Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-10116-00637
Entry Name
UniProt Accession
Theoretical PI
6.68
Molecular Weight
134374.16
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;
Gene Name
Kcnma1
Gene Synonyms/Alias
Kcnma;
Created Date
13-APR-2004
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
119
Canonical
LKYLWTVCCHCGGKT
[2]
S-Palmitoylation
120
Canonical
KYLWTVCCHCGGKTK
[2]
S-Palmitoylation
122
Canonical
LWTVCCHCGGKTKEA
[2]
S-Palmitoylation
718
Isoform 8
YKRMSRACCFDCGRS
[1]
S-Palmitoylation
719
Isoform 8
KRMSRACCFDCGRSE
[1]
S-Palmitoylation
Organism
Rattus norvegicus (Rat)
NCBI Taxa ID
10116
Reference
[1] 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]
[2] Kim S, Lee BC, Lee AR, Won S, Park CS. Effects of palmitoylation on thediffusional movement of BKCa channels in live cells. FEBS Lett. 2014 Mar3;588(5):713-9. doi: 10.1016/j.febslet.2014.01.014. Epub 2014 Jan 23. PubMedPMID: 24462688.[PMID:24462688]
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 87 Extracellular.
Transmembrane: 88 108 Helical; Name=Segment S0.
Topological domain: 109 179 Cytoplasmic.
Transmembrane: 180 200 Helical; Name=Segment S1.
Topological domain: 201 215 Extracellular.
Transmembrane: 216 236 Helical; Name=Segment S2.
Topological domain: 237 240 Cytoplasmic.
Transmembrane: 241 261 Helical; Name=Segment S3.
Topological domain: 262 265 Extracellular.
Transmembrane: 266 286 Helical; Voltage-sensor; Name=Segment S4.
Topological domain: 287 301 Cytoplasmic.
Transmembrane: 302 322 Helical; Name=Segment S5.
Topological domain: 323 336 Extracellular.
Topological domain: 360 368 Extracellular.
Transmembrane: 369 389 Helical; Name=Segment S6.
Topological domain: 390 1209 Cytoplasmic.
Domain: 416 559 RCK N-terminal.
Region: 557 577 Segment S7.
Region: 614 634 Segment S8.
Region: 682 686 Heme-binding motif.
Region: 784 804 Segment S9.
Region: 1006 1026 Segment S10.
Motif: 353 356 Selectivity for potassium.
Motif: 977 999 Calcium bowl.
Metal binding site: 440 440 Magnesium.
Metal binding site: 463 463 Magnesium.
Metal binding site: 465 465 Magnesium.
Metal binding site: 986 986 Calcium; via carbonyl oxygen.
Metal binding site: 989 989 Calcium; via carbonyl oxygen.
Metal binding site: 992 992 Calcium.
Metal binding site: 994 994 Calcium.
Protein Length
1209 AA.
Protein Sequence
(Canonical)
MANGGGGGGG GSSGSSGGGG GGGGGETALR MSSNIHANHL SLDASSSSSS SSSSSSSSSS  60
SVHEPKMDAL IIPVTMEVPC DSRGQRMWWA FLASSMVTFF GGLFIILLWR TLKYLWTVCC  120
HCGGKTKEAQ KINNGSSQAD GTLKPVDEKE EVVAAEVGWM TSVKDWAGVM ISAQTLTGRV  180
LVVLVFALSI GALVIYFIDS SNPIESCQNF YKDFTLQIDM AFNVFFLLYF GLRFIAANDK  240
LWFWLEVNSV VDFFTVPPVF VSVYLNRSWL GLRFLRALRL IQFSEILQFL NILKTSNSIK  300
LVNLLSIFIS TWLTAAGFIH LVENSGDPWE NFQNNQALTY WECVYLLMVT MSTVGYGDVY  360
AKTTLGRLFM VFFILGGLAM FASYVPEIIE LIGNRKKYGG SYSAVSGRKH IVVCGHITLE  420
SVSNFLKDFL HKDRDDVNVE IVFLHNISPN LELEALFKRH FTQVEFYQGS VLNPHDLARV  480
KIESADACLI LANKYCADPD AEDASNIMRV ISIKNYHPKI RIITQMLQYH NKAHLLNIPS  540
WNWKEGDDAI CLAELKLGFI AQSCLAQGLS TMLANLFSMR SFIKIEEDTW QKYYLEGVSN  600
EMYTEYLSSA FVGLSFPTVC ELCFVKLKLL MIAIEYKSAN RESRSRKRIL INPGNHLKIQ  660
EGTLGFFIAS DAKEVKRAFF YCKACHDDVT DPKRIKKCGC RRLEDEQPPT LSPKKKQRNG  720
GMRNSPNTSP KLMRHDPLLI PGNDQIDNMD SNVKKYDSTG MFHWCAPKEI EKVILTRSEA  780
AMTVLSGHVV VCIFGDVSSA LIGLRNLVMP LRASNFHYHE LKHIVFVGSI EYLKREWETL  840
HNFPKVSILP GTPLSRADLR AVNINLCDMC VILSANQNNI DDTSLQDKEC ILASLNIKSM  900
QFDDSIGVLQ ANSQGFTPPG MDRSSPDNSP VHGMLRQPSI TTGVNIPIIT ELAKPGKLPL  960
VSVNQEKNSG THILMITELV NDTNVQFLDQ DDDDDPDTEL YLTQPFACGT AFAVSVLDSL  1020
MSATYFNDNI LTLIRTLVTG GATPELEALI AEENALRGGY STPQTLANRD RCRVAQLALL  1080
DGPFADLGDG GCYGDLFCKA LKTYNMLCFG IYRLRDAHLS TPSQCTKRYV ITNPPYEFEL  1140
VPTDLIFCLM QFDHNAGQSR ASLSHSSHSS QSSSKKSSSV HSIPSTANRP NRPKSRESRD  1200
KQKKEMVYR                                                          1209
Protein Sequence
(Isoform 8)
MANGGGGGGG GSSGSSGGGG GGGGGETALR MSSNIHANHL SLDASSSSSS SSSSSSSSSS  60
SVHEPKMDAL IIPVTMEVPC DSRGQRMWWA FLASSMVTFF GGLFIILLWR TLKYLWTVCC  120
HCGGKTKEAQ KINNGSSQAD GTLKPVDEKE EVVAAEVGWM TSVKDWAGVM ISAQTLTGRV  180
LVVLVFALSI GALVIYFIDS SNPIESCQNF YKDFTLQIDM AFNVFFLLYF GLRFIAANDK  240
LWFWLEVNSV VDFFTVPPVF VSVYLNRSWL GLRFLRALRL IQFSEILQFL NILKTSNSIK  300
LVNLLSIFIS TWLTAAGFIH LVENSGDPWE NFQNNQALTY WECVYLLMVT MSTVGYGDVY  360
AKTTLGRLFM VFFILGGLAM FASYVPEIIE LIGNRKKYGG SYSAVSGRKH IVVCGHITLE  420
SVSNFLKDFL HKDRDDVNVE IVFLHNISPN LELEALFKRH FTQVEFYQGS VLNPHDLARV  480
KIESADACLI LANKYCADPD AEDASNIMRV ISIKNYHPKI RIITQMLQYH NKAHLLNIPS  540
WNWKEGDDAI CLAELKLGFI AQSCLAQGLS TMLANLFSMR SFIKIEEDTW QKYYLEGVSN  600
EMYTEYLSSA FVGLSFPTVC ELCFVKLKLL MIAIEYKSAN RESRSRKRIL INPGNHLKIQ  660
EGTLGFFIAS DAKEVKRAFF YCKACHDDVT DPKRIKKCGC RRLIYSKMSI YKRMSRACCF  720
DCGRSERDCS CMSGRVRGNV DTLERNFPLS SVSVNDCSTS FRAFEDEQPP TLSPKKKQRN  780
GGMRNSPNTS PKLMRHDPLL IPGNDQIDNM DSNVKKYDST GMFHWCAPKE IEKVILTRSE  840
AAMTVLSGHV VVCIFGDVSS ALIGLRNLVM PLRASNFHYH ELKHIVFVGS IEYLKREWET  900
LHNFPKVSIL PGTPLSRADL RAVNINLCDM CVILSANQNN IDDTSLQDKE CILASLNIKS  960
MQFDDSIGVL QANSQGFTPP GMDRSSPDNS PVHGMLRQPS ITTGVNIPII TELVNDTNVQ  1020
FLDQDDDDDP DTELYLTQPF ACGTAFAVSV LDSLMSATYF NDNILTLIRT LVTGGATPEL  1080
EALIAEENAL RGGYSTPQTL ANRDRCRVAQ LALLDGPFAD LGDGGCYGDL FCKALKTYNM  1140
LCFGIYRLRD AHLSTPSQCT KRYVITNPPY EFELVPTDLI FCLMQFDHNA GQSRASLSHS  1200
SHSSQSSSKK SSSVHSIPST ANRPNRPKSR ESRDKQKKEM VYR                    1243
FASTA
(Canonical)
>LipidDB-10116-00637|Q62976
MANGGGGGGGGSSGSSGGGGGGGGGETALRMSSNIHANHLSLDASSSSSSSSSSSSSSSS
SVHEPKMDALIIPVTMEVPCDSRGQRMWWAFLASSMVTFFGGLFIILLWRTLKYLWTVCC
HCGGKTKEAQKINNGSSQADGTLKPVDEKEEVVAAEVGWMTSVKDWAGVMISAQTLTGRV
LVVLVFALSIGALVIYFIDSSNPIESCQNFYKDFTLQIDMAFNVFFLLYFGLRFIAANDK
LWFWLEVNSVVDFFTVPPVFVSVYLNRSWLGLRFLRALRLIQFSEILQFLNILKTSNSIK
LVNLLSIFISTWLTAAGFIHLVENSGDPWENFQNNQALTYWECVYLLMVTMSTVGYGDVY
AKTTLGRLFMVFFILGGLAMFASYVPEIIELIGNRKKYGGSYSAVSGRKHIVVCGHITLE
SVSNFLKDFLHKDRDDVNVEIVFLHNISPNLELEALFKRHFTQVEFYQGSVLNPHDLARV
KIESADACLILANKYCADPDAEDASNIMRVISIKNYHPKIRIITQMLQYHNKAHLLNIPS
WNWKEGDDAICLAELKLGFIAQSCLAQGLSTMLANLFSMRSFIKIEEDTWQKYYLEGVSN
EMYTEYLSSAFVGLSFPTVCELCFVKLKLLMIAIEYKSANRESRSRKRILINPGNHLKIQ
EGTLGFFIASDAKEVKRAFFYCKACHDDVTDPKRIKKCGCRRLEDEQPPTLSPKKKQRNG
GMRNSPNTSPKLMRHDPLLIPGNDQIDNMDSNVKKYDSTGMFHWCAPKEIEKVILTRSEA
AMTVLSGHVVVCIFGDVSSALIGLRNLVMPLRASNFHYHELKHIVFVGSIEYLKREWETL
HNFPKVSILPGTPLSRADLRAVNINLCDMCVILSANQNNIDDTSLQDKECILASLNIKSM
QFDDSIGVLQANSQGFTPPGMDRSSPDNSPVHGMLRQPSITTGVNIPIITELAKPGKLPL
VSVNQEKNSGTHILMITELVNDTNVQFLDQDDDDDPDTELYLTQPFACGTAFAVSVLDSL
MSATYFNDNILTLIRTLVTGGATPELEALIAEENALRGGYSTPQTLANRDRCRVAQLALL
DGPFADLGDGGCYGDLFCKALKTYNMLCFGIYRLRDAHLSTPSQCTKRYVITNPPYEFEL
VPTDLIFCLMQFDHNAGQSRASLSHSSHSSQSSSKKSSSVHSIPSTANRPNRPKSRESRD
KQKKEMVYR
FASTA
(Isoform 8)
>LipidDB-10116-00637|Q62976-8
MANGGGGGGGGSSGSSGGGGGGGGGETALRMSSNIHANHLSLDASSSSSSSSSSSSSSSS
SVHEPKMDALIIPVTMEVPCDSRGQRMWWAFLASSMVTFFGGLFIILLWRTLKYLWTVCC
HCGGKTKEAQKINNGSSQADGTLKPVDEKEEVVAAEVGWMTSVKDWAGVMISAQTLTGRV
LVVLVFALSIGALVIYFIDSSNPIESCQNFYKDFTLQIDMAFNVFFLLYFGLRFIAANDK
LWFWLEVNSVVDFFTVPPVFVSVYLNRSWLGLRFLRALRLIQFSEILQFLNILKTSNSIK
LVNLLSIFISTWLTAAGFIHLVENSGDPWENFQNNQALTYWECVYLLMVTMSTVGYGDVY
AKTTLGRLFMVFFILGGLAMFASYVPEIIELIGNRKKYGGSYSAVSGRKHIVVCGHITLE
SVSNFLKDFLHKDRDDVNVEIVFLHNISPNLELEALFKRHFTQVEFYQGSVLNPHDLARV
KIESADACLILANKYCADPDAEDASNIMRVISIKNYHPKIRIITQMLQYHNKAHLLNIPS
WNWKEGDDAICLAELKLGFIAQSCLAQGLSTMLANLFSMRSFIKIEEDTWQKYYLEGVSN
EMYTEYLSSAFVGLSFPTVCELCFVKLKLLMIAIEYKSANRESRSRKRILINPGNHLKIQ
EGTLGFFIASDAKEVKRAFFYCKACHDDVTDPKRIKKCGCRRLIYSKMSIYKRMSRACCF
DCGRSERDCSCMSGRVRGNVDTLERNFPLSSVSVNDCSTSFRAFEDEQPPTLSPKKKQRN
GGMRNSPNTSPKLMRHDPLLIPGNDQIDNMDSNVKKYDSTGMFHWCAPKEIEKVILTRSE
AAMTVLSGHVVVCIFGDVSSALIGLRNLVMPLRASNFHYHELKHIVFVGSIEYLKREWET
LHNFPKVSILPGTPLSRADLRAVNINLCDMCVILSANQNNIDDTSLQDKECILASLNIKS
MQFDDSIGVLQANSQGFTPPGMDRSSPDNSPVHGMLRQPSITTGVNIPIITELVNDTNVQ
FLDQDDDDDPDTELYLTQPFACGTAFAVSVLDSLMSATYFNDNILTLIRTLVTGGATPEL
EALIAEENALRGGYSTPQTLANRDRCRVAQLALLDGPFADLGDGGCYGDLFCKALKTYNM
LCFGIYRLRDAHLSTPSQCTKRYVITNPPYEFELVPTDLIFCLMQFDHNAGQSRASLSHS
SHSSQSSSKKSSSVHSIPSTANRPNRPKSRESRDKQKKEMVYR
Gene Ontology
GO:0016324; C:apical plasma membrane; IBA:RefGenome
GO:0030425; C:dendrite; IDA:RGD
GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW
GO:0009897; C:external side of plasma membrane; IDA:RGD
GO:0043025; C:neuronal cell body; IDA:RGD
GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD
GO:0005886; C:plasma membrane; IDA:RGD
GO:0048787; C:presynaptic active zone membrane; IDA:RGD
GO:0043234; C:protein complex; IDA:RGD
GO:0008076; C:voltage-gated potassium channel complex; IBA:RefGenome
GO:0015269; F:calcium-activated potassium channel activity; IDA:RGD
GO:0060072; F:large conductance calcium-activated potassium channel activity; IDA:RGD
GO:0046872; F:metal ion binding; IEA:UniProtKB-KW
GO:0032403; F:protein complex binding; IPI:RGD
GO:0042803; F:protein homodimerization activity; IDA:RGD
GO:0005249; F:voltage-gated potassium channel activity; IBA:RefGenome
GO:0071805; P:potassium ion transmembrane transport; IBA:RefGenome
GO:0051289; P:protein homotetramerization; IDA:RGD
GO:0042312; P:regulation of vasodilation; IDA:RGD
GO:0051592; P:response to calcium ion; IDA:RGD
GO:0031960; P:response to corticosteroid; IDA:RGD
GO:0043627; P:response to estrogen; IDA:RGD
GO:0001666; P:response to hypoxia; IDA:RGD
GO:0009268; P:response to pH; IDA:RGD
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;