KCMA1_MOUSE
ID KCMA1_MOUSE Reviewed; 1209 AA.
AC Q08460; Q64703; Q8VHF1; Q9R196;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2004, sequence version 2.
DT 03-AUG-2022, entry version 205.
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 Short=mSlo1;
DE AltName: Full=Slowpoke homolog;
DE Short=Slo homolog;
DE Short=mSlo;
GN Name=Kcnma1; Synonyms=Kcnma;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 Drosophila
RT calcium-activated potassium channel gene, slowpoke.";
RL Hum. Mol. Genet. 3:1239-1243(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 26-1209 (ISOFORMS 2 AND 5), AND FUNCTION.
RC TISSUE=Brain;
RX PubMed=7687074; DOI=10.1126/science.7687074;
RA Butler A., Tsunoda S., McCobb D.P., Wei A., Salkoff L.;
RT "mSlo, a complex mouse gene encoding 'maxi' calcium-activated potassium
RT channels.";
RL Science 261:221-224(1993).
RN [3]
RP MUTAGENESIS OF VAL-151.
RX PubMed=16341213; DOI=10.1038/nn1602;
RA Liu J., Asuncion-Chin M., Liu P., Dopico A.M.;
RT "CaM kinase II phosphorylation of slo Thr107 regulates activity and ethanol
RT responses of BK channels.";
RL Nat. Neurosci. 9:41-49(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 66-1209 (ISOFORM 4).
RC TISSUE=Pituitary anterior lobe;
RX PubMed=10517674; DOI=10.1210/mend.13.10.0355;
RA Shipston M.J., Duncan R.R., Clark A.G., Antoni F.A., Tian L.;
RT "Molecular components of large conductance calcium-activated potassium (BK)
RT channels in mouse pituitary corticotropes.";
RL Mol. Endocrinol. 13:1728-1737(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 66-1209 (ISOFORM 3).
RC STRAIN=NIH Swiss; TISSUE=Parotid gland;
RX PubMed=12388098; DOI=10.1152/ajpcell.00044.2002;
RA Nehrke K., Quinn C.C., Begenisich T.;
RT "Molecular identification of Ca2+-activated K+ channels in parotid acinar
RT cells.";
RL Am. J. Physiol. 284:C535-C546(2003).
RN [6]
RP INTERACTION WITH KCNMB3.
RX PubMed=10804197; DOI=10.1523/jneurosci.20-10-03563.2000;
RA Weiger T.M., Holmqvist M.H., Levitan I.B., Clark F.T., Sprague S.,
RA Huang W.-J., Ge P., Wang C., Lawson D., Jurman M.E., Glucksmann M.A.,
RA Silos-Santiago I., DiStefano P.S., Curtis R.;
RT "A novel nervous system beta subunit that downregulates human large
RT conductance calcium-dependent potassium channels.";
RL J. Neurosci. 20:3563-3570(2000).
RN [7]
RP MUTAGENESIS OF ARG-272; ARG-278; GLU-284 AND GLN-287.
RX PubMed=11112549; DOI=10.1021/bi001509+;
RA Cui J., Aldrich R.W.;
RT "Allosteric linkage between voltage and Ca(2+)-dependent activation of BK-
RT type mslo1 K(+) channels.";
RL Biochemistry 39:15612-15619(2000).
RN [8]
RP CALCIUM-BINDING, AND MUTAGENESIS OF 992-ASP--ASP-996.
RX PubMed=12149279; DOI=10.1085/jgp.20028627;
RA Bao L., Rapin A.M., Holmstrand E.C., Cox D.H.;
RT "Elimination of the BK(Ca) channel's high-affinity Ca(2+) sensitivity.";
RL J. Gen. Physiol. 120:173-189(2002).
RN [9]
RP MAGNESIUM-BINDING, AND MUTAGENESIS OF GLU-439; HIS-444; THR-461; GLN-462
RP AND GLU-464.
RX PubMed=12192410; DOI=10.1038/nature00941;
RA Shi J., Krishnamoorthy G., Yang Y., Hu L., Chaturvedi N., Harilal D.,
RA Qin J., Cui J.;
RT "Mechanism of magnesium activation of calcium-activated potassium
RT channels.";
RL Nature 418:876-880(2002).
RN [10]
RP CALCIUM-BINDING, MAGNESIUM-BINDING, AND MUTAGENESIS OF ASP-427; ASP-432;
RP ASP-434 AND GLU-464.
RX PubMed=12192411; DOI=10.1038/nature00956;
RA Xia X.-M., Zeng X., Lingle C.J.;
RT "Multiple regulatory sites in large-conductance calcium-activated potassium
RT channels.";
RL Nature 418:880-884(2002).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-709; SER-711; SER-724;
RP SER-728; THR-916; SER-924 AND SER-928, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT THR-670 AND SER-672 (ISOFORM 2), AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [12]
RP INTERACTION WITH RAB11B.
RX PubMed=22935415; DOI=10.1016/j.bbrc.2012.08.067;
RA Sokolowski S., Harvey M., Sakai Y., Jordan A., Sokolowski B.;
RT "The large conductance calcium-activated K(+) channel interacts with the
RT small GTPase Rab11b.";
RL Biochem. Biophys. Res. Commun. 426:221-225(2012).
CC -!- FUNCTION: Potassium channel activated by both membrane depolarization
CC or increase in cytosolic Ca(2+) that mediates export of K(+). It is
CC also activated by the concentration of cytosolic Mg(2+). Its activation
CC dampens the excitatory events that elevate the cytosolic Ca(2+)
CC concentration and/or depolarize the cell membrane. It therefore
CC contributes to repolarization of the membrane potential. Plays a key
CC role in controlling excitability in a number of systems, such as
CC regulation of the contraction of smooth muscle, the tuning of hair
CC cells in the cochlea, regulation of transmitter release, and innate
CC immunity. In smooth muscles, its activation by high level of Ca(2+),
CC caused 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 hair
CC cell and thereby helps to establish a tonotopic map. Kinetics of KCNMA1
CC channels are determined by alternative splicing, phosphorylation status
CC and its combination with modulating beta subunits. Highly sensitive to
CC both iberiotoxin (IbTx) and charybdotoxin (CTX).
CC {ECO:0000269|PubMed:7687074}.
CC -!- ACTIVITY REGULATION: Ethanol and carbon monoxide-bound heme increase
CC channel activation. Heme inhibits channel activation (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Homotetramer; which constitutes the calcium-activated
CC potassium channel. Interacts with beta subunits KCNMB1, KCNMB2, KCNMB3
CC and KCNMB4. Interacts with gamma subunits LRRC26, LRRC38, LRRC52 and
CC LRRC55. Beta and gamma subunits are accessory, and modulate its
CC activity (By similarity). Interacts with RAB11B. {ECO:0000250,
CC ECO:0000269|PubMed:10804197, ECO:0000269|PubMed:22935415}.
CC -!- INTERACTION:
CC Q08460; P63260: Actg1; NbExp=4; IntAct=EBI-1633915, EBI-351301;
CC Q08460; P48036: Anxa5; NbExp=4; IntAct=EBI-1633915, EBI-1184119;
CC Q08460; Q00623: Apoa1; NbExp=4; IntAct=EBI-1633915, EBI-1634106;
CC Q08460; P62204: Calm3; NbExp=4; IntAct=EBI-1633915, EBI-397460;
CC Q08460; Q60598: Cttn; NbExp=2; IntAct=EBI-1633915, EBI-397955;
CC Q08460; P16858: Gapdh; NbExp=3; IntAct=EBI-1633915, EBI-444871;
CC Q08460; P84075: Hpca; NbExp=3; IntAct=EBI-1633915, EBI-2128343;
CC Q08460; O88952: Lin7c; NbExp=4; IntAct=EBI-1633915, EBI-821316;
CC Q08460; P27573: Mpz; NbExp=4; IntAct=EBI-1633915, EBI-1634589;
CC Q08460; P61982: Ywhag; NbExp=4; IntAct=EBI-1633915, EBI-359843;
CC Q08460; P08251: ATP1B1; Xeno; NbExp=5; IntAct=EBI-1633915, EBI-7206371;
CC Q08460; P46109: CRKL; Xeno; NbExp=5; IntAct=EBI-1633915, EBI-910;
CC Q08460; Q14247: CTTN; Xeno; NbExp=3; IntAct=EBI-1633915, EBI-351886;
CC Q08460; O75791: GRAP2; Xeno; NbExp=3; IntAct=EBI-1633915, EBI-740418;
CC Q08460-4; Q8CAE3: Kcnmb1; NbExp=2; IntAct=EBI-15575817, EBI-15575793;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Comment=May be partially controlled by hormonal stress. Additional
CC isoforms seem to exist.;
CC Name=1;
CC IsoId=Q08460-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q08460-2; Sequence=VSP_009960, VSP_009961, VSP_009962,
CC VSP_009964, VSP_009965;
CC Name=3;
CC IsoId=Q08460-3; Sequence=VSP_009961, VSP_009964;
CC Name=4; Synonyms=STREX-1;
CC IsoId=Q08460-4; Sequence=VSP_009961, VSP_009963, VSP_009964;
CC Name=5;
CC IsoId=Q08460-5; Sequence=VSP_009959;
CC -!- DOMAIN: The S0 segment is essential for the modulation by the accessory
CC 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 the
CC voltage-sensor.
CC -!- DOMAIN: The pore-forming domain (also referred as P region) is imbedded
CC into the membrane, and forms the selectivity filter of the pore. It
CC contains the signature sequence of potassium channels that displays
CC selectivity to potassium.
CC -!- DOMAIN: The RCK N-terminal domain mediates the homotetramerization,
CC thereby promoting the assembly of monomers into functional potassium
CC channel. It includes binding sites for Ca(2+) and Mg(2+).
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 Ca(2+)
CC 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 (By similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylated (Probable). Phosphorylation by kinases such as PKA
CC and/or PKG. In smooth muscles, phosphorylation affects its activity.
CC {ECO:0000305}.
CC -!- PTM: Palmitoylation by ZDHHC22 and ZDHHC23 within the intracellular
CC linker between the S0 and S1 transmembrane domains regulates
CC localization to the plasma membrane. Depalmitoylated by LYPLA1 and
CC LYPLAL1, leading to retard exit from the trans-Golgi network (By
CC similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: The protein was initially thought to contain two
CC functionally distinct parts: The core channel (from the N-terminus to
CC the S9 segment) that mediates the channel activity, and the cytoplasmic
CC tail (from the S9 segment to the C-terminus) that mediates the calcium
CC sensing. The situation is however more complex, since the core channel
CC contains binding sites for Ca(2+) and Mg(2+).
CC -!- SIMILARITY: Belongs to the potassium channel family. Calcium-activated
CC (TC 1.A.1.3) subfamily. KCa1.1/KCNMA1 sub-subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA50215.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U09383; AAA50215.1; ALT_INIT; mRNA.
DR EMBL; L16912; AAA39746.1; -; mRNA.
DR EMBL; AF156674; AAD49225.1; -; mRNA.
DR EMBL; AF465244; AAL69971.1; -; mRNA.
DR CCDS; CCDS79275.1; -. [Q08460-3]
DR CCDS; CCDS79276.1; -. [Q08460-4]
DR CCDS; CCDS79277.1; -. [Q08460-1]
DR PIR; A48206; A48206.
DR PIR; I49017; I49017.
DR RefSeq; NP_001240294.1; NM_001253365.1.
DR RefSeq; NP_001240298.1; NM_001253369.1.
DR RefSeq; NP_034740.2; NM_010610.3.
DR AlphaFoldDB; Q08460; -.
DR BMRB; Q08460; -.
DR SMR; Q08460; -.
DR BioGRID; 200913; 185.
DR DIP; DIP-42413N; -.
DR IntAct; Q08460; 200.
DR MINT; Q08460; -.
DR STRING; 10090.ENSMUSP00000140275; -.
DR ChEMBL; CHEMBL2800; -.
DR DrugBank; DB08837; Tetraethylammonium.
DR GuidetoPHARMACOLOGY; 380; -.
DR iPTMnet; Q08460; -.
DR PhosphoSitePlus; Q08460; -.
DR SwissPalm; Q08460; -.
DR MaxQB; Q08460; -.
DR PaxDb; Q08460; -.
DR PeptideAtlas; Q08460; -.
DR PRIDE; Q08460; -.
DR ProteomicsDB; 269190; -. [Q08460-1]
DR ProteomicsDB; 269191; -. [Q08460-2]
DR ProteomicsDB; 269192; -. [Q08460-3]
DR ProteomicsDB; 269193; -. [Q08460-4]
DR ProteomicsDB; 269194; -. [Q08460-5]
DR ABCD; Q08460; 3 sequenced antibodies.
DR DNASU; 16531; -.
DR GeneID; 16531; -.
DR KEGG; mmu:16531; -.
DR UCSC; uc029sfy.1; mouse. [Q08460-2]
DR CTD; 3778; -.
DR MGI; MGI:99923; Kcnma1.
DR eggNOG; KOG1420; Eukaryota.
DR InParanoid; Q08460; -.
DR OrthoDB; 124461at2759; -.
DR PhylomeDB; Q08460; -.
DR Reactome; R-MMU-1296052; Ca2+ activated K+ channels.
DR BioGRID-ORCS; 16531; 0 hits in 67 CRISPR screens.
DR ChiTaRS; Kcnma1; mouse.
DR PRO; PR:Q08460; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q08460; protein.
DR GO; GO:0016324; C:apical plasma membrane; IDA:MGI.
DR GO; GO:0005901; C:caveola; ISO:MGI.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IDA:MGI.
DR GO; GO:0099059; C:integral component of presynaptic active zone membrane; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0045211; C:postsynaptic membrane; IDA:MGI.
DR GO; GO:0048787; C:presynaptic active zone membrane; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0016528; C:sarcoplasm; IDA:MGI.
DR GO; GO:0043195; C:terminal bouton; IDA:MGI.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; IGI:MGI.
DR GO; GO:0003779; F:actin binding; ISO:MGI.
DR GO; GO:0015269; F:calcium-activated potassium channel activity; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; IDA:MGI.
DR GO; GO:0060072; F:large conductance calcium-activated potassium channel activity; IDA:MGI.
DR GO; GO:0099507; F:ligand-gated ion channel activity involved in regulation of presynaptic membrane potential; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005267; F:potassium channel activity; IMP:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; IDA:MGI.
DR GO; GO:0007628; P:adult walking behavior; IMP:MGI.
DR GO; GO:0097746; P:blood vessel diameter maintenance; ISO:MGI.
DR GO; GO:0030007; P:cellular potassium ion homeostasis; ISO:MGI.
DR GO; GO:0007268; P:chemical synaptic transmission; IMP:MGI.
DR GO; GO:0007623; P:circadian rhythm; IMP:MGI.
DR GO; GO:0002069; P:columnar/cuboidal epithelial cell maturation; IMP:MGI.
DR GO; GO:0060082; P:eye blink reflex; IMP:MGI.
DR GO; GO:0042491; P:inner ear auditory receptor cell differentiation; IMP:MGI.
DR GO; GO:0045475; P:locomotor rhythm; IMP:MGI.
DR GO; GO:0060073; P:micturition; IMP:MGI.
DR GO; GO:0045794; P:negative regulation of cell volume; IMP:MGI.
DR GO; GO:1904348; P:negative regulation of small intestine smooth muscle contraction; ISO:MGI.
DR GO; GO:0050885; P:neuromuscular process controlling balance; IMP:MGI.
DR GO; GO:0042551; P:neuron maturation; IMP:MGI.
DR GO; GO:0019228; P:neuronal action potential; IMP:MGI.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR GO; GO:0043525; P:positive regulation of neuron apoptotic process; ISO:MGI.
DR GO; GO:0006813; P:potassium ion transport; IDA:MGI.
DR GO; GO:0032344; P:regulation of aldosterone metabolic process; IMP:MGI.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR GO; GO:0042391; P:regulation of membrane potential; IDA:MGI.
DR GO; GO:0060087; P:relaxation of vascular associated smooth muscle; IMP:MGI.
DR GO; GO:0051592; P:response to calcium ion; ISO:MGI.
DR GO; GO:0034465; P:response to carbon monoxide; ISO:MGI.
DR GO; GO:0031960; P:response to corticosteroid; ISO:MGI.
DR GO; GO:0043627; P:response to estrogen; ISO:MGI.
DR GO; GO:0001666; P:response to hypoxia; IDA:MGI.
DR GO; GO:0006970; P:response to osmotic stress; ISO:MGI.
DR GO; GO:0009268; P:response to pH; ISO:MGI.
DR GO; GO:0046541; P:saliva secretion; IGI:MGI.
DR GO; GO:0007605; P:sensory perception of sound; IMP:MGI.
DR GO; GO:0060083; P:smooth muscle contraction involved in micturition; IMP:MGI.
DR GO; GO:0042311; P:vasodilation; IMP:MGI.
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 PANTHER; PTHR10027:SF28; PTHR10027:SF28; 2.
DR Pfam; PF03493; BK_channel_a; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Cell membrane; Ion channel; Ion transport;
KW Lipoprotein; Magnesium; Membrane; Metal-binding; Palmitate; Phosphoprotein;
KW Potassium; Potassium channel; Potassium transport; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1..1209
FT /note="Calcium-activated potassium channel subunit alpha-1"
FT /id="PRO_0000054134"
FT TOPO_DOM 1..86
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 87..107
FT /note="Helical; Name=Segment S0"
FT /evidence="ECO:0000255"
FT TOPO_DOM 108..178
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 179..199
FT /note="Helical; Name=Segment S1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 200..214
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 215..235
FT /note="Helical; Name=Segment S2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 236..239
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 240..260
FT /note="Helical; Name=Segment S3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 261..264
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 265..285
FT /note="Helical; Voltage-sensor; Name=Segment S4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 286..300
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 301..321
FT /note="Helical; Name=Segment S5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 322..335
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT INTRAMEM 336..358
FT /note="Pore-forming; Name=P region"
FT /evidence="ECO:0000255"
FT TOPO_DOM 359..367
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 368..388
FT /note="Helical; Name=Segment S6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 389..1209
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 415..558
FT /note="RCK N-terminal"
FT REGION 1..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 556..576
FT /note="Segment S7"
FT REGION 613..633
FT /note="Segment S8"
FT REGION 681..685
FT /note="Heme-binding motif"
FT REGION 703..733
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 783..803
FT /note="Segment S9"
FT REGION 1005..1025
FT /note="Segment S10"
FT REGION 1159..1209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 352..355
FT /note="Selectivity for potassium"
FT MOTIF 976..998
FT /note="Calcium bowl"
FT COMPBIAS 26..61
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 712..730
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1159..1190
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1191..1209
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 439
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000305"
FT BINDING 462
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000305"
FT BINDING 464
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000305"
FT BINDING 985
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 988
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 991
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 993
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT MOD_RES 709
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 711
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 724
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 728
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 916
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 924
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 928
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1194
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q28204"
FT MOD_RES 1197
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q28204"
FT LIPID 118
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 119
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 121
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..65
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:7687074"
FT /id="VSP_009959"
FT VAR_SEQ 1..50
FT /note="MANGGGGGGGSSGGGGGGGGGSGLRMSSNIHANNLSLDASSSSSSSSSSS
FT -> MELEHPKSPPYP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:7687074"
FT /id="VSP_009960"
FT VAR_SEQ 643..646
FT /note="Missing (in isoform 2, isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:10517674,
FT ECO:0000303|PubMed:12388098, ECO:0000303|PubMed:7687074"
FT /id="VSP_009961"
FT VAR_SEQ 702
FT /note="L -> LIYF (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:7687074"
FT /id="VSP_009962"
FT VAR_SEQ 702
FT /note="L -> PKMSIYKRMRRACCFDCGRSERDCSCMSGRVRGNVDTLERTFPLSSV
FT SVNDCSTSFRAF (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:10517674"
FT /id="VSP_009963"
FT VAR_SEQ 948..974
FT /note="Missing (in isoform 2, isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:10517674,
FT ECO:0000303|PubMed:12388098, ECO:0000303|PubMed:7687074"
FT /id="VSP_009964"
FT VAR_SEQ 1203..1209
FT /note="RKEMVYR -> ATRMTRMGQAEKKWFTDEPDNAYPRNIQIKPMSTHMANQIN
FT QYKSTSSLIPPIREVEDEC (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:7687074"
FT /id="VSP_009965"
FT MUTAGEN 151
FT /note="V->T: Loss of phosphorylation-independent activation
FT of channel activity by ethanol. CaMK2-dependent
FT phosphorylation leads to populations of partially
FT phosphorylated tetramers with a range of responses to
FT ethanol from activation to inhibition."
FT /evidence="ECO:0000269|PubMed:16341213"
FT MUTAGEN 272
FT /note="R->Q: Alters the voltage-dependent gating."
FT /evidence="ECO:0000269|PubMed:11112549"
FT MUTAGEN 278
FT /note="R->Q: Alters the voltage-dependent gating."
FT /evidence="ECO:0000269|PubMed:11112549"
FT MUTAGEN 284
FT /note="E->R: Alters the voltage-dependent gating; when
FT associated with R-287."
FT /evidence="ECO:0000269|PubMed:11112549"
FT MUTAGEN 287
FT /note="Q->R: Alters the voltage-dependent gating; when
FT associated with K-284."
FT /evidence="ECO:0000269|PubMed:11112549"
FT MUTAGEN 427
FT /note="D->A: Does not affect sensitivity to Ca(2+)."
FT /evidence="ECO:0000269|PubMed:12192411"
FT MUTAGEN 432
FT /note="D->A: Reduced sensitivity to Ca(2+)."
FT /evidence="ECO:0000269|PubMed:12192411"
FT MUTAGEN 434
FT /note="D->A: Does not affect sensitivity to Ca(2+)."
FT /evidence="ECO:0000269|PubMed:12192411"
FT MUTAGEN 439
FT /note="E->A: Abolishes sensitivity to Mg(2+), but not
FT sensitivity to Ca(2+)."
FT /evidence="ECO:0000269|PubMed:12192410"
FT MUTAGEN 444
FT /note="H->G: Reduces sensitivity to Mg(2+), but not
FT sensitivity to Ca(2+)."
FT /evidence="ECO:0000269|PubMed:12192410"
FT MUTAGEN 461
FT /note="T->A: Reduces sensitivity to Mg(2+), but not
FT sensitivity to Ca(2+)."
FT /evidence="ECO:0000269|PubMed:12192410"
FT MUTAGEN 462
FT /note="Q->C: Reduces sensitivity to Mg(2+), but not
FT sensitivity to Ca(2+)."
FT /evidence="ECO:0000269|PubMed:12192410"
FT MUTAGEN 464
FT /note="E->D,A: Remains sensitive to Mg(2+)."
FT /evidence="ECO:0000269|PubMed:12192410,
FT ECO:0000269|PubMed:12192411"
FT MUTAGEN 464
FT /note="E->N: Abolishes sensitivity to Mg(2+), but not
FT sensitivity to Ca(2+)."
FT /evidence="ECO:0000269|PubMed:12192410,
FT ECO:0000269|PubMed:12192411"
FT MUTAGEN 992..996
FT /note="DDDPD->AAAAA: Alters calcium binding."
FT /evidence="ECO:0000269|PubMed:12149279"
FT MOD_RES Q08460-2:670
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES Q08460-2:672
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 1209 AA; 134396 MW; 9E07ABF5DCFA62DF CRC64;
MANGGGGGGG SSGGGGGGGG GSGLRMSSNI HANNLSLDAS SSSSSSSSSS SSSSSSSSSS
VHEPKMDALI IPVTMEVPCD SRGQRMWWAF LASSMVTFFG GLFIILLWRT LKYLWTVCCH
CGGKTKEAQK INNGSSQADG TLKPVDEKEE VVAAEVGWMT 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 ESRSRKRILI NPGNHLKIQE
GTLGFFIASD AKEVKRAFFY CKACHDDVTD PKRIKKCGCR RLEDEQPPTL SPKKKQRNGG
MRNSPNTSPK LMRHDPLLIP GNDQIDNMDS NVKKYDSTGM FHWCAPKEIE KVILTRSEAA
MTVLSGHVVV CIFGDVSSAL IGLRNLVMPL RASNFHYHEL KHIVFVGSIE YLKREWETLH
NFPKVSILPG TPLSRADLRA VNINLCDMCV ILSANQNNID DTSLQDKECI LASLNIKSMQ
FDDSIGVLQA NSQGFTPPGM DRSSPDNSPV HGMLRQPSIT TGVNIPIITE LAKPGKLPLV
SVNQEKNSGT HILMITELVN DTNVQFLDQD DDDDPDTELY LTQPFACGTA FAVSVLDSLM
SATYFNDNIL TLIRTLVTGG ATPELEALIA EENALRGGYS TPQTLANRDR CRVAQLALLD
GPFADLGDGG CYGDLFCKAL KTYNMLCFGI YRLRDAHLST PSQCTKRYVI TNPPYEFELV
PTDLIFCLMQ FDHNAGQSRA SLSHSSHSSQ SSSKKSSSVH SIPSTANRPN RPKSRESRDK
QNRKEMVYR
