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Voltage-dependent L-type calcium channel subunit alpha-1C (Calcium channel, L type, alpha-1 polypeptide, isoform 1, cardiac muscle) (MELC-CC) (Mouse brain class C) (MBC) (Voltage-gated calcium channel subunit alpha Cav1.2)

 CAC1C_MOUSE             Reviewed;        2139 AA.
Q01815; Q04476; Q61242; Q99242;
15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
12-SEP-2018, entry version 187.
RecName: Full=Voltage-dependent L-type calcium channel subunit alpha-1C;
AltName: Full=Calcium channel, L type, alpha-1 polypeptide, isoform 1, cardiac muscle;
AltName: Full=MELC-CC;
AltName: Full=Mouse brain class C;
Short=MBC;
AltName: Full=Voltage-gated calcium channel subunit alpha Cav1.2;
Name=Cacna1c; Synonyms=Cach2, Cacn2, Cacnl1a1, Cchl1a1;
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], ALTERNATIVE SPLICING, AND TISSUE
SPECIFICITY.
TISSUE=Brain;
PubMed=1385406;
Ma W.-J., Holz R.W., Uhler M.D.;
"Expression of a cDNA for a neuronal calcium channel alpha1 subunit
enhances secretion from adrenal chromaffin cells.";
J. Biol. Chem. 267:22728-22732(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 1162-1455 (ISOFORMS 1 AND 2).
STRAIN=ICR; TISSUE=Ovary;
PubMed=2173707;
Perez-Reyes E., Wei X., Castellano A., Birnbaumer L.;
"Molecular diversity of L-type calcium channels. Evidence for
alternative splicing of the transcripts of three non-allelic genes.";
J. Biol. Chem. 265:20430-20436(1990).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 762-1070.
Chaudhari N.;
Submitted (JAN-1993) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 265-2139 (ISOFORM 3).
STRAIN=DBA/2J; TISSUE=Erythroleukemia;
PubMed=7814415; DOI=10.1074/jbc.270.1.483;
Ma Y., Kobrinsky E., Marks A.R.;
"Cloning and expression of a novel truncated calcium channel from non-
excitable cells.";
J. Biol. Chem. 270:483-493(1995).
[5]
DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
PubMed=10973973; DOI=10.1074/jbc.M006467200;
Seisenberger C., Specht V., Welling A., Platzer J., Pfeifer A.,
Kuehbandner S., Striessnig J., Klugbauer N., Feil R., Hofmann F.;
"Functional embryonic cardiomyocytes after disruption of the L-type
alpha1C (Cav1.2) calcium channel gene in the mouse.";
J. Biol. Chem. 275:39193-39199(2000).
[6]
FUNCTION, ACTIVITY REGULATION, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
PubMed=14609949; DOI=10.1093/emboj/cdg583;
Moosmang S., Schulla V., Welling A., Feil R., Feil S., Wegener J.W.,
Hofmann F., Klugbauer N.;
"Dominant role of smooth muscle L-type calcium channel Cav1.2 for
blood pressure regulation.";
EMBO J. 22:6027-6034(2003).
[7]
INTERACTION WITH CABP5, TISSUE SPECIFICITY, FUNCTION, AND SUBCELLULAR
LOCATION.
PubMed=18586882; DOI=10.1167/iovs.08-2236;
Rieke F., Lee A., Haeseleer F.;
"Characterization of Ca2+-binding protein 5 knockout mouse retina.";
Invest. Ophthalmol. Vis. Sci. 49:5126-5135(2008).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-469; THR-476; SER-808;
SER-815; SER-1670 AND SER-1691, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Heart, and Lung;
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).
[9]
INTERACTION WITH CIB1.
PubMed=20639889; DOI=10.1038/nm.2181;
Heineke J., Auger-Messier M., Correll R.N., Xu J., Benard M.J.,
Yuan W., Drexler H., Parise L.V., Molkentin J.D.;
"CIB1 is a regulator of pathological cardiac hypertrophy.";
Nat. Med. 16:872-879(2010).
[10]
FUNCTION, ACTIVITY REGULATION, SUBCELLULAR LOCATION, TISSUE
SPECIFICITY, AND MUTAGENESIS OF 1794-HIS--PRO-1796 AND
1797-PRO--LEU-2139.
PubMed=21216955; DOI=10.1074/jbc.M110.175307;
Fu Y., Westenbroek R.E., Yu F.H., Clark J.P. III, Marshall M.R.,
Scheuer T., Catterall W.A.;
"Deletion of the distal C terminus of CaV1.2 channels leads to loss of
beta-adrenergic regulation and heart failure in vivo.";
J. Biol. Chem. 286:12617-12626(2011).
[11]
FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-1670, AND
PHOSPHORYLATION AT SER-1897.
PubMed=25368181; DOI=10.1073/pnas.1419129111;
Fu Y., Westenbroek R.E., Scheuer T., Catterall W.A.;
"Basal and beta-adrenergic regulation of the cardiac calcium channel
CaV1.2 requires phosphorylation of serine 1700.";
Proc. Natl. Acad. Sci. U.S.A. 111:16598-16603(2014).
[12]
FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-1897, AND
MUTAGENESIS OF SER-1897.
PubMed=28119464; DOI=10.1126/scisignal.aaf9647;
Nystoriak M.A., Nieves-Cintron M., Patriarchi T., Buonarati O.R.,
Prada M.P., Morotti S., Grandi E., Fernandes J.D., Forbush K.,
Hofmann F., Sasse K.C., Scott J.D., Ward S.M., Hell J.W., Navedo M.F.;
"Ser1928 phosphorylation by PKA stimulates the L-type Ca2+ channel
CaV1.2 and vasoconstriction during acute hyperglycemia and diabetes.";
Sci. Signal. 10:0-0(2017).
-!- FUNCTION: Pore-forming, alpha-1C subunit of the voltage-gated
calcium channel that gives rise to L-type calcium currents
(PubMed:14609949, PubMed:18586882, PubMed:21216955,
PubMed:25368181, PubMed:28119464). Mediates influx of calcium ions
into the cytoplasm, and thereby triggers calcium release from the
sarcoplasm (By similarity). Plays an important role in excitation-
contraction coupling in the heart. Required for normal heart
development and normal regulation of heart rhythm
(PubMed:21216955). Required for normal contraction of smooth
muscle cells in blood vessels and in the intestine. Essential for
normal blood pressure regulation via its role in the contraction
of arterial smooth muscle cells (PubMed:14609949,
PubMed:28119464). Long-lasting (L-type) calcium channels belong to
the 'high-voltage activated' (HVA) group (Probable).
{ECO:0000250|UniProtKB:P15381, ECO:0000269|PubMed:14609949,
ECO:0000269|PubMed:18586882, ECO:0000269|PubMed:21216955,
ECO:0000269|PubMed:25368181, ECO:0000269|PubMed:28119464,
ECO:0000305}.
-!- ACTIVITY REGULATION: Inhibited by dihydropyridines (DHP), such as
isradipine (PubMed:14609949, PubMed:21216955). Inhibited by
nifedipine. Channel activity is regulated by Ca(2+) and
calmodulin. Binding of STAC1, STAC2 or STAC3 to a region that
overlaps with the calmodulin binding site inhibits channel
inactivation by Ca(2+) and calmodulin (By similarity). Binding of
calmodulin or CABP1 at the same regulatory sites results in
opposite effects on the channel function. Shear stress and
pressure increases calcium channel activity (By similarity).
{ECO:0000250|UniProtKB:P15381, ECO:0000250|UniProtKB:Q13936,
ECO:0000269|PubMed:14609949, ECO:0000269|PubMed:21216955}.
-!- SUBUNIT: Component of a calcium channel complex consisting of a
pore-forming alpha subunit (CACNA1C) and ancillary beta, gamma and
delta subunits. The channel complex contains alpha, beta, gamma
and delta subunits in a 1:1:1:1 ratio, i.e. it contains only one
of each type of subunit. CACNA1C channel activity is modulated by
ancillary subunits, such as CACNB1, CACNB2, CACNB3, CACNA2D1 and
CACNA2D4 (By similarity). Intereracts with the gamma subunits
CACNG4, CACNG6, CACNG7 and CACNG8 (By similarity). Interacts with
CACNB1 (By similarity). Interacts with CACNB2. Identified in a
complex with CACNA2D4 and CACNB3. Interacts with CACNB3. Interacts
with CACNA2D1. Interacts with CACNA2D4. Interacts with CALM1.
Interacts (via the N-terminus and the C-terminal C and IQ motifs)
with CABP1; this inhibits Ca(2+)-dependent channel inactivation.
The binding via the C motif is calcium independent whereas the
binding via IQ requires the presence of calcium and is mutually
exclusive with calmodulin binding (By similarity). The binding to
the cytoplasmic N-terminal domain is calcium independent but is
essential for the channel modulation (By similarity). Interacts
(via C-terminal CDB motif) with CABP5; in a calcium-dependent
manner (PubMed:18586882). Interacts with CIB1; the interaction
increases upon cardiomyocytes hypertrophy (PubMed:20639889).
Interacts with STAC2 and STAC3; this inhibits channel inactivation
(By similarity). {ECO:0000250|UniProtKB:P15381,
ECO:0000250|UniProtKB:Q13936, ECO:0000269|PubMed:18586882,
ECO:0000269|PubMed:20639889}.
-!- INTERACTION:
P51637:Cav3; NbExp=4; IntAct=EBI-644904, EBI-298576;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14609949,
ECO:0000269|PubMed:18586882, ECO:0000269|PubMed:21216955}; Multi-
pass membrane protein {ECO:0000305}. Cell membrane, sarcolemma
{ECO:0000269|PubMed:25368181, ECO:0000269|PubMed:28119464}; Multi-
pass membrane protein {ECO:0000305}. Perikaryon
{ECO:0000250|UniProtKB:P22002}. Cell junction, synapse,
postsynaptic cell membrane, postsynaptic density
{ECO:0000250|UniProtKB:P22002}. Cell projection, dendrite
{ECO:0000250|UniProtKB:P22002}. Note=Colocalizes with ryanodine
receptors in distinct clusters at the junctional membrane, where
the sarcolemma and the sarcoplasmic reticulum are in close
contact. The interaction between RRAD and CACNB2 promotes the
expression of CACNA1C at the cell membrane.
{ECO:0000250|UniProtKB:P15381}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Comment=Additional isoforms seem to exist.;
Name=1; Synonyms=CACH2A;
IsoId=Q01815-1; Sequence=Displayed;
Name=2; Synonyms=CACH2D;
IsoId=Q01815-2; Sequence=VSP_000900, VSP_000901;
Name=3; Synonyms=Truncated;
IsoId=Q01815-3; Sequence=VSP_000896, VSP_000897, VSP_000898,
VSP_000899, VSP_000901;
-!- TISSUE SPECIFICITY: Detected in embryonic heart (PubMed:10973973,
PubMed:21216955). Detected in retina in rod bipolar cells
(PubMed:18586882). Detected in tibialis artery (at protein level)
(PubMed:14609949). Detected in smooth muscle cells from tibialis
artery and in mesenteric artery (PubMed:14609949). High expression
in heart, followed by brain and spinal cord (PubMed:1385406).
{ECO:0000269|PubMed:10973973, ECO:0000269|PubMed:1385406,
ECO:0000269|PubMed:14609949, ECO:0000269|PubMed:18586882,
ECO:0000269|PubMed:21216955}.
-!- DOMAIN: Each of the four internal repeats contains five
hydrophobic transmembrane segments (S1, S2, S3, S5, S6) and one
positively charged transmembrane segment (S4). S4 segments
probably represent the voltage-sensor and are characterized by a
series of positively charged amino acids at every third position.
-!- DOMAIN: Binding of intracellular calcium through the EF-hand motif
inhibits the opening of the channel.
{ECO:0000250|UniProtKB:P15381}.
-!- PTM: Phosphorylation by PKA activates the channel. Elevated levels
of blood glucose lead to increased phosphorylation by PKA.
{ECO:0000269|PubMed:28119464}.
-!- DISRUPTION PHENOTYPE: Mutant embryos appear normal and have normal
heartbeat at 12.5 dpc. All are dead by 14.5 dpc.
{ECO:0000269|PubMed:10973973}.
-!- SIMILARITY: Belongs to the calcium channel alpha-1 subunit (TC
1.A.1.11) family. CACNA1C subfamily. {ECO:0000305}.
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EMBL; L01776; AAB59633.1; -; mRNA.
EMBL; M57973; AAA63291.1; -; mRNA.
EMBL; L06233; AAA37351.1; -; mRNA.
EMBL; U17869; AAA62612.1; -; mRNA.
CCDS; CCDS71821.1; -. [Q01815-3]
CCDS; CCDS80590.1; -. [Q01815-1]
PIR; A44467; A44467.
RefSeq; NP_001153005.1; NM_001159533.2. [Q01815-1]
UniGene; Mm.41628; -.
UniGene; Mm.436656; -.
ProteinModelPortal; Q01815; -.
SMR; Q01815; -.
BioGrid; 198432; 4.
ComplexPortal; CPX-3194; Cardiac muscle VGCC complex.
CORUM; Q01815; -.
DIP; DIP-32232N; -.
IntAct; Q01815; 93.
MINT; Q01815; -.
BindingDB; Q01815; -.
ChEMBL; CHEMBL2529; -.
GuidetoPHARMACOLOGY; 529; -.
TCDB; 1.A.1.11.6; the voltage-gated ion channel (vic) superfamily.
iPTMnet; Q01815; -.
PhosphoSitePlus; Q01815; -.
SwissPalm; Q01815; -.
MaxQB; Q01815; -.
PeptideAtlas; Q01815; -.
PRIDE; Q01815; -.
Ensembl; ENSMUST00000075591; ENSMUSP00000075021; ENSMUSG00000051331. [Q01815-1]
Ensembl; ENSMUST00000078320; ENSMUSP00000077433; ENSMUSG00000051331. [Q01815-1]
Ensembl; ENSMUST00000112825; ENSMUSP00000108444; ENSMUSG00000051331. [Q01815-3]
GeneID; 12288; -.
KEGG; mmu:12288; -.
UCSC; uc009dls.3; mouse. [Q01815-3]
UCSC; uc012erl.2; mouse. [Q01815-1]
CTD; 775; -.
MGI; MGI:103013; Cacna1c.
GeneTree; ENSGT00830000128247; -.
HOGENOM; HOG000231529; -.
HOVERGEN; HBG050763; -.
InParanoid; Q01815; -.
KO; K04850; -.
PhylomeDB; Q01815; -.
Reactome; R-MMU-422356; Regulation of insulin secretion.
Reactome; R-MMU-5576892; Phase 0 - rapid depolarisation.
Reactome; R-MMU-5576893; Phase 2 - plateau phase.
ChiTaRS; Cacna1c; mouse.
PRO; PR:Q01815; -.
Proteomes; UP000000589; Chromosome 6.
Bgee; ENSMUSG00000051331; Expressed in 195 organ(s), highest expression level in heart.
ExpressionAtlas; Q01815; baseline and differential.
Genevisible; Q01815; MM.
GO; GO:0002095; C:caveolar macromolecular signaling complex; IDA:MGI.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0030425; C:dendrite; ISO:MGI.
GO; GO:0043198; C:dendritic shaft; IDA:MGI.
GO; GO:0016021; C:integral component of membrane; ISO:MGI.
GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
GO; GO:1990454; C:L-type voltage-gated calcium channel complex; ISS:UniProtKB.
GO; GO:0016020; C:membrane; IDA:MGI.
GO; GO:0043025; C:neuronal cell body; IDA:MGI.
GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IDA:MGI.
GO; GO:0014069; C:postsynaptic density; ISO:MGI.
GO; GO:0045211; C:postsynaptic membrane; ISS:SynGO.
GO; GO:0042734; C:presynaptic membrane; ISO:MGI.
GO; GO:0032991; C:protein-containing complex; ISO:MGI.
GO; GO:0042383; C:sarcolemma; ISO:MGI.
GO; GO:0030315; C:T-tubule; IDA:MGI.
GO; GO:0005891; C:voltage-gated calcium channel complex; ISS:BHF-UCL.
GO; GO:0030018; C:Z disc; IDA:MGI.
GO; GO:0051393; F:alpha-actinin binding; ISS:BHF-UCL.
GO; GO:0005516; F:calmodulin binding; ISO:MGI.
GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL.
GO; GO:0008331; F:high voltage-gated calcium channel activity; ISS:UniProtKB.
GO; GO:0044325; F:ion channel binding; ISO:MGI.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
GO; GO:0051721; F:protein phosphatase 2A binding; ISO:MGI.
GO; GO:0031369; F:translation initiation factor binding; ISO:MGI.
GO; GO:0005245; F:voltage-gated calcium channel activity; IDA:MGI.
GO; GO:0086056; F:voltage-gated calcium channel activity involved in AV node cell action potential; ISS:BHF-UCL.
GO; GO:0086007; F:voltage-gated calcium channel activity involved in cardiac muscle cell action potential; ISS:BHF-UCL.
GO; GO:1905030; F:voltage-gated ion channel activity involved in regulation of postsynaptic membrane potential; IMP:SynGO.
GO; GO:0007628; P:adult walking behavior; IGI:MGI.
GO; GO:0070509; P:calcium ion import; ISO:MGI.
GO; GO:0017156; P:calcium ion regulated exocytosis; IMP:MGI.
GO; GO:0070588; P:calcium ion transmembrane transport; ISO:MGI.
GO; GO:0061577; P:calcium ion transmembrane transport via high voltage-gated calcium channel; ISS:UniProtKB.
GO; GO:0006816; P:calcium ion transport; IDA:MGI.
GO; GO:0060402; P:calcium ion transport into cytosol; ISS:UniProtKB.
GO; GO:0043010; P:camera-type eye development; ISO:MGI.
GO; GO:0061337; P:cardiac conduction; ISS:UniProtKB.
GO; GO:0086002; P:cardiac muscle cell action potential involved in contraction; ISS:BHF-UCL.
GO; GO:0006874; P:cellular calcium ion homeostasis; IMP:MGI.
GO; GO:0007268; P:chemical synaptic transmission; IMP:MGI.
GO; GO:0035115; P:embryonic forelimb morphogenesis; ISO:MGI.
GO; GO:0042593; P:glucose homeostasis; IMP:MGI.
GO; GO:0030252; P:growth hormone secretion; IDA:MGI.
GO; GO:0007507; P:heart development; ISO:MGI.
GO; GO:0002520; P:immune system development; ISO:MGI.
GO; GO:0030073; P:insulin secretion; IMP:MGI.
GO; GO:0086010; P:membrane depolarization during action potential; IBA:GO_Central.
GO; GO:0098912; P:membrane depolarization during atrial cardiac muscle cell action potential; ISS:BHF-UCL.
GO; GO:0086045; P:membrane depolarization during AV node cell action potential; ISS:BHF-UCL.
GO; GO:0086012; P:membrane depolarization during cardiac muscle cell action potential; ISS:BHF-UCL.
GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISO:MGI.
GO; GO:0008217; P:regulation of blood pressure; IMP:MGI.
GO; GO:0010881; P:regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion; ISS:UniProtKB.
GO; GO:0086091; P:regulation of heart rate by cardiac conduction; ISS:BHF-UCL.
GO; GO:0046620; P:regulation of organ growth; IMP:MGI.
GO; GO:0019229; P:regulation of vasoconstriction; IMP:MGI.
GO; GO:0098911; P:regulation of ventricular cardiac muscle cell action potential; ISS:BHF-UCL.
GO; GO:0006939; P:smooth muscle contraction; IMP:MGI.
GO; GO:0060083; P:smooth muscle contraction involved in micturition; IMP:MGI.
GO; GO:0008542; P:visual learning; IMP:MGI.
Gene3D; 1.20.120.350; -; 4.
InterPro; IPR031688; CAC1F_C.
InterPro; IPR031649; GPHH_dom.
InterPro; IPR005821; Ion_trans_dom.
InterPro; IPR014873; VDCC_a1su_IQ.
InterPro; IPR005451; VDCC_L_a1csu.
InterPro; IPR005446; VDCC_L_a1su.
InterPro; IPR002077; VDCCAlpha1.
InterPro; IPR027359; Volt_channel_dom_sf.
Pfam; PF08763; Ca_chan_IQ; 1.
Pfam; PF16885; CAC1F_C; 1.
Pfam; PF16905; GPHH; 1.
Pfam; PF00520; Ion_trans; 4.
PRINTS; PR00167; CACHANNEL.
PRINTS; PR01630; LVDCCALPHA1.
PRINTS; PR01635; LVDCCALPHA1C.
SMART; SM01062; Ca_chan_IQ; 1.
1: Evidence at protein level;
Alternative splicing; Calcium; Calcium channel; Calcium transport;
Calmodulin-binding; Cell junction; Cell membrane; Cell projection;
Complete proteome; Disulfide bond; Glycoprotein; Ion channel;
Ion transport; Membrane; Metal-binding; Phosphoprotein;
Postsynaptic cell membrane; Reference proteome; Repeat; Synapse;
Transmembrane; Transmembrane helix; Transport; Voltage-gated channel.
CHAIN 1 2139 Voltage-dependent L-type calcium channel
subunit alpha-1C.
/FTId=PRO_0000053929.
TOPO_DOM 1 124 Cytoplasmic. {ECO:0000305}.
TRANSMEM 125 143 Helical; Name=S1 of repeat I.
{ECO:0000250|UniProtKB:P07293}.
TOPO_DOM 144 158 Extracellular. {ECO:0000305}.
TRANSMEM 159 179 Helical; Name=S2 of repeat I.
{ECO:0000250|UniProtKB:P07293}.
TOPO_DOM 180 188 Cytoplasmic. {ECO:0000305}.
TRANSMEM 189 209 Helical; Name=S3 of repeat I.
{ECO:0000250|UniProtKB:P07293}.
TOPO_DOM 210 232 Extracellular. {ECO:0000305}.
TRANSMEM 233 251 Helical; Name=S4 of repeat I.
{ECO:0000250|UniProtKB:P07293}.
TOPO_DOM 252 268 Cytoplasmic. {ECO:0000305}.
TRANSMEM 269 290 Helical; Name=S5 of repeat I.
{ECO:0000250|UniProtKB:P07293}.
TOPO_DOM 291 350 Extracellular. {ECO:0000305}.
INTRAMEM 351 372 Pore-forming.
{ECO:0000250|UniProtKB:P07293}.
TOPO_DOM 373 380 Extracellular. {ECO:0000305}.
TRANSMEM 381 401 Helical; Name=S6 of repeat I.
{ECO:0000250|UniProtKB:P07293}.
TOPO_DOM 402 524 Cytoplasmic. {ECO:0000305}.
TRANSMEM 525 543 Helical; Name=S1 of repeat II.
{ECO:0000250|UniProtKB:P07293}.
TOPO_DOM 544 554 Extracellular. {ECO:0000305}.
TRANSMEM 555 575 Helical; Name=S2 of repeat II.
{ECO:0000250|UniProtKB:P07293}.
TOPO_DOM 576 586 Cytoplasmic. {ECO:0000305}.
TRANSMEM 587 606 Helical; Name=S3 of repeat II.
{ECO:0000250|UniProtKB:P07293}.
TOPO_DOM 607 615 Extracellular. {ECO:0000305}.
TRANSMEM 616 634 Helical; Name=S4 of repeat II.
{ECO:0000250|UniProtKB:P07293}.
TOPO_DOM 635 653 Cytoplasmic. {ECO:0000305}.
TRANSMEM 654 673 Helical; Name=S5 of repeat II.
{ECO:0000250|UniProtKB:P07293}.
TOPO_DOM 674 693 Extracellular. {ECO:0000305}.
INTRAMEM 694 715 Pore-forming.
{ECO:0000250|UniProtKB:P07293}.
TOPO_DOM 716 725 Extracellular. {ECO:0000305}.
TRANSMEM 726 745 Helical; Name=S6 of repeat II.
{ECO:0000250|UniProtKB:P07293}.
TOPO_DOM 746 900 Cytoplasmic. {ECO:0000305}.
TRANSMEM 901 919 Helical; Name=S1 of repeat III.
{ECO:0000250|UniProtKB:P07293}.
TOPO_DOM 920 931 Extracellular. {ECO:0000305}.
TRANSMEM 932 951 Helical; Name=S2 of repeat III.
{ECO:0000250|UniProtKB:P07293}.
TOPO_DOM 952 967 Cytoplasmic. {ECO:0000305}.
TRANSMEM 968 986 Helical; Name=S3 of repeat III.
{ECO:0000250|UniProtKB:P07293}.
TOPO_DOM 987 993 Extracellular. {ECO:0000305}.
TRANSMEM 994 1012 Helical; Name=S4 of repeat III.
{ECO:0000250|UniProtKB:P07293}.
TOPO_DOM 1013 1031 Cytoplasmic. {ECO:0000305}.
TRANSMEM 1032 1051 Helical; Name=S5 of repeat III.
{ECO:0000250|UniProtKB:P07293}.
TOPO_DOM 1052 1101 Extracellular. {ECO:0000305}.
INTRAMEM 1102 1122 Pore-forming.
{ECO:0000250|UniProtKB:P07293}.
TOPO_DOM 1123 1139 Extracellular. {ECO:0000305}.
TRANSMEM 1140 1161 Helical; Name=S6 of repeat III.
{ECO:0000250|UniProtKB:P07293}.
TOPO_DOM 1162 1219 Cytoplasmic. {ECO:0000305}.
TRANSMEM 1220 1241 Helical; Name=S1 of repeat IV.
{ECO:0000250|UniProtKB:P07293}.
TOPO_DOM 1242 1249 Extracellular. {ECO:0000305}.
TRANSMEM 1250 1271 Helical; Name=S2 of repeat IV.
{ECO:0000250|UniProtKB:P07293}.
TOPO_DOM 1272 1281 Cytoplasmic. {ECO:0000305}.
TRANSMEM 1282 1301 Helical; Name=S3 of repeat IV.
{ECO:0000250|UniProtKB:P07293}.
TOPO_DOM 1302 1324 Extracellular. {ECO:0000305}.
TRANSMEM 1325 1343 Helical; Name=S4 of repeat IV.
{ECO:0000250|UniProtKB:P07293}.
TOPO_DOM 1344 1361 Cytoplasmic. {ECO:0000305}.
TRANSMEM 1362 1382 Helical; Name=S5 of repeat IV.
{ECO:0000250|UniProtKB:P07293}.
TOPO_DOM 1383 1404 Extracellular. {ECO:0000305}.
INTRAMEM 1405 1423 Pore-forming.
{ECO:0000250|UniProtKB:P07293}.
TOPO_DOM 1424 1451 Extracellular. {ECO:0000305}.
TRANSMEM 1452 1476 Helical; Name=S6 of repeat IV.
{ECO:0000250|UniProtKB:P07293}.
TOPO_DOM 1477 2139 Cytoplasmic. {ECO:0000305}.
REPEAT 111 408 I.
REPEAT 510 756 II.
REPEAT 887 1169 III.
REPEAT 1206 1479 IV.
CA_BIND 1505 1516 {ECO:0000250}.
REGION 47 68 Calmodulin-binding.
{ECO:0000250|UniProtKB:Q13936}.
REGION 428 445 AID/alpha-interaction domain; mediates
interaction with the beta subunit.
{ECO:0000250|UniProtKB:P22002}.
REGION 829 876 Interaction with STAC2.
{ECO:0000250|UniProtKB:Q13936}.
REGION 1089 1178 Dihydropyridine binding.
{ECO:0000250|UniProtKB:P07293}.
REGION 1430 1498 Dihydropyridine binding.
{ECO:0000250|UniProtKB:P07293}.
REGION 1444 1486 Phenylalkylamine binding.
{ECO:0000250|UniProtKB:P07293}.
REGION 1611 1644 Calmodulin-binding.
{ECO:0000250|UniProtKB:Q13936}.
REGION 1611 1638 Important for interaction with STAC1,
STAC2 and STAC3.
{ECO:0000250|UniProtKB:P15381}.
REGION 1617 1637 Calmodulin-binding IQ region.
{ECO:0000250|UniProtKB:Q13936}.
REGION 1651 1670 Important for localization in at the
junctional membrane.
{ECO:0000250|UniProtKB:P15381}.
MOTIF 361 364 Selectivity filter of repeat I.
{ECO:0000250|UniProtKB:P07293}.
MOTIF 704 707 Selectivity filter of repeat II.
{ECO:0000250|UniProtKB:P07293}.
MOTIF 1113 1116 Selectivity filter of repeat III.
{ECO:0000250|UniProtKB:P07293}.
MOTIF 1414 1417 Selectivity filter of repeat IV.
{ECO:0000250|UniProtKB:P07293}.
COMPBIAS 654 660 Poly-Leu.
COMPBIAS 768 774 Poly-Glu.
COMPBIAS 1147 1153 Poly-Ile.
METAL 363 363 Calcium. {ECO:0000250|UniProtKB:P07293}.
METAL 706 706 Calcium. {ECO:0000250|UniProtKB:P07293}.
METAL 1115 1115 Calcium. {ECO:0000250|UniProtKB:P07293}.
SITE 363 363 Calcium ion selectivity and permeability.
{ECO:0000250|UniProtKB:P15381}.
SITE 706 706 Calcium ion selectivity and permeability.
{ECO:0000250|UniProtKB:P15381}.
SITE 1115 1115 Calcium ion selectivity and permeability.
{ECO:0000250|UniProtKB:P15381}.
SITE 1416 1416 Calcium ion selectivity and permeability.
{ECO:0000250|UniProtKB:P15381}.
MOD_RES 469 469 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 476 476 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 808 808 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 815 815 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1487 1487 Phosphoserine; by PKA. {ECO:0000255}.
MOD_RES 1670 1670 Phosphoserine.
{ECO:0000244|PubMed:21183079,
ECO:0000305|PubMed:25368181}.
MOD_RES 1691 1691 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1889 1889 Phosphoserine; by PKA. {ECO:0000255}.
MOD_RES 1897 1897 Phosphoserine; by PKA.
{ECO:0000269|PubMed:25368181,
ECO:0000269|PubMed:28119464}.
CARBOHYD 153 153 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 328 328 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1388 1388 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1439 1439 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 298 326 {ECO:0000250|UniProtKB:P07293}.
DISULFID 316 332 {ECO:0000250|UniProtKB:P07293}.
DISULFID 1058 1069 {ECO:0000250|UniProtKB:P07293}.
DISULFID 1431 1447 {ECO:0000250|UniProtKB:P07293}.
VAR_SEQ 1 264 Missing (in isoform 3).
{ECO:0000303|PubMed:7814415}.
/FTId=VSP_000896.
VAR_SEQ 372 391 MQDAMGYELPWVYFVSLVIF -> VNDAVGRDWPWIYFVTL
III (in isoform 3).
{ECO:0000303|PubMed:7814415}.
/FTId=VSP_000897.
VAR_SEQ 464 464 M -> RGAPAGLHDQKKGKFAWFSHSTETHV (in
isoform 3). {ECO:0000303|PubMed:7814415}.
/FTId=VSP_000898.
VAR_SEQ 932 951 Missing (in isoform 3).
{ECO:0000303|PubMed:7814415}.
/FTId=VSP_000899.
VAR_SEQ 1277 1304 GYFSDPWNVFDFLIVIGSIIDVILSETN -> HYFCDAWNT
FDALIVVGSIVDIAITEVH (in isoform 2).
{ECO:0000303|PubMed:2173707}.
/FTId=VSP_000900.
VAR_SEQ 1305 1315 Missing (in isoform 2 and isoform 3).
{ECO:0000303|PubMed:2173707,
ECO:0000303|PubMed:7814415}.
/FTId=VSP_000901.
MUTAGEN 1670 1670 S->A: Expected to abolish a
phosphorylation site. Decreased channel
activity. No effect on phosphorylation at
S-1897. Causes heart hypertrophy and
decreased exercise tolerance in adult
mice. {ECO:0000269|PubMed:25368181}.
MUTAGEN 1794 1796 HGP->LSK: Strongly decreased channel
activity due to decreased expression at
the cell membrane, leading to hypertrophy
of the right heart ventricle, heart
failure and perinatal death; when
associated with 1797-P--L-2139 DEL.
{ECO:0000269|PubMed:21216955}.
MUTAGEN 1797 2139 Missing: Strongly decreased channel
activity due to decreased expression at
the cell membrane, leading to hypertrophy
of the right heart ventricle, heart
failure and perinatal death; when
associated with 1794-L--K-1796.
{ECO:0000269|PubMed:21216955}.
MUTAGEN 1897 1897 S->A: Loss of phosphorylation site.
Abolishes increased vasoconstriction in
response to elevated blood glucose.
{ECO:0000269|PubMed:28119464}.
CONFLICT 310 310 E -> K (in Ref. 4; AAA62612).
{ECO:0000305}.
CONFLICT 477 477 E -> D (in Ref. 4; AAA62612).
{ECO:0000305}.
CONFLICT 555 555 V -> D (in Ref. 4; AAA62612).
{ECO:0000305}.
CONFLICT 811 812 AD -> GS (in Ref. 4; AAA62612).
{ECO:0000305}.
CONFLICT 822 822 N -> H (in Ref. 4; AAA62612).
{ECO:0000305}.
CONFLICT 825 825 D -> A (in Ref. 4; AAA62612).
{ECO:0000305}.
CONFLICT 831 831 N -> P (in Ref. 4; AAA62612).
{ECO:0000305}.
CONFLICT 837 841 HSNPD -> TPTQT (in Ref. 3; AAA37351).
{ECO:0000305}.
CONFLICT 934 938 GNADY -> FYFDI (in Ref. 3; AAA37351).
{ECO:0000305}.
CONFLICT 942 942 S -> T (in Ref. 3; AAA37351).
{ECO:0000305}.
CONFLICT 946 946 L -> I (in Ref. 3; AAA37351).
{ECO:0000305}.
CONFLICT 949 949 I -> A (in Ref. 3; AAA37351).
{ECO:0000305}.
CONFLICT 977 978 VS -> LC (in Ref. 4; AAA62612).
{ECO:0000305}.
CONFLICT 1065 1065 T -> A (in Ref. 4; AAA62612).
{ECO:0000305}.
CONFLICT 1507 1507 E -> K (in Ref. 4; AAA62612).
{ECO:0000305}.
CONFLICT 1525 1525 Q -> H (in Ref. 4; AAA62612).
{ECO:0000305}.
CONFLICT 1633 1633 K -> E (in Ref. 4; AAA62612).
{ECO:0000305}.
CONFLICT 1959 1959 G -> A (in Ref. 4; AAA62612).
{ECO:0000305}.
CONFLICT 1963 1964 RP -> ST (in Ref. 4; AAA62612).
{ECO:0000305}.
CONFLICT 1970 1970 T -> H (in Ref. 4; AAA62612).
{ECO:0000305}.
CONFLICT 1974 1974 E -> K (in Ref. 4; AAA62612).
{ECO:0000305}.
CONFLICT 2086 2086 A -> R (in Ref. 4; AAA62612).
{ECO:0000305}.
CONFLICT 2097 2097 F -> L (in Ref. 4; AAA62612).
{ECO:0000305}.
CONFLICT 2110 2110 A -> V (in Ref. 4; AAA62612).
{ECO:0000305}.
SEQUENCE 2139 AA; 240138 MW; B564C57A8644E165 CRC64;
MVNENTRMYV PEENHQGSNY GSPRPAHANM NANAAAGLAP EHIPTPGAAL SWQAAIDAAR
QAKLMGSAGN ATISTVSSTQ RKRQQYGKPK KQGGTTATRP PRALLCLTLK NPIRRACISI
VEWKPFEIII LLTIFANCVA LAIYIPFPED DSNATNSNLE RVEYLFLIIF TVEAFLKVIA
YGLLFHPNAY LRNGWNLLDF IIVVVGLFSA ILEQATKADG ANALGGKGAG FDVKALRAFR
VLRPLRLVSG VPSLQVVLNS IIKAMVPLLH IALLVLFVII IYAIIGLELF MGKMHKTCYN
QEGIIDVPAE EDPSPCALET GHGRQCQNGT VCKPGWDGPK HGITNFDNFA FAMLTVFQCI
TMEGWTDVLY WMQDAMGYEL PWVYFVSLVI FGSFFVLNLV LGVLSGEFSK EREKAKARGD
FQKLREKQQL EEDLKGYLDW ITQAEDIDPE NEDEGMDEDK PRNMSMPTSE TESVNTENVA
GGDIEGENCG ARLAHRISKS KFSRYWRRWN RFCRRKCRAA VKSNVFYWLV IFLVFLNTLT
IASEHYNQPH WLTEVQDTAN KALLALFTAE MLLKMYSLGL QAYFVSLFNR FDCFIVCGGI
LETILVETKI MSPLGISVLR CVRLLRIFKI TRYWNSLSNL VASLLNSVRS IASLLLLLFL
FIIIFSLLGM QLFGGKFNFD EMQTRRSTFD NFPQSLLTVF QILTGEDWNS VMYDGIMAYG
GPSFPGMLVC IYFIILFICG NYILLNVFLA IAVDNLADAE SLTSAQKEEE EEKERKKLAR
TASPEKKQEV MEKPAVEESK EEKIELKSIT ADGESPPTTK INMDDLQPSE NEDKSPHSNP
DTAGEEDEEE PEMPVGPRPR PLSELHLKEK AVPMPEASAF FIFSPNNRFR LQCHRIVNDT
IFTNLILFFI LLSSISLAAE DPVQHTSFRN HILGNADYVF TSIFTLEIIL KMTAYGAFLH
KGSFCRNYFN ILDLLVVSVS LISFGIQSSA INVVKILRVL RVLRPLRAIN RAKGLKHVVQ
CVFVAIRTIG NIVIVTTLLQ FMFACIGVQL FKGKLYTCSD SSKQTEAECK GNYITYKDGE
VDHPIIQPRS WENSKFDFDN VLAAMMALFT VSTFEGWPEL LYRSIDSHTE DKGPIYNYRV
EISIFFIIYI IIIAFFMMNI FVGFVIVTFQ EQGEQEYKNC ELDKNQRQCV EYALKARPLR
RYIPKNQHQY KVWYVVNSTY FEYLMFVLIL LNTICLAMQH YGQSCLFKIA MNILNMLFTG
LFTVEMILKL IAFKPKGYFS DPWNVFDFLI VIGSIIDVIL SETNPAEHTQ CSPSMSAEEN
SRISITFFRL FRVMRLVKLL SRGEGIRTLL WTFIKSFQAL PYVALLIVML FFIYAVIGMQ
VFGKIALNDT TEINRNNNFQ TFPQAVLLLF RCATGEAWQD IMLACMPGKK CAPESEPSNS
TEGETPCGSS FAVFYFISFY MLCAFLIINL FVAVIMDNFD YLTRDWSILG PHHLDEFKRI
WAEYDPEAKG RIKHLDVVTL LRRIQPPLGF GKLCPHRVAC KRLVSMNMPL NSDGTVMFNA
TLFALVRTAL RIKTEGNLEQ ANEELRAIIK KIWKRTSMKL LDQVVPPAGD DEVTVGKFYA
TFLIQEYFRK FKKRKEQGLV GKPSQRNALS LQAGLRTLHD IGPEIRRAIS GDLTAEEELD
KAMKEAVSAA SEDDIFRRAG GLFGNHVTYY QSDSRGNFPQ TFATQRPLHI NKTGNNQADT
ESPSHEKLVD STFTPSSYSS TGSNANINNA NNTALGRFPH PAGYSSTVST VEGHGPPLSP
AVRVQEAAWK LSSKRCHSRE SQGATVNQEI FPDETRSVRM SEEAEYCSEP SLLSTDMFSY
QEDEHRQLTC PEEDKREIQP SPKRSFLRSA SLGRRASFHL ECLKRQKDQG GDISQKTALP
LHLVHHQALA VAGLSPLLQR SHSPTTFPRP CPTPPVTPGS RGRPLRPIPT LRLEGAESSE
KLNSSFPSIH CSSWSEETTA CSGSSSMARR ARPVSLTVPS QAGAPGRQFH GSASSLVEAV
LISEGLGQFA QDPKFIEVTT QELADACDMT IEEMENAADN ILSGGAQQSP NGTLLPFVNC
RDPGQDRAVA PEDESCAYAL GRGRSEEALA DSRSYVSNL


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