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Q08460 (KCMA1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 138. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Kcnma1
Synonyms:Kcnma
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1209 AA.
Sequence statusComplete.
Protein existenceEvidence 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. 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). Ref.2

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. 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. Ref.6 Ref.11

Subcellular location

Cell membrane; Multi-pass membrane protein By similarity.

Domain

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.

Post-translational modification

Phosphorylated Probable. 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.

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.

Sequence caution

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

Ontologies

Keywords
   Biological processIon transport
Potassium transport
Transport
   Cellular componentCell membrane
Membrane
   Coding sequence diversityAlternative splicing
   DomainTransmembrane
Transmembrane helix
   LigandCalcium
Magnesium
Metal-binding
Potassium
   Molecular functionIon channel
Potassium channel
Voltage-gated channel
   PTMLipoprotein
Palmitate
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processadult walking behavior

Inferred from mutant phenotype PubMed 15184377PubMed 15194823. Source: MGI

auditory receptor cell differentiation

Inferred from mutant phenotype PubMed 15328414PubMed 17074442. Source: MGI

cell maturation

Inferred from mutant phenotype PubMed 15328414. Source: MGI

circadian rhythm

Inferred from mutant phenotype PubMed 16845385. Source: MGI

eye blink reflex

Inferred from mutant phenotype PubMed 15194823. Source: MGI

locomotor rhythm

Inferred from mutant phenotype PubMed 16845385. Source: MGI

micturition

Inferred from mutant phenotype PubMed 15184377. Source: MGI

negative regulation of cell volume

Inferred from mutant phenotype PubMed 16873365. Source: MGI

neuromuscular process controlling balance

Inferred from mutant phenotype PubMed 15184377PubMed 15194823. Source: MGI

neuronal action potential

Inferred from mutant phenotype PubMed 16845385. Source: MGI

potassium ion transmembrane transport

Inferred from Biological aspect of Ancestor. Source: RefGenome

potassium ion transport

Inferred from direct assay Ref.4Ref.2. Source: MGI

protein homooligomerization

Inferred from direct assay PubMed 17303127. Source: MGI

regulation of aldosterone metabolic process

Inferred from mutant phenotype PubMed 17122062. Source: MGI

regulation of membrane potential

Inferred from direct assay Ref.2. Source: MGI

relaxation of vascular smooth muscle

Inferred from mutant phenotype PubMed 15867178. Source: MGI

response to hypoxia

Inferred from direct assay PubMed 16306267. Source: MGI

saliva secretion

Inferred from genetic interaction PubMed 16873365. Source: MGI

sensory perception of sound

Inferred from mutant phenotype PubMed 15328414PubMed 16763026. Source: MGI

smooth muscle contraction involved in micturition

Inferred from mutant phenotype PubMed 15827347. Source: MGI

synaptic transmission

Inferred from mutant phenotype PubMed 15194823. Source: MGI

vasodilation

Inferred from mutant phenotype PubMed 15867178. Source: MGI

   Cellular_componentapical plasma membrane

Inferred from direct assay PubMed 17135251. Source: MGI

cytoplasm

Inferred from direct assay PubMed 12952984. Source: MGI

endoplasmic reticulum

Inferred from direct assay PubMed 17303127. Source: MGI

external side of plasma membrane

Inferred from direct assay PubMed 17303127. Source: MGI

integral component of membrane

Inferred from direct assay Ref.5. Source: MGI

plasma membrane

Inferred from direct assay Ref.4PubMed 12952984. Source: MGI

postsynaptic membrane

Inferred from direct assay PubMed 15328414. Source: MGI

terminal bouton

Inferred from direct assay PubMed 15328414. Source: MGI

voltage-gated potassium channel complex

Inferred from genetic interaction Ref.5. Source: MGI

   Molecular_functioncalcium-activated potassium channel activity

Inferred from direct assay Ref.4PubMed 16081418PubMed 16306267PubMed 17303127Ref.2. Source: MGI

large conductance calcium-activated potassium channel activity

Inferred from direct assay Ref.5. Source: MGI

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

potassium channel activity

Inferred from mutant phenotype PubMed 17135251. Source: MGI

voltage-gated potassium channel activity

Inferred from direct assay Ref.2PubMed 16081418. Source: MGI

Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]

Note: May be partially controlled by hormonal stress. Additional isoforms seem to exist.
Isoform 1 (identifier: Q08460-1)

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: Q08460-2)

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
Isoform 3 (identifier: Q08460-3)

The sequence of this isoform differs from the canonical sequence as follows:
     643-646: Missing.
     948-974: Missing.
Isoform 4 (identifier: Q08460-4)

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.
Isoform 5 (identifier: Q08460-5)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12091209Calcium-activated potassium channel subunit alpha-1
PRO_0000054134

Regions

Topological domain1 – 8686Extracellular Potential
Transmembrane87 – 10721Helical; Name=Segment S0; Potential
Topological domain108 – 17871Cytoplasmic Potential
Transmembrane179 – 19921Helical; Name=Segment S1; Potential
Topological domain200 – 21415Extracellular Potential
Transmembrane215 – 23521Helical; Name=Segment S2; Potential
Topological domain236 – 2394Cytoplasmic Potential
Transmembrane240 – 26021Helical; Name=Segment S3; Potential
Topological domain261 – 2644Extracellular Potential
Transmembrane265 – 28521Helical; Voltage-sensor; Name=Segment S4; Potential
Topological domain286 – 30015Cytoplasmic Potential
Transmembrane301 – 32121Helical; Name=Segment S5; Potential
Topological domain322 – 33514Extracellular Potential
Intramembrane336 – 35823Pore-forming; Name=P region; Potential
Topological domain359 – 3679Extracellular Potential
Transmembrane368 – 38821Helical; Name=Segment S6; Potential
Topological domain389 – 1209821Cytoplasmic Potential
Domain415 – 558144RCK N-terminal
Region556 – 57621Segment S7
Region613 – 63321Segment S8
Region681 – 6855Heme-binding motif
Region783 – 80321Segment S9
Region1005 – 102521Segment S10
Motif352 – 3554Selectivity for potassium
Motif976 – 99823Calcium bowl
Compositional bias4 – 107Poly-Gly
Compositional bias13 – 2311Poly-Gly
Compositional bias40 – 6021Poly-Ser

Sites

Metal binding4391Magnesium Probable
Metal binding4621Magnesium Probable
Metal binding4641Magnesium Probable
Metal binding9851Calcium; via carbonyl oxygen By similarity
Metal binding9881Calcium; via carbonyl oxygen By similarity
Metal binding9911Calcium By similarity
Metal binding9931Calcium By similarity

Amino acid modifications

Lipidation1181S-palmitoyl cysteine By similarity
Lipidation1191S-palmitoyl cysteine By similarity
Lipidation1211S-palmitoyl cysteine By similarity

Natural variations

Alternative sequence1 – 6565Missing in isoform 5.
VSP_009959
Alternative sequence1 – 5050MANGG…SSSSS → MELEHPKSPPYP in isoform 2.
VSP_009960
Alternative sequence643 – 6464Missing in isoform 2, isoform 3 and isoform 4.
VSP_009961
Alternative sequence7021L → LIYF in isoform 2.
VSP_009962
Alternative sequence7021L → PKMSIYKRMRRACCFDCGRS ERDCSCMSGRVRGNVDTLER TFPLSSVSVNDCSTSFRAF in isoform 4.
VSP_009963
Alternative sequence948 – 97427Missing in isoform 2, isoform 3 and isoform 4.
VSP_009964
Alternative sequence1203 – 12097RKEMVYR → ATRMTRMGQAEKKWFTDEPD NAYPRNIQIKPMSTHMANQI NQYKSTSSLIPPIREVEDEC in isoform 2.
VSP_009965

Experimental info

Mutagenesis1511V → 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. Ref.3
Mutagenesis2721R → Q: Alters the voltage-dependent gating. Ref.7
Mutagenesis2781R → Q: Alters the voltage-dependent gating. Ref.7
Mutagenesis2841E → R: Alters the voltage-dependent gating; when associated with R-287. Ref.7
Mutagenesis2871Q → R: Alters the voltage-dependent gating; when associated with K-284. Ref.7
Mutagenesis4271D → A: Does not affect sensitivity to Ca(2+). Ref.10
Mutagenesis4321D → A: Reduced sensitivity to Ca(2+). Ref.10
Mutagenesis4341D → A: Does not affect sensitivity to Ca(2+). Ref.10
Mutagenesis4391E → A: Abolishes sensitivity to Mg(2+), but not sensitivity to Ca(2+). Ref.9
Mutagenesis4441H → G: Reduces sensitivity to Mg(2+), but not sensitivity to Ca(2+). Ref.9
Mutagenesis4611T → A: Reduces sensitivity to Mg(2+), but not sensitivity to Ca(2+). Ref.9
Mutagenesis4621Q → C: Reduces sensitivity to Mg(2+), but not sensitivity to Ca(2+). Ref.9
Mutagenesis4641E → D or A: Remains sensitive to Mg(2+). Ref.9 Ref.10
Mutagenesis4641E → N: Abolishes sensitivity to Mg(2+), but not sensitivity to Ca(2+). Ref.9 Ref.10
Mutagenesis992 – 9965DDDPD → AAAAA: Alters calcium binding. Ref.8

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified April 13, 2004. Version 2.
Checksum: 9E07ABF5DCFA62DF

FASTA1,209134,396
        10         20         30         40         50         60 
MANGGGGGGG SSGGGGGGGG GSGLRMSSNI HANNLSLDAS SSSSSSSSSS SSSSSSSSSS 

        70         80         90        100        110        120 
VHEPKMDALI IPVTMEVPCD SRGQRMWWAF LASSMVTFFG GLFIILLWRT LKYLWTVCCH 

       130        140        150        160        170        180 
CGGKTKEAQK INNGSSQADG TLKPVDEKEE VVAAEVGWMT SVKDWAGVMI SAQTLTGRVL 

       190        200        210        220        230        240 
VVLVFALSIG ALVIYFIDSS NPIESCQNFY KDFTLQIDMA FNVFFLLYFG LRFIAANDKL 

       250        260        270        280        290        300 
WFWLEVNSVV DFFTVPPVFV SVYLNRSWLG LRFLRALRLI QFSEILQFLN ILKTSNSIKL 

       310        320        330        340        350        360 
VNLLSIFIST WLTAAGFIHL VENSGDPWEN FQNNQALTYW ECVYLLMVTM STVGYGDVYA 

       370        380        390        400        410        420 
KTTLGRLFMV FFILGGLAMF ASYVPEIIEL IGNRKKYGGS YSAVSGRKHI VVCGHITLES 

       430        440        450        460        470        480 
VSNFLKDFLH KDRDDVNVEI VFLHNISPNL ELEALFKRHF TQVEFYQGSV LNPHDLARVK 

       490        500        510        520        530        540 
IESADACLIL ANKYCADPDA EDASNIMRVI SIKNYHPKIR IITQMLQYHN KAHLLNIPSW 

       550        560        570        580        590        600 
NWKEGDDAIC LAELKLGFIA QSCLAQGLST MLANLFSMRS FIKIEEDTWQ KYYLEGVSNE 

       610        620        630        640        650        660 
MYTEYLSSAF VGLSFPTVCE LCFVKLKLLM IAIEYKSANR ESRSRKRILI NPGNHLKIQE 

       670        680        690        700        710        720 
GTLGFFIASD AKEVKRAFFY CKACHDDVTD PKRIKKCGCR RLEDEQPPTL SPKKKQRNGG 

       730        740        750        760        770        780 
MRNSPNTSPK LMRHDPLLIP GNDQIDNMDS NVKKYDSTGM FHWCAPKEIE KVILTRSEAA 

       790        800        810        820        830        840 
MTVLSGHVVV CIFGDVSSAL IGLRNLVMPL RASNFHYHEL KHIVFVGSIE YLKREWETLH 

       850        860        870        880        890        900 
NFPKVSILPG TPLSRADLRA VNINLCDMCV ILSANQNNID DTSLQDKECI LASLNIKSMQ 

       910        920        930        940        950        960 
FDDSIGVLQA NSQGFTPPGM DRSSPDNSPV HGMLRQPSIT TGVNIPIITE LAKPGKLPLV 

       970        980        990       1000       1010       1020 
SVNQEKNSGT HILMITELVN DTNVQFLDQD DDDDPDTELY LTQPFACGTA FAVSVLDSLM 

      1030       1040       1050       1060       1070       1080 
SATYFNDNIL TLIRTLVTGG ATPELEALIA EENALRGGYS TPQTLANRDR CRVAQLALLD 

      1090       1100       1110       1120       1130       1140 
GPFADLGDGG CYGDLFCKAL KTYNMLCFGI YRLRDAHLST PSQCTKRYVI TNPPYEFELV 

      1150       1160       1170       1180       1190       1200 
PTDLIFCLMQ FDHNAGQSRA SLSHSSHSSQ SSSKKSSSVH SIPSTANRPN RPKSRESRDK 


QNRKEMVYR 

« Hide

Isoform 2 [UniParc].

Checksum: 1E13E02FF1398741
Show »

FASTA1,196134,573
Isoform 3 [UniParc].

Checksum: 99B595E2DCAC798D
Show »

FASTA1,178130,968
Isoform 4 (STREX-1) [UniParc].

Checksum: 2063B0C61095EAB0
Show »

FASTA1,236137,559
Isoform 5 [UniParc].

Checksum: 6F6028D132C562E4
Show »

FASTA1,144128,691

References

[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U09383 mRNA. Translation: AAA50215.1. Different initiation.
L16912 mRNA. Translation: AAA39746.1.
AF156674 mRNA. Translation: AAD49225.1.
AF465244 mRNA. Translation: AAL69971.1.
PIRA48206.
I49017.
RefSeqNP_001240294.1. NM_001253365.1.
NP_001240298.1. NM_001253369.1.
NP_034740.2. NM_010610.3.
UniGeneMm.343607.
Mm.486347.

3D structure databases

ProteinModelPortalQ08460.
SMRQ08460. Positions 223-393, 396-1155.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid200913. 1 interaction.
IntActQ08460. 192 interactions.
MINTMINT-1203219.

Chemistry

ChEMBLCHEMBL2800.
GuidetoPHARMACOLOGY380.

PTM databases

PhosphoSiteQ08460.

Proteomic databases

PaxDbQ08460.
PRIDEQ08460.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID16531.
KEGGmmu:16531.
UCSCuc007sme.3. mouse. [Q08460-4]
uc007smh.2. mouse. [Q08460-1]
uc007smi.2. mouse. [Q08460-3]
uc029sfy.1. mouse. [Q08460-2]

Organism-specific databases

CTD3778.
MGIMGI:99923. Kcnma1.

Phylogenomic databases

eggNOGCOG1226.
HOGENOMHOG000019856.
HOVERGENHBG052222.
KOK04936.
PhylomeDBQ08460.

Gene expression databases

GenevestigatorQ08460.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
InterProIPR024939. 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]
PANTHERPTHR10027:SF3. PTHR10027:SF3. 1 hit.
PfamPF03493. BK_channel_a. 1 hit.
PF00520. Ion_trans. 1 hit.
PF02254. TrkA_N. 1 hit.
[Graphical view]
PRINTSPR01449. BKCHANNELA.
PR00169. KCHANNEL.
ProtoNetSearch...

Other

ChiTaRSKCNMA1. mouse.
NextBio289945.
PROQ08460.
SOURCESearch...

Entry information

Entry nameKCMA1_MOUSE
AccessionPrimary (citable) accession number: Q08460
Secondary accession number(s): Q64703, Q8VHF1, Q9R196
Entry history
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: April 13, 2004
Last modified: April 16, 2014
This is version 138 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot