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Q08460

- KCMA1_MOUSE

UniProt

Q08460 - KCMA1_MOUSE

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Protein
Calcium-activated potassium channel subunit alpha-1
Gene
Kcnma1, Kcnma
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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. 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).1 Publication

Enzyme regulationi

Ethanol and carbon monoxide-bound heme increase channel activation. Heme inhibits channel activation By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi439 – 4391Magnesium Inferred
Metal bindingi462 – 4621Magnesium Inferred
Metal bindingi464 – 4641Magnesium Inferred
Metal bindingi985 – 9851Calcium; via carbonyl oxygen By similarity
Metal bindingi988 – 9881Calcium; via carbonyl oxygen By similarity
Metal bindingi991 – 9911Calcium By similarity
Metal bindingi993 – 9931Calcium By similarity

GO - Molecular functioni

  1. calcium-activated potassium channel activity Source: MGI
  2. large conductance calcium-activated potassium channel activity Source: UniProt
  3. metal ion binding Source: UniProtKB-KW
  4. potassium channel activity Source: MGI
  5. protein binding Source: IntAct
  6. voltage-gated potassium channel activity Source: MGI

GO - Biological processi

  1. adult walking behavior Source: MGI
  2. auditory receptor cell differentiation Source: MGI
  3. cell maturation Source: MGI
  4. circadian rhythm Source: MGI
  5. eye blink reflex Source: MGI
  6. locomotor rhythm Source: MGI
  7. micturition Source: MGI
  8. negative regulation of cell volume Source: MGI
  9. neuromuscular process controlling balance Source: MGI
  10. neuronal action potential Source: MGI
  11. potassium ion transmembrane transport Source: RefGenome
  12. potassium ion transport Source: MGI
  13. protein homooligomerization Source: MGI
  14. regulation of aldosterone metabolic process Source: MGI
  15. regulation of membrane potential Source: MGI
  16. relaxation of vascular smooth muscle Source: MGI
  17. response to hypoxia Source: MGI
  18. saliva secretion Source: MGI
  19. sensory perception of sound Source: MGI
  20. smooth muscle contraction involved in micturition Source: MGI
  21. synaptic transmission Source: MGI
  22. vasodilation Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Ion channel, Potassium channel, Voltage-gated channel

Keywords - Biological processi

Ion transport, Potassium transport, Transport

Keywords - Ligandi

Calcium, Magnesium, Metal-binding, Potassium

Names & Taxonomyi

Protein namesi
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
Short name:
mSlo1
Slowpoke homolog
Short name:
Slo homolog
Short name:
mSlo
Gene namesi
Name:Kcnma1
Synonyms:Kcnma
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Unplaced

Organism-specific databases

MGIiMGI:99923. Kcnma1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 8686Extracellular Reviewed prediction
Add
BLAST
Transmembranei87 – 10721Helical; Name=Segment S0; Reviewed prediction
Add
BLAST
Topological domaini108 – 17871Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei179 – 19921Helical; Name=Segment S1; Reviewed prediction
Add
BLAST
Topological domaini200 – 21415Extracellular Reviewed prediction
Add
BLAST
Transmembranei215 – 23521Helical; Name=Segment S2; Reviewed prediction
Add
BLAST
Topological domaini236 – 2394Cytoplasmic Reviewed prediction
Transmembranei240 – 26021Helical; Name=Segment S3; Reviewed prediction
Add
BLAST
Topological domaini261 – 2644Extracellular Reviewed prediction
Transmembranei265 – 28521Helical; Voltage-sensor; Name=Segment S4; Reviewed prediction
Add
BLAST
Topological domaini286 – 30015Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei301 – 32121Helical; Name=Segment S5; Reviewed prediction
Add
BLAST
Topological domaini322 – 33514Extracellular Reviewed prediction
Add
BLAST
Intramembranei336 – 35823Pore-forming; Name=P region; Reviewed prediction
Add
BLAST
Topological domaini359 – 3679Extracellular Reviewed prediction
Transmembranei368 – 38821Helical; Name=Segment S6; Reviewed prediction
Add
BLAST
Topological domaini389 – 1209821Cytoplasmic Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. apical plasma membrane Source: MGI
  2. cytoplasm Source: MGI
  3. endoplasmic reticulum Source: MGI
  4. external side of plasma membrane Source: MGI
  5. integral component of membrane Source: MGI
  6. plasma membrane Source: MGI
  7. postsynaptic membrane Source: MGI
  8. terminal bouton Source: MGI
  9. voltage-gated potassium channel complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi151 – 1511V → T: Loss of phosphorylation-independent activation of channel activity by ethanol. CaMK2-dependent phosphorylation leads to populations of partially phosphorylated tetramers with a range of responses to ethanol from activation to inhibition. 1 Publication
Mutagenesisi272 – 2721R → Q: Alters the voltage-dependent gating. 1 Publication
Mutagenesisi278 – 2781R → Q: Alters the voltage-dependent gating. 1 Publication
Mutagenesisi284 – 2841E → R: Alters the voltage-dependent gating; when associated with R-287. 1 Publication
Mutagenesisi287 – 2871Q → R: Alters the voltage-dependent gating; when associated with K-284. 1 Publication
Mutagenesisi427 – 4271D → A: Does not affect sensitivity to Ca(2+). 1 Publication
Mutagenesisi432 – 4321D → A: Reduced sensitivity to Ca(2+). 1 Publication
Mutagenesisi434 – 4341D → A: Does not affect sensitivity to Ca(2+). 1 Publication
Mutagenesisi439 – 4391E → A: Abolishes sensitivity to Mg(2+), but not sensitivity to Ca(2+). 1 Publication
Mutagenesisi444 – 4441H → G: Reduces sensitivity to Mg(2+), but not sensitivity to Ca(2+). 1 Publication
Mutagenesisi461 – 4611T → A: Reduces sensitivity to Mg(2+), but not sensitivity to Ca(2+). 1 Publication
Mutagenesisi462 – 4621Q → C: Reduces sensitivity to Mg(2+), but not sensitivity to Ca(2+). 1 Publication
Mutagenesisi464 – 4641E → D or A: Remains sensitive to Mg(2+). 2 Publications
Mutagenesisi464 – 4641E → N: Abolishes sensitivity to Mg(2+), but not sensitivity to Ca(2+). 2 Publications
Mutagenesisi992 – 9965DDDPD → AAAAA: Alters calcium binding. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12091209Calcium-activated potassium channel subunit alpha-1
PRO_0000054134Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi118 – 1181S-palmitoyl cysteine By similarity
Lipidationi119 – 1191S-palmitoyl cysteine By similarity
Lipidationi121 – 1211S-palmitoyl cysteine By similarity

Post-translational modificationi

Phosphorylated Inferred. Phosphorylation by kinases such as PKA and/or PKG. In smooth muscles, phosphorylation affects its activity.
Palmitoylation by ZDHHC22 and ZDHHC23 within the intracellular linker between the S0 and S1 transmembrane domains regulates localization to the plasma membrane. Depalmitoylated by LYPLA1 and LYPLAL1, leading to retard exit from the trans-Golgi network By similarity.

Keywords - PTMi

Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

PaxDbiQ08460.
PRIDEiQ08460.

PTM databases

PhosphoSiteiQ08460.

Expressioni

Gene expression databases

GenevestigatoriQ08460.

Interactioni

Subunit structurei

Homotetramer; which constitutes the calcium-activated potassium channel. Interacts with beta subunits KCNMB1, KCNMB2, KCNMB3 and KCNMB4. Interacts with gamma subunits LRRC26, LRRC38, LRRC52 and LRRC55. Beta and gamma subunits are accessory, and modulate its activity By similarity. Interacts with RAB11B.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Actg1P632604EBI-1633915,EBI-351301
Anxa5P480364EBI-1633915,EBI-1184119
Apoa1Q006234EBI-1633915,EBI-1634106
ATP1B1P082515EBI-1633915,EBI-7206371From a different organism.
Calm3P622044EBI-1633915,EBI-397460
CRKLP461095EBI-1633915,EBI-910From a different organism.
CTTNQ142473EBI-1633915,EBI-351886From a different organism.
CttnQ605982EBI-1633915,EBI-397955
GapdhP168583EBI-1633915,EBI-444871
GRAP2O757913EBI-1633915,EBI-740418From a different organism.
HpcaP840753EBI-1633915,EBI-2128343
Lin7cO889524EBI-1633915,EBI-821316
MpzP275734EBI-1633915,EBI-1634589
YwhagP619824EBI-1633915,EBI-359843

Protein-protein interaction databases

BioGridi200913. 1 interaction.
IntActiQ08460. 192 interactions.
MINTiMINT-1203219.

Structurei

3D structure databases

ProteinModelPortaliQ08460.
SMRiQ08460. Positions 161-1155.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini415 – 558144RCK N-terminal
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni556 – 57621Segment S7
Add
BLAST
Regioni613 – 63321Segment S8
Add
BLAST
Regioni681 – 6855Heme-binding motif
Regioni783 – 80321Segment S9
Add
BLAST
Regioni1005 – 102521Segment S10
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi352 – 3554Selectivity for potassium
Motifi976 – 99823Calcium bowl
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi4 – 107Poly-Gly
Compositional biasi13 – 2311Poly-Gly
Add
BLAST
Compositional biasi40 – 6021Poly-Ser
Add
BLAST

Domaini

The S0 segment is essential for the modulation by the accessory beta subunits KCNMB1, KCNMB2, KCNMB3 and KCNMB4.
The S4 segment, which is characterized by a series of positively charged amino acids at every third position, is part of the voltage-sensor.
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.
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+.
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.
The heme-binding motif mediates inhibition of channel activation by heme. Carbon monoxide-bound heme leads to increased channel activation By similarity.

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1226.
HOGENOMiHOG000019856.
HOVERGENiHBG052222.
KOiK04936.
PhylomeDBiQ08460.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR005821. Ion_trans_dom.
IPR003091. K_chnl.
IPR003929. K_chnl_Ca-activ_BK_asu.
IPR016040. NAD(P)-bd_dom.
IPR003148. RCK_N.
[Graphical view]
PfamiPF03493. BK_channel_a. 1 hit.
PF00520. Ion_trans. 1 hit.
PF02254. TrkA_N. 1 hit.
[Graphical view]
PRINTSiPR01449. BKCHANNELA.
PR00169. KCHANNEL.

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. Align

Note: May be partially controlled by hormonal stress. Additional isoforms seem to exist.

Isoform 1 (identifier: Q08460-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MANGGGGGGG SSGGGGGGGG GSGLRMSSNI HANNLSLDAS SSSSSSSSSS     50
SSSSSSSSSS VHEPKMDALI IPVTMEVPCD SRGQRMWWAF LASSMVTFFG 100
GLFIILLWRT LKYLWTVCCH CGGKTKEAQK INNGSSQADG TLKPVDEKEE 150
VVAAEVGWMT SVKDWAGVMI SAQTLTGRVL VVLVFALSIG ALVIYFIDSS 200
NPIESCQNFY KDFTLQIDMA FNVFFLLYFG LRFIAANDKL WFWLEVNSVV 250
DFFTVPPVFV SVYLNRSWLG LRFLRALRLI QFSEILQFLN ILKTSNSIKL 300
VNLLSIFIST WLTAAGFIHL VENSGDPWEN FQNNQALTYW ECVYLLMVTM 350
STVGYGDVYA KTTLGRLFMV FFILGGLAMF ASYVPEIIEL IGNRKKYGGS 400
YSAVSGRKHI VVCGHITLES VSNFLKDFLH KDRDDVNVEI VFLHNISPNL 450
ELEALFKRHF TQVEFYQGSV LNPHDLARVK IESADACLIL ANKYCADPDA 500
EDASNIMRVI SIKNYHPKIR IITQMLQYHN KAHLLNIPSW NWKEGDDAIC 550
LAELKLGFIA QSCLAQGLST MLANLFSMRS FIKIEEDTWQ KYYLEGVSNE 600
MYTEYLSSAF VGLSFPTVCE LCFVKLKLLM IAIEYKSANR ESRSRKRILI 650
NPGNHLKIQE GTLGFFIASD AKEVKRAFFY CKACHDDVTD PKRIKKCGCR 700
RLEDEQPPTL SPKKKQRNGG MRNSPNTSPK LMRHDPLLIP GNDQIDNMDS 750
NVKKYDSTGM FHWCAPKEIE KVILTRSEAA MTVLSGHVVV CIFGDVSSAL 800
IGLRNLVMPL RASNFHYHEL KHIVFVGSIE YLKREWETLH NFPKVSILPG 850
TPLSRADLRA VNINLCDMCV ILSANQNNID DTSLQDKECI LASLNIKSMQ 900
FDDSIGVLQA NSQGFTPPGM DRSSPDNSPV HGMLRQPSIT TGVNIPIITE 950
LAKPGKLPLV SVNQEKNSGT HILMITELVN DTNVQFLDQD DDDDPDTELY 1000
LTQPFACGTA FAVSVLDSLM SATYFNDNIL TLIRTLVTGG ATPELEALIA 1050
EENALRGGYS TPQTLANRDR CRVAQLALLD GPFADLGDGG CYGDLFCKAL 1100
KTYNMLCFGI YRLRDAHLST PSQCTKRYVI TNPPYEFELV PTDLIFCLMQ 1150
FDHNAGQSRA SLSHSSHSSQ SSSKKSSSVH SIPSTANRPN RPKSRESRDK 1200
QNRKEMVYR 1209
Length:1,209
Mass (Da):134,396
Last modified:April 13, 2004 - v2
Checksum:i9E07ABF5DCFA62DF
GO
Isoform 2 (identifier: Q08460-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-50: MANGGGGGGGSSGGGGGGGGGSGLRMSSNIHANNLSLDASSSSSSSSSSS → MELEHPKSPPYP
     643-646: Missing.
     702-702: L → LIYF
     948-974: Missing.
     1203-1209: RKEMVYR → ATRMTRMGQAEKKWFTDEPDNAYPRNIQIKPMSTHMANQINQYKSTSSLIPPIREVEDEC

Show »
Length:1,196
Mass (Da):134,573
Checksum:i1E13E02FF1398741
GO
Isoform 3 (identifier: Q08460-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     643-646: Missing.
     948-974: Missing.

Show »
Length:1,178
Mass (Da):130,968
Checksum:i99B595E2DCAC798D
GO
Isoform 4 (identifier: Q08460-4) [UniParc]FASTAAdd to Basket

Also known as: STREX-1

The sequence of this isoform differs from the canonical sequence as follows:
     643-646: Missing.
     702-702: L → PKMSIYKRMRRACCFDCGRSERDCSCMSGRVRGNVDTLERTFPLSSVSVNDCSTSFRAF
     948-974: Missing.

Show »
Length:1,236
Mass (Da):137,559
Checksum:i2063B0C61095EAB0
GO
Isoform 5 (identifier: Q08460-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-65: Missing.

Show »
Length:1,144
Mass (Da):128,691
Checksum:i6F6028D132C562E4
GO

Sequence cautioni

The sequence AAA50215.1 differs from that shown. Reason: Erroneous initiation.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 6565Missing in isoform 5.
VSP_009959Add
BLAST
Alternative sequencei1 – 5050MANGG…SSSSS → MELEHPKSPPYP in isoform 2.
VSP_009960Add
BLAST
Alternative sequencei643 – 6464Missing in isoform 2, isoform 3 and isoform 4.
VSP_009961
Alternative sequencei702 – 7021L → LIYF in isoform 2.
VSP_009962
Alternative sequencei702 – 7021L → PKMSIYKRMRRACCFDCGRS ERDCSCMSGRVRGNVDTLER TFPLSSVSVNDCSTSFRAF in isoform 4.
VSP_009963
Alternative sequencei948 – 97427Missing in isoform 2, isoform 3 and isoform 4.
VSP_009964Add
BLAST
Alternative sequencei1203 – 12097RKEMVYR → ATRMTRMGQAEKKWFTDEPD NAYPRNIQIKPMSTHMANQI NQYKSTSSLIPPIREVEDEC in isoform 2.
VSP_009965

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U09383 mRNA. Translation: AAA50215.1. Different initiation.
L16912 mRNA. Translation: AAA39746.1.
AF156674 mRNA. Translation: AAD49225.1.
AF465244 mRNA. Translation: AAL69971.1.
PIRiA48206.
I49017.
RefSeqiNP_001240294.1. NM_001253365.1.
NP_001240298.1. NM_001253369.1.
NP_034740.2. NM_010610.3.
UniGeneiMm.343607.
Mm.486347.

Genome annotation databases

GeneIDi16531.
KEGGimmu:16531.
UCSCiuc007sme.3. mouse. [Q08460-4]
uc007smh.2. mouse. [Q08460-1]
uc007smi.2. mouse. [Q08460-3]
uc029sfy.1. mouse. [Q08460-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U09383 mRNA. Translation: AAA50215.1 . Different initiation.
L16912 mRNA. Translation: AAA39746.1 .
AF156674 mRNA. Translation: AAD49225.1 .
AF465244 mRNA. Translation: AAL69971.1 .
PIRi A48206.
I49017.
RefSeqi NP_001240294.1. NM_001253365.1.
NP_001240298.1. NM_001253369.1.
NP_034740.2. NM_010610.3.
UniGenei Mm.343607.
Mm.486347.

3D structure databases

ProteinModelPortali Q08460.
SMRi Q08460. Positions 161-1155.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 200913. 1 interaction.
IntActi Q08460. 192 interactions.
MINTi MINT-1203219.

Chemistry

ChEMBLi CHEMBL2800.
GuidetoPHARMACOLOGYi 380.

PTM databases

PhosphoSitei Q08460.

Proteomic databases

PaxDbi Q08460.
PRIDEi Q08460.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 16531.
KEGGi mmu:16531.
UCSCi uc007sme.3. mouse. [Q08460-4 ]
uc007smh.2. mouse. [Q08460-1 ]
uc007smi.2. mouse. [Q08460-3 ]
uc029sfy.1. mouse. [Q08460-2 ]

Organism-specific databases

CTDi 3778.
MGIi MGI:99923. Kcnma1.

Phylogenomic databases

eggNOGi COG1226.
HOGENOMi HOG000019856.
HOVERGENi HBG052222.
KOi K04936.
PhylomeDBi Q08460.

Miscellaneous databases

ChiTaRSi KCNMA1. mouse.
NextBioi 289945.
PROi Q08460.
SOURCEi Search...

Gene expression databases

Genevestigatori Q08460.

Family and domain databases

Gene3Di 3.40.50.720. 1 hit.
InterProi IPR005821. Ion_trans_dom.
IPR003091. K_chnl.
IPR003929. K_chnl_Ca-activ_BK_asu.
IPR016040. NAD(P)-bd_dom.
IPR003148. RCK_N.
[Graphical view ]
Pfami PF03493. BK_channel_a. 1 hit.
PF00520. Ion_trans. 1 hit.
PF02254. TrkA_N. 1 hit.
[Graphical view ]
PRINTSi PR01449. BKCHANNELA.
PR00169. KCHANNEL.
ProtoNeti Search...

Publicationsi

  1. "Cloning and characterization of human and mouse homologs of the Drosophila calcium-activated potassium channel gene, slowpoke."
    Pallanck L., Ganetzky B.
    Hum. Mol. Genet. 3:1239-1243(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Brain.
  2. "mSlo, a complex mouse gene encoding 'maxi' calcium-activated potassium channels."
    Butler A., Tsunoda S., McCobb D.P., Wei A., Salkoff L.
    Science 261:221-224(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 26-1209 (ISOFORMS 2 AND 5), FUNCTION.
    Tissue: Brain.
  3. "CaM kinase II phosphorylation of slo Thr107 regulates activity and ethanol responses of BK channels."
    Liu J., Asuncion-Chin M., Liu P., Dopico A.M.
    Nat. Neurosci. 9:41-49(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF VAL-151.
  4. "Molecular components of large conductance calcium-activated potassium (BK) channels in mouse pituitary corticotropes."
    Shipston M.J., Duncan R.R., Clark A.G., Antoni F.A., Tian L.
    Mol. Endocrinol. 13:1728-1737(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 66-1209 (ISOFORM 4).
    Tissue: Pituitary anterior lobe.
  5. "Molecular identification of Ca2+-activated K+ channels in parotid acinar cells."
    Nehrke K., Quinn C.C., Begenisich T.
    Am. J. Physiol. 284:C535-C546(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 66-1209 (ISOFORM 3).
    Strain: NIH Swiss.
    Tissue: Parotid gland.
  6. "A novel nervous system beta subunit that downregulates human large conductance calcium-dependent potassium channels."
    Weiger T.M., Holmqvist M.H., Levitan I.B., Clark F.T., Sprague S., Huang W.-J., Ge P., Wang C., Lawson D., Jurman M.E., Glucksmann M.A., Silos-Santiago I., DiStefano P.S., Curtis R.
    J. Neurosci. 20:3563-3570(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH KCNMB3.
  7. "Allosteric linkage between voltage and Ca(2+)-dependent activation of BK-type mslo1 K(+) channels."
    Cui J., Aldrich R.W.
    Biochemistry 39:15612-15619(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF ARG-272; ARG-278; GLU-284 AND GLN-287.
  8. "Elimination of the BK(Ca) channel's high-affinity Ca(2+) sensitivity."
    Bao L., Rapin A.M., Holmstrand E.C., Cox D.H.
    J. Gen. Physiol. 120:173-189(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: CALCIUM-BINDING, MUTAGENESIS OF 992-ASP--ASP-996.
  9. "Mechanism of magnesium activation of calcium-activated potassium channels."
    Shi J., Krishnamoorthy G., Yang Y., Hu L., Chaturvedi N., Harilal D., Qin J., Cui J.
    Nature 418:876-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: MAGNESIUM-BINDING, MUTAGENESIS OF GLU-439; HIS-444; THR-461; GLN-462 AND GLU-464.
  10. "Multiple regulatory sites in large-conductance calcium-activated potassium channels."
    Xia X.-M., Zeng X., Lingle C.J.
    Nature 418:880-884(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: CALCIUM-BINDING, MAGNESIUM-BINDING, MUTAGENESIS OF ASP-427; ASP-432; ASP-434 AND GLU-464.
  11. "The large conductance calcium-activated K(+) channel interacts with the small GTPase Rab11b."
    Sokolowski S., Harvey M., Sakai Y., Jordan A., Sokolowski B.
    Biochem. Biophys. Res. Commun. 426:221-225(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RAB11B.

Entry informationi

Entry nameiKCMA1_MOUSE
AccessioniPrimary (citable) accession number: Q08460
Secondary accession number(s): Q64703, Q8VHF1, Q9R196
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: April 13, 2004
Last modified: July 9, 2014
This is version 141 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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+.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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