Transmembrane: 240 260 Helical; Name=Segment S3.
Topological domain: 261 264 Extracellular.
Transmembrane: 265 285 Helical; Name=Segment S4.
Topological domain: 286 300 Cytoplasmic.
Transmembrane: 301 321 Helical; Name=Segment S5.
Topological domain: 322 335 Extracellular.
Topological domain: 359 367 Extracellular.
Transmembrane: 368 388 Helical; Name=Segment S6.
Topological domain: 389 1236 Cytoplasmic.
Domain: 415 558 RCK N-terminal.
Region: 556 576 Segment S7.
Region: 613 633 Segment S8.
Region: 677 681 Heme-binding motif.
Region: 837 857 Segment S9.
Region: 1032 1052 Segment S10.
Motif: 352 355 Selectivity for potassium.
Motif: 1003 1025 Calcium bowl.
Metal binding site: 439 439 Magnesium.
Metal binding site: 462 462 Magnesium.
Metal binding site: 464 464 Magnesium.
Metal binding site: 1012 1012 Calcium; via carbonyl oxygen.
Metal binding site: 1015 1015 Calcium; via carbonyl oxygen.
Metal binding site: 1018 1018 Calcium.
Metal binding site: 1020 1020 Calcium.
Protein Length
1236 AA.
Protein Sequence
(Canonical)
MANGGGGGGG SSGGGGGGGG SSLRMSSNIH ANHLSLDASS SSSSSSSSSS SSSSSSSSSS  60
VHEPKMDALI IPVTMEVPCD SRGQRMWWAF LASSMVTFFG GLFIILLWRT LKYLWTVCCH  120
CGGKTKEAQK INNGSSQADG TLKPVDEKEE AVAAEVGWMT SVKDWAGVMI SAQTLTGRVL  180
VVLVFALSIG ALVIYFIDSS NPIESCQNFY KDFTLQIDMA FNVFFLLYFG LRFIAANDKL  240
WFWLEVNSVV DFFTVPPVFV SVYLNRSWLG LRFLRALRLI QFSEILQFLN ILKTSNSIKL  300
VNLLSIFIST WLTAAGFIHL VENSGDPWEN FQNNQALTYW ECVYLLMVTM STVGYGDVYA  360
KTTLGRLFMV FFILGGLAMF ASYVPEIIEL IGNRKKYGGS YSAVSGRKHI VVCGHITLES  420
VSNFLKDFLH KDRDDVNVEI VFLHNISPNL ELEALFKRHF TQVEFYQGSV LNPHDLARVK  480
IESADACLIL ANKYCADPDA EDASNIMRVI SIKNYHPKIR IITQMLQYHN KAHLLNIPSW  540
NWKEGDDAIC LAELKLGFIA QSCLAQGLST MLANLFSMRS FIKIEEDTWQ KYYLEGVSNE  600
MYTEYLSSAF VGLSFPTVCE LCFVKLKLLM IAIEYKSANR ESRILINPGN HLKIQEGTLG  660
FFIASDAKEV KRAFFYCKAC HDDITDPKRI KKCGCKRPKM SIYKRMRRAC CFDCGRSERD  720
CSCMSGRVRG NVDTLERAFP LSSVSVNDCS TSFRAFEDEQ PSTLSPKKKQ RNGGMRNSPN  780
TSPKLMRHDP LLIPGNDQID NMDSNVKKYD STGMFHWCAP KEIEKVILTR SEAAMTVLSG  840
HVVVCIFGDV SSALIGLRNL VMPLRASNFH YHELKHIVFV GSIEYLKREW ETLHNFPKVS  900
ILPGTPLSRA DLRAVNINLC DMCVILSANQ NNIDDTSLQD KECILASLNI KSMQFDDSIG  960
VLQANSQGFT PPGMDRSSPD NSPVHGMLRQ PSITTGVNIP IITELVNDTN VQFLDQDDDD  1020
DPDTELYLTQ PFACGTAFAV SVLDSLMSAT YFNDNILTLI RTLVTGGATP ELEALIAEEN  1080
ALRGGYSTPQ TLANRDRCRV AQLALLDGPF ADLGDGGCYG DLFCKALKTY NMLCFGIYRL  1140
RDAHLSTPSQ CTKRYVITNP PYEFELVPTD LIFCLMQFDH NAGQSRASLS HSSHSSQSSS  1200
KKSSSVHSIP STANRQNRPK SRESRDKQKY VQEERL                            1236
FASTA
(Canonical)
>LipidDB-9606-01309|Q12791
MANGGGGGGGSSGGGGGGGGSSLRMSSNIHANHLSLDASSSSSSSSSSSSSSSSSSSSSS
VHEPKMDALIIPVTMEVPCDSRGQRMWWAFLASSMVTFFGGLFIILLWRTLKYLWTVCCH
CGGKTKEAQKINNGSSQADGTLKPVDEKEEAVAAEVGWMTSVKDWAGVMISAQTLTGRVL
VVLVFALSIGALVIYFIDSSNPIESCQNFYKDFTLQIDMAFNVFFLLYFGLRFIAANDKL
WFWLEVNSVVDFFTVPPVFVSVYLNRSWLGLRFLRALRLIQFSEILQFLNILKTSNSIKL
VNLLSIFISTWLTAAGFIHLVENSGDPWENFQNNQALTYWECVYLLMVTMSTVGYGDVYA
KTTLGRLFMVFFILGGLAMFASYVPEIIELIGNRKKYGGSYSAVSGRKHIVVCGHITLES
VSNFLKDFLHKDRDDVNVEIVFLHNISPNLELEALFKRHFTQVEFYQGSVLNPHDLARVK
IESADACLILANKYCADPDAEDASNIMRVISIKNYHPKIRIITQMLQYHNKAHLLNIPSW
NWKEGDDAICLAELKLGFIAQSCLAQGLSTMLANLFSMRSFIKIEEDTWQKYYLEGVSNE
MYTEYLSSAFVGLSFPTVCELCFVKLKLLMIAIEYKSANRESRILINPGNHLKIQEGTLG
FFIASDAKEVKRAFFYCKACHDDITDPKRIKKCGCKRPKMSIYKRMRRACCFDCGRSERD
CSCMSGRVRGNVDTLERAFPLSSVSVNDCSTSFRAFEDEQPSTLSPKKKQRNGGMRNSPN
TSPKLMRHDPLLIPGNDQIDNMDSNVKKYDSTGMFHWCAPKEIEKVILTRSEAAMTVLSG
HVVVCIFGDVSSALIGLRNLVMPLRASNFHYHELKHIVFVGSIEYLKREWETLHNFPKVS
ILPGTPLSRADLRAVNINLCDMCVILSANQNNIDDTSLQDKECILASLNIKSMQFDDSIG
VLQANSQGFTPPGMDRSSPDNSPVHGMLRQPSITTGVNIPIITELVNDTNVQFLDQDDDD
DPDTELYLTQPFACGTAFAVSVLDSLMSATYFNDNILTLIRTLVTGGATPELEALIAEEN
ALRGGYSTPQTLANRDRCRVAQLALLDGPFADLGDGGCYGDLFCKALKTYNMLCFGIYRL
RDAHLSTPSQCTKRYVITNPPYEFELVPTDLIFCLMQFDHNAGQSRASLSHSSHSSQSSS
KKSSSVHSIPSTANRQNRPKSRESRDKQKYVQEERL
Gene Ontology
GO:0016324; C:apical plasma membrane; IDA:UniProtKB
GO:0005901; C:caveola; IDA:BHF-UCL
GO:0070062; C:extracellular vesicular exosome; IDA:UniProt
GO:0016021; C:integral component of membrane; IDA:UniProtKB
GO:0005886; C:plasma membrane; TAS:Reactome
GO:0008076; C:voltage-gated potassium channel complex; IDA:UniProtKB
GO:0003779; F:actin binding; IDA:BHF-UCL
GO:0015269; F:calcium-activated potassium channel activity; IDA:UniProtKB
GO:0060072; F:large conductance calcium-activated potassium channel activity; IDA:UniProtKB
GO:0046872; F:metal ion binding; IEA:UniProtKB-KW
GO:0005249; F:voltage-gated potassium channel activity; IDA:UniProtKB
GO:0007596; P:blood coagulation; TAS:Reactome
GO:0030007; P:cellular potassium ion homeostasis; IDA:UniProtKB
GO:0060073; P:micturition; IDA:UniProtKB
GO:0045794; P:negative regulation of cell volume; IDA:UniProtKB
GO:0043065; P:positive regulation of apoptotic process; IMP:UniProtKB
GO:0071805; P:potassium ion transmembrane transport; IBA:RefGenome
GO:0006813; P:potassium ion transport; IDA:UniProtKB
GO:0042391; P:regulation of membrane potential; IDA:UniProtKB
GO:0051592; P:response to calcium ion; IDA:UniProtKB
GO:0034465; P:response to carbon monoxide; IDA:UniProtKB
GO:0001666; P:response to hypoxia; IDA:UniProtKB
GO:0006970; P:response to osmotic stress; IDA:UniProtKB
GO:0060083; P:smooth muscle contraction involved in micturition; IDA:UniProtKB
GO:0007268; P:synaptic transmission; TAS:Reactome
Interpro
InterPro; IPR005821; Ion_trans_dom
InterPro; IPR003091; K_chnl
InterPro; IPR003929; K_chnl_Ca-activ_BK_asu
InterPro; IPR016040; NAD(P)-bd_dom
InterPro; IPR003148; RCK_N
Pfam
Pfam; PF03493; BK_channel_a;
Pfam; PF00520; Ion_trans;
Pfam; PF02254; TrkA_N;
SMART
PROSITE
PRINTS
PRINTS; PR01449; BKCHANNELA;
PRINTS; PR00169; KCHANNEL;