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Q08460

- KCMA1_MOUSE

UniProt

Q08460 - KCMA1_MOUSE

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
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    • History
      Entry version 142 (01 Oct 2014)
      Sequence version 2 (13 Apr 2004)
      Previous versions | rss
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    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. 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

    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

    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. 2 Publications
    Mutagenesisi272 – 2721R → Q: Alters the voltage-dependent gating. 2 Publications
    Mutagenesisi278 – 2781R → Q: Alters the voltage-dependent gating. 2 Publications
    Mutagenesisi284 – 2841E → R: Alters the voltage-dependent gating; when associated with R-287. 2 Publications
    Mutagenesisi287 – 2871Q → R: Alters the voltage-dependent gating; when associated with K-284. 2 Publications
    Mutagenesisi427 – 4271D → A: Does not affect sensitivity to Ca(2+). 2 Publications
    Mutagenesisi432 – 4321D → A: Reduced sensitivity to Ca(2+). 2 Publications
    Mutagenesisi434 – 4341D → A: Does not affect sensitivity to Ca(2+). 2 Publications
    Mutagenesisi439 – 4391E → A: Abolishes sensitivity to Mg(2+), but not sensitivity to Ca(2+). 2 Publications
    Mutagenesisi444 – 4441H → G: Reduces sensitivity to Mg(2+), but not sensitivity to Ca(2+). 2 Publications
    Mutagenesisi461 – 4611T → A: Reduces sensitivity to Mg(2+), but not sensitivity to Ca(2+). 2 Publications
    Mutagenesisi462 – 4621Q → C: Reduces sensitivity to Mg(2+), but not sensitivity to Ca(2+). 2 Publications
    Mutagenesisi464 – 4641E → D or A: Remains sensitive to Mg(2+). 3 Publications
    Mutagenesisi464 – 4641E → N: Abolishes sensitivity to Mg(2+), but not sensitivity to Ca(2+). 3 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

    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 161-1155.
    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.
    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. 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 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: October 1, 2014
    This is version 142 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