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Database: UniProt
Entry: KCMA1_HUMAN
LinkDB: KCMA1_HUMAN
Original site: KCMA1_HUMAN 
ID   KCMA1_HUMAN             Reviewed;        1236 AA.
AC   Q12791; F8WA96; Q12886; Q12917; Q12921; Q12960; Q13150; Q5JQ23;
AC   Q5SQR9; Q96LG8; Q9UBB0; Q9UCX0; Q9UQK6;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   13-APR-2004, sequence version 2.
DT   22-NOV-2017, entry version 177.
DE   RecName: Full=Calcium-activated potassium channel subunit alpha-1;
DE   AltName: Full=BK channel;
DE   AltName: Full=BKCA alpha;
DE   AltName: Full=Calcium-activated potassium channel, subfamily M subunit alpha-1;
DE   AltName: Full=K(VCA)alpha;
DE   AltName: Full=KCa1.1;
DE   AltName: Full=Maxi K channel;
DE            Short=MaxiK;
DE   AltName: Full=Slo-alpha;
DE   AltName: Full=Slo1;
DE   AltName: Full=Slowpoke homolog;
DE            Short=Slo homolog;
DE            Short=hSlo;
GN   Name=KCNMA1; Synonyms=KCNMA, SLO;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
RC   TISSUE=Substantia nigra;
RX   PubMed=7877450; DOI=10.1016/0169-328X(94)90203-8;
RA   Dworetzky S.I., Trojnacki J.T., Gribkoff V.K.;
RT   "Cloning and expression of a human large-conductance calcium-activated
RT   potassium channel.";
RL   Brain Res. Mol. Brain Res. 27:189-193(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
RC   TISSUE=Aortic smooth muscle, and Umbilical smooth muscle;
RX   PubMed=7573516;
RA   McCobb D.P., Fowler N.L., Featherstone T., Lingle C.J., Saito M.,
RA   Krause J.E., Salkoff L.;
RT   "A human calcium-activated potassium channel gene expressed in
RT   vascular smooth muscle.";
RL   Am. J. Physiol. 269:H767-H777(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15164054; DOI=10.1038/nature02462;
RA   Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA   Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA   Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA   Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA   Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
RA   Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
RA   Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA   Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
RA   Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
RA   Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
RA   Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
RA   Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
RA   Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
RA   Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
RA   Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
RA   Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
RA   Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
RA   Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
RA   Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA   Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
RA   Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
RA   Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
RA   Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
RA   Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
RA   Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT   "The DNA sequence and comparative analysis of human chromosome 10.";
RL   Nature 429:375-381(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 5 AND 6).
RC   TISSUE=Cerebellum, Neuroectoderm, and Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 17-1236 (ISOFORM 5).
RX   PubMed=7993625; DOI=10.1016/0896-6273(94)90418-9;
RA   Tseng-Crank J., Foster C.D., Krause J.D., Mertz R., Godinot N.,
RA   DiChiara T.J., Reinhart P.H.;
RT   "Cloning, expression, and distribution of functionally distinct
RT   Ca(2+)-activated K+ channel isoforms from human brain.";
RL   Neuron 13:1315-1330(1994).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 21-1236 (ISOFORM 5).
RC   TISSUE=Myometrium;
RX   PubMed=12434576;
RA   Mazzone J.N., Kaiser R.A., Buxton I.L.O.;
RT   "Calcium-activated potassium channel expression in human myometrium:
RT   effect of pregnancy.";
RL   Proc. West. Pharmacol. Soc. 45:184-186(2002).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 21-1236 (ISOFORM 1), AND NUCLEOTIDE
RP   SEQUENCE [MRNA] OF 25-1236 (ISOFORM 2).
RC   TISSUE=Heart;
RA   Naruse K.;
RT   "BK variant from human heart.";
RL   Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 24-670 (ISOFORM 3), AND NUCLEOTIDE
RP   SEQUENCE [MRNA] OF 323-1236 (ISOFORM 4).
RC   TISSUE=Muscle;
RX   PubMed=7987297; DOI=10.1093/hmg/3.8.1239;
RA   Pallanck L., Ganetzky B.;
RT   "Cloning and characterization of human and mouse homologs of the
RT   Drosophila calcium-activated potassium channel gene, slowpoke.";
RL   Hum. Mol. Genet. 3:1239-1243(1994).
RN   [10]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 25-1236 (ISOFORM 5).
RC   TISSUE=Lens epithelium;
RA   Rae J.L., Shepard A.R.;
RT   "Identification of potassium channels in human lens epithelium.";
RL   (In) Civan M.M. (eds.);
RL   Current topics in membranes. The eye's aqueous humor - from secretion
RL   to glaucoma, pp.45:69-104, Academic Press, San Diego (1998).
RN   [11]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 38-1236 (ISOFORM 5), AND NUCLEOTIDE
RP   SEQUENCE [MRNA] OF 693-764 (ISOFORM 4).
RC   TISSUE=Myometrium;
RX   PubMed=8821792;
RA   Wallner M., Meera P., Ottolia M., Kaczorowski G.J., Latorre R.,
RA   Garcia M.L., Stefani E., Toro L.;
RT   "Characterization of and modulation by a beta-subunit of a human maxi
RT   KCa channel cloned from myometrium.";
RL   Recept. Channels 3:185-199(1995).
RN   [12]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 66-1236 (ISOFORM 5).
RC   TISSUE=Pulmonary artery;
RA   Cairns V.R., Aebly M.R., Rusch N.J.;
RT   "Cloning and characterization of BKCA alpha subunit from human
RT   pulmonary artery.";
RL   Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN   [13]
RP   ALTERNATIVE SPLICING (ISOFORM 7), AND TISSUE SPECIFICITY.
RC   TISSUE=Glioblastoma;
RX   PubMed=11880513;
RA   Liu X., Chang Y., Reinhart P.H., Sontheimer H., Chang Y.;
RT   "Cloning and characterization of glioma BK, a novel BK channel isoform
RT   highly expressed in human glioma cells.";
RL   J. Neurosci. 22:1840-1849(2002).
RN   [14]
RP   ERRATUM.
RA   Liu X., Chang Y., Reinhart P.H., Sontheimer H., Chang Y.;
RL   J. Neurosci. 22:1B-1B(2002).
RN   [15]
RP   DOMAIN S0.
RX   PubMed=8962157; DOI=10.1073/pnas.93.25.14922;
RA   Wallner M., Meera P., Toro L.;
RT   "Determinant for beta-subunit regulation in high-conductance voltage-
RT   activated and Ca(2+)-sensitive K+ channels: an additional
RT   transmembrane region at the N-terminus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 93:14922-14927(1996).
RN   [16]
RP   MEMBRANE TOPOLOGY.
RX   PubMed=9391153; DOI=10.1073/pnas.94.25.14066;
RA   Meera P., Wallner M., Song M., Toro L.;
RT   "Large conductance voltage- and calcium-dependent K+ channel, a
RT   distinct member of voltage-dependent ion channels with seven N-
RT   terminal transmembrane segments (S0-S6), an extracellular N-terminus,
RT   and an intracellular (S9-S10) C-terminus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 94:14066-14071(1997).
RN   [17]
RP   DOMAIN S4, AND MUTAGENESIS OF LEU-269; ARG-272; ARG-275; ARG-278;
RP   GLN-281 AND GLU-284.
RX   PubMed=9829973; DOI=10.1074/jbc.273.49.32430;
RA   Diaz L., Meera P., Amigo J., Stefani E., Alvarez O., Toro L.,
RA   Latorre R.;
RT   "Role of the S4 segment in a voltage-dependent calcium-sensitive
RT   potassium (hSlo) channel.";
RL   J. Biol. Chem. 273:32430-32436(1998).
RN   [18]
RP   INTERACTION WITH KCNMB2.
RX   PubMed=10097176; DOI=10.1073/pnas.96.7.4137;
RA   Wallner M., Meera P., Toro L.;
RT   "Molecular basis of fast inactivation in voltage and Ca2+-activated K+
RT   channels: a transmembrane beta-subunit homolog.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:4137-4142(1999).
RN   [19]
RP   INTERACTION WITH KCNMB3 AND KCNMB4.
RX   PubMed=10692449; DOI=10.1074/jbc.275.9.6453;
RA   Brenner R., Jegla T.J., Wickenden A., Liu Y., Aldrich R.W.;
RT   "Cloning and functional characterization of novel large conductance
RT   calcium-activated potassium channel beta subunits, hKCNMB3 and
RT   hKCNMB4.";
RL   J. Biol. Chem. 275:6453-6461(2000).
RN   [20]
RP   HOMOTETRAMERIZATION, AND MUTAGENESIS OF 354-GLY--GLY-356.
RX   PubMed=11604135; DOI=10.1016/S0896-6273(01)00444-5;
RA   Quirk J.C., Reinhart P.H.;
RT   "Identification of a novel tetramerization domain in large conductance
RT   K(ca) channels.";
RL   Neuron 32:13-23(2001).
RN   [21]
RP   INTERACTION WITH KCNMB1; KCNMB2; KCNMB3 AND KCNMB4.
RX   PubMed=11880485;
RA   Wang Y.-W., Ding J.-P., Xia X.-M., Lingle C.J.;
RT   "Consequences of the stoichiometry of Slo1 alpha and auxiliary beta
RT   subunits on functional properties of large-conductance Ca2+-activated
RT   K+ channels.";
RL   J. Neurosci. 22:1550-1561(2002).
RN   [22]
RP   ENZYME REGULATION, AND MUTAGENESIS OF CYS-680 AND HIS-681.
RX   PubMed=14523450; DOI=10.1038/nature02003;
RA   Tang X.D., Xu R., Reynolds M.F., Garcia M.L., Heinemann S.H.,
RA   Hoshi T.;
RT   "Haem can bind to and inhibit mammalian calcium-dependent Slo1 BK
RT   channels.";
RL   Nature 425:531-535(2003).
RN   [23]
RP   REVIEW.
RX   PubMed=12566537; DOI=10.1085/jgp.20028721;
RA   Magleby K.L.;
RT   "Gating mechanism of BK (Slo1) channels: so near, yet so far.";
RL   J. Gen. Physiol. 121:81-96(2003).
RN   [24]
RP   SUBCELLULAR LOCATION, PALMITOYLATION AT CYS-118; CYS-119 AND CYS-121,
RP   AND MUTAGENESIS OF CYS-118; CYS-119 AND CYS-121.
RX   PubMed=20693285; DOI=10.1074/jbc.M110.153940;
RA   Jeffries O., Geiger N., Rowe I.C., Tian L., McClafferty H., Chen L.,
RA   Bi D., Knaus H.G., Ruth P., Shipston M.J.;
RT   "Palmitoylation of the S0-S1 linker regulates cell surface expression
RT   of voltage- and calcium-activated potassium (BK) channels.";
RL   J. Biol. Chem. 285:33307-33314(2010).
RN   [25]
RP   SUBCELLULAR LOCATION, PALMITOYLATION AT CYS-118; CYS-119 AND CYS-121,
RP   DEPALMITOYLATION, AND MUTAGENESIS OF CYS-118; CYS-119 AND CYS-121.
RX   PubMed=22399288; DOI=10.1074/jbc.M111.335547;
RA   Tian L., McClafferty H., Knaus H.G., Ruth P., Shipston M.J.;
RT   "Distinct acyl protein transferases and thioesterases control surface
RT   expression of calcium-activated potassium channels.";
RL   J. Biol. Chem. 287:14718-14725(2012).
RN   [26]
RP   INTERACTION WITH LRRC26.
RX   PubMed=20613726; DOI=10.1038/nature09162;
RA   Yan J., Aldrich R.W.;
RT   "LRRC26 auxiliary protein allows BK channel activation at resting
RT   voltage without calcium.";
RL   Nature 466:513-516(2010).
RN   [27]
RP   MUTAGENESIS OF THR-352; PHE-380; ALA-381 AND VAL-384.
RX   PubMed=20430843; DOI=10.1124/jpet.110.166017;
RA   Gordon E., Semus S.F., Lozinskaya I.M., Lin Z., Xu X.;
RT   "Characterizing the role of Thr352 in the inhibition of the large
RT   conductance Ca2+-activated K+ channels by 1-[1-Hexyl-6-(methyloxy)-1H-
RT   indazol-3-yl]-2-methyl-1-propanone.";
RL   J. Pharmacol. Exp. Ther. 334:402-409(2010).
RN   [28]
RP   INTERACTION WITH GAMMA SUBUNITS LRRC26; LRRC38; LRRC52 AND LRRC55.
RX   PubMed=22547800; DOI=10.1073/pnas.1205435109;
RA   Yan J., Aldrich R.W.;
RT   "BK potassium channel modulation by leucine-rich repeat-containing
RT   proteins.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:7917-7922(2012).
RN   [29]
RP   X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 406-1179, CALCIUM-BINDING
RP   SITES, AND SUBUNIT.
RX   PubMed=20508092; DOI=10.1126/science.1190414;
RA   Yuan P., Leonetti M.D., Pico A.R., Hsiung Y., MacKinnon R.;
RT   "Structure of the human BK channel Ca2+-activation apparatus at 3.0 A
RT   resolution.";
RL   Science 329:182-186(2010).
RN   [30]
RP   VARIANT PNKD3 GLY-434.
RX   PubMed=15937479; DOI=10.1038/ng1585;
RA   Du W., Bautista J.F., Yang H., Diez-Sampedro A., You S.-A., Wang L.,
RA   Kotagal P., Lueders H.O., Shi J., Cui J., Richerson G.B., Wang Q.K.;
RT   "Calcium-sensitive potassium channelopathy in human epilepsy and
RT   paroxysmal movement disorder.";
RL   Nat. Genet. 37:733-738(2005).
RN   [31]
RP   VARIANTS PNKD3 LYS-884 AND SER-1053.
RX   PubMed=26195193; DOI=10.1002/mds.26216;
RA   Zhang Z.B., Tian M.Q., Gao K., Jiang Y.W., Wu Y.;
RT   "De novo KCNMA1 mutations in children with early-onset paroxysmal
RT   dyskinesia and developmental delay.";
RL   Mov. Disord. 30:1290-1292(2015).
CC   -!- FUNCTION: Potassium channel activated by both membrane
CC       depolarization or increase in cytosolic Ca(2+) that mediates
CC       export of K(+). It is also activated by the concentration of
CC       cytosolic Mg(2+). Its activation dampens the excitatory events
CC       that elevate the cytosolic Ca(2+) concentration and/or depolarize
CC       the cell membrane. It therefore contributes to repolarization of
CC       the membrane potential. Plays a key role in controlling
CC       excitability in a number of systems, such as regulation of the
CC       contraction of smooth muscle, the tuning of hair cells in the
CC       cochlea, regulation of transmitter release, and innate immunity.
CC       In smooth muscles, its activation by high level of Ca(2+), caused
CC       by ryanodine receptors in the sarcoplasmic reticulum, regulates
CC       the membrane potential. In cochlea cells, its number and kinetic
CC       properties partly determine the characteristic frequency of each
CC       hair cell and thereby helps to establish a tonotopic map. Kinetics
CC       of KCNMA1 channels are determined by alternative splicing,
CC       phosphorylation status and its combination with modulating beta
CC       subunits. Highly sensitive to both iberiotoxin (IbTx) and
CC       charybdotoxin (CTX).
CC   -!- ENZYME REGULATION: Ethanol and carbon monoxide-bound heme increase
CC       channel activation. Heme inhibits channel activation.
CC       {ECO:0000269|PubMed:14523450}.
CC   -!- SUBUNIT: Homotetramer; which constitutes the calcium-activated
CC       potassium channel. Interacts with RAB11B (By similarity).
CC       Interacts with beta subunits KCNMB1, KCNMB2, KCNMB3 and KCNMB4.
CC       Interacts with gamma subunits LRRC26, LRRC38, LRRC52 and LRRC55.
CC       Beta and gamma subunits are accessory, and modulate its activity.
CC       {ECO:0000250, ECO:0000269|PubMed:10097176,
CC       ECO:0000269|PubMed:10692449, ECO:0000269|PubMed:11880485,
CC       ECO:0000269|PubMed:20508092, ECO:0000269|PubMed:20613726,
CC       ECO:0000269|PubMed:22547800}.
CC   -!- INTERACTION:
CC       Q6NXK8-1:Asic1 (xeno); NbExp=2; IntAct=EBI-1220676, EBI-15686410;
CC       Q2I0M4:LRRC26; NbExp=3; IntAct=EBI-1220676, EBI-15863320;
CC       P21731-3:TBXA2R; NbExp=7; IntAct=EBI-15861807, EBI-15885629;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20693285,
CC       ECO:0000269|PubMed:22399288}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:20693285, ECO:0000269|PubMed:22399288}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=7;
CC         Comment=May be partially controlled by hormonal stress.
CC         Additional isoforms seem to exist.;
CC       Name=1; Synonyms=SAKCA;
CC         IsoId=Q12791-1; Sequence=Displayed;
CC       Name=2; Synonyms=BKTM;
CC         IsoId=Q12791-2; Sequence=VSP_009955, VSP_009958;
CC       Name=3;
CC         IsoId=Q12791-3; Sequence=VSP_009954;
CC       Name=4; Synonyms=hbr5;
CC         IsoId=Q12791-4; Sequence=VSP_009956;
CC       Name=5;
CC         IsoId=Q12791-5; Sequence=VSP_009955;
CC       Name=6;
CC         IsoId=Q12791-6; Sequence=VSP_009952, VSP_009953;
CC         Note=No experimental confirmation available.;
CC       Name=7; Synonyms=gBK;
CC         IsoId=Q12791-7; Sequence=VSP_009957;
CC         Note=Ref.13 (no nucleotide entry) sequence is in conflict in
CC         positions: 726:FS->SF. {ECO:0000305};
CC   -!- TISSUE SPECIFICITY: Widely expressed. Except in myocytes, it is
CC       almost ubiquitously expressed. {ECO:0000269|PubMed:11880513}.
CC   -!- DOMAIN: The S0 segment is essential for the modulation by the
CC       accessory beta subunits KCNMB1, KCNMB2, KCNMB3 and KCNMB4.
CC   -!- DOMAIN: The S4 segment, which is characterized by a series of
CC       positively charged amino acids at every third position, is part of
CC       the voltage-sensor.
CC   -!- DOMAIN: The pore-forming domain (also referred as P region) is
CC       imbedded into the membrane, and forms the selectivity filter of
CC       the pore. It contains the signature sequence of potassium channels
CC       that displays selectivity to potassium.
CC   -!- DOMAIN: The RCK N-terminal domain mediates the
CC       homotetramerization, thereby promoting the assembly of monomers
CC       into functional potassium channel. It includes binding sites for
CC       Ca(2+) and Mg(2+) (By similarity). {ECO:0000250}.
CC   -!- DOMAIN: The calcium bowl constitutes one of the Ca(2+) sensors and
CC       probably acts as a Ca(2+)-binding site. There are however other
CC       Ca(2+) sensors regions required for activation of the channel.
CC   -!- DOMAIN: The heme-binding motif mediates inhibition of channel
CC       activation by heme. Carbon monoxide-bound heme leads to increased
CC       channel activation.
CC   -!- PTM: Phosphorylated (Probable). Phosphorylation by kinases such as
CC       PKA and/or PKG. In smooth muscles, phosphorylation affects its
CC       activity. {ECO:0000305}.
CC   -!- PTM: Palmitoylation by ZDHHC22 and ZDHHC23 within the
CC       intracellular linker between the S0 and S1 transmembrane domains
CC       regulates localization to the plasma membrane. Depalmitoylated by
CC       LYPLA1 and LYPLAL1, leading to retard exit from the trans-Golgi
CC       network. {ECO:0000269|PubMed:20693285,
CC       ECO:0000269|PubMed:22399288}.
CC   -!- DISEASE: Paroxysmal nonkinesigenic dyskinesia, 3, with or without
CC       generalized epilepsy (PNKD3) [MIM:609446]: An autosomal dominant
CC       neurologic disorder characterized by absence seizures, generalized
CC       tonic-clonic seizures, paroxysmal nonkinesigenic dyskinesia and
CC       involuntary dystonic or choreiform movements. Onset is usually in
CC       childhood. Patients may have seizures only, dyskinesia only, or
CC       both. {ECO:0000269|PubMed:15937479, ECO:0000269|PubMed:26195193}.
CC       Note=The disease is caused by mutations affecting the gene
CC       represented in this entry.
CC   -!- MISCELLANEOUS: The protein was initially thought to contain two
CC       functionally distinct parts: The core channel (from the N-terminus
CC       to the S9 segment) that mediates the channel activity, and the
CC       cytoplasmic tail (from the S9 segment to the C-terminus) that
CC       mediates the calcium sensing. The situation is however more
CC       complex, since the core channel also contains binding sites for
CC       Ca(2+) and Mg(2+).
CC   -!- SIMILARITY: Belongs to the potassium channel family. Calcium-
CC       activated (TC 1.A.1.3) subfamily. KCa1.1/KCNMA1 sub-subfamily.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA50216.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the N-terminal part.; Evidence={ECO:0000305};
CC       Sequence=AAB65837.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
CC       Sequence=AAC50353.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
CC       Sequence=AAK91504.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
CC       Sequence=BAD06365.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
DR   EMBL; U13913; AAA85104.1; -; mRNA.
DR   EMBL; U23767; AAA92290.1; -; mRNA.
DR   EMBL; AL157833; CAI39730.1; -; Genomic_DNA.
DR   EMBL; AL731560; CAI39730.1; JOINED; Genomic_DNA.
DR   EMBL; AL731556; CAI39730.1; JOINED; Genomic_DNA.
DR   EMBL; AL627447; CAI39730.1; JOINED; Genomic_DNA.
DR   EMBL; AC021032; CAI39730.1; JOINED; Genomic_DNA.
DR   EMBL; AC011439; CAI39730.1; JOINED; Genomic_DNA.
DR   EMBL; AL157833; CAI39736.1; -; Genomic_DNA.
DR   EMBL; AC011439; CAI39736.1; JOINED; Genomic_DNA.
DR   EMBL; AC021032; CAI39736.1; JOINED; Genomic_DNA.
DR   EMBL; AL627447; CAI39736.1; JOINED; Genomic_DNA.
DR   EMBL; AL731556; CAI39736.1; JOINED; Genomic_DNA.
DR   EMBL; AL731560; CAI39736.1; JOINED; Genomic_DNA.
DR   EMBL; AL627447; CAI16162.1; -; Genomic_DNA.
DR   EMBL; AL731560; CAI16162.1; JOINED; Genomic_DNA.
DR   EMBL; AL731556; CAI16162.1; JOINED; Genomic_DNA.
DR   EMBL; AC021032; CAI16162.1; JOINED; Genomic_DNA.
DR   EMBL; AC011439; CAI16162.1; JOINED; Genomic_DNA.
DR   EMBL; AL157833; CAI16162.1; JOINED; Genomic_DNA.
DR   EMBL; AL627447; CAI16171.1; -; Genomic_DNA.
DR   EMBL; AC011439; CAI16171.1; JOINED; Genomic_DNA.
DR   EMBL; AC021032; CAI16171.1; JOINED; Genomic_DNA.
DR   EMBL; AL157833; CAI16171.1; JOINED; Genomic_DNA.
DR   EMBL; AL731556; CAI16171.1; JOINED; Genomic_DNA.
DR   EMBL; AL731560; CAI16171.1; JOINED; Genomic_DNA.
DR   EMBL; AL731556; CAI14074.1; -; Genomic_DNA.
DR   EMBL; AC011439; CAI14074.1; JOINED; Genomic_DNA.
DR   EMBL; AL157833; CAI14074.1; JOINED; Genomic_DNA.
DR   EMBL; AC021032; CAI14074.1; JOINED; Genomic_DNA.
DR   EMBL; AL731560; CAI14074.1; JOINED; Genomic_DNA.
DR   EMBL; AL627447; CAI14074.1; JOINED; Genomic_DNA.
DR   EMBL; AL731556; CAI14082.1; -; Genomic_DNA.
DR   EMBL; AC011439; CAI14082.1; JOINED; Genomic_DNA.
DR   EMBL; AC021032; CAI14082.1; JOINED; Genomic_DNA.
DR   EMBL; AL157833; CAI14082.1; JOINED; Genomic_DNA.
DR   EMBL; AL627447; CAI14082.1; JOINED; Genomic_DNA.
DR   EMBL; AL731560; CAI14082.1; JOINED; Genomic_DNA.
DR   EMBL; AL731560; CAI40870.1; -; Genomic_DNA.
DR   EMBL; AL157833; CAI40870.1; JOINED; Genomic_DNA.
DR   EMBL; AL731556; CAI40870.1; JOINED; Genomic_DNA.
DR   EMBL; AC021032; CAI40870.1; JOINED; Genomic_DNA.
DR   EMBL; AC011439; CAI40870.1; JOINED; Genomic_DNA.
DR   EMBL; AL627447; CAI40870.1; JOINED; Genomic_DNA.
DR   EMBL; AL731560; CAI40877.1; -; Genomic_DNA.
DR   EMBL; AC011439; CAI40877.1; JOINED; Genomic_DNA.
DR   EMBL; AC021032; CAI40877.1; JOINED; Genomic_DNA.
DR   EMBL; AL157833; CAI40877.1; JOINED; Genomic_DNA.
DR   EMBL; AL627447; CAI40877.1; JOINED; Genomic_DNA.
DR   EMBL; AL731556; CAI40877.1; JOINED; Genomic_DNA.
DR   EMBL; AC067745; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL607069; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL731575; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471083; EAW54599.1; -; Genomic_DNA.
DR   EMBL; BC062659; AAH62659.1; -; mRNA.
DR   EMBL; BC137115; AAI37116.1; -; mRNA.
DR   EMBL; BC137137; AAI37138.1; -; mRNA.
DR   EMBL; U11717; AAC50353.1; ALT_INIT; mRNA.
DR   EMBL; AY040849; AAK91504.1; ALT_INIT; mRNA.
DR   EMBL; AB113575; BAD06397.1; -; mRNA.
DR   EMBL; AB113382; BAD06365.1; ALT_INIT; mRNA.
DR   EMBL; U02632; AAA50173.1; -; mRNA.
DR   EMBL; U09384; AAA50216.1; ALT_SEQ; mRNA.
DR   EMBL; AF025999; AAB88802.1; -; mRNA.
DR   EMBL; U11058; AAB65837.1; ALT_INIT; mRNA.
DR   EMBL; AF118141; AAD31173.1; -; mRNA.
DR   CCDS; CCDS53545.1; -. [Q12791-2]
DR   CCDS; CCDS60569.1; -. [Q12791-1]
DR   CCDS; CCDS60571.1; -. [Q12791-6]
DR   CCDS; CCDS7352.1; -. [Q12791-5]
DR   PIR; I38596; I38596.
DR   PIR; S62904; S62904.
DR   RefSeq; NP_001014797.1; NM_001014797.2.
DR   RefSeq; NP_001154824.1; NM_001161352.1. [Q12791-1]
DR   RefSeq; NP_001154825.1; NM_001161353.1. [Q12791-2]
DR   RefSeq; NP_001258447.1; NM_001271518.1.
DR   RefSeq; NP_001258451.1; NM_001271522.1. [Q12791-6]
DR   RefSeq; NP_002238.2; NM_002247.3. [Q12791-5]
DR   UniGene; Hs.144795; -.
DR   UniGene; Hs.658064; -.
DR   PDB; 2K44; NMR; -; A=257-284.
DR   PDB; 3MT5; X-ray; 3.00 A; A=406-1179.
DR   PDB; 3NAF; X-ray; 3.10 A; A=395-681, A=782-1182.
DR   PDBsum; 2K44; -.
DR   PDBsum; 3MT5; -.
DR   PDBsum; 3NAF; -.
DR   ProteinModelPortal; Q12791; -.
DR   SMR; Q12791; -.
DR   BioGrid; 109979; 11.
DR   CORUM; Q12791; -.
DR   DIP; DIP-29729N; -.
DR   IntAct; Q12791; 5.
DR   MINT; MINT-4825316; -.
DR   BindingDB; Q12791; -.
DR   ChEMBL; CHEMBL4304; -.
DR   DrugBank; DB00436; Bendroflumethiazide.
DR   DrugBank; DB00356; Chlorzoxazone.
DR   DrugBank; DB01003; Cromoglicic acid.
DR   DrugBank; DB01119; Diazoxide.
DR   DrugBank; DB01159; Halothane.
DR   DrugBank; DB00999; Hydrochlorothiazide.
DR   DrugBank; DB00774; Hydroflumethiazide.
DR   DrugBank; DB01110; Miconazole.
DR   DrugBank; DB00721; Procaine.
DR   GuidetoPHARMACOLOGY; 380; -.
DR   iPTMnet; Q12791; -.
DR   PhosphoSitePlus; Q12791; -.
DR   SwissPalm; Q12791; -.
DR   BioMuta; KCNMA1; -.
DR   DMDM; 46396283; -.
DR   MaxQB; Q12791; -.
DR   PeptideAtlas; Q12791; -.
DR   PRIDE; Q12791; -.
DR   Ensembl; ENST00000286627; ENSP00000286627; ENSG00000156113. [Q12791-5]
DR   Ensembl; ENST00000286628; ENSP00000286628; ENSG00000156113. [Q12791-1]
DR   Ensembl; ENST00000434208; ENSP00000402150; ENSG00000156113. [Q12791-4]
DR   Ensembl; ENST00000480683; ENSP00000474686; ENSG00000156113. [Q12791-6]
DR   Ensembl; ENST00000626620; ENSP00000485867; ENSG00000156113. [Q12791-2]
DR   Ensembl; ENST00000638575; ENSP00000492049; ENSG00000156113. [Q12791-7]
DR   Ensembl; ENST00000638759; ENSP00000492632; ENSG00000156113. [Q12791-3]
DR   Ensembl; ENST00000640969; ENSP00000492200; ENSG00000156113. [Q12791-4]
DR   GeneID; 3778; -.
DR   KEGG; hsa:3778; -.
DR   UCSC; uc001jxm.4; human. [Q12791-1]
DR   CTD; 3778; -.
DR   DisGeNET; 3778; -.
DR   EuPathDB; HostDB:ENSG00000156113.20; -.
DR   GeneCards; KCNMA1; -.
DR   HGNC; HGNC:6284; KCNMA1.
DR   HPA; HPA054648; -.
DR   MalaCards; KCNMA1; -.
DR   MIM; 600150; gene.
DR   MIM; 609446; phenotype.
DR   neXtProt; NX_Q12791; -.
DR   OpenTargets; ENSG00000156113; -.
DR   Orphanet; 79137; Generalized epilepsy - paroxysmal dyskinesia.
DR   PharmGKB; PA220; -.
DR   GeneTree; ENSGT00530000063026; -.
DR   HOVERGEN; HBG052222; -.
DR   InParanoid; Q12791; -.
DR   KO; K04936; -.
DR   PhylomeDB; Q12791; -.
DR   TreeFam; TF314283; -.
DR   Reactome; R-HSA-1296052; Ca2+ activated K+ channels.
DR   Reactome; R-HSA-418457; cGMP effects.
DR   SIGNOR; Q12791; -.
DR   ChiTaRS; KCNMA1; human.
DR   EvolutionaryTrace; Q12791; -.
DR   GenomeRNAi; 3778; -.
DR   PRO; PR:Q12791; -.
DR   Proteomes; UP000005640; Chromosome 10.
DR   Bgee; ENSG00000156113; -.
DR   ExpressionAtlas; Q12791; baseline and differential.
DR   Genevisible; Q12791; HS.
DR   GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR   GO; GO:0005901; C:caveola; IDA:BHF-UCL.
DR   GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
DR   GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0008076; C:voltage-gated potassium channel complex; IDA:UniProtKB.
DR   GO; GO:0003779; F:actin binding; IDA:BHF-UCL.
DR   GO; GO:0015269; F:calcium-activated potassium channel activity; IDA:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0060072; F:large conductance calcium-activated potassium channel activity; IDA:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005249; F:voltage-gated potassium channel activity; IDA:UniProtKB.
DR   GO; GO:0030007; P:cellular potassium ion homeostasis; IDA:UniProtKB.
DR   GO; GO:0060073; P:micturition; IDA:UniProtKB.
DR   GO; GO:0045794; P:negative regulation of cell volume; IDA:UniProtKB.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; IMP:UniProtKB.
DR   GO; GO:0006813; P:potassium ion transport; IDA:UniProtKB.
DR   GO; GO:0042391; P:regulation of membrane potential; IDA:UniProtKB.
DR   GO; GO:0051592; P:response to calcium ion; IDA:UniProtKB.
DR   GO; GO:0034465; P:response to carbon monoxide; IDA:UniProtKB.
DR   GO; GO:0001666; P:response to hypoxia; IDA:UniProtKB.
DR   GO; GO:0006970; P:response to osmotic stress; IDA:UniProtKB.
DR   GO; GO:0060083; P:smooth muscle contraction involved in micturition; IDA:UniProtKB.
DR   InterPro; IPR024939; Ca-act_K_channel_Slo-1.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR003929; K_chnl_BK_asu.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR028325; VG_K_chnl.
DR   PANTHER; PTHR10027:SF28; PTHR10027:SF28; 2.
DR   Pfam; PF03493; BK_channel_a; 1.
DR   Pfam; PF00520; Ion_trans; 1.
DR   PRINTS; PR00169; KCHANNEL.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Calcium; Cell membrane;
KW   Complete proteome; Disease mutation; Epilepsy; Ion channel;
KW   Ion transport; Lipoprotein; Magnesium; Membrane; Metal-binding;
KW   Palmitate; Phosphoprotein; Potassium; Potassium channel;
KW   Potassium transport; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport; Voltage-gated channel.
FT   CHAIN         1   1236       Calcium-activated potassium channel
FT                                subunit alpha-1.
FT                                /FTId=PRO_0000054132.
FT   TOPO_DOM      1     86       Extracellular. {ECO:0000255}.
FT   TRANSMEM     87    107       Helical; Name=Segment S0. {ECO:0000255}.
FT   TOPO_DOM    108    178       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    179    199       Helical; Name=Segment S1. {ECO:0000255}.
FT   TOPO_DOM    200    214       Extracellular. {ECO:0000255}.
FT   TRANSMEM    215    235       Helical; Name=Segment S2. {ECO:0000255}.
FT   TOPO_DOM    236    239       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    240    260       Helical; Name=Segment S3. {ECO:0000255}.
FT   TOPO_DOM    261    264       Extracellular. {ECO:0000255}.
FT   TRANSMEM    265    285       Helical; Name=Segment S4. {ECO:0000255}.
FT   TOPO_DOM    286    300       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    301    321       Helical; Name=Segment S5. {ECO:0000255}.
FT   TOPO_DOM    322    335       Extracellular. {ECO:0000255}.
FT   INTRAMEM    336    358       Pore-forming; Name=P region.
FT                                {ECO:0000255}.
FT   TOPO_DOM    359    367       Extracellular. {ECO:0000255}.
FT   TRANSMEM    368    388       Helical; Name=Segment S6. {ECO:0000255}.
FT   TOPO_DOM    389   1236       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN      415    558       RCK N-terminal.
FT   REGION      556    576       Segment S7.
FT   REGION      613    633       Segment S8.
FT   REGION      677    681       Heme-binding motif.
FT   REGION      837    857       Segment S9.
FT   REGION     1032   1052       Segment S10.
FT   MOTIF       352    355       Selectivity for potassium.
FT   MOTIF      1003   1025       Calcium bowl.
FT   COMPBIAS      4     10       Poly-Gly.
FT   COMPBIAS     13     20       Poly-Gly.
FT   COMPBIAS     39     60       Poly-Ser.
FT   METAL       439    439       Magnesium. {ECO:0000250}.
FT   METAL       462    462       Magnesium. {ECO:0000250}.
FT   METAL       464    464       Magnesium. {ECO:0000250}.
FT   METAL      1012   1012       Calcium; via carbonyl oxygen.
FT   METAL      1015   1015       Calcium; via carbonyl oxygen.
FT   METAL      1018   1018       Calcium.
FT   METAL      1020   1020       Calcium.
FT   MOD_RES     763    763       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q08460}.
FT   MOD_RES     765    765       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q08460}.
FT   MOD_RES     778    778       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q08460}.
FT   MOD_RES     782    782       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q08460}.
FT   MOD_RES     970    970       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q08460}.
FT   MOD_RES     978    978       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q08460}.
FT   MOD_RES     982    982       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q08460}.
FT   LIPID       118    118       S-palmitoyl cysteine.
FT                                {ECO:0000269|PubMed:20693285,
FT                                ECO:0000269|PubMed:22399288}.
FT   LIPID       119    119       S-palmitoyl cysteine.
FT                                {ECO:0000269|PubMed:20693285,
FT                                ECO:0000269|PubMed:22399288}.
FT   LIPID       121    121       S-palmitoyl cysteine.
FT                                {ECO:0000269|PubMed:20693285,
FT                                ECO:0000269|PubMed:22399288}.
FT   VAR_SEQ     127    168       EAQKINNGSSQADGTLKPVDEKEEAVAAEVGWMTSVKDWAG
FT                                V -> ATHFGSPEMPPAARSWSGSPPEAAVLRGASSLALEV
FT                                ARCRRL (in isoform 6).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_009952.
FT   VAR_SEQ     169   1236       Missing (in isoform 6).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_009953.
FT   VAR_SEQ     643    643       R -> RSRKR (in isoform 3).
FT                                {ECO:0000303|PubMed:7987297}.
FT                                /FTId=VSP_009954.
FT   VAR_SEQ     698    756       PKMSIYKRMRRACCFDCGRSERDCSCMSGRVRGNVDTLERA
FT                                FPLSSVSVNDCSTSFRAF -> L (in isoform 2 and
FT                                isoform 5). {ECO:0000303|PubMed:12434576,
FT                                ECO:0000303|PubMed:15489334,
FT                                ECO:0000303|PubMed:7573516,
FT                                ECO:0000303|PubMed:7877450,
FT                                ECO:0000303|PubMed:7993625,
FT                                ECO:0000303|PubMed:8821792,
FT                                ECO:0000303|Ref.10, ECO:0000303|Ref.12,
FT                                ECO:0000303|Ref.8}.
FT                                /FTId=VSP_009955.
FT   VAR_SEQ     698    756       PKMSIYKRMRRACCFDCGRSERDCSCMSGRVRGNVDTLERA
FT                                FPLSSVSVNDCSTSFRAF -> LKVAARSRYSKDPFEFKKE
FT                                TPNSRLVTEPV (in isoform 4).
FT                                {ECO:0000303|PubMed:7987297,
FT                                ECO:0000303|PubMed:8821792}.
FT                                /FTId=VSP_009956.
FT   VAR_SEQ     698    756       PKMSIYKRMRRACCFDCGRSERDCSCMSGRVRGNVDTLERA
FT                                FPLSSVSVNDCSTSFRAF -> RWEEHCSLWRLESKGNVRR
FT                                LNYCRGQQTFSVKVKVAARSRYSKDPFEFKKETPNSRLVTE
FT                                PV (in isoform 7). {ECO:0000305}.
FT                                /FTId=VSP_009957.
FT   VAR_SEQ     828    828       L -> LVTGWMPYLGPRVLMTCLDIGVVCMPTDIQSTSPAS
FT                                IKKFKE (in isoform 2).
FT                                {ECO:0000303|Ref.8}.
FT                                /FTId=VSP_009958.
FT   VARIANT     434    434       D -> G (in PNKD3; may have a synergistic
FT                                effect with ethanol in the triggering of
FT                                symptoms; dbSNP:rs137853333).
FT                                {ECO:0000269|PubMed:15937479}.
FT                                /FTId=VAR_023821.
FT   VARIANT     884    884       E -> K (in PNKD3).
FT                                {ECO:0000269|PubMed:26195193}.
FT                                /FTId=VAR_079156.
FT   VARIANT    1053   1053       N -> S (in PNKD3).
FT                                {ECO:0000269|PubMed:26195193}.
FT                                /FTId=VAR_079157.
FT   MUTAGEN     118    118       C->A: Decreased localization to the
FT                                plasma membrane. Abolishes localization
FT                                to the plasma membrane; when associated
FT                                with A-119 and A-121.
FT                                {ECO:0000269|PubMed:20693285,
FT                                ECO:0000269|PubMed:22399288}.
FT   MUTAGEN     119    119       C->A: Decreased localization to the
FT                                plasma membrane. Abolishes localization
FT                                to the plasma membrane; when associated
FT                                with A-118 and A-121.
FT                                {ECO:0000269|PubMed:20693285,
FT                                ECO:0000269|PubMed:22399288}.
FT   MUTAGEN     121    121       C->A: Decreased localization to the
FT                                plasma membrane. Abolishes localization
FT                                to the plasma membrane; when associated
FT                                with A-119 and A-121.
FT                                {ECO:0000269|PubMed:20693285,
FT                                ECO:0000269|PubMed:22399288}.
FT   MUTAGEN     269    269       L->R,H: No effect in the coupling between
FT                                calcium and channel opening.
FT                                {ECO:0000269|PubMed:9829973}.
FT   MUTAGEN     272    272       R->E: Induces reduction in the coupling
FT                                between calcium and channel opening.
FT                                {ECO:0000269|PubMed:9829973}.
FT   MUTAGEN     275    275       R->N: Induces reduction in the coupling
FT                                between calcium and channel opening.
FT                                {ECO:0000269|PubMed:9829973}.
FT   MUTAGEN     278    278       R->Q: Induces reduction in the coupling
FT                                between calcium and channel opening.
FT                                {ECO:0000269|PubMed:9829973}.
FT   MUTAGEN     281    281       Q->R: No effect in the coupling between
FT                                calcium and channel opening.
FT                                {ECO:0000269|PubMed:9829973}.
FT   MUTAGEN     284    284       E->K: No effect in the coupling between
FT                                calcium and channel opening.
FT                                {ECO:0000269|PubMed:9829973}.
FT   MUTAGEN     352    352       T->S: Activated at more negative
FT                                voltages. Slower rate of inactivation.
FT                                Impaired inhibition by HMIMP. No effect
FT                                on channel inhibition by Iberiotoxin.
FT                                {ECO:0000269|PubMed:20430843}.
FT   MUTAGEN     354    356       GYG->AAA: Loss of function.
FT                                {ECO:0000269|PubMed:11604135}.
FT   MUTAGEN     380    380       F->A: Loss of function.
FT                                {ECO:0000269|PubMed:20430843}.
FT   MUTAGEN     381    381       A->S: Activated at more negative
FT                                voltages. No effect on inhibition by
FT                                HMIMP. {ECO:0000269|PubMed:20430843}.
FT   MUTAGEN     384    384       V->I: No effect on activation voltage. No
FT                                effect on inhibition by HMIMP.
FT                                {ECO:0000269|PubMed:20430843}.
FT   MUTAGEN     680    680       C->S: Loss of heme-induced channel
FT                                inhibition.
FT                                {ECO:0000269|PubMed:14523450}.
FT   MUTAGEN     681    681       H->R: Loss of heme-induced channel
FT                                inhibition.
FT                                {ECO:0000269|PubMed:14523450}.
FT   CONFLICT     25     25       M -> N (in Ref. 9; AAA50216).
FT                                {ECO:0000305}.
FT   CONFLICT     35     35       S -> G (in Ref. 9; AAA50216).
FT                                {ECO:0000305}.
FT   CONFLICT     38     38       A -> V (in Ref. 1; AAA85104).
FT                                {ECO:0000305}.
FT   CONFLICT    449    449       N -> D (in Ref. 12; AAD31173).
FT                                {ECO:0000305}.
FT   CONFLICT    805    805       N -> H (in Ref. 6; AAC50353).
FT                                {ECO:0000305}.
FT   CONFLICT   1152   1152       T -> A (in Ref. 12; AAD31173).
FT                                {ECO:0000305}.
FT   CONFLICT   1230   1236       YVQEERL -> KEMVYR (in Ref. 3; CAI39730/
FT                                CAI40870/CAI14074/CAI16162).
FT                                {ECO:0000305}.
FT   HELIX       261    270       {ECO:0000244|PDB:2K44}.
FT   HELIX       277    280       {ECO:0000244|PDB:2K44}.
FT   STRAND      409    415       {ECO:0000244|PDB:3MT5}.
FT   HELIX       418    431       {ECO:0000244|PDB:3MT5}.
FT   TURN        433    437       {ECO:0000244|PDB:3MT5}.
FT   STRAND      439    443       {ECO:0000244|PDB:3MT5}.
FT   HELIX       450    453       {ECO:0000244|PDB:3MT5}.
FT   HELIX       456    459       {ECO:0000244|PDB:3MT5}.
FT   STRAND      461    466       {ECO:0000244|PDB:3MT5}.
FT   STRAND      470    472       {ECO:0000244|PDB:3NAF}.
FT   HELIX       473    478       {ECO:0000244|PDB:3MT5}.
FT   HELIX       481    483       {ECO:0000244|PDB:3MT5}.
FT   STRAND      485    490       {ECO:0000244|PDB:3MT5}.
FT   HELIX       498    515       {ECO:0000244|PDB:3MT5}.
FT   STRAND      521    526       {ECO:0000244|PDB:3MT5}.
FT   HELIX       528    531       {ECO:0000244|PDB:3MT5}.
FT   HELIX       532    536       {ECO:0000244|PDB:3MT5}.
FT   TURN        542    545       {ECO:0000244|PDB:3MT5}.
FT   STRAND      547    550       {ECO:0000244|PDB:3MT5}.
FT   HELIX       551    564       {ECO:0000244|PDB:3MT5}.
FT   HELIX       568    573       {ECO:0000244|PDB:3MT5}.
FT   TURN        574    576       {ECO:0000244|PDB:3MT5}.
FT   STRAND      586    588       {ECO:0000244|PDB:3MT5}.
FT   HELIX       589    597       {ECO:0000244|PDB:3MT5}.
FT   STRAND      600    605       {ECO:0000244|PDB:3MT5}.
FT   HELIX       608    610       {ECO:0000244|PDB:3MT5}.
FT   HELIX       615    624       {ECO:0000244|PDB:3MT5}.
FT   STRAND      629    634       {ECO:0000244|PDB:3MT5}.
FT   STRAND      638    640       {ECO:0000244|PDB:3NAF}.
FT   STRAND      645    647       {ECO:0000244|PDB:3MT5}.
FT   STRAND      659    665       {ECO:0000244|PDB:3MT5}.
FT   HELIX       667    671       {ECO:0000244|PDB:3MT5}.
FT   TURN        672    674       {ECO:0000244|PDB:3MT5}.
FT   HELIX       685    689       {ECO:0000244|PDB:3NAF}.
FT   HELIX       803    805       {ECO:0000244|PDB:3MT5}.
FT   HELIX       823    825       {ECO:0000244|PDB:3MT5}.
FT   HELIX       830    835       {ECO:0000244|PDB:3MT5}.
FT   STRAND      842    847       {ECO:0000244|PDB:3MT5}.
FT   STRAND      850    852       {ECO:0000244|PDB:3NAF}.
FT   HELIX       858    861       {ECO:0000244|PDB:3MT5}.
FT   HELIX       863    865       {ECO:0000244|PDB:3MT5}.
FT   STRAND      867    869       {ECO:0000244|PDB:3NAF}.
FT   HELIX       871    873       {ECO:0000244|PDB:3MT5}.
FT   STRAND      877    881       {ECO:0000244|PDB:3MT5}.
FT   HELIX       883    893       {ECO:0000244|PDB:3MT5}.
FT   STRAND      896    904       {ECO:0000244|PDB:3MT5}.
FT   HELIX       909    914       {ECO:0000244|PDB:3MT5}.
FT   HELIX       917    919       {ECO:0000244|PDB:3MT5}.
FT   STRAND      921    927       {ECO:0000244|PDB:3MT5}.
FT   STRAND      936    938       {ECO:0000244|PDB:3NAF}.
FT   HELIX       941    951       {ECO:0000244|PDB:3MT5}.
FT   HELIX       996    998       {ECO:0000244|PDB:3MT5}.
FT   STRAND     1001   1006       {ECO:0000244|PDB:3MT5}.
FT   HELIX      1008   1011       {ECO:0000244|PDB:3MT5}.
FT   STRAND     1016   1018       {ECO:0000244|PDB:3MT5}.
FT   HELIX      1026   1028       {ECO:0000244|PDB:3MT5}.
FT   HELIX      1030   1033       {ECO:0000244|PDB:3MT5}.
FT   STRAND     1037   1039       {ECO:0000244|PDB:3MT5}.
FT   HELIX      1040   1044       {ECO:0000244|PDB:3MT5}.
FT   HELIX      1046   1052       {ECO:0000244|PDB:3MT5}.
FT   HELIX      1054   1064       {ECO:0000244|PDB:3MT5}.
FT   HELIX      1073   1079       {ECO:0000244|PDB:3MT5}.
FT   HELIX      1089   1093       {ECO:0000244|PDB:3MT5}.
FT   STRAND     1099   1104       {ECO:0000244|PDB:3MT5}.
FT   TURN       1105   1107       {ECO:0000244|PDB:3MT5}.
FT   TURN       1109   1111       {ECO:0000244|PDB:3MT5}.
FT   HELIX      1112   1114       {ECO:0000244|PDB:3MT5}.
FT   HELIX      1119   1129       {ECO:0000244|PDB:3MT5}.
FT   STRAND     1133   1141       {ECO:0000244|PDB:3MT5}.
FT   STRAND     1144   1146       {ECO:0000244|PDB:3NAF}.
FT   STRAND     1154   1159       {ECO:0000244|PDB:3MT5}.
FT   STRAND     1171   1176       {ECO:0000244|PDB:3MT5}.
SQ   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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