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Calcium-activated potassium channel subunit alpha-1 (BK channel) (BKCA alpha) (Calcium-activated potassium channel, subfamily M subunit alpha-1) (K(VCA)alpha) (KCa1.1) (Maxi K channel) (MaxiK) (Slo-alpha) (Slo1) (Slowpoke homolog) (Slo homolog) (hSlo)

 KCMA1_HUMAN             Reviewed;        1236 AA.
Q12791; F8WA96; Q12886; Q12917; Q12921; Q12960; Q13150; Q5JQ23;
Q5SQR9; Q96LG8; Q9UBB0; Q9UCX0; Q9UQK6;
13-APR-2004, integrated into UniProtKB/Swiss-Prot.
13-APR-2004, sequence version 2.
22-NOV-2017, entry version 177.
RecName: Full=Calcium-activated potassium channel subunit alpha-1;
AltName: Full=BK channel;
AltName: Full=BKCA alpha;
AltName: Full=Calcium-activated potassium channel, subfamily M subunit alpha-1;
AltName: Full=K(VCA)alpha;
AltName: Full=KCa1.1;
AltName: Full=Maxi K channel;
Short=MaxiK;
AltName: Full=Slo-alpha;
AltName: Full=Slo1;
AltName: Full=Slowpoke homolog;
Short=Slo homolog;
Short=hSlo;
Name=KCNMA1; Synonyms=KCNMA, SLO;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
TISSUE=Substantia nigra;
PubMed=7877450; DOI=10.1016/0169-328X(94)90203-8;
Dworetzky S.I., Trojnacki J.T., Gribkoff V.K.;
"Cloning and expression of a human large-conductance calcium-activated
potassium channel.";
Brain Res. Mol. Brain Res. 27:189-193(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
TISSUE=Aortic smooth muscle, and Umbilical smooth muscle;
PubMed=7573516;
McCobb D.P., Fowler N.L., Featherstone T., Lingle C.J., Saito M.,
Krause J.E., Salkoff L.;
"A human calcium-activated potassium channel gene expressed in
vascular smooth muscle.";
Am. J. Physiol. 269:H767-H777(1995).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164054; DOI=10.1038/nature02462;
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 5 AND 6).
TISSUE=Cerebellum, Neuroectoderm, and Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 17-1236 (ISOFORM 5).
PubMed=7993625; DOI=10.1016/0896-6273(94)90418-9;
Tseng-Crank J., Foster C.D., Krause J.D., Mertz R., Godinot N.,
DiChiara T.J., Reinhart P.H.;
"Cloning, expression, and distribution of functionally distinct
Ca(2+)-activated K+ channel isoforms from human brain.";
Neuron 13:1315-1330(1994).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 21-1236 (ISOFORM 5).
TISSUE=Myometrium;
PubMed=12434576;
Mazzone J.N., Kaiser R.A., Buxton I.L.O.;
"Calcium-activated potassium channel expression in human myometrium:
effect of pregnancy.";
Proc. West. Pharmacol. Soc. 45:184-186(2002).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 21-1236 (ISOFORM 1), AND NUCLEOTIDE
SEQUENCE [MRNA] OF 25-1236 (ISOFORM 2).
TISSUE=Heart;
Naruse K.;
"BK variant from human heart.";
Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 24-670 (ISOFORM 3), AND NUCLEOTIDE
SEQUENCE [MRNA] OF 323-1236 (ISOFORM 4).
TISSUE=Muscle;
PubMed=7987297; DOI=10.1093/hmg/3.8.1239;
Pallanck L., Ganetzky B.;
"Cloning and characterization of human and mouse homologs of the
Drosophila calcium-activated potassium channel gene, slowpoke.";
Hum. Mol. Genet. 3:1239-1243(1994).
[10]
NUCLEOTIDE SEQUENCE [MRNA] OF 25-1236 (ISOFORM 5).
TISSUE=Lens epithelium;
Rae J.L., Shepard A.R.;
"Identification of potassium channels in human lens epithelium.";
(In) Civan M.M. (eds.);
Current topics in membranes. The eye's aqueous humor - from secretion
to glaucoma, pp.45:69-104, Academic Press, San Diego (1998).
[11]
NUCLEOTIDE SEQUENCE [MRNA] OF 38-1236 (ISOFORM 5), AND NUCLEOTIDE
SEQUENCE [MRNA] OF 693-764 (ISOFORM 4).
TISSUE=Myometrium;
PubMed=8821792;
Wallner M., Meera P., Ottolia M., Kaczorowski G.J., Latorre R.,
Garcia M.L., Stefani E., Toro L.;
"Characterization of and modulation by a beta-subunit of a human maxi
KCa channel cloned from myometrium.";
Recept. Channels 3:185-199(1995).
[12]
NUCLEOTIDE SEQUENCE [MRNA] OF 66-1236 (ISOFORM 5).
TISSUE=Pulmonary artery;
Cairns V.R., Aebly M.R., Rusch N.J.;
"Cloning and characterization of BKCA alpha subunit from human
pulmonary artery.";
Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
[13]
ALTERNATIVE SPLICING (ISOFORM 7), AND TISSUE SPECIFICITY.
TISSUE=Glioblastoma;
PubMed=11880513;
Liu X., Chang Y., Reinhart P.H., Sontheimer H., Chang Y.;
"Cloning and characterization of glioma BK, a novel BK channel isoform
highly expressed in human glioma cells.";
J. Neurosci. 22:1840-1849(2002).
[14]
ERRATUM.
Liu X., Chang Y., Reinhart P.H., Sontheimer H., Chang Y.;
J. Neurosci. 22:1B-1B(2002).
[15]
DOMAIN S0.
PubMed=8962157; DOI=10.1073/pnas.93.25.14922;
Wallner M., Meera P., Toro L.;
"Determinant for beta-subunit regulation in high-conductance voltage-
activated and Ca(2+)-sensitive K+ channels: an additional
transmembrane region at the N-terminus.";
Proc. Natl. Acad. Sci. U.S.A. 93:14922-14927(1996).
[16]
MEMBRANE TOPOLOGY.
PubMed=9391153; DOI=10.1073/pnas.94.25.14066;
Meera P., Wallner M., Song M., Toro L.;
"Large conductance voltage- and calcium-dependent K+ channel, a
distinct member of voltage-dependent ion channels with seven N-
terminal transmembrane segments (S0-S6), an extracellular N-terminus,
and an intracellular (S9-S10) C-terminus.";
Proc. Natl. Acad. Sci. U.S.A. 94:14066-14071(1997).
[17]
DOMAIN S4, AND MUTAGENESIS OF LEU-269; ARG-272; ARG-275; ARG-278;
GLN-281 AND GLU-284.
PubMed=9829973; DOI=10.1074/jbc.273.49.32430;
Diaz L., Meera P., Amigo J., Stefani E., Alvarez O., Toro L.,
Latorre R.;
"Role of the S4 segment in a voltage-dependent calcium-sensitive
potassium (hSlo) channel.";
J. Biol. Chem. 273:32430-32436(1998).
[18]
INTERACTION WITH KCNMB2.
PubMed=10097176; DOI=10.1073/pnas.96.7.4137;
Wallner M., Meera P., Toro L.;
"Molecular basis of fast inactivation in voltage and Ca2+-activated K+
channels: a transmembrane beta-subunit homolog.";
Proc. Natl. Acad. Sci. U.S.A. 96:4137-4142(1999).
[19]
INTERACTION WITH KCNMB3 AND KCNMB4.
PubMed=10692449; DOI=10.1074/jbc.275.9.6453;
Brenner R., Jegla T.J., Wickenden A., Liu Y., Aldrich R.W.;
"Cloning and functional characterization of novel large conductance
calcium-activated potassium channel beta subunits, hKCNMB3 and
hKCNMB4.";
J. Biol. Chem. 275:6453-6461(2000).
[20]
HOMOTETRAMERIZATION, AND MUTAGENESIS OF 354-GLY--GLY-356.
PubMed=11604135; DOI=10.1016/S0896-6273(01)00444-5;
Quirk J.C., Reinhart P.H.;
"Identification of a novel tetramerization domain in large conductance
K(ca) channels.";
Neuron 32:13-23(2001).
[21]
INTERACTION WITH KCNMB1; KCNMB2; KCNMB3 AND KCNMB4.
PubMed=11880485;
Wang Y.-W., Ding J.-P., Xia X.-M., Lingle C.J.;
"Consequences of the stoichiometry of Slo1 alpha and auxiliary beta
subunits on functional properties of large-conductance Ca2+-activated
K+ channels.";
J. Neurosci. 22:1550-1561(2002).
[22]
ENZYME REGULATION, AND MUTAGENESIS OF CYS-680 AND HIS-681.
PubMed=14523450; DOI=10.1038/nature02003;
Tang X.D., Xu R., Reynolds M.F., Garcia M.L., Heinemann S.H.,
Hoshi T.;
"Haem can bind to and inhibit mammalian calcium-dependent Slo1 BK
channels.";
Nature 425:531-535(2003).
[23]
REVIEW.
PubMed=12566537; DOI=10.1085/jgp.20028721;
Magleby K.L.;
"Gating mechanism of BK (Slo1) channels: so near, yet so far.";
J. Gen. Physiol. 121:81-96(2003).
[24]
SUBCELLULAR LOCATION, PALMITOYLATION AT CYS-118; CYS-119 AND CYS-121,
AND MUTAGENESIS OF CYS-118; CYS-119 AND CYS-121.
PubMed=20693285; DOI=10.1074/jbc.M110.153940;
Jeffries O., Geiger N., Rowe I.C., Tian L., McClafferty H., Chen L.,
Bi D., Knaus H.G., Ruth P., Shipston M.J.;
"Palmitoylation of the S0-S1 linker regulates cell surface expression
of voltage- and calcium-activated potassium (BK) channels.";
J. Biol. Chem. 285:33307-33314(2010).
[25]
SUBCELLULAR LOCATION, PALMITOYLATION AT CYS-118; CYS-119 AND CYS-121,
DEPALMITOYLATION, AND MUTAGENESIS OF CYS-118; CYS-119 AND CYS-121.
PubMed=22399288; DOI=10.1074/jbc.M111.335547;
Tian L., McClafferty H., Knaus H.G., Ruth P., Shipston M.J.;
"Distinct acyl protein transferases and thioesterases control surface
expression of calcium-activated potassium channels.";
J. Biol. Chem. 287:14718-14725(2012).
[26]
INTERACTION WITH LRRC26.
PubMed=20613726; DOI=10.1038/nature09162;
Yan J., Aldrich R.W.;
"LRRC26 auxiliary protein allows BK channel activation at resting
voltage without calcium.";
Nature 466:513-516(2010).
[27]
MUTAGENESIS OF THR-352; PHE-380; ALA-381 AND VAL-384.
PubMed=20430843; DOI=10.1124/jpet.110.166017;
Gordon E., Semus S.F., Lozinskaya I.M., Lin Z., Xu X.;
"Characterizing the role of Thr352 in the inhibition of the large
conductance Ca2+-activated K+ channels by 1-[1-Hexyl-6-(methyloxy)-1H-
indazol-3-yl]-2-methyl-1-propanone.";
J. Pharmacol. Exp. Ther. 334:402-409(2010).
[28]
INTERACTION WITH GAMMA SUBUNITS LRRC26; LRRC38; LRRC52 AND LRRC55.
PubMed=22547800; DOI=10.1073/pnas.1205435109;
Yan J., Aldrich R.W.;
"BK potassium channel modulation by leucine-rich repeat-containing
proteins.";
Proc. Natl. Acad. Sci. U.S.A. 109:7917-7922(2012).
[29]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 406-1179, CALCIUM-BINDING
SITES, AND SUBUNIT.
PubMed=20508092; DOI=10.1126/science.1190414;
Yuan P., Leonetti M.D., Pico A.R., Hsiung Y., MacKinnon R.;
"Structure of the human BK channel Ca2+-activation apparatus at 3.0 A
resolution.";
Science 329:182-186(2010).
[30]
VARIANT PNKD3 GLY-434.
PubMed=15937479; DOI=10.1038/ng1585;
Du W., Bautista J.F., Yang H., Diez-Sampedro A., You S.-A., Wang L.,
Kotagal P., Lueders H.O., Shi J., Cui J., Richerson G.B., Wang Q.K.;
"Calcium-sensitive potassium channelopathy in human epilepsy and
paroxysmal movement disorder.";
Nat. Genet. 37:733-738(2005).
[31]
VARIANTS PNKD3 LYS-884 AND SER-1053.
PubMed=26195193; DOI=10.1002/mds.26216;
Zhang Z.B., Tian M.Q., Gao K., Jiang Y.W., Wu Y.;
"De novo KCNMA1 mutations in children with early-onset paroxysmal
dyskinesia and developmental delay.";
Mov. Disord. 30:1290-1292(2015).
-!- FUNCTION: Potassium channel activated by both membrane
depolarization or increase in cytosolic Ca(2+) that mediates
export of K(+). It is also activated by the concentration of
cytosolic Mg(2+). Its activation dampens the excitatory events
that elevate the cytosolic Ca(2+) 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 Ca(2+), 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).
-!- ENZYME REGULATION: Ethanol and carbon monoxide-bound heme increase
channel activation. Heme inhibits channel activation.
{ECO:0000269|PubMed:14523450}.
-!- SUBUNIT: Homotetramer; which constitutes the calcium-activated
potassium channel. Interacts with RAB11B (By similarity).
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.
{ECO:0000250, ECO:0000269|PubMed:10097176,
ECO:0000269|PubMed:10692449, ECO:0000269|PubMed:11880485,
ECO:0000269|PubMed:20508092, ECO:0000269|PubMed:20613726,
ECO:0000269|PubMed:22547800}.
-!- INTERACTION:
Q6NXK8-1:Asic1 (xeno); NbExp=2; IntAct=EBI-1220676, EBI-15686410;
Q2I0M4:LRRC26; NbExp=3; IntAct=EBI-1220676, EBI-15863320;
P21731-3:TBXA2R; NbExp=7; IntAct=EBI-15861807, EBI-15885629;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20693285,
ECO:0000269|PubMed:22399288}; Multi-pass membrane protein
{ECO:0000269|PubMed:20693285, ECO:0000269|PubMed:22399288}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=7;
Comment=May be partially controlled by hormonal stress.
Additional isoforms seem to exist.;
Name=1; Synonyms=SAKCA;
IsoId=Q12791-1; Sequence=Displayed;
Name=2; Synonyms=BKTM;
IsoId=Q12791-2; Sequence=VSP_009955, VSP_009958;
Name=3;
IsoId=Q12791-3; Sequence=VSP_009954;
Name=4; Synonyms=hbr5;
IsoId=Q12791-4; Sequence=VSP_009956;
Name=5;
IsoId=Q12791-5; Sequence=VSP_009955;
Name=6;
IsoId=Q12791-6; Sequence=VSP_009952, VSP_009953;
Note=No experimental confirmation available.;
Name=7; Synonyms=gBK;
IsoId=Q12791-7; Sequence=VSP_009957;
Note=Ref.13 (no nucleotide entry) sequence is in conflict in
positions: 726:FS->SF. {ECO:0000305};
-!- TISSUE SPECIFICITY: Widely expressed. Except in myocytes, it is
almost ubiquitously expressed. {ECO:0000269|PubMed:11880513}.
-!- DOMAIN: The S0 segment is essential for the modulation by the
accessory beta subunits KCNMB1, KCNMB2, KCNMB3 and KCNMB4.
-!- DOMAIN: The S4 segment, which is characterized by a series of
positively charged amino acids at every third position, is part of
the voltage-sensor.
-!- DOMAIN: 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.
-!- DOMAIN: The RCK N-terminal domain mediates the
homotetramerization, thereby promoting the assembly of monomers
into functional potassium channel. It includes binding sites for
Ca(2+) and Mg(2+) (By similarity). {ECO:0000250}.
-!- DOMAIN: The calcium bowl constitutes one of the Ca(2+) sensors and
probably acts as a Ca(2+)-binding site. There are however other
Ca(2+) sensors regions required for activation of the channel.
-!- DOMAIN: The heme-binding motif mediates inhibition of channel
activation by heme. Carbon monoxide-bound heme leads to increased
channel activation.
-!- PTM: Phosphorylated (Probable). Phosphorylation by kinases such as
PKA and/or PKG. In smooth muscles, phosphorylation affects its
activity. {ECO:0000305}.
-!- PTM: 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. {ECO:0000269|PubMed:20693285,
ECO:0000269|PubMed:22399288}.
-!- DISEASE: Paroxysmal nonkinesigenic dyskinesia, 3, with or without
generalized epilepsy (PNKD3) [MIM:609446]: An autosomal dominant
neurologic disorder characterized by absence seizures, generalized
tonic-clonic seizures, paroxysmal nonkinesigenic dyskinesia and
involuntary dystonic or choreiform movements. Onset is usually in
childhood. Patients may have seizures only, dyskinesia only, or
both. {ECO:0000269|PubMed:15937479, ECO:0000269|PubMed:26195193}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- 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 also contains binding sites for
Ca(2+) and Mg(2+).
-!- SIMILARITY: Belongs to the potassium channel family. Calcium-
activated (TC 1.A.1.3) subfamily. KCa1.1/KCNMA1 sub-subfamily.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA50216.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the N-terminal part.; Evidence={ECO:0000305};
Sequence=AAB65837.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAC50353.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAK91504.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAD06365.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; U13913; AAA85104.1; -; mRNA.
EMBL; U23767; AAA92290.1; -; mRNA.
EMBL; AL157833; CAI39730.1; -; Genomic_DNA.
EMBL; AL731560; CAI39730.1; JOINED; Genomic_DNA.
EMBL; AL731556; CAI39730.1; JOINED; Genomic_DNA.
EMBL; AL627447; CAI39730.1; JOINED; Genomic_DNA.
EMBL; AC021032; CAI39730.1; JOINED; Genomic_DNA.
EMBL; AC011439; CAI39730.1; JOINED; Genomic_DNA.
EMBL; AL157833; CAI39736.1; -; Genomic_DNA.
EMBL; AC011439; CAI39736.1; JOINED; Genomic_DNA.
EMBL; AC021032; CAI39736.1; JOINED; Genomic_DNA.
EMBL; AL627447; CAI39736.1; JOINED; Genomic_DNA.
EMBL; AL731556; CAI39736.1; JOINED; Genomic_DNA.
EMBL; AL731560; CAI39736.1; JOINED; Genomic_DNA.
EMBL; AL627447; CAI16162.1; -; Genomic_DNA.
EMBL; AL731560; CAI16162.1; JOINED; Genomic_DNA.
EMBL; AL731556; CAI16162.1; JOINED; Genomic_DNA.
EMBL; AC021032; CAI16162.1; JOINED; Genomic_DNA.
EMBL; AC011439; CAI16162.1; JOINED; Genomic_DNA.
EMBL; AL157833; CAI16162.1; JOINED; Genomic_DNA.
EMBL; AL627447; CAI16171.1; -; Genomic_DNA.
EMBL; AC011439; CAI16171.1; JOINED; Genomic_DNA.
EMBL; AC021032; CAI16171.1; JOINED; Genomic_DNA.
EMBL; AL157833; CAI16171.1; JOINED; Genomic_DNA.
EMBL; AL731556; CAI16171.1; JOINED; Genomic_DNA.
EMBL; AL731560; CAI16171.1; JOINED; Genomic_DNA.
EMBL; AL731556; CAI14074.1; -; Genomic_DNA.
EMBL; AC011439; CAI14074.1; JOINED; Genomic_DNA.
EMBL; AL157833; CAI14074.1; JOINED; Genomic_DNA.
EMBL; AC021032; CAI14074.1; JOINED; Genomic_DNA.
EMBL; AL731560; CAI14074.1; JOINED; Genomic_DNA.
EMBL; AL627447; CAI14074.1; JOINED; Genomic_DNA.
EMBL; AL731556; CAI14082.1; -; Genomic_DNA.
EMBL; AC011439; CAI14082.1; JOINED; Genomic_DNA.
EMBL; AC021032; CAI14082.1; JOINED; Genomic_DNA.
EMBL; AL157833; CAI14082.1; JOINED; Genomic_DNA.
EMBL; AL627447; CAI14082.1; JOINED; Genomic_DNA.
EMBL; AL731560; CAI14082.1; JOINED; Genomic_DNA.
EMBL; AL731560; CAI40870.1; -; Genomic_DNA.
EMBL; AL157833; CAI40870.1; JOINED; Genomic_DNA.
EMBL; AL731556; CAI40870.1; JOINED; Genomic_DNA.
EMBL; AC021032; CAI40870.1; JOINED; Genomic_DNA.
EMBL; AC011439; CAI40870.1; JOINED; Genomic_DNA.
EMBL; AL627447; CAI40870.1; JOINED; Genomic_DNA.
EMBL; AL731560; CAI40877.1; -; Genomic_DNA.
EMBL; AC011439; CAI40877.1; JOINED; Genomic_DNA.
EMBL; AC021032; CAI40877.1; JOINED; Genomic_DNA.
EMBL; AL157833; CAI40877.1; JOINED; Genomic_DNA.
EMBL; AL627447; CAI40877.1; JOINED; Genomic_DNA.
EMBL; AL731556; CAI40877.1; JOINED; Genomic_DNA.
EMBL; AC067745; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL607069; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL731575; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471083; EAW54599.1; -; Genomic_DNA.
EMBL; BC062659; AAH62659.1; -; mRNA.
EMBL; BC137115; AAI37116.1; -; mRNA.
EMBL; BC137137; AAI37138.1; -; mRNA.
EMBL; U11717; AAC50353.1; ALT_INIT; mRNA.
EMBL; AY040849; AAK91504.1; ALT_INIT; mRNA.
EMBL; AB113575; BAD06397.1; -; mRNA.
EMBL; AB113382; BAD06365.1; ALT_INIT; mRNA.
EMBL; U02632; AAA50173.1; -; mRNA.
EMBL; U09384; AAA50216.1; ALT_SEQ; mRNA.
EMBL; AF025999; AAB88802.1; -; mRNA.
EMBL; U11058; AAB65837.1; ALT_INIT; mRNA.
EMBL; AF118141; AAD31173.1; -; mRNA.
CCDS; CCDS53545.1; -. [Q12791-2]
CCDS; CCDS60569.1; -. [Q12791-1]
CCDS; CCDS60571.1; -. [Q12791-6]
CCDS; CCDS7352.1; -. [Q12791-5]
PIR; I38596; I38596.
PIR; S62904; S62904.
RefSeq; NP_001014797.1; NM_001014797.2.
RefSeq; NP_001154824.1; NM_001161352.1. [Q12791-1]
RefSeq; NP_001154825.1; NM_001161353.1. [Q12791-2]
RefSeq; NP_001258447.1; NM_001271518.1.
RefSeq; NP_001258451.1; NM_001271522.1. [Q12791-6]
RefSeq; NP_002238.2; NM_002247.3. [Q12791-5]
UniGene; Hs.144795; -.
UniGene; Hs.658064; -.
PDB; 2K44; NMR; -; A=257-284.
PDB; 3MT5; X-ray; 3.00 A; A=406-1179.
PDB; 3NAF; X-ray; 3.10 A; A=395-681, A=782-1182.
PDBsum; 2K44; -.
PDBsum; 3MT5; -.
PDBsum; 3NAF; -.
ProteinModelPortal; Q12791; -.
SMR; Q12791; -.
BioGrid; 109979; 11.
CORUM; Q12791; -.
DIP; DIP-29729N; -.
IntAct; Q12791; 5.
MINT; MINT-4825316; -.
BindingDB; Q12791; -.
ChEMBL; CHEMBL4304; -.
DrugBank; DB00436; Bendroflumethiazide.
DrugBank; DB00356; Chlorzoxazone.
DrugBank; DB01003; Cromoglicic acid.
DrugBank; DB01119; Diazoxide.
DrugBank; DB01159; Halothane.
DrugBank; DB00999; Hydrochlorothiazide.
DrugBank; DB00774; Hydroflumethiazide.
DrugBank; DB01110; Miconazole.
DrugBank; DB00721; Procaine.
GuidetoPHARMACOLOGY; 380; -.
iPTMnet; Q12791; -.
PhosphoSitePlus; Q12791; -.
SwissPalm; Q12791; -.
BioMuta; KCNMA1; -.
DMDM; 46396283; -.
MaxQB; Q12791; -.
PeptideAtlas; Q12791; -.
PRIDE; Q12791; -.
Ensembl; ENST00000286627; ENSP00000286627; ENSG00000156113. [Q12791-5]
Ensembl; ENST00000286628; ENSP00000286628; ENSG00000156113. [Q12791-1]
Ensembl; ENST00000434208; ENSP00000402150; ENSG00000156113. [Q12791-4]
Ensembl; ENST00000480683; ENSP00000474686; ENSG00000156113. [Q12791-6]
Ensembl; ENST00000626620; ENSP00000485867; ENSG00000156113. [Q12791-2]
Ensembl; ENST00000638575; ENSP00000492049; ENSG00000156113. [Q12791-7]
Ensembl; ENST00000638759; ENSP00000492632; ENSG00000156113. [Q12791-3]
Ensembl; ENST00000640969; ENSP00000492200; ENSG00000156113. [Q12791-4]
GeneID; 3778; -.
KEGG; hsa:3778; -.
UCSC; uc001jxm.4; human. [Q12791-1]
CTD; 3778; -.
DisGeNET; 3778; -.
EuPathDB; HostDB:ENSG00000156113.20; -.
GeneCards; KCNMA1; -.
HGNC; HGNC:6284; KCNMA1.
HPA; HPA054648; -.
MalaCards; KCNMA1; -.
MIM; 600150; gene.
MIM; 609446; phenotype.
neXtProt; NX_Q12791; -.
OpenTargets; ENSG00000156113; -.
Orphanet; 79137; Generalized epilepsy - paroxysmal dyskinesia.
PharmGKB; PA220; -.
GeneTree; ENSGT00530000063026; -.
HOVERGEN; HBG052222; -.
InParanoid; Q12791; -.
KO; K04936; -.
PhylomeDB; Q12791; -.
TreeFam; TF314283; -.
Reactome; R-HSA-1296052; Ca2+ activated K+ channels.
Reactome; R-HSA-418457; cGMP effects.
SIGNOR; Q12791; -.
ChiTaRS; KCNMA1; human.
EvolutionaryTrace; Q12791; -.
GenomeRNAi; 3778; -.
PRO; PR:Q12791; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000156113; -.
ExpressionAtlas; Q12791; baseline and differential.
Genevisible; Q12791; HS.
GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
GO; GO:0005901; C:caveola; IDA:BHF-UCL.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0008076; C:voltage-gated potassium channel complex; IDA:UniProtKB.
GO; GO:0003779; F:actin binding; IDA:BHF-UCL.
GO; GO:0015269; F:calcium-activated potassium channel activity; IDA:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0060072; F:large conductance calcium-activated potassium channel activity; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0005249; F:voltage-gated potassium channel activity; IDA:UniProtKB.
GO; GO:0030007; P:cellular potassium ion homeostasis; IDA:UniProtKB.
GO; GO:0060073; P:micturition; IDA:UniProtKB.
GO; GO:0045794; P:negative regulation of cell volume; IDA:UniProtKB.
GO; GO:0043065; P:positive regulation of apoptotic process; IMP:UniProtKB.
GO; GO:0006813; P:potassium ion transport; IDA:UniProtKB.
GO; GO:0042391; P:regulation of membrane potential; IDA:UniProtKB.
GO; GO:0051592; P:response to calcium ion; IDA:UniProtKB.
GO; GO:0034465; P:response to carbon monoxide; IDA:UniProtKB.
GO; GO:0001666; P:response to hypoxia; IDA:UniProtKB.
GO; GO:0006970; P:response to osmotic stress; IDA:UniProtKB.
GO; GO:0060083; P:smooth muscle contraction involved in micturition; IDA:UniProtKB.
InterPro; IPR024939; Ca-act_K_channel_Slo-1.
InterPro; IPR005821; Ion_trans_dom.
InterPro; IPR003929; K_chnl_BK_asu.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
InterPro; IPR028325; VG_K_chnl.
PANTHER; PTHR10027:SF28; PTHR10027:SF28; 2.
Pfam; PF03493; BK_channel_a; 1.
Pfam; PF00520; Ion_trans; 1.
PRINTS; PR00169; KCHANNEL.
SUPFAM; SSF51735; SSF51735; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Calcium; Cell membrane;
Complete proteome; Disease mutation; Epilepsy; Ion channel;
Ion transport; Lipoprotein; Magnesium; Membrane; Metal-binding;
Palmitate; Phosphoprotein; Potassium; Potassium channel;
Potassium transport; Reference proteome; Transmembrane;
Transmembrane helix; Transport; Voltage-gated channel.
CHAIN 1 1236 Calcium-activated potassium channel
subunit alpha-1.
/FTId=PRO_0000054132.
TOPO_DOM 1 86 Extracellular. {ECO:0000255}.
TRANSMEM 87 107 Helical; Name=Segment S0. {ECO:0000255}.
TOPO_DOM 108 178 Cytoplasmic. {ECO:0000255}.
TRANSMEM 179 199 Helical; Name=Segment S1. {ECO:0000255}.
TOPO_DOM 200 214 Extracellular. {ECO:0000255}.
TRANSMEM 215 235 Helical; Name=Segment S2. {ECO:0000255}.
TOPO_DOM 236 239 Cytoplasmic. {ECO:0000255}.
TRANSMEM 240 260 Helical; Name=Segment S3. {ECO:0000255}.
TOPO_DOM 261 264 Extracellular. {ECO:0000255}.
TRANSMEM 265 285 Helical; Name=Segment S4. {ECO:0000255}.
TOPO_DOM 286 300 Cytoplasmic. {ECO:0000255}.
TRANSMEM 301 321 Helical; Name=Segment S5. {ECO:0000255}.
TOPO_DOM 322 335 Extracellular. {ECO:0000255}.
INTRAMEM 336 358 Pore-forming; Name=P region.
{ECO:0000255}.
TOPO_DOM 359 367 Extracellular. {ECO:0000255}.
TRANSMEM 368 388 Helical; Name=Segment S6. {ECO:0000255}.
TOPO_DOM 389 1236 Cytoplasmic. {ECO:0000255}.
DOMAIN 415 558 RCK N-terminal.
REGION 556 576 Segment S7.
REGION 613 633 Segment S8.
REGION 677 681 Heme-binding motif.
REGION 837 857 Segment S9.
REGION 1032 1052 Segment S10.
MOTIF 352 355 Selectivity for potassium.
MOTIF 1003 1025 Calcium bowl.
COMPBIAS 4 10 Poly-Gly.
COMPBIAS 13 20 Poly-Gly.
COMPBIAS 39 60 Poly-Ser.
METAL 439 439 Magnesium. {ECO:0000250}.
METAL 462 462 Magnesium. {ECO:0000250}.
METAL 464 464 Magnesium. {ECO:0000250}.
METAL 1012 1012 Calcium; via carbonyl oxygen.
METAL 1015 1015 Calcium; via carbonyl oxygen.
METAL 1018 1018 Calcium.
METAL 1020 1020 Calcium.
MOD_RES 763 763 Phosphothreonine.
{ECO:0000250|UniProtKB:Q08460}.
MOD_RES 765 765 Phosphoserine.
{ECO:0000250|UniProtKB:Q08460}.
MOD_RES 778 778 Phosphoserine.
{ECO:0000250|UniProtKB:Q08460}.
MOD_RES 782 782 Phosphoserine.
{ECO:0000250|UniProtKB:Q08460}.
MOD_RES 970 970 Phosphothreonine.
{ECO:0000250|UniProtKB:Q08460}.
MOD_RES 978 978 Phosphoserine.
{ECO:0000250|UniProtKB:Q08460}.
MOD_RES 982 982 Phosphoserine.
{ECO:0000250|UniProtKB:Q08460}.
LIPID 118 118 S-palmitoyl cysteine.
{ECO:0000269|PubMed:20693285,
ECO:0000269|PubMed:22399288}.
LIPID 119 119 S-palmitoyl cysteine.
{ECO:0000269|PubMed:20693285,
ECO:0000269|PubMed:22399288}.
LIPID 121 121 S-palmitoyl cysteine.
{ECO:0000269|PubMed:20693285,
ECO:0000269|PubMed:22399288}.
VAR_SEQ 127 168 EAQKINNGSSQADGTLKPVDEKEEAVAAEVGWMTSVKDWAG
V -> ATHFGSPEMPPAARSWSGSPPEAAVLRGASSLALEV
ARCRRL (in isoform 6).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_009952.
VAR_SEQ 169 1236 Missing (in isoform 6).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_009953.
VAR_SEQ 643 643 R -> RSRKR (in isoform 3).
{ECO:0000303|PubMed:7987297}.
/FTId=VSP_009954.
VAR_SEQ 698 756 PKMSIYKRMRRACCFDCGRSERDCSCMSGRVRGNVDTLERA
FPLSSVSVNDCSTSFRAF -> L (in isoform 2 and
isoform 5). {ECO:0000303|PubMed:12434576,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:7573516,
ECO:0000303|PubMed:7877450,
ECO:0000303|PubMed:7993625,
ECO:0000303|PubMed:8821792,
ECO:0000303|Ref.10, ECO:0000303|Ref.12,
ECO:0000303|Ref.8}.
/FTId=VSP_009955.
VAR_SEQ 698 756 PKMSIYKRMRRACCFDCGRSERDCSCMSGRVRGNVDTLERA
FPLSSVSVNDCSTSFRAF -> LKVAARSRYSKDPFEFKKE
TPNSRLVTEPV (in isoform 4).
{ECO:0000303|PubMed:7987297,
ECO:0000303|PubMed:8821792}.
/FTId=VSP_009956.
VAR_SEQ 698 756 PKMSIYKRMRRACCFDCGRSERDCSCMSGRVRGNVDTLERA
FPLSSVSVNDCSTSFRAF -> RWEEHCSLWRLESKGNVRR
LNYCRGQQTFSVKVKVAARSRYSKDPFEFKKETPNSRLVTE
PV (in isoform 7). {ECO:0000305}.
/FTId=VSP_009957.
VAR_SEQ 828 828 L -> LVTGWMPYLGPRVLMTCLDIGVVCMPTDIQSTSPAS
IKKFKE (in isoform 2).
{ECO:0000303|Ref.8}.
/FTId=VSP_009958.
VARIANT 434 434 D -> G (in PNKD3; may have a synergistic
effect with ethanol in the triggering of
symptoms; dbSNP:rs137853333).
{ECO:0000269|PubMed:15937479}.
/FTId=VAR_023821.
VARIANT 884 884 E -> K (in PNKD3).
{ECO:0000269|PubMed:26195193}.
/FTId=VAR_079156.
VARIANT 1053 1053 N -> S (in PNKD3).
{ECO:0000269|PubMed:26195193}.
/FTId=VAR_079157.
MUTAGEN 118 118 C->A: Decreased localization to the
plasma membrane. Abolishes localization
to the plasma membrane; when associated
with A-119 and A-121.
{ECO:0000269|PubMed:20693285,
ECO:0000269|PubMed:22399288}.
MUTAGEN 119 119 C->A: Decreased localization to the
plasma membrane. Abolishes localization
to the plasma membrane; when associated
with A-118 and A-121.
{ECO:0000269|PubMed:20693285,
ECO:0000269|PubMed:22399288}.
MUTAGEN 121 121 C->A: Decreased localization to the
plasma membrane. Abolishes localization
to the plasma membrane; when associated
with A-119 and A-121.
{ECO:0000269|PubMed:20693285,
ECO:0000269|PubMed:22399288}.
MUTAGEN 269 269 L->R,H: No effect in the coupling between
calcium and channel opening.
{ECO:0000269|PubMed:9829973}.
MUTAGEN 272 272 R->E: Induces reduction in the coupling
between calcium and channel opening.
{ECO:0000269|PubMed:9829973}.
MUTAGEN 275 275 R->N: Induces reduction in the coupling
between calcium and channel opening.
{ECO:0000269|PubMed:9829973}.
MUTAGEN 278 278 R->Q: Induces reduction in the coupling
between calcium and channel opening.
{ECO:0000269|PubMed:9829973}.
MUTAGEN 281 281 Q->R: No effect in the coupling between
calcium and channel opening.
{ECO:0000269|PubMed:9829973}.
MUTAGEN 284 284 E->K: No effect in the coupling between
calcium and channel opening.
{ECO:0000269|PubMed:9829973}.
MUTAGEN 352 352 T->S: Activated at more negative
voltages. Slower rate of inactivation.
Impaired inhibition by HMIMP. No effect
on channel inhibition by Iberiotoxin.
{ECO:0000269|PubMed:20430843}.
MUTAGEN 354 356 GYG->AAA: Loss of function.
{ECO:0000269|PubMed:11604135}.
MUTAGEN 380 380 F->A: Loss of function.
{ECO:0000269|PubMed:20430843}.
MUTAGEN 381 381 A->S: Activated at more negative
voltages. No effect on inhibition by
HMIMP. {ECO:0000269|PubMed:20430843}.
MUTAGEN 384 384 V->I: No effect on activation voltage. No
effect on inhibition by HMIMP.
{ECO:0000269|PubMed:20430843}.
MUTAGEN 680 680 C->S: Loss of heme-induced channel
inhibition.
{ECO:0000269|PubMed:14523450}.
MUTAGEN 681 681 H->R: Loss of heme-induced channel
inhibition.
{ECO:0000269|PubMed:14523450}.
CONFLICT 25 25 M -> N (in Ref. 9; AAA50216).
{ECO:0000305}.
CONFLICT 35 35 S -> G (in Ref. 9; AAA50216).
{ECO:0000305}.
CONFLICT 38 38 A -> V (in Ref. 1; AAA85104).
{ECO:0000305}.
CONFLICT 449 449 N -> D (in Ref. 12; AAD31173).
{ECO:0000305}.
CONFLICT 805 805 N -> H (in Ref. 6; AAC50353).
{ECO:0000305}.
CONFLICT 1152 1152 T -> A (in Ref. 12; AAD31173).
{ECO:0000305}.
CONFLICT 1230 1236 YVQEERL -> KEMVYR (in Ref. 3; CAI39730/
CAI40870/CAI14074/CAI16162).
{ECO:0000305}.
HELIX 261 270 {ECO:0000244|PDB:2K44}.
HELIX 277 280 {ECO:0000244|PDB:2K44}.
STRAND 409 415 {ECO:0000244|PDB:3MT5}.
HELIX 418 431 {ECO:0000244|PDB:3MT5}.
TURN 433 437 {ECO:0000244|PDB:3MT5}.
STRAND 439 443 {ECO:0000244|PDB:3MT5}.
HELIX 450 453 {ECO:0000244|PDB:3MT5}.
HELIX 456 459 {ECO:0000244|PDB:3MT5}.
STRAND 461 466 {ECO:0000244|PDB:3MT5}.
STRAND 470 472 {ECO:0000244|PDB:3NAF}.
HELIX 473 478 {ECO:0000244|PDB:3MT5}.
HELIX 481 483 {ECO:0000244|PDB:3MT5}.
STRAND 485 490 {ECO:0000244|PDB:3MT5}.
HELIX 498 515 {ECO:0000244|PDB:3MT5}.
STRAND 521 526 {ECO:0000244|PDB:3MT5}.
HELIX 528 531 {ECO:0000244|PDB:3MT5}.
HELIX 532 536 {ECO:0000244|PDB:3MT5}.
TURN 542 545 {ECO:0000244|PDB:3MT5}.
STRAND 547 550 {ECO:0000244|PDB:3MT5}.
HELIX 551 564 {ECO:0000244|PDB:3MT5}.
HELIX 568 573 {ECO:0000244|PDB:3MT5}.
TURN 574 576 {ECO:0000244|PDB:3MT5}.
STRAND 586 588 {ECO:0000244|PDB:3MT5}.
HELIX 589 597 {ECO:0000244|PDB:3MT5}.
STRAND 600 605 {ECO:0000244|PDB:3MT5}.
HELIX 608 610 {ECO:0000244|PDB:3MT5}.
HELIX 615 624 {ECO:0000244|PDB:3MT5}.
STRAND 629 634 {ECO:0000244|PDB:3MT5}.
STRAND 638 640 {ECO:0000244|PDB:3NAF}.
STRAND 645 647 {ECO:0000244|PDB:3MT5}.
STRAND 659 665 {ECO:0000244|PDB:3MT5}.
HELIX 667 671 {ECO:0000244|PDB:3MT5}.
TURN 672 674 {ECO:0000244|PDB:3MT5}.
HELIX 685 689 {ECO:0000244|PDB:3NAF}.
HELIX 803 805 {ECO:0000244|PDB:3MT5}.
HELIX 823 825 {ECO:0000244|PDB:3MT5}.
HELIX 830 835 {ECO:0000244|PDB:3MT5}.
STRAND 842 847 {ECO:0000244|PDB:3MT5}.
STRAND 850 852 {ECO:0000244|PDB:3NAF}.
HELIX 858 861 {ECO:0000244|PDB:3MT5}.
HELIX 863 865 {ECO:0000244|PDB:3MT5}.
STRAND 867 869 {ECO:0000244|PDB:3NAF}.
HELIX 871 873 {ECO:0000244|PDB:3MT5}.
STRAND 877 881 {ECO:0000244|PDB:3MT5}.
HELIX 883 893 {ECO:0000244|PDB:3MT5}.
STRAND 896 904 {ECO:0000244|PDB:3MT5}.
HELIX 909 914 {ECO:0000244|PDB:3MT5}.
HELIX 917 919 {ECO:0000244|PDB:3MT5}.
STRAND 921 927 {ECO:0000244|PDB:3MT5}.
STRAND 936 938 {ECO:0000244|PDB:3NAF}.
HELIX 941 951 {ECO:0000244|PDB:3MT5}.
HELIX 996 998 {ECO:0000244|PDB:3MT5}.
STRAND 1001 1006 {ECO:0000244|PDB:3MT5}.
HELIX 1008 1011 {ECO:0000244|PDB:3MT5}.
STRAND 1016 1018 {ECO:0000244|PDB:3MT5}.
HELIX 1026 1028 {ECO:0000244|PDB:3MT5}.
HELIX 1030 1033 {ECO:0000244|PDB:3MT5}.
STRAND 1037 1039 {ECO:0000244|PDB:3MT5}.
HELIX 1040 1044 {ECO:0000244|PDB:3MT5}.
HELIX 1046 1052 {ECO:0000244|PDB:3MT5}.
HELIX 1054 1064 {ECO:0000244|PDB:3MT5}.
HELIX 1073 1079 {ECO:0000244|PDB:3MT5}.
HELIX 1089 1093 {ECO:0000244|PDB:3MT5}.
STRAND 1099 1104 {ECO:0000244|PDB:3MT5}.
TURN 1105 1107 {ECO:0000244|PDB:3MT5}.
TURN 1109 1111 {ECO:0000244|PDB:3MT5}.
HELIX 1112 1114 {ECO:0000244|PDB:3MT5}.
HELIX 1119 1129 {ECO:0000244|PDB:3MT5}.
STRAND 1133 1141 {ECO:0000244|PDB:3MT5}.
STRAND 1144 1146 {ECO:0000244|PDB:3NAF}.
STRAND 1154 1159 {ECO:0000244|PDB:3MT5}.
STRAND 1171 1176 {ECO:0000244|PDB:3MT5}.
SEQUENCE 1236 AA; 137560 MW; DF9BFEAF374BE553 CRC64;
MANGGGGGGG SSGGGGGGGG SSLRMSSNIH ANHLSLDASS SSSSSSSSSS SSSSSSSSSS
VHEPKMDALI IPVTMEVPCD SRGQRMWWAF LASSMVTFFG GLFIILLWRT LKYLWTVCCH
CGGKTKEAQK INNGSSQADG TLKPVDEKEE AVAAEVGWMT SVKDWAGVMI SAQTLTGRVL
VVLVFALSIG ALVIYFIDSS NPIESCQNFY KDFTLQIDMA FNVFFLLYFG LRFIAANDKL
WFWLEVNSVV DFFTVPPVFV SVYLNRSWLG LRFLRALRLI QFSEILQFLN ILKTSNSIKL
VNLLSIFIST WLTAAGFIHL VENSGDPWEN FQNNQALTYW ECVYLLMVTM STVGYGDVYA
KTTLGRLFMV FFILGGLAMF ASYVPEIIEL IGNRKKYGGS YSAVSGRKHI VVCGHITLES
VSNFLKDFLH KDRDDVNVEI VFLHNISPNL ELEALFKRHF TQVEFYQGSV LNPHDLARVK
IESADACLIL ANKYCADPDA EDASNIMRVI SIKNYHPKIR IITQMLQYHN KAHLLNIPSW
NWKEGDDAIC LAELKLGFIA QSCLAQGLST MLANLFSMRS FIKIEEDTWQ KYYLEGVSNE
MYTEYLSSAF VGLSFPTVCE LCFVKLKLLM IAIEYKSANR ESRILINPGN HLKIQEGTLG
FFIASDAKEV KRAFFYCKAC HDDITDPKRI KKCGCKRPKM SIYKRMRRAC CFDCGRSERD
CSCMSGRVRG NVDTLERAFP LSSVSVNDCS TSFRAFEDEQ PSTLSPKKKQ RNGGMRNSPN
TSPKLMRHDP LLIPGNDQID NMDSNVKKYD STGMFHWCAP KEIEKVILTR SEAAMTVLSG
HVVVCIFGDV SSALIGLRNL VMPLRASNFH YHELKHIVFV GSIEYLKREW ETLHNFPKVS
ILPGTPLSRA DLRAVNINLC DMCVILSANQ NNIDDTSLQD KECILASLNI KSMQFDDSIG
VLQANSQGFT PPGMDRSSPD NSPVHGMLRQ PSITTGVNIP IITELVNDTN VQFLDQDDDD
DPDTELYLTQ PFACGTAFAV SVLDSLMSAT YFNDNILTLI RTLVTGGATP ELEALIAEEN
ALRGGYSTPQ TLANRDRCRV AQLALLDGPF ADLGDGGCYG DLFCKALKTY NMLCFGIYRL
RDAHLSTPSQ CTKRYVITNP PYEFELVPTD LIFCLMQFDH NAGQSRASLS HSSHSSQSSS
KKSSSVHSIP STANRQNRPK SRESRDKQKY VQEERL


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