Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-10090-01066
Entry Name
UniProt Accession
Theoretical PI
6.75
Molecular Weight
134396.12
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; mSlo1; Slowpoke homolog; Slo homolog; mSlo;
Gene Name
Kcnma1
Gene Synonyms/Alias
Kcnma;
Created Date
13-APR-2004
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
53
Isoform 5
LKYLWTVCCHCGGKT
[1]
S-Palmitoylation
54
Isoform 5
KYLWTVCCHCGGKTK
[1]
S-Palmitoylation
56
Isoform 5
LWTVCCHCGGKTKEA
[1]
S-Palmitoylation
710
Isoform 4
YKRMRRACCFDCGRS
[2]
S-Palmitoylation
711
Isoform 4
KRMRRACCFDCGRSE
[2]
S-Palmitoylation
Organism
Mus musculus (Mouse)
NCBI Taxa ID
10090
Reference
[1] Jeffries O, Geiger N, Rowe IC, Tian L, McClafferty H, Chen L, Bi D, Knaus HG, Ruth P, Shipston MJ. Palmitoylation of the S0-S1 linker regulates cell surfaceexpression of voltage- and calcium-activated potassium (BK) channels. J BiolChem. 2010 Oct 22;285(43):33307-14. doi: 10.1074/jbc.M110.153940. Epub 2010 Aug6.[PMID:20693285]
[2] Jeffries O, Tian L, McClafferty H, Shipston MJ. An electrostatic switchcontrols palmitoylation of the large conductance voltage- and calcium-activatedpotassium (BK) channel. J Biol Chem. 2012 Jan 6;287(2):1468-77. doi:10.1074/jbc.M111.224840. Epub 2011 Nov 14.[PMID:22084244]
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; Voltage-sensor; 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 1209 Cytoplasmic.
Domain: 415 558 RCK N-terminal.
Region: 556 576 Segment S7.
Region: 613 633 Segment S8.
Region: 681 685 Heme-binding motif.
Region: 783 803 Segment S9.
Region: 1005 1025 Segment S10.
Motif: 352 355 Selectivity for potassium.
Motif: 976 998 Calcium bowl.
Metal binding site: 439 439 Magnesium.
Metal binding site: 462 462 Magnesium.
Metal binding site: 464 464 Magnesium.
Metal binding site: 985 985 Calcium; via carbonyl oxygen.
Metal binding site: 988 988 Calcium; via carbonyl oxygen.
Metal binding site: 991 991 Calcium.
Metal binding site: 993 993 Calcium.
Protein Length
1209 AA.
Protein Sequence
(Isoform 4)
MANGGGGGGG SSGGGGGGGG GSGLRMSSNI HANNLSLDAS SSSSSSSSSS SSSSSSSSSS  60
VHEPKMDALI IPVTMEVPCD SRGQRMWWAF LASSMVTFFG GLFIILLWRT LKYLWTVCCH  120
CGGKTKEAQK INNGSSQADG TLKPVDEKEE VVAAEVGWMT 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 HDDVTDPKRI KKCGCRRPKM SIYKRMRRAC CFDCGRSERD  720
CSCMSGRVRG NVDTLERTFP LSSVSVNDCS TSFRAFEDEQ PPTLSPKKKQ 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 STANRPNRPK SRESRDKQNR KEMVYR                            1236
Protein Sequence
(Isoform 5)
MDALIIPVTM EVPCDSRGQR MWWAFLASSM VTFFGGLFII LLWRTLKYLW TVCCHCGGKT  60
KEAQKINNGS SQADGTLKPV DEKEEVVAAE VGWMTSVKDW AGVMISAQTL TGRVLVVLVF  120
ALSIGALVIY FIDSSNPIES CQNFYKDFTL QIDMAFNVFF LLYFGLRFIA ANDKLWFWLE  180
VNSVVDFFTV PPVFVSVYLN RSWLGLRFLR ALRLIQFSEI LQFLNILKTS NSIKLVNLLS  240
IFISTWLTAA GFIHLVENSG DPWENFQNNQ ALTYWECVYL LMVTMSTVGY GDVYAKTTLG  300
RLFMVFFILG GLAMFASYVP EIIELIGNRK KYGGSYSAVS GRKHIVVCGH ITLESVSNFL  360
KDFLHKDRDD VNVEIVFLHN ISPNLELEAL FKRHFTQVEF YQGSVLNPHD LARVKIESAD  420
ACLILANKYC ADPDAEDASN IMRVISIKNY HPKIRIITQM LQYHNKAHLL NIPSWNWKEG  480
DDAICLAELK LGFIAQSCLA QGLSTMLANL FSMRSFIKIE EDTWQKYYLE GVSNEMYTEY  540
LSSAFVGLSF PTVCELCFVK LKLLMIAIEY KSANRESRSR KRILINPGNH LKIQEGTLGF  600
FIASDAKEVK RAFFYCKACH DDVTDPKRIK KCGCRRLEDE QPPTLSPKKK QRNGGMRNSP  660
NTSPKLMRHD PLLIPGNDQI DNMDSNVKKY DSTGMFHWCA PKEIEKVILT RSEAAMTVLS  720
GHVVVCIFGD VSSALIGLRN LVMPLRASNF HYHELKHIVF VGSIEYLKRE WETLHNFPKV  780
SILPGTPLSR ADLRAVNINL CDMCVILSAN QNNIDDTSLQ DKECILASLN IKSMQFDDSI  840
GVLQANSQGF TPPGMDRSSP DNSPVHGMLR QPSITTGVNI PIITELAKPG KLPLVSVNQE  900
KNSGTHILMI TELVNDTNVQ FLDQDDDDDP DTELYLTQPF ACGTAFAVSV LDSLMSATYF  960
NDNILTLIRT LVTGGATPEL EALIAEENAL RGGYSTPQTL ANRDRCRVAQ LALLDGPFAD  1020
LGDGGCYGDL FCKALKTYNM LCFGIYRLRD AHLSTPSQCT KRYVITNPPY EFELVPTDLI  1080
FCLMQFDHNA GQSRASLSHS SHSSQSSSKK SSSVHSIPST ANRPNRPKSR ESRDKQNRKE  1140
MVYR                                                               1144
FASTA
(Isoform 4)
>LipidDB-10090-01066|Q08460-4
MANGGGGGGGSSGGGGGGGGGSGLRMSSNIHANNLSLDASSSSSSSSSSSSSSSSSSSSS
VHEPKMDALIIPVTMEVPCDSRGQRMWWAFLASSMVTFFGGLFIILLWRTLKYLWTVCCH
CGGKTKEAQKINNGSSQADGTLKPVDEKEEVVAAEVGWMTSVKDWAGVMISAQTLTGRVL
VVLVFALSIGALVIYFIDSSNPIESCQNFYKDFTLQIDMAFNVFFLLYFGLRFIAANDKL
WFWLEVNSVVDFFTVPPVFVSVYLNRSWLGLRFLRALRLIQFSEILQFLNILKTSNSIKL
VNLLSIFISTWLTAAGFIHLVENSGDPWENFQNNQALTYWECVYLLMVTMSTVGYGDVYA
KTTLGRLFMVFFILGGLAMFASYVPEIIELIGNRKKYGGSYSAVSGRKHIVVCGHITLES
VSNFLKDFLHKDRDDVNVEIVFLHNISPNLELEALFKRHFTQVEFYQGSVLNPHDLARVK
IESADACLILANKYCADPDAEDASNIMRVISIKNYHPKIRIITQMLQYHNKAHLLNIPSW
NWKEGDDAICLAELKLGFIAQSCLAQGLSTMLANLFSMRSFIKIEEDTWQKYYLEGVSNE
MYTEYLSSAFVGLSFPTVCELCFVKLKLLMIAIEYKSANRESRILINPGNHLKIQEGTLG
FFIASDAKEVKRAFFYCKACHDDVTDPKRIKKCGCRRPKMSIYKRMRRACCFDCGRSERD
CSCMSGRVRGNVDTLERTFPLSSVSVNDCSTSFRAFEDEQPPTLSPKKKQRNGGMRNSPN
TSPKLMRHDPLLIPGNDQIDNMDSNVKKYDSTGMFHWCAPKEIEKVILTRSEAAMTVLSG
HVVVCIFGDVSSALIGLRNLVMPLRASNFHYHELKHIVFVGSIEYLKREWETLHNFPKVS
ILPGTPLSRADLRAVNINLCDMCVILSANQNNIDDTSLQDKECILASLNIKSMQFDDSIG
VLQANSQGFTPPGMDRSSPDNSPVHGMLRQPSITTGVNIPIITELVNDTNVQFLDQDDDD
DPDTELYLTQPFACGTAFAVSVLDSLMSATYFNDNILTLIRTLVTGGATPELEALIAEEN
ALRGGYSTPQTLANRDRCRVAQLALLDGPFADLGDGGCYGDLFCKALKTYNMLCFGIYRL
RDAHLSTPSQCTKRYVITNPPYEFELVPTDLIFCLMQFDHNAGQSRASLSHSSHSSQSSS
KKSSSVHSIPSTANRPNRPKSRESRDKQNRKEMVYR
FASTA
(Isoform 5)
>LipidDB-10090-01066|Q08460-5
MDALIIPVTMEVPCDSRGQRMWWAFLASSMVTFFGGLFIILLWRTLKYLWTVCCHCGGKT
KEAQKINNGSSQADGTLKPVDEKEEVVAAEVGWMTSVKDWAGVMISAQTLTGRVLVVLVF
ALSIGALVIYFIDSSNPIESCQNFYKDFTLQIDMAFNVFFLLYFGLRFIAANDKLWFWLE
VNSVVDFFTVPPVFVSVYLNRSWLGLRFLRALRLIQFSEILQFLNILKTSNSIKLVNLLS
IFISTWLTAAGFIHLVENSGDPWENFQNNQALTYWECVYLLMVTMSTVGYGDVYAKTTLG
RLFMVFFILGGLAMFASYVPEIIELIGNRKKYGGSYSAVSGRKHIVVCGHITLESVSNFL
KDFLHKDRDDVNVEIVFLHNISPNLELEALFKRHFTQVEFYQGSVLNPHDLARVKIESAD
ACLILANKYCADPDAEDASNIMRVISIKNYHPKIRIITQMLQYHNKAHLLNIPSWNWKEG
DDAICLAELKLGFIAQSCLAQGLSTMLANLFSMRSFIKIEEDTWQKYYLEGVSNEMYTEY
LSSAFVGLSFPTVCELCFVKLKLLMIAIEYKSANRESRSRKRILINPGNHLKIQEGTLGF
FIASDAKEVKRAFFYCKACHDDVTDPKRIKKCGCRRLEDEQPPTLSPKKKQRNGGMRNSP
NTSPKLMRHDPLLIPGNDQIDNMDSNVKKYDSTGMFHWCAPKEIEKVILTRSEAAMTVLS
GHVVVCIFGDVSSALIGLRNLVMPLRASNFHYHELKHIVFVGSIEYLKREWETLHNFPKV
SILPGTPLSRADLRAVNINLCDMCVILSANQNNIDDTSLQDKECILASLNIKSMQFDDSI
GVLQANSQGFTPPGMDRSSPDNSPVHGMLRQPSITTGVNIPIITELAKPGKLPLVSVNQE
KNSGTHILMITELVNDTNVQFLDQDDDDDPDTELYLTQPFACGTAFAVSVLDSLMSATYF
NDNILTLIRTLVTGGATPELEALIAEENALRGGYSTPQTLANRDRCRVAQLALLDGPFAD
LGDGGCYGDLFCKALKTYNMLCFGIYRLRDAHLSTPSQCTKRYVITNPPYEFELVPTDLI
FCLMQFDHNAGQSRASLSHSSHSSQSSSKKSSSVHSIPSTANRPNRPKSRESRDKQNRKE
MVYR
Gene Ontology
GO:0016324; C:apical plasma membrane; IDA:MGI
GO:0005737; C:cytoplasm; IDA:MGI
GO:0005783; C:endoplasmic reticulum; IDA:MGI
GO:0009897; C:external side of plasma membrane; IDA:MGI
GO:0016021; C:integral component of membrane; IDA:MGI
GO:0005886; C:plasma membrane; IDA:MGI
GO:0045211; C:postsynaptic membrane; IDA:MGI
GO:0043195; C:terminal bouton; IDA:MGI
GO:0008076; C:voltage-gated potassium channel complex; IGI:MGI
GO:0015269; F:calcium-activated potassium channel activity; IDA:MGI
GO:0060072; F:large conductance calcium-activated potassium channel activity; IMP:UniProt
GO:0046872; F:metal ion binding; IEA:UniProtKB-KW
GO:0005267; F:potassium channel activity; IMP:MGI
GO:0005249; F:voltage-gated potassium channel activity; IDA:MGI
GO:0007628; P:adult walking behavior; IMP:MGI
GO:0042491; P:auditory receptor cell differentiation; IMP:MGI
GO:0048469; P:cell maturation; IMP:MGI
GO:0007623; P:circadian rhythm; IMP:MGI
GO:0060082; P:eye blink reflex; IMP:MGI
GO:0045475; P:locomotor rhythm; IMP:MGI
GO:0060073; P:micturition; IMP:MGI
GO:0045794; P:negative regulation of cell volume; IMP:MGI
GO:0050885; P:neuromuscular process controlling balance; IMP:MGI
GO:0019228; P:neuronal action potential; IMP:MGI
GO:0071805; P:potassium ion transmembrane transport; IBA:RefGenome
GO:0006813; P:potassium ion transport; IDA:MGI
GO:0051260; P:protein homooligomerization; IDA:MGI
GO:0032344; P:regulation of aldosterone metabolic process; IMP:MGI
GO:0042391; P:regulation of membrane potential; IDA:MGI
GO:0060087; P:relaxation of vascular smooth muscle; IMP:MGI
GO:0001666; P:response to hypoxia; IDA:MGI
GO:0046541; P:saliva secretion; IGI:MGI
GO:0007605; P:sensory perception of sound; IMP:MGI
GO:0060083; P:smooth muscle contraction involved in micturition; IMP:MGI
GO:0007268; P:synaptic transmission; IMP:MGI
GO:0042311; P:vasodilation; IMP:MGI
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;