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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

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).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi439 – 4391MagnesiumCurated
Metal bindingi462 – 4621MagnesiumCurated
Metal bindingi464 – 4641MagnesiumCurated
Metal bindingi985 – 9851Calcium; via carbonyl oxygenBy similarity
Metal bindingi988 – 9881Calcium; via carbonyl oxygenBy similarity
Metal bindingi991 – 9911CalciumBy similarity
Metal bindingi993 – 9931CalciumBy 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. 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

Cell membrane By similarity; Multi-pass membrane protein By similarity

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-1PRO_0000054134Add
BLAST

Amino acid modifications

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

Post-translational modificationi

Phosphorylated (Probable). Phosphorylation by kinases such as PKA and/or PKG. In smooth muscles, phosphorylation affects its activity.Curated
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).By similarity

Keywords - PTMi

Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

MaxQBiQ08460.
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.By similarity2 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 223-1155.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 8686ExtracellularSequence AnalysisAdd
BLAST
Topological domaini108 – 17871CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini200 – 21415ExtracellularSequence AnalysisAdd
BLAST
Topological domaini236 – 2394CytoplasmicSequence Analysis
Topological domaini261 – 2644ExtracellularSequence Analysis
Topological domaini286 – 30015CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini322 – 33514ExtracellularSequence AnalysisAdd
BLAST
Topological domaini359 – 3679ExtracellularSequence Analysis
Topological domaini389 – 1209821CytoplasmicSequence AnalysisAdd
BLAST

Intramembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Intramembranei336 – 35823Pore-forming; Name=P regionSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei87 – 10721Helical; Name=Segment S0Sequence AnalysisAdd
BLAST
Transmembranei179 – 19921Helical; Name=Segment S1Sequence AnalysisAdd
BLAST
Transmembranei215 – 23521Helical; Name=Segment S2Sequence AnalysisAdd
BLAST
Transmembranei240 – 26021Helical; Name=Segment S3Sequence AnalysisAdd
BLAST
Transmembranei265 – 28521Helical; Voltage-sensor; Name=Segment S4Sequence AnalysisAdd
BLAST
Transmembranei301 – 32121Helical; Name=Segment S5Sequence AnalysisAdd
BLAST
Transmembranei368 – 38821Helical; Name=Segment S6Sequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni556 – 57621Segment S7Add
BLAST
Regioni613 – 63321Segment S8Add
BLAST
Regioni681 – 6855Heme-binding motif
Regioni783 – 80321Segment S9Add
BLAST
Regioni1005 – 102521Segment S10Add
BLAST

Motif

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

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi4 – 107Poly-Gly
Compositional biasi13 – 2311Poly-GlyAdd
BLAST
Compositional biasi40 – 6021Poly-SerAdd
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).By similarity

Sequence similaritiesi

Contains 1 RCK N-terminal domain.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1226.
HOGENOMiHOG000019856.
HOVERGENiHBG052222.
InParanoidiQ08460.
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

        10         20         30         40         50
MANGGGGGGG SSGGGGGGGG GSGLRMSSNI HANNLSLDAS SSSSSSSSSS
60 70 80 90 100
SSSSSSSSSS VHEPKMDALI IPVTMEVPCD SRGQRMWWAF LASSMVTFFG
110 120 130 140 150
GLFIILLWRT LKYLWTVCCH CGGKTKEAQK INNGSSQADG TLKPVDEKEE
160 170 180 190 200
VVAAEVGWMT SVKDWAGVMI SAQTLTGRVL VVLVFALSIG ALVIYFIDSS
210 220 230 240 250
NPIESCQNFY KDFTLQIDMA FNVFFLLYFG LRFIAANDKL WFWLEVNSVV
260 270 280 290 300
DFFTVPPVFV SVYLNRSWLG LRFLRALRLI QFSEILQFLN ILKTSNSIKL
310 320 330 340 350
VNLLSIFIST WLTAAGFIHL VENSGDPWEN FQNNQALTYW ECVYLLMVTM
360 370 380 390 400
STVGYGDVYA KTTLGRLFMV FFILGGLAMF ASYVPEIIEL IGNRKKYGGS
410 420 430 440 450
YSAVSGRKHI VVCGHITLES VSNFLKDFLH KDRDDVNVEI VFLHNISPNL
460 470 480 490 500
ELEALFKRHF TQVEFYQGSV LNPHDLARVK IESADACLIL ANKYCADPDA
510 520 530 540 550
EDASNIMRVI SIKNYHPKIR IITQMLQYHN KAHLLNIPSW NWKEGDDAIC
560 570 580 590 600
LAELKLGFIA QSCLAQGLST MLANLFSMRS FIKIEEDTWQ KYYLEGVSNE
610 620 630 640 650
MYTEYLSSAF VGLSFPTVCE LCFVKLKLLM IAIEYKSANR ESRSRKRILI
660 670 680 690 700
NPGNHLKIQE GTLGFFIASD AKEVKRAFFY CKACHDDVTD PKRIKKCGCR
710 720 730 740 750
RLEDEQPPTL SPKKKQRNGG MRNSPNTSPK LMRHDPLLIP GNDQIDNMDS
760 770 780 790 800
NVKKYDSTGM FHWCAPKEIE KVILTRSEAA MTVLSGHVVV CIFGDVSSAL
810 820 830 840 850
IGLRNLVMPL RASNFHYHEL KHIVFVGSIE YLKREWETLH NFPKVSILPG
860 870 880 890 900
TPLSRADLRA VNINLCDMCV ILSANQNNID DTSLQDKECI LASLNIKSMQ
910 920 930 940 950
FDDSIGVLQA NSQGFTPPGM DRSSPDNSPV HGMLRQPSIT TGVNIPIITE
960 970 980 990 1000
LAKPGKLPLV SVNQEKNSGT HILMITELVN DTNVQFLDQD DDDDPDTELY
1010 1020 1030 1040 1050
LTQPFACGTA FAVSVLDSLM SATYFNDNIL TLIRTLVTGG ATPELEALIA
1060 1070 1080 1090 1100
EENALRGGYS TPQTLANRDR CRVAQLALLD GPFADLGDGG CYGDLFCKAL
1110 1120 1130 1140 1150
KTYNMLCFGI YRLRDAHLST PSQCTKRYVI TNPPYEFELV PTDLIFCLMQ
1160 1170 1180 1190 1200
FDHNAGQSRA SLSHSSHSSQ SSSKKSSSVH SIPSTANRPN RPKSRESRDK

QNRKEMVYR
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. 1 PublicationVSP_009959Add
BLAST
Alternative sequencei1 – 5050MANGG…SSSSS → MELEHPKSPPYP in isoform 2. 1 PublicationVSP_009960Add
BLAST
Alternative sequencei643 – 6464Missing in isoform 2, isoform 3 and isoform 4. 3 PublicationsVSP_009961
Alternative sequencei702 – 7021L → LIYF in isoform 2. 1 PublicationVSP_009962
Alternative sequencei702 – 7021L → PKMSIYKRMRRACCFDCGRS ERDCSCMSGRVRGNVDTLER TFPLSSVSVNDCSTSFRAF in isoform 4. 1 PublicationVSP_009963
Alternative sequencei948 – 97427Missing in isoform 2, isoform 3 and isoform 4. 3 PublicationsVSP_009964Add
BLAST
Alternative sequencei1203 – 12097RKEMVYR → ATRMTRMGQAEKKWFTDEPD NAYPRNIQIKPMSTHMANQI NQYKSTSSLIPPIREVEDEC in isoform 2. 1 PublicationVSP_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 223-1155.
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

MaxQBi Q08460.
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.
InParanoidi Q08460.
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: October 29, 2014
This is version 143 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