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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) (mSlo1) (Slowpoke homolog) (Slo homolog) (mSlo)

 KCMA1_MOUSE             Reviewed;        1209 AA.
Q08460; Q64703; Q8VHF1; Q9R196;
13-APR-2004, integrated into UniProtKB/Swiss-Prot.
13-APR-2004, sequence version 2.
25-OCT-2017, entry version 174.
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;
Short=mSlo1;
AltName: Full=Slowpoke homolog;
Short=Slo homolog;
Short=mSlo;
Name=Kcnma1; Synonyms=Kcnma;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Brain;
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).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 26-1209 (ISOFORMS 2 AND 5), AND
FUNCTION.
TISSUE=Brain;
PubMed=7687074; DOI=10.1126/science.7687074;
Butler A., Tsunoda S., McCobb D.P., Wei A., Salkoff L.;
"mSlo, a complex mouse gene encoding 'maxi' calcium-activated
potassium channels.";
Science 261:221-224(1993).
[3]
MUTAGENESIS OF VAL-151.
PubMed=16341213; DOI=10.1038/nn1602;
Liu J., Asuncion-Chin M., Liu P., Dopico A.M.;
"CaM kinase II phosphorylation of slo Thr107 regulates activity and
ethanol responses of BK channels.";
Nat. Neurosci. 9:41-49(2006).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 66-1209 (ISOFORM 4).
TISSUE=Pituitary anterior lobe;
PubMed=10517674; DOI=10.1210/mend.13.10.0355;
Shipston M.J., Duncan R.R., Clark A.G., Antoni F.A., Tian L.;
"Molecular components of large conductance calcium-activated potassium
(BK) channels in mouse pituitary corticotropes.";
Mol. Endocrinol. 13:1728-1737(1999).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 66-1209 (ISOFORM 3).
STRAIN=NIH Swiss; TISSUE=Parotid gland;
PubMed=12388098; DOI=10.1152/ajpcell.00044.2002;
Nehrke K., Quinn C.C., Begenisich T.;
"Molecular identification of Ca2+-activated K+ channels in parotid
acinar cells.";
Am. J. Physiol. 284:C535-C546(2003).
[6]
INTERACTION WITH KCNMB3.
PubMed=10804197;
Weiger T.M., Holmqvist M.H., Levitan I.B., Clark F.T., Sprague S.,
Huang W.-J., Ge P., Wang C., Lawson D., Jurman M.E., Glucksmann M.A.,
Silos-Santiago I., DiStefano P.S., Curtis R.;
"A novel nervous system beta subunit that downregulates human large
conductance calcium-dependent potassium channels.";
J. Neurosci. 20:3563-3570(2000).
[7]
MUTAGENESIS OF ARG-272; ARG-278; GLU-284 AND GLN-287.
PubMed=11112549; DOI=10.1021/bi001509+;
Cui J., Aldrich R.W.;
"Allosteric linkage between voltage and Ca(2+)-dependent activation of
BK-type mslo1 K(+) channels.";
Biochemistry 39:15612-15619(2000).
[8]
CALCIUM-BINDING, AND MUTAGENESIS OF 992-ASP--ASP-996.
PubMed=12149279; DOI=10.1085/jgp.20028627;
Bao L., Rapin A.M., Holmstrand E.C., Cox D.H.;
"Elimination of the BK(Ca) channel's high-affinity Ca(2+)
sensitivity.";
J. Gen. Physiol. 120:173-189(2002).
[9]
MAGNESIUM-BINDING, AND MUTAGENESIS OF GLU-439; HIS-444; THR-461;
GLN-462 AND GLU-464.
PubMed=12192410; DOI=10.1038/nature00941;
Shi J., Krishnamoorthy G., Yang Y., Hu L., Chaturvedi N., Harilal D.,
Qin J., Cui J.;
"Mechanism of magnesium activation of calcium-activated potassium
channels.";
Nature 418:876-880(2002).
[10]
CALCIUM-BINDING, MAGNESIUM-BINDING, AND MUTAGENESIS OF ASP-427;
ASP-432; ASP-434 AND GLU-464.
PubMed=12192411; DOI=10.1038/nature00956;
Xia X.-M., Zeng X., Lingle C.J.;
"Multiple regulatory sites in large-conductance calcium-activated
potassium channels.";
Nature 418:880-884(2002).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-709; SER-711; SER-724;
SER-728; THR-916; SER-924 AND SER-928, PHOSPHORYLATION [LARGE SCALE
ANALYSIS] AT THR-670 AND SER-672 (ISOFORM 2), AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[12]
INTERACTION WITH RAB11B.
PubMed=22935415; DOI=10.1016/j.bbrc.2012.08.067;
Sokolowski S., Harvey M., Sakai Y., Jordan A., Sokolowski B.;
"The large conductance calcium-activated K(+) channel interacts with
the small GTPase Rab11b.";
Biochem. Biophys. Res. Commun. 426:221-225(2012).
-!- 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). {ECO:0000269|PubMed:7687074}.
-!- ENZYME REGULATION: Ethanol and carbon monoxide-bound heme increase
channel activation. Heme inhibits channel activation (By
similarity). {ECO:0000250}.
-!- SUBUNIT: Homotetramer; which constitutes the calcium-activated
potassium channel. Interacts with beta subunits KCNMB1, KCNMB2,
KCNMB3 and KCNMB4. Interacts with gamma subunits LRRC26, LRRC38,
LRRC52 and LRRC55. Beta and gamma subunits are accessory, and
modulate its activity (By similarity). Interacts with RAB11B.
{ECO:0000250, ECO:0000269|PubMed:10804197,
ECO:0000269|PubMed:22935415}.
-!- INTERACTION:
P63260:Actg1; NbExp=4; IntAct=EBI-1633915, EBI-351301;
P48036:Anxa5; NbExp=4; IntAct=EBI-1633915, EBI-1184119;
Q00623:Apoa1; NbExp=4; IntAct=EBI-1633915, EBI-1634106;
P08251:ATP1B1 (xeno); NbExp=5; IntAct=EBI-1633915, EBI-7206371;
P62204:Calm3; NbExp=4; IntAct=EBI-1633915, EBI-397460;
P46109:CRKL (xeno); NbExp=5; IntAct=EBI-1633915, EBI-910;
Q14247:CTTN (xeno); NbExp=3; IntAct=EBI-1633915, EBI-351886;
Q60598:Cttn; NbExp=2; IntAct=EBI-1633915, EBI-397955;
P16858:Gapdh; NbExp=3; IntAct=EBI-1633915, EBI-444871;
O75791:GRAP2 (xeno); NbExp=3; IntAct=EBI-1633915, EBI-740418;
P84075:Hpca; NbExp=3; IntAct=EBI-1633915, EBI-2128343;
Q8CAE3:Kcnmb1; NbExp=2; IntAct=EBI-15575817, EBI-15575793;
O88952:Lin7c; NbExp=4; IntAct=EBI-1633915, EBI-821316;
P27573:Mpz; NbExp=4; IntAct=EBI-1633915, EBI-1634589;
P61982:Ywhag; NbExp=4; IntAct=EBI-1633915, EBI-359843;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass
membrane protein {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Comment=May be partially controlled by hormonal stress.
Additional isoforms seem to exist.;
Name=1;
IsoId=Q08460-1; Sequence=Displayed;
Name=2;
IsoId=Q08460-2; Sequence=VSP_009960, VSP_009961, VSP_009962,
VSP_009964, VSP_009965;
Note=Contains a phosphothreonine at position 670. Contains a
phosphoserine at position 672. {ECO:0000244|PubMed:21183079};
Name=3;
IsoId=Q08460-3; Sequence=VSP_009961, VSP_009964;
Name=4; Synonyms=STREX-1;
IsoId=Q08460-4; Sequence=VSP_009961, VSP_009963, VSP_009964;
Name=5;
IsoId=Q08460-5; Sequence=VSP_009959;
-!- 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+).
-!- 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 (By similarity). {ECO:0000250}.
-!- 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 (By similarity). {ECO:0000250}.
-!- MISCELLANEOUS: The protein was initially thought to contain two
functionally distinct parts: The core channel (from the N-terminus
to the S9 segment) that mediates the channel activity, and the
cytoplasmic tail (from the S9 segment to the C-terminus) that
mediates the calcium sensing. The situation is however more
complex, since the core channel contains binding sites for 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=AAA50215.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; U09383; AAA50215.1; ALT_INIT; mRNA.
EMBL; L16912; AAA39746.1; -; mRNA.
EMBL; AF156674; AAD49225.1; -; mRNA.
EMBL; AF465244; AAL69971.1; -; mRNA.
CCDS; CCDS79275.1; -. [Q08460-3]
CCDS; CCDS79276.1; -. [Q08460-4]
CCDS; CCDS79277.1; -. [Q08460-1]
PIR; A48206; A48206.
PIR; I49017; I49017.
RefSeq; NP_001240294.1; NM_001253365.1.
RefSeq; NP_001240298.1; NM_001253369.1.
RefSeq; NP_034740.2; NM_010610.3.
UniGene; Mm.343607; -.
UniGene; Mm.486347; -.
ProteinModelPortal; Q08460; -.
SMR; Q08460; -.
BioGrid; 200913; 179.
DIP; DIP-42413N; -.
IntAct; Q08460; 194.
MINT; MINT-1203219; -.
STRING; 10090.ENSMUSP00000136447; -.
ChEMBL; CHEMBL2800; -.
DrugBank; DB08837; Tetraethylammonium.
GuidetoPHARMACOLOGY; 380; -.
iPTMnet; Q08460; -.
PhosphoSitePlus; Q08460; -.
SwissPalm; Q08460; -.
MaxQB; Q08460; -.
PaxDb; Q08460; -.
PeptideAtlas; Q08460; -.
PRIDE; Q08460; -.
GeneID; 16531; -.
KEGG; mmu:16531; -.
UCSC; uc029sfy.1; mouse. [Q08460-2]
CTD; 3778; -.
MGI; MGI:99923; Kcnma1.
eggNOG; KOG1420; Eukaryota.
eggNOG; ENOG410YUX1; LUCA.
HOGENOM; HOG000019856; -.
HOVERGEN; HBG052222; -.
InParanoid; Q08460; -.
KO; K04936; -.
PhylomeDB; Q08460; -.
ChiTaRS; Kcnma1; mouse.
PRO; PR:Q08460; -.
Proteomes; UP000000589; Unplaced.
GO; GO:0016324; C:apical plasma membrane; IDA:MGI.
GO; GO:0005901; C:caveola; ISO:MGI.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0016021; C:integral component of membrane; IDA:MGI.
GO; GO:0005886; C:plasma membrane; IDA:MGI.
GO; GO:0045211; C:postsynaptic membrane; IDA:MGI.
GO; GO:0043195; C:terminal bouton; IDA:MGI.
GO; GO:0008076; C:voltage-gated potassium channel complex; IGI:MGI.
GO; GO:0003779; F:actin binding; ISO:MGI.
GO; GO:0015269; F:calcium-activated potassium channel activity; IDA:MGI.
GO; GO:0060072; F:large conductance calcium-activated potassium channel activity; IDA:MGI.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0005267; F:potassium channel activity; IMP:MGI.
GO; GO:0005249; F:voltage-gated potassium channel activity; IDA:MGI.
GO; GO:0007628; P:adult walking behavior; IMP:MGI.
GO; GO:0042491; P:auditory receptor cell differentiation; IMP:MGI.
GO; GO:0048469; P:cell maturation; IMP:MGI.
GO; GO:0030007; P:cellular potassium ion homeostasis; ISO:MGI.
GO; GO:0007268; P:chemical synaptic transmission; IMP:MGI.
GO; GO:0007623; P:circadian rhythm; IMP:MGI.
GO; GO:0060082; P:eye blink reflex; IMP:MGI.
GO; GO:0045475; P:locomotor rhythm; IMP:MGI.
GO; GO:0060073; P:micturition; IMP:MGI.
GO; GO:0045794; P:negative regulation of cell volume; IMP:MGI.
GO; GO:0050885; P:neuromuscular process controlling balance; IMP:MGI.
GO; GO:0019228; P:neuronal action potential; IMP:MGI.
GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
GO; GO:0006813; P:potassium ion transport; IDA:MGI.
GO; GO:0051260; P:protein homooligomerization; IDA:MGI.
GO; GO:0032344; P:regulation of aldosterone metabolic process; IMP:MGI.
GO; GO:0042391; P:regulation of membrane potential; IDA:MGI.
GO; GO:0060087; P:relaxation of vascular smooth muscle; IMP:MGI.
GO; GO:0051592; P:response to calcium ion; ISO:MGI.
GO; GO:0034465; P:response to carbon monoxide; ISO:MGI.
GO; GO:0001666; P:response to hypoxia; IDA:MGI.
GO; GO:0006970; P:response to osmotic stress; ISO:MGI.
GO; GO:0046541; P:saliva secretion; IGI:MGI.
GO; GO:0007605; P:sensory perception of sound; IMP:MGI.
GO; GO:0060083; P:smooth muscle contraction involved in micturition; IMP:MGI.
GO; GO:0042311; P:vasodilation; IMP:MGI.
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;
Alternative splicing; Calcium; Cell membrane; Complete proteome;
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 1209 Calcium-activated potassium channel
subunit alpha-1.
/FTId=PRO_0000054134.
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; Voltage-sensor; 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 1209 Cytoplasmic. {ECO:0000255}.
DOMAIN 415 558 RCK N-terminal.
REGION 556 576 Segment S7.
REGION 613 633 Segment S8.
REGION 681 685 Heme-binding motif.
REGION 783 803 Segment S9.
REGION 1005 1025 Segment S10.
MOTIF 352 355 Selectivity for potassium.
MOTIF 976 998 Calcium bowl.
COMPBIAS 4 10 Poly-Gly.
COMPBIAS 13 23 Poly-Gly.
COMPBIAS 40 60 Poly-Ser.
METAL 439 439 Magnesium. {ECO:0000305}.
METAL 462 462 Magnesium. {ECO:0000305}.
METAL 464 464 Magnesium. {ECO:0000305}.
METAL 985 985 Calcium; via carbonyl oxygen.
{ECO:0000250}.
METAL 988 988 Calcium; via carbonyl oxygen.
{ECO:0000250}.
METAL 991 991 Calcium. {ECO:0000250}.
METAL 993 993 Calcium. {ECO:0000250}.
MOD_RES 709 709 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 711 711 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 724 724 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 728 728 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 916 916 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 924 924 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 928 928 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
LIPID 118 118 S-palmitoyl cysteine. {ECO:0000250}.
LIPID 119 119 S-palmitoyl cysteine. {ECO:0000250}.
LIPID 121 121 S-palmitoyl cysteine. {ECO:0000250}.
VAR_SEQ 1 65 Missing (in isoform 5).
{ECO:0000303|PubMed:7687074}.
/FTId=VSP_009959.
VAR_SEQ 1 50 MANGGGGGGGSSGGGGGGGGGSGLRMSSNIHANNLSLDASS
SSSSSSSSS -> MELEHPKSPPYP (in isoform 2).
{ECO:0000303|PubMed:7687074}.
/FTId=VSP_009960.
VAR_SEQ 643 646 Missing (in isoform 2, isoform 3 and
isoform 4). {ECO:0000303|PubMed:10517674,
ECO:0000303|PubMed:12388098,
ECO:0000303|PubMed:7687074}.
/FTId=VSP_009961.
VAR_SEQ 702 702 L -> LIYF (in isoform 2).
{ECO:0000303|PubMed:7687074}.
/FTId=VSP_009962.
VAR_SEQ 702 702 L -> PKMSIYKRMRRACCFDCGRSERDCSCMSGRVRGNVD
TLERTFPLSSVSVNDCSTSFRAF (in isoform 4).
{ECO:0000303|PubMed:10517674}.
/FTId=VSP_009963.
VAR_SEQ 948 974 Missing (in isoform 2, isoform 3 and
isoform 4). {ECO:0000303|PubMed:10517674,
ECO:0000303|PubMed:12388098,
ECO:0000303|PubMed:7687074}.
/FTId=VSP_009964.
VAR_SEQ 1203 1209 RKEMVYR -> ATRMTRMGQAEKKWFTDEPDNAYPRNIQIK
PMSTHMANQINQYKSTSSLIPPIREVEDEC (in
isoform 2). {ECO:0000303|PubMed:7687074}.
/FTId=VSP_009965.
MUTAGEN 151 151 V->T: Loss of phosphorylation-independent
activation of channel activity by
ethanol. CaMK2-dependent phosphorylation
leads to populations of partially
phosphorylated tetramers with a range of
responses to ethanol from activation to
inhibition.
{ECO:0000269|PubMed:16341213}.
MUTAGEN 272 272 R->Q: Alters the voltage-dependent
gating. {ECO:0000269|PubMed:11112549}.
MUTAGEN 278 278 R->Q: Alters the voltage-dependent
gating. {ECO:0000269|PubMed:11112549}.
MUTAGEN 284 284 E->R: Alters the voltage-dependent
gating; when associated with R-287.
{ECO:0000269|PubMed:11112549}.
MUTAGEN 287 287 Q->R: Alters the voltage-dependent
gating; when associated with K-284.
{ECO:0000269|PubMed:11112549}.
MUTAGEN 427 427 D->A: Does not affect sensitivity to
Ca(2+). {ECO:0000269|PubMed:12192411}.
MUTAGEN 432 432 D->A: Reduced sensitivity to Ca(2+).
{ECO:0000269|PubMed:12192411}.
MUTAGEN 434 434 D->A: Does not affect sensitivity to
Ca(2+). {ECO:0000269|PubMed:12192411}.
MUTAGEN 439 439 E->A: Abolishes sensitivity to Mg(2+),
but not sensitivity to Ca(2+).
{ECO:0000269|PubMed:12192410}.
MUTAGEN 444 444 H->G: Reduces sensitivity to Mg(2+), but
not sensitivity to Ca(2+).
{ECO:0000269|PubMed:12192410}.
MUTAGEN 461 461 T->A: Reduces sensitivity to Mg(2+), but
not sensitivity to Ca(2+).
{ECO:0000269|PubMed:12192410}.
MUTAGEN 462 462 Q->C: Reduces sensitivity to Mg(2+), but
not sensitivity to Ca(2+).
{ECO:0000269|PubMed:12192410}.
MUTAGEN 464 464 E->D,A: Remains sensitive to Mg(2+).
{ECO:0000269|PubMed:12192410,
ECO:0000269|PubMed:12192411}.
MUTAGEN 464 464 E->N: Abolishes sensitivity to Mg(2+),
but not sensitivity to Ca(2+).
{ECO:0000269|PubMed:12192410,
ECO:0000269|PubMed:12192411}.
MUTAGEN 992 996 DDDPD->AAAAA: Alters calcium binding.
{ECO:0000269|PubMed:12149279}.
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


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