| Tag |
Content |
LipidDB ID |
LipidDB-9031-01184 |
Entry Name |
|
UniProt Accession |
|
Theoretical PI |
6.2 |
Molecular Weight |
127646.69 |
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; Slo homolog; cSlo; |
Gene Name |
KCNMA1 |
Gene Synonyms/Alias |
KCNMA; |
Created Date |
13-APR-2004 |
| Lipid Modification Sites |
|---|
| Position |
Sequence Form |
Peptide |
References |
Modification Type |
669 | Isoform 3 | YKRMKLACCFDCGRS | [1] | S-Palmitoylation | 670 | Isoform 3 | KRMKLACCFDCGRSE | [1] | S-Palmitoylation |
|
Organism |
Gallus gallus (Chicken) |
NCBI Taxa ID |
9031 |
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. Highly sensitive to both iberiotoxin (IbTx) and charybdotoxin (CTX). |
Sequence Annotation |
Topological domain: 1 44 Extracellular.
Transmembrane: 45 65 Helical; Name=Segment S0.
Topological domain: 66 137 Cytoplasmic.
Transmembrane: 138 158 Helical; Name=Segment S1.
Topological domain: 159 173 Extracellular.
Transmembrane: 174 194 Helical; Name=Segment S2.
Topological domain: 195 198 Cytoplasmic.
Transmembrane: 199 219 Helical; Name=Segment S3.
Topological domain: 220 223 Extracellular.
Transmembrane: 224 244 Helical; Voltage-sensor; Name=Segment S4.
Topological domain: 245 259 Cytoplasmic.
Transmembrane: 260 280 Helical; Name=Segment S5.
Topological domain: 281 294 Extracellular.
Topological domain: 318 326 Extracellular.
Transmembrane: 327 347 Helical; Name=Segment S6.
Topological domain: 348 1137 Cytoplasmic.
Domain: 374 517 RCK N-terminal.
Region: 515 535 Segment S7.
Region: 572 592 Segment S8.
Region: 636 640 Heme-binding motif.
Region: 738 758 Segment S9.
Region: 933 953 Segment S10.
Motif: 311 314 Selectivity for potassium.
Motif: 904 926 Calcium bowl.
Metal binding site: 398 398 Magnesium.
Metal binding site: 421 421 Magnesium.
Metal binding site: 423 423 Magnesium.
Metal binding site: 913 913 Calcium; via carbonyl oxygen.
Metal binding site: 916 916 Calcium; via carbonyl oxygen.
Metal binding site: 919 919 Calcium.
Metal binding site: 921 921 Calcium.
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Protein Length |
1137 AA. |
Protein Sequence
(Isoform 3) |
MSNNINANNL NTDSSSSPVN VPKMDALIIP VTMEVPCDSR GQRMWWAFLA SSMVTFFGGL 60
FIILLWRTLK YLWTVCCHCG VKNKEAQKIN GGGDTQADGA CKPTDEKEEN VAAEVGWMTS 120
VKDWAGVMIS AQTLTGRVLV VLVFALSIGA LVIYFIDSSN PIESCQNFYK DFTLQIDMAF 180
NVFFLLYFGL RFIAANDKLW FWLEVNSVVD FFTVPPVFVS VYLNRSWLGL RFLRALRLIQ 240
FSEILQFLNI LKTSNSIKLV NLCSIFISTW LTAAGFIHLV ENSGDPWENF QNNQQLTYWE 300
CVYLLMVTMS TVGYGDVYAK TTLGRLFMVF FILGGLAMFA SYVPEIIELI GNRKKYGGSY 360
SAVSGRKHIV VCGHITLESV SNFLKDFLHK DRDDVNVEIV FLHNISPNLE LEALFKRHFT 420
QVEFYQGSVL NPHDLARVKI ESADACLILA NKYCADPDAE DASNIMRVIS IKNYHPKIRI 480
ITQMLQYHNK AHLLNIPSWN WKEGDDAICL AELKLGFIAQ SCLAPGLSTM LANLFSMRSF 540
IKIEEDTWQK YYLEGVANEM YTEYLSSAFV GLSFPAVCEL VFAKLKLLMI AIEYKSEKRE 600
SSILINPGNH VKIQEGTLGF FIASDAKEVK RAFFYCKACH DDITDPKRIK KCGCKRPKMS 660
IYKRMKLACC FDCGRSERDC SCMSGSVHSN MDTLERAFPL SSVSVNDCST SLRAFEDEQP 720
STLSPKKKQR NGGMRNSPNS SPKLMRHDPL LIPGNEQIDN MDANVKKYDS TGMFHWCPAK 780
DIEKVILTRS EAAMTVLSGH VVVCIFGDVK SALIGLRNLV MPLRASNFHY HELKHIVFVG 840
SLEYLRREWE TLHNFPKVSI LPGTPLSRAD LRAVNINLCD MCVILSANQN NIDDASLQDK 900
ECILASLNIK SMQFDDSIGV LQANSQGFTP PGMDRSSPDN SPVHGLLRQP SITTGANIPI 960
ITELVNDSNV QFLDQDDDDD PDTELYLTQP FACGTAFAVS VLDSLMSATY FNDNILTLIR 1020
TLVTGGATPE LEALIAEENA LRGGYSTPQT LANRDRCRVA QLALYDGPFA DLGDGGCYGD 1080
LFCKALKTYN MLCFGIYRLR DAHLSTPSQC TKRYVITNPP YEFELVPTDL IFCLMQFDHN 1140
AGQSRASLSH SSHSSYSSSK KSSSVHSIPS TANRPNRTKT RDSREKQKYV QEDRL 1195
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FASTA
(Isoform 3) |
>LipidDB-9031-01184|Q8AYS8-3
MSNNINANNLNTDSSSSPVNVPKMDALIIPVTMEVPCDSRGQRMWWAFLASSMVTFFGGL
FIILLWRTLKYLWTVCCHCGVKNKEAQKINGGGDTQADGACKPTDEKEENVAAEVGWMTS
VKDWAGVMISAQTLTGRVLVVLVFALSIGALVIYFIDSSNPIESCQNFYKDFTLQIDMAF
NVFFLLYFGLRFIAANDKLWFWLEVNSVVDFFTVPPVFVSVYLNRSWLGLRFLRALRLIQ
FSEILQFLNILKTSNSIKLVNLCSIFISTWLTAAGFIHLVENSGDPWENFQNNQQLTYWE
CVYLLMVTMSTVGYGDVYAKTTLGRLFMVFFILGGLAMFASYVPEIIELIGNRKKYGGSY
SAVSGRKHIVVCGHITLESVSNFLKDFLHKDRDDVNVEIVFLHNISPNLELEALFKRHFT
QVEFYQGSVLNPHDLARVKIESADACLILANKYCADPDAEDASNIMRVISIKNYHPKIRI
ITQMLQYHNKAHLLNIPSWNWKEGDDAICLAELKLGFIAQSCLAPGLSTMLANLFSMRSF
IKIEEDTWQKYYLEGVANEMYTEYLSSAFVGLSFPAVCELVFAKLKLLMIAIEYKSEKRE
SSILINPGNHVKIQEGTLGFFIASDAKEVKRAFFYCKACHDDITDPKRIKKCGCKRPKMS
IYKRMKLACCFDCGRSERDCSCMSGSVHSNMDTLERAFPLSSVSVNDCSTSLRAFEDEQP
STLSPKKKQRNGGMRNSPNSSPKLMRHDPLLIPGNEQIDNMDANVKKYDSTGMFHWCPAK
DIEKVILTRSEAAMTVLSGHVVVCIFGDVKSALIGLRNLVMPLRASNFHYHELKHIVFVG
SLEYLRREWETLHNFPKVSILPGTPLSRADLRAVNINLCDMCVILSANQNNIDDASLQDK
ECILASLNIKSMQFDDSIGVLQANSQGFTPPGMDRSSPDNSPVHGLLRQPSITTGANIPI
ITELVNDSNVQFLDQDDDDDPDTELYLTQPFACGTAFAVSVLDSLMSATYFNDNILTLIR
TLVTGGATPELEALIAEENALRGGYSTPQTLANRDRCRVAQLALYDGPFADLGDGGCYGD
LFCKALKTYNMLCFGIYRLRDAHLSTPSQCTKRYVITNPPYEFELVPTDLIFCLMQFDHN
AGQSRASLSHSSHSSYSSSKKSSSVHSIPSTANRPNRTKTRDSREKQKYVQEDRL
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Gene Ontology |
GO:0008076; C:voltage-gated potassium channel complex; IBA:RefGenome GO:0060072; F:large conductance calcium-activated potassium channel activity; IBA:RefGenome GO:0046872; F:metal ion binding; IEA:UniProtKB-KW GO:0005249; F:voltage-gated potassium channel activity; IBA:RefGenome GO:0071805; P:potassium ion transmembrane transport; IBA:RefGenome |
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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