Q8AYS8 (KCMA1_CHICK) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 86.
History...
Names·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Calcium-activated potassium channel subunit alpha-1 Alternative name(s): BK channel BKCA alpha Calcium-activated potassium channel, subfamily M subunit alpha-1 K(VCA)alpha KCa1.1 Maxi K channel Short name=MaxiK Slo-alpha Slo1 Slowpoke homolog Short name=Slo homolog Short name=cSlo | ||||
| Gene names |
| ||||
| Organism | Gallus gallus (Chicken) [Reference proteome] | ||||
| Taxonomic identifier | 9031 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galliformes › Phasianidae › Phasianinae › Gallus![]() |
Protein attributes
| Sequence length | 1137 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Potassium channel activated by both membrane depolarization or increase in cytosolic Ca2+ that mediates export of K+. It is also activated by the concentration of cytosolic Mg2+. Its activation dampens the excitatory events that elevate the cytosolic Ca2+ 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 Ca2+, 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). Ref.6 |
| Enzyme regulation | Ethanol and carbon monoxide-bound heme increase channel activation. Heme inhibits channel activation By similarity. |
| Subunit structure | Homotetramer; which constitutes the calcium-activated potassium channel By similarity. |
| Subcellular location | Membrane; Multi-pass membrane protein By similarity. |
| Domain | The S0 segment is essential for the modulation by the accessory beta subunits By similarity. The S4 segment, which is characterized by a series of positively charged amino acids at every third position, is part of the voltage-sensor By similarity. The pore-forming domain (also referred as P region) is imbedded into the membrane, and forms the selectivity filter of the pore. It contains the signature sequence of potassium channels that displays selectivity to potassium By similarity. The RCK N-terminal domain mediates the homotetramerization, thereby promoting the assembly of monomers into functional potassium channel. It includes binding sites for Ca2+ and Mg2+ By similarity. The calcium bowl constitutes one of the Ca2+ sensors and probably acts as a Ca2+-binding site. There are however other Ca2+ sensors regions required for activation of the channel By similarity. The heme-binding motif mediates inhibition of channel activation by heme. Carbon monoxide-bound heme leads to increased channel activation By similarity. |
| Miscellaneous | The protein was initially thought to contain two functionally distinct parts: The core channel (from the N-terminus to the S9 segment) that mediates the channel activity, and the cytoplasmic tail (from the S9 segment to the C-terminus) that mediates the calcium sensing. The situation is however more complex, since the core channel contains binding sites for Ca2+ and Mg2+. |
| Sequence similarities | Belongs to the potassium channel family. Calcium-activated (TC 1.A.1.3) subfamily. KCa1.1/KCNMA1 sub-subfamily. [View classification] Contains 1 RCK N-terminal domain. |
| Caution | It is uncertain whether Met-1 is the initiator or if the sequence starts further upstream. |
Ontologies
Binary interactions
Alternative products
| This entry describes 10 isoforms produced by alternative splicing. [Align] [Select] Note: Additional isoforms seem to exist. | ||||||
| Isoform 1 (identifier: Q8AYS8-1) This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. | ||||||
| Isoform 2 (identifier: Q8AYS8-2) The sequence of this isoform differs from the canonical sequence as follows: 602-602: S → RSRKR | ||||||
| Isoform 3 (identifier: Q8AYS8-3) The sequence of this isoform differs from the canonical sequence as follows: 657-657: L → PKMSIYKRMKLACCFDCGRSERDCSCMSGSVHSNMDTLERAFPLSSVSVNDCSTSLRAF | ||||||
| Isoform 4 (identifier: Q8AYS8-4) The sequence of this isoform differs from the canonical sequence as follows: 1130-1137: KYVQEDRL → NSTRMNRMGQEKKWFTDEPDNAYPRNIQIKPMSTHMANQINQYKSTSSLIPPIREVEDEC | ||||||
| Isoform 5 (identifier: Q8AYS8-5) Also known as: IK; The sequence of this isoform differs from the canonical sequence as follows: 906-906: L → LAKPGKLLPLVSISQEKNSGTQILMITEL | ||||||
| Isoform 6 (identifier: Q8AYS8-6) The sequence of this isoform differs from the canonical sequence as follows: 657-657: L → IYF | ||||||
| Isoform 7 (identifier: Q8AYS8-7) The sequence of this isoform differs from the canonical sequence as follows: 1-17: MSNNINANNLNTDSSSS → MKPFEVSLPPPPPS | ||||||
| Isoform 8 (identifier: Q8AYS8-8) The sequence of this isoform differs from the canonical sequence as follows: 160-160: N → KSRTADSLI | ||||||
| Isoform 9 (identifier: Q8AYS8-9) The sequence of this isoform differs from the canonical sequence as follows: 602-602: S → RSRKRYALFVTFPSNLNPTST | ||||||
| Isoform 10 (identifier: Q8AYS8-10) The sequence of this isoform differs from the canonical sequence as follows: 687-687: M → MRFSCPFLP |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 1137 | 1137 | Calcium-activated potassium channel subunit alpha-1 | PRO_0000054138 | |||||
Regions | |||||||||
| Topological domain | 1 – 44 | 44 | Extracellular Potential | ||||||
| Transmembrane | 45 – 65 | 21 | Helical; Name=Segment S0; Potential | ||||||
| Topological domain | 66 – 137 | 72 | Cytoplasmic Potential | ||||||
| Transmembrane | 138 – 158 | 21 | Helical; Name=Segment S1; Potential | ||||||
| Topological domain | 159 – 173 | 15 | Extracellular Potential | ||||||
| Transmembrane | 174 – 194 | 21 | Helical; Name=Segment S2; Potential | ||||||
| Topological domain | 195 – 198 | 4 | Cytoplasmic Potential | ||||||
| Transmembrane | 199 – 219 | 21 | Helical; Name=Segment S3; Potential | ||||||
| Topological domain | 220 – 223 | 4 | Extracellular Potential | ||||||
| Transmembrane | 224 – 244 | 21 | Helical; Voltage-sensor; Name=Segment S4; Potential | ||||||
| Topological domain | 245 – 259 | 15 | Cytoplasmic Potential | ||||||
| Transmembrane | 260 – 280 | 21 | Helical; Name=Segment S5; Potential | ||||||
| Topological domain | 281 – 294 | 14 | Extracellular Potential | ||||||
| Intramembrane | 295 – 317 | 23 | Pore-forming; Name=P region; Potential | ||||||
| Topological domain | 318 – 326 | 9 | Extracellular Potential | ||||||
| Transmembrane | 327 – 347 | 21 | Helical; Name=Segment S6; Potential | ||||||
| Topological domain | 348 – 1137 | 790 | Cytoplasmic Potential | ||||||
| Domain | 374 – 517 | 144 | RCK N-terminal | ||||||
| Region | 515 – 535 | 21 | Segment S7 | ||||||
| Region | 572 – 592 | 21 | Segment S8 | ||||||
| Region | 636 – 640 | 5 | Heme-binding motif | ||||||
| Region | 738 – 758 | 21 | Segment S9 | ||||||
| Region | 933 – 953 | 21 | Segment S10 | ||||||
| Motif | 311 – 314 | 4 | Selectivity for potassium | ||||||
| Motif | 904 – 926 | 23 | Calcium bowl | ||||||
Sites | |||||||||
| Metal binding | 398 | 1 | Magnesium By similarity | ||||||
| Metal binding | 421 | 1 | Magnesium By similarity | ||||||
| Metal binding | 423 | 1 | Magnesium By similarity | ||||||
| Metal binding | 913 | 1 | Calcium; via carbonyl oxygen By similarity | ||||||
| Metal binding | 916 | 1 | Calcium; via carbonyl oxygen By similarity | ||||||
| Metal binding | 919 | 1 | Calcium By similarity | ||||||
| Metal binding | 921 | 1 | Calcium By similarity | ||||||
Natural variations | |||||||||
| Alternative sequence | 1 – 17 | 17 | MSNNI…DSSSS → MKPFEVSLPPPPPS in isoform 7. | VSP_009983 | |||||
| Alternative sequence | 160 | 1 | N → KSRTADSLI in isoform 8. | VSP_009984 | |||||
| Alternative sequence | 602 | 1 | S → RSRKR in isoform 2. | VSP_009985 | |||||
| Alternative sequence | 602 | 1 | S → RSRKRYALFVTFPSNLNPTS T in isoform 9. | VSP_009986 | |||||
| Alternative sequence | 657 | 1 | L → PKMSIYKRMKLACCFDCGRS ERDCSCMSGSVHSNMDTLER AFPLSSVSVNDCSTSLRAF in isoform 3. | VSP_009987 | |||||
| Alternative sequence | 657 | 1 | L → IYF in isoform 6. | VSP_009988 | |||||
| Alternative sequence | 687 | 1 | M → MRFSCPFLP in isoform 10. | VSP_009989 | |||||
| Alternative sequence | 906 | 1 | L → LAKPGKLLPLVSISQEKNSG TQILMITEL in isoform 5. | VSP_009990 | |||||
| Alternative sequence | 1130 – 1137 | 8 | KYVQEDRL → NSTRMNRMGQEKKWFTDEPD NAYPRNIQIKPMSTHMANQI NQYKSTSSLIPPIREVEDEC in isoform 4. | VSP_009991 | |||||
Experimental info | |||||||||
| Sequence conflict | 96 | 1 | Q → R in AAC60378. Ref.1 | ||||||
| Sequence conflict | 397 | 1 | V → I in AAC60378. Ref.1 | ||||||
| Sequence conflict | 409 | 1 | L → P in AAC35370. Ref.4 | ||||||
| Sequence conflict | 522 | 1 | C → S in AAC60378. Ref.1 | ||||||
| Sequence conflict | 712 | 1 | S → W in BAC20639. Ref.5 | ||||||
| Sequence conflict | 937 | 1 | T → P in BAC20639. Ref.5 | ||||||
| Sequence conflict | 941 | 1 | V → D in BAC20639. Ref.5 | ||||||
| Sequence conflict | 1034 | 1 | L → F in AAC35370. Ref.4 | ||||||
Sequences
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References
| [1] | "CSlo encodes calcium-activated potassium channels in the chick's cochlea." Jiang G.J., Zidanic M., Michaels R.L., Michael T.H., Griguer C., Fuchs P.A. Proc. R. Soc. B 264:731-737(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE OF 398-1137 (ISOFORM 4). Strain: Leghorn. Tissue: Cochlear duct. |
| [2] | "Distribution of Ca2+-activated K+ channel isoforms along the tonotopic gradient of the chicken's cochlea." Rosenblatt K.P., Sun Z.-P., Heller S., Hudspeth A.J. Neuron 19:1061-1075(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4; 5; 6; 7; 8; 9 AND 10). Strain: White leghorn. Tissue: Brain. |
| [3] | "Molecular biology and electrophysiology of calcium-activated potassium channels from lens epithelium." Rae J.L., Shepard A.R. Curr. Eye Res. 17:264-275(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Strain: White leghorn. Tissue: Lens epithelium. |
| [4] | "Characterization of a newly found stretch-activated KCa,ATP channel in cultured chick ventricular myocytes." Kawakubo T., Naruse K., Matsubara T., Hotta N., Sokabe M. Am. J. Physiol. 276:H1827-H1838(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 24-1137 (ISOFORM 3). |
| [5] | "Posttranslational regulation of Ca(2+)-activated K+ currents by a target-derived factor in developing parasympathetic neurons." Subramony P., Raucher S., Dryer L., Dryer S.E. Neuron 17:115-124(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 710-973 (ISOFORM 5). |
| [6] | "A molecular mechanism for electrical tuning of cochlear hair cells." Ramanathan K., Michael T.H., Jiang G.-J., Hiel H., Fuchs P.A. Science 283:215-217(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | U23821 mRNA. Translation: AAC60378.1. U23823 mRNA. Translation: AAC60125.1. U73189 mRNA. Translation: AAB17873.1. AF087663 mRNA. Translation: AAC35370.1. AB072618 mRNA. Translation: BAC20639.1. |
| IPI | IPI00572258. IPI00573276. IPI00577303. IPI00579525. IPI00581229. IPI00588093. IPI00589569. IPI00593457. IPI00601382. IPI00963770. |
| RefSeq | NP_989555.1. NM_204224.1. |
| UniGene | Gga.3260. |
3D structure databases | |
| ProteinModelPortal | Q8AYS8. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | Q8AYS8. 107 interactions. |
| MINT | MINT-7260456. |
Proteomic databases | |
| PaxDb | Q8AYS8. |
| PRIDE | Q8AYS8. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 374065. |
| KEGG | gga:374065. |
Organism-specific databases | |
| CTD | 3778. |
Phylogenomic databases | |
| eggNOG | COG1226. |
| HOVERGEN | HBG052222. |
| InParanoid | Q8AYS8. |
| KO | K04936. |
| OrthoDB | EOG4QFWCD. |
Family and domain databases | |
| Gene3D | 3.40.50.720. 1 hit. |
| InterPro | IPR024939. Ca-act_K_channel_Slo. IPR005821. Ion_trans_dom. IPR003091. K_chnl. IPR003929. K_chnl_Ca-activ_BK_asu. IPR016040. NAD(P)-bd_dom. IPR003148. RCK_N. [Graphical view] |
| PANTHER | PTHR10027:SF3. PTHR10027:SF3. 1 hit. |
| Pfam | PF03493. BK_channel_a. 1 hit. PF00520. Ion_trans. 1 hit. PF02254. TrkA_N. 1 hit. [Graphical view] |
| PRINTS | PR01449. BKCHANNELA. PR00169. KCHANNEL. |
| PROSITE | PS51201. RCK_N. False negative. [Graphical view] |
| ProtoNet | Search... |
Other | |
| NextBio | 20813586. |
Entry information
| Entry name | KCMA1_CHICK | ||||||||
| Accession | Primary (citable) accession number: Q8AYS8 Secondary accession number(s): O12942 Q9PS76 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with
