Go Annotations as Summary Text (Tabular View) (GO Graph)

GO curators for mouse genes have assigned the following annotations to the gene product of Kcnma1. (This text reflects annotations as of Thursday, July 24, 2014.) MGI curation of this mouse gene is considered complete, including annotations derived from the biomedical literature as of July 3, 2007. If you know of any additional information regarding this mouse gene please let us know. Please supply mouse gene symbol and a PubMed ID.

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Summary from NCBI RefSeq

[Summary is not available for the mouse gene. This summary is for the human ortholog.] MaxiK channels are large conductance, voltage and calcium-sensitive potassium channels which are fundamental to the control of smooth muscle tone and neuronal excitability. MaxiK channels can be formed by 2 subunits: the pore-forming alpha subunit, which is the product of this gene, and the modulatory beta subunit. Intracellular calcium regulates the physical association between the alpha and beta subunits. Alternatively spliced transcript variants encoding different isoforms have been identified. [provided by RefSeq, Jul 2008]

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Summary text based on GO annotations supported by experimental evidence in mouse

• Researchers have inferred from direct assay, that the gene product of Kcnma1
  • participates in the following biological processes:
    • potassium ion transport ^{[1, 20]}
    • protein homooligomerization ^[7]
    • regulation of membrane potential ^[1]
    • response to hypoxia ^[8]
  • performs the following molecular functions:
    • calcium-activated potassium channel activity ^{[1, 2, 7, 8, 20]}
    • large conductance calcium-activated potassium channel activity ^[12]
    • voltage-gated potassium channel activity ^{[1, 2]}
  • is located in the following cellular components:
    • apical plasma membrane ^[15]
    • cytoplasm ^[3]
    • endoplasmic reticulum ^[7]
    • external side of plasma membrane ^[7]
    • integral component of membrane ^[12]
    • plasma membrane ^{[3, 20]}
    • postsynaptic membrane ^[17]
    • terminal bouton ^[17]
• The gene product of Kcnma1 has been shown to bind to the gene products of Actg1, Anxa5, Apoa1, Cttn, Hpca, Lin7c, Mpz, Ywhag. ^{[5, 6, 22]}
• Researchers have inferred, based on phenotypic analysis of mouse mutants, that the gene product of Kcnma1
  • participates in the following biological processes:
    • adult walking behavior ^{[10, 19]}
    • auditory receptor cell differentiation ^{[4, 17]}
    • cell maturation ^[17]
    • circadian rhythm ^[9]
    • eye blink reflex ^[19]
    • locomotor rhythm ^[9]
    • micturition ^[10]
    • negative regulation of cell volume ^[16]
    • neuromuscular process controlling balance ^{[10, 19]}
    • neuronal action potential ^[9]
    • regulation of aldosterone metabolic process ^[11]
    • regulation of ion transmembrane transport ^[10]
    • regulation of membrane potential ^{[13, 19]}
    • relaxation of vascular smooth muscle ^[18]
    • sensory perception of sound ^{[13, 17]}
    • smooth muscle contraction involved in micturition ^[21]
    • synaptic transmission ^[19]
    • vasodilation ^[18]
  • performs the following molecular functions:
    • calcium-activated potassium channel activity ^[10]
    • large conductance calcium-activated potassium channel activity ^{[14, 16]}
    • potassium channel activity ^[15]
    • voltage-gated potassium channel activity ^[10]
• Researchers have inferred, based on genetic interactions, that the gene product of Kcnma1
  • participates in the following biological processes:
    • potassium ion transmembrane transport based on interactions with Kcnn4 ^[16]
    • saliva secretion based on interactions with Kcnn4 ^[16]
  • performs the following molecular functions:
    • calcium-activated potassium channel activity based on interactions with Kcnmb1, Kcnmb4 ^[12]
    • potassium channel activity based on interactions with Kcnn4 ^[16]
  • is located in the following cellular components:
    • voltage-gated potassium channel complex based on interactions with Kcnmb1, Kcnmb4 ^[12]
• Based on the experimental annotations above, MGI curators have inferred, that the gene product of Kcnma1
  • is located in the following cellular components:
    • integral component of membrane ^[1]

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Summary text based on GO annotations supported by experimental evidence in other organisms

• From comparative sequence analysis (see table for details), MGI curators have determined that the gene product of Kcnma1:
  • participates in the following biological processes:
    • cellular potassium ion homeostasis
    • micturition
    • negative regulation of cell volume
    • positive regulation of apoptotic process
    • potassium ion transmembrane transport
    • potassium ion transport
    • protein homotetramerization
    • regulation of membrane potential
    • regulation of vasodilation
    • response to calcium ion
    • response to carbon monoxide
    • response to corticosteroid
    • response to estrogen
    • response to hypoxia
    • response to osmotic stress
    • response to pH
    • smooth muscle contraction involved in micturition
  • performs the following molecular functions:
    • actin binding
    • calcium-activated potassium channel activity
    • large conductance calcium-activated potassium channel activity
    • protein complex binding
    • protein homodimerization activity
    • voltage-gated potassium channel activity
  • is located in the following cellular components:
    • apical plasma membrane
    • caveola
    • dendrite
    • external side of plasma membrane
    • extracellular vesicular exosome
    • integral component of membrane
    • neuronal cell body
    • perinuclear region of cytoplasm
    • plasma membrane
    • presynaptic active zone membrane
    • protein complex
    • voltage-gated potassium channel complex

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Summary text based on GO annotations supported by structural data

• Kcnma1 encodes a protein or proteins that contain the following InterPro domains: F-MuLV receptor-binding, Ion transport domain, NAD(P)-binding domain, Potassium channel, calcium-activated, BK, alpha subunit, Regulator of K+ conductance, N-terminal, TLV/ENV coat polyprotein, Voltage-dependent potassium channel, indicating that the gene product:
  • participates in the following biological processes:
    • ion transport
    • transmembrane transport
  • performs the following molecular functions:
    • ion channel activity
  • is located in the following cellular components:
    • membrane

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Summary text for additional MGI annotations

• Automated translation to GO terms of SwissProt keywords that describe Kcnma1 indicates that it:
  • participates in the following biological processes:
    • ion transport
    • transport
  • performs the following molecular functions:
    • metal ion binding
    • voltage-gated ion channel activity
  • is located in the following cellular components:
    • membrane
    • viral envelope
    • virion

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References

1. Butler A et al. (1993) mSlo, a complex mouse gene encoding maxi calcium-activated potassium channels. Science, 261:221-4. (PubMed:7687074)
2. Chen L et al. (2005) Functionally diverse complement of large conductance calcium- and voltage-activated potassium channel (BK) alpha-subunits generated from a single site of splicing. J Biol Chem, 280:33599-609. (PubMed:16081418)
3. Eghbali M et al. (2003) Diminished surface clustering and increased perinuclear accumulation of large conductance Ca2+-activated K+ channel in mouse myometrium with pregnancy. J Biol Chem, 278:45311-7. (PubMed:12952984)
4. Engel J et al. (2006) Two classes of outer hair cells along the tonotopic axis of the cochlea. Neuroscience, 143:837-49. (PubMed:17074442)
5. Jha S et al. (2009) The beta1 subunit of Na+/K+-ATPase interacts with BKCa channels and affects their steady-state expression on the cell surface. FEBS Lett, 583:3109-14. (PubMed:19729011)
6. Kathiresan T et al. (2009) A protein interaction network for the large conductance Ca2+-activated K+ channel in the mouse cochlea. Mol Cell Proteomics, null:null. (PubMed:19423573)
7. Ma D et al. (2007) Differential trafficking of carboxyl isoforms of Ca(2+)-gated (Slo1) potassium channels. FEBS Lett, 581:1000-8. (PubMed:17303127)
8. McCartney CE et al. (2005) A cysteine-rich motif confers hypoxia sensitivity to mammalian large conductance voltage- and Ca-activated K (BK) channel alpha-subunits. Proc Natl Acad Sci U S A, 102:17870-6. (PubMed:16306267)
9. Meredith AL et al. (2006) BK calcium-activated potassium channels regulate circadian behavioral rhythms and pacemaker output. Nat Neurosci, 9:1041-1049. (PubMed:16845385)
10. Meredith AL et al. (2004) Overactive bladder and incontinence in the absence of the BK large conductance Ca2+-activated K+ channel. J Biol Chem, 279:36746-52. (PubMed:15184377)
11. Nagai T et al. (2006) The rewards of nicotine: regulation by tissue plasminogen activator-plasmin system through protease activated receptor-1. J Neurosci, 26:12374-83. (PubMed:17122062)
12. Nehrke K et al. (2003) Molecular identification of Ca2+-activated K+ channels in parotid acinar cells. Am J Physiol Cell Physiol, 284:C535-46. (PubMed:12388098)
13. Oliver D et al. (2006) The role of BKCa channels in electrical signal encoding in the mammalian auditory periphery. J Neurosci, 26:6181-9. (PubMed:16763026)
14. Pan NC et al. (2014) Activation of galanin receptor 2 stimulates large conductance Ca(2+)-dependent K(+) (BK) channels through the IP3 pathway in human embryonic kidney (HEK293) cells. Biochem Biophys Res Commun, 446:316-21. (PubMed:24602615)
15. Pyott SJ et al. (2007) Cochlear function in mice lacking the BK channel alpha, beta1, or beta4 subunits. J Biol Chem, 282:3312-24. (PubMed:17135251)
16. Romanenko V et al. (2006) Molecular identification and physiological roles of parotid acinar cell maxi-K channels. J Biol Chem, 281:27964-72. (PubMed:16873365)
17. Ruttiger L et al. (2004) Deletion of the Ca2+-activated potassium (BK) alpha-subunit but not the BKbeta1-subunit leads to progressive hearing loss. Proc Natl Acad Sci U S A, 101:12922-7. (PubMed:15328414)
18. Sausbier M et al. (2005) Elevated blood pressure linked to primary hyperaldosteronism and impaired vasodilation in BK channel-deficient mice. Circulation, 112:60-8. (PubMed:15867178)
19. Sausbier M et al. (2004) Cerebellar ataxia and Purkinje cell dysfunction caused by Ca2+-activated K+ channel deficiency. Proc Natl Acad Sci U S A, 101:9474-8. (PubMed:15194823)
20. Shipston MJ et al. (1999) Molecular components of large conductance calcium-activated potassium (BK) channels in mouse pituitary corticotropes. Mol Endocrinol, 13:1728-37. (PubMed:10517674)
21. Thorneloe KS et al. (2005) Urodynamic properties and neurotransmitter dependence of urinary bladder contractility in the BK channel deletion model of overactive bladder. Am J Physiol Renal Physiol, 289:F604-10. (PubMed:15827347)
22. Tian L et al. (2006) A noncanonical SH3 domain binding motif links BK channels to the actin cytoskeleton via the SH3 adapter cortactin. FASEB J, 20:2588-90. (PubMed:17065230)

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Gene Ontology Evidence Code Abbreviations:

EXP Inferred from experiment

IC Inferred by curator

IDA Inferred from direct assay

IEA Inferred from electronic annotation

IGI Inferred from genetic interaction

IMP Inferred from mutant phenotype

IPI Inferred from physical interaction

ISS Inferred from sequence or structural similarity

ISO Inferred from sequence orthology

ISA Inferred from sequence alignment

ISM Inferred from sequence model

NAS Non-traceable author statement

ND No biological data available

RCA Reviewed computational analysis

TAS Traceable author statement

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