| UniProt ID | KCMA1_CHICK | |
|---|---|---|
| UniProt AC | Q8AYS8 | |
| Protein Name | Calcium-activated potassium channel subunit alpha-1 | |
| Gene Name | KCNMA1 | |
| Organism | Gallus gallus (Chicken). | |
| Sequence Length | 1137 | |
| Subcellular Localization |
Membrane Multi-pass membrane protein. |
|
| Protein 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).. | |
| Protein Sequence | MSNNINANNLNTDSSSSPVNVPKMDALIIPVTMEVPCDSRGQRMWWAFLASSMVTFFGGLFIILLWRTLKYLWTVCCHCGVKNKEAQKINGGGDTQADGACKPTDEKEENVAAEVGWMTSVKDWAGVMISAQTLTGRVLVVLVFALSIGALVIYFIDSSNPIESCQNFYKDFTLQIDMAFNVFFLLYFGLRFIAANDKLWFWLEVNSVVDFFTVPPVFVSVYLNRSWLGLRFLRALRLIQFSEILQFLNILKTSNSIKLVNLCSIFISTWLTAAGFIHLVENSGDPWENFQNNQQLTYWECVYLLMVTMSTVGYGDVYAKTTLGRLFMVFFILGGLAMFASYVPEIIELIGNRKKYGGSYSAVSGRKHIVVCGHITLESVSNFLKDFLHKDRDDVNVEIVFLHNISPNLELEALFKRHFTQVEFYQGSVLNPHDLARVKIESADACLILANKYCADPDAEDASNIMRVISIKNYHPKIRIITQMLQYHNKAHLLNIPSWNWKEGDDAICLAELKLGFIAQSCLAPGLSTMLANLFSMRSFIKIEEDTWQKYYLEGVANEMYTEYLSSAFVGLSFPAVCELVFAKLKLLMIAIEYKSEKRESSILINPGNHVKIQEGTLGFFIASDAKEVKRAFFYCKACHDDITDPKRIKKCGCKRLEDEQPSTLSPKKKQRNGGMRNSPNSSPKLMRHDPLLIPGNEQIDNMDANVKKYDSTGMFHWCPAKDIEKVILTRSEAAMTVLSGHVVVCIFGDVKSALIGLRNLVMPLRASNFHYHELKHIVFVGSLEYLRREWETLHNFPKVSILPGTPLSRADLRAVNINLCDMCVILSANQNNIDDASLQDKECILASLNIKSMQFDDSIGVLQANSQGFTPPGMDRSSPDNSPVHGLLRQPSITTGANIPIITELVNDSNVQFLDQDDDDDPDTELYLTQPFACGTAFAVSVLDSLMSATYFNDNILTLIRTLVTGGATPELEALIAEENALRGGYSTPQTLANRDRCRVAQLALYDGPFADLGDGGCYGDLFCKALKTYNMLCFGIYRLRDAHLSTPSQCTKRYVITNPPYEFELVPTDLIFCLMQFDHNAGQSRASLSHSSHSSYSSSKKSSSVHSIPSTANRPNRTKTRDSREKQKYVQEDRL | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 871 | Phosphorylation | QANSQGFTPPGMDRS ECCCCCCCCCCCCCC | 35.08 | - | |
| 883 | Phosphorylation | DRSSPDNSPVHGLLR CCCCCCCCCCCCHHC | 35.36 | - | |
| 989 | Phosphorylation | ALRGGYSTPQTLANR HHCCCCCCHHHHCCH | 15.78 | - |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
| 871 | T | Phosphorylation | Kinase | CDK5 | Q00535 | PSP |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of KCMA1_CHICK !! | ||||||
* Distance = the distance between SAP position and PTM sites.
| Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
|---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of KCMA1_CHICK !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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