| Tag |
Content |
LipidDB ID |
LipidDB-9986-00991 |
Entry Name |
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UniProt Accession |
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Theoretical PI |
6.32 |
Molecular Weight |
130924.94 |
Genbank Protein ID |
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Genbank Nucleotide ID |
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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; RbSlo; Slo homolog; |
Gene Name |
KCNMA1 |
Gene Synonyms/Alias |
KCNMA; |
Created Date |
13-APR-2004 |
| Lipid Modification Sites |
|---|
| Position |
Sequence Form |
Peptide |
References |
Modification Type |
711 | Isoform 3 | YKRMRRACCFGCGRS | [1] | S-Palmitoylation | 712 | Isoform 3 | KRMRRACCFGCGRSE | [1] | S-Palmitoylation |
|
Organism |
Oryctolagus cuniculus (Rabbit) |
NCBI Taxa ID |
9986 |
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]
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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) (By similarity). |
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 1179 Cytoplasmic.
Domain: 416 559 RCK N-terminal.
Region: 557 577 Segment S7.
Region: 614 634 Segment S8.
Region: 678 682 Heme-binding motif.
Region: 780 800 Segment S9.
Region: 975 995 Segment S10.
Motif: 353 356 Selectivity for potassium.
Motif: 946 968 Calcium bowl.
Metal binding site: 440 440 Magnesium.
Metal binding site: 463 463 Magnesium.
Metal binding site: 465 465 Magnesium.
Metal binding site: 955 955 Calcium; via carbonyl oxygen.
Metal binding site: 958 958 Calcium; via carbonyl oxygen.
Metal binding site: 961 961 Calcium.
Metal binding site: 963 963 Calcium.
|
Protein Length |
1179 AA. |
Protein Sequence
(Isoform 3) |
MANGGGGGGG SSGGGGGGGG GGSGLRMSSN IHASHLSLDA SSSSSSSSSS SSSSSSSSSS 60
SVHEPKMDAL IIPVTMEVPC DSRGQRMWWA FLASSMVTFF GGLFIILLWR TLKYLWTVCC 120
HCGGKAKEAQ KINNGSSQAD GTLKPVDEKE EAVAAEVGWM 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 RESRILINPG NHLKIQEGTL 660
GFFIASDAKE VKRAFFYCKA CHDDITDPKR IKKCGCKRPK MSIYKRMRRA CCFGCGRSER 720
DCSCMSGRVR GHVDTLGRAF PLSSVSVSDC CTRFRAFEDE QPSTLSPKKK QRNGGMRNSP 780
NSSPKLMRHD PLLIPGNDQI DNMDSNVKKY DSTGMFHWCA PKEIEKVILT RSEAAMTVLS 840
GHVVVCIFGD VSSALIGLRN LVMPLRASNF HYHELKHIVF VGSIEYLKRE WETLHNFPKV 900
SILPGTPLSR ADLRAVNINL CDMCVILSAN QNNIDDTSLQ DKECILASLN IKSMQFDDSI 960
GVLQANSQGF TPPGMDRSSP DNSPVHGMLR QPSITTGVNI PIITELVNDT NVQFLDQDDD 1020
DDPDTELYLT QPFACGTAFA VSVLDSLMSA TYFNDNILTL IRTLVTGGAT PELEALIAEE 1080
NALRGGYSTP QTLANRDRCR VAQLALLDGP FADLGDGGCY GDLFCKALKT YNMLCFGIYR 1140
LRDAHLSTPS QCTKRYVITN PPYEFELVPT DLIFCLMQFD HNAGQSRASL SHSSHSSQSS 1200
SKKSSSVHSI PSTANRQNRP KSRESRDKQK YVQEERL 1237
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FASTA
(Isoform 3) |
>LipidDB-9986-00991|Q9BG98-3
MANGGGGGGGSSGGGGGGGGGGSGLRMSSNIHASHLSLDASSSSSSSSSSSSSSSSSSSS
SVHEPKMDALIIPVTMEVPCDSRGQRMWWAFLASSMVTFFGGLFIILLWRTLKYLWTVCC
HCGGKAKEAQKINNGSSQADGTLKPVDEKEEAVAAEVGWMTSVKDWAGVMISAQTLTGRV
LVVLVFALSIGALVIYFIDSSNPIESCQNFYKDFTLQIDMAFNVFFLLYFGLRFIAANDK
LWFWLEVNSVVDFFTVPPVFVSVYLNRSWLGLRFLRALRLIQFSEILQFLNILKTSNSIK
LVNLLSIFISTWLTAAGFIHLVENSGDPWENFQNNQALTYWECVYLLMVTMSTVGYGDVY
AKTTLGRLFMVFFILGGLAMFASYVPEIIELIGNRKKYGGSYSAVSGRKHIVVCGHITLE
SVSNFLKDFLHKDRDDVNVEIVFLHNISPNLELEALFKRHFTQVEFYQGSVLNPHDLARV
KIESADACLILANKYCADPDAEDASNIMRVISIKNYHPKIRIITQMLQYHNKAHLLNIPS
WNWKEGDDAICLAELKLGFIAQSCLAQGLSTMLANLFSMRSFIKIEEDTWQKYYLEGVSN
EMYTEYLSSAFVGLSFPTVCELCFVKLKLLMIAIEYKSANRESRILINPGNHLKIQEGTL
GFFIASDAKEVKRAFFYCKACHDDITDPKRIKKCGCKRPKMSIYKRMRRACCFGCGRSER
DCSCMSGRVRGHVDTLGRAFPLSSVSVSDCCTRFRAFEDEQPSTLSPKKKQRNGGMRNSP
NSSPKLMRHDPLLIPGNDQIDNMDSNVKKYDSTGMFHWCAPKEIEKVILTRSEAAMTVLS
GHVVVCIFGDVSSALIGLRNLVMPLRASNFHYHELKHIVFVGSIEYLKREWETLHNFPKV
SILPGTPLSRADLRAVNINLCDMCVILSANQNNIDDTSLQDKECILASLNIKSMQFDDSI
GVLQANSQGFTPPGMDRSSPDNSPVHGMLRQPSITTGVNIPIITELVNDTNVQFLDQDDD
DDPDTELYLTQPFACGTAFAVSVLDSLMSATYFNDNILTLIRTLVTGGATPELEALIAEE
NALRGGYSTPQTLANRDRCRVAQLALLDGPFADLGDGGCYGDLFCKALKTYNMLCFGIYR
LRDAHLSTPSQCTKRYVITNPPYEFELVPTDLIFCLMQFDHNAGQSRASLSHSSHSSQSS
SKKSSSVHSIPSTANRQNRPKSRESRDKQKYVQEERL
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Gene Ontology |
GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW GO:0005886; C:plasma membrane; IEA:UniProtKB-KW GO:0015269; F:calcium-activated potassium channel activity; IEA:InterPro GO:0046872; F:metal ion binding; IEA:UniProtKB-KW GO:0005244; F:voltage-gated ion channel activity; IEA:UniProtKB-KW |
Interpro |
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Pfam |
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SMART |
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PROSITE |
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PRINTS |
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