Protein Details: KCa1.1 (large conductance calcium-activated potassium channels)

Protein ID

ICDB_Pro_0781

Protein Name

KCa1.1 (large conductance calcium-activated potassium channels)

Gene Name

Kcnma1; Kcnma

Organism

Mus musculus (Mouse)

Length

1209 amino acids

AlphaFoldDB

AF-Q08460-F1-model_v4.pdb

Function

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

MANGGGGGGGSSGGGGGGGGGSGLRMSSNIHANNLSLDASSSSSSSSSSSSSSSSSSSSSVHEPKMDALIIPVTMEVPCDSRGQRMWWAFLASSMVTFFGGLFIILLWRTLKYLWTVCCHCGGKTKEAQKINNGSSQADGTLKPVDEKEEVVAAEVGWMTSVKDWAGVMISAQTLTGRVLVVLVFALSIGALVIYFIDSSNPIESCQNFYKDFTLQIDMAFNVFFLLYFGLRFIAANDKLWFWLEVNSVVDFFTVPPVFVSVYLNRSWLGLRFLRALRLIQFSEILQFLNILKTSNSIKLVNLLSIFISTWLTAAGFIHLVENSGDPWENFQNNQALTYWECVYLLMVTMSTVGYGDVYAKTTLGRLFMVFFILGGLAMFASYVPEIIELIGNRKKYGGSYSAVSGRKHIVVCGHITLESVSNFLKDFLHKDRDDVNVEIVFLHNISPNLELEALFKRHFTQVEFYQGSVLNPHDLARVKIESADACLILANKYCADPDAEDASNIMRVISIKNYHPKIRIITQMLQYHNKAHLLNIPSWNWKEGDDAICLAELKLGFIAQSCLAQGLSTMLANLFSMRSFIKIEEDTWQKYYLEGVSNEMYTEYLSSAFVGLSFPTVCELCFVKLKLLMIAIEYKSANRESRSRKRILINPGNHLKIQEGTLGFFIASDAKEVKRAFFYCKACHDDVTDPKRIKKCGCRRLEDEQPPTLSPKKKQRNGGMRNSPNTSPKLMRHDPLLIPGNDQIDNMDSNVKKYDSTGMFHWCAPKEIEKVILTRSEAAMTVLSGHVVVCIFGDVSSALIGLRNLVMPLRASNFHYHELKHIVFVGSIEYLKREWETLHNFPKVSILPGTPLSRADLRAVNINLCDMCVILSANQNNIDDTSLQDKECILASLNIKSMQFDDSIGVLQANSQGFTPPGMDRSSPDNSPVHGMLRQPSITTGVNIPIITELAKPGKLPLVSVNQEKNSGTHILMITELVNDTNVQFLDQDDDDDPDTELYLTQPFACGTAFAVSVLDSLMSATYFNDNILTLIRTLVTGGATPELEALIAEENALRGGYSTPQTLANRDRCRVAQLALLDGPFADLGDGGCYGDLFCKALKTYNMLCFGIYRLRDAHLSTPSQCTKRYVITNPPYEFELVPTDLIFCLMQFDHNAGQSRASLSHSSHSSQSSSKKSSSVHSIPSTANRPNRPKSRESRDKQNRKEMVYR

PDB Structures

Ligand Binding

1. DICL_CP

2. DICL_Pep

Binding Site

439;462;464;985;988;991;993

Disease

Location

DOI ID

10.1093/hmg/3.8.1239; 10.1126/science.7687074; 10.1038/nn1602; 10.1210/mend.13.10.0355; 10.1152/ajpcell.00044.2002; 10.1523/jneurosci.20-10-03563.2000; 10.1021/bi001509+; 10.1085/jgp.20028627; 10.1038/nature00941; 10.1038/nature00956; 10.1016/j.cell.2010.12.001; 10.1016/j.bbrc.2012.08.067

RefSeq

NP_001240294.1; NP_001240298.1; NP_034740.2

Feature