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Voltage-dependent L-type calcium channel subunit alpha-1C (Calcium channel, L type, alpha-1 polypeptide, isoform 1, cardiac muscle) (Smooth muscle calcium channel blocker receptor) (CACB-receptor) (Voltage-gated calcium channel subunit alpha Cav1.2)

 CAC1C_RABIT             Reviewed;        2171 AA.
P15381; Q03716; Q28676; Q99243;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
01-APR-1990, sequence version 1.
12-SEP-2018, entry version 148.
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=Smooth muscle calcium channel blocker receptor;
Short=CACB-receptor;
AltName: Full=Voltage-gated calcium channel subunit alpha Cav1.2;
Name=CACNA1C; Synonyms=CACH2, CACN2, CACNL1A1, CCHL1A1;
Oryctolagus cuniculus (Rabbit).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae;
Oryctolagus.
NCBI_TaxID=9986;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND
ACTIVITY REGULATION.
TISSUE=Heart;
PubMed=2474130; DOI=10.1038/340230a0;
Mikami A., Imoto K., Tanabe T., Ni Idomme T., Mori Y., Takeshima H.,
Narumiya S., Numa S.;
"Primary structure and functional expression of the cardiac
dihydropyridine-sensitive calcium channel.";
Nature 340:230-233(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
TISSUE=Heart, and Lung;
PubMed=2169433; DOI=10.1016/0014-5793(90)81205-3;
Biel M., Ruth P., Bosse E., Hullin R., Stuehmer W., Flockerzi V.,
Hoffmann F.;
"Primary structure and functional expression of a high voltage
activated calcium channel from rabbit lung.";
FEBS Lett. 269:409-412(1990).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-98 (ISOFORM 5).
TISSUE=Heart muscle;
PubMed=1652442; DOI=10.1111/j.1432-1033.1991.tb21051.x;
Biel M., Hullin R., Freundner S., Singer D., Dascal N., Flockerzi V.,
Hofmann F.;
"Tissue-specific expression of high-voltage-activated dihydropyridine-
sensitive L-type calcium channels.";
Eur. J. Biochem. 200:81-88(1991).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 1192-1485 (ISOFORM 2).
TISSUE=Heart;
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).
[5]
FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS, CALCIUM-BINDING, AND
SITE.
PubMed=8232554; DOI=10.1038/366158a0;
Yang J., Ellinor P.T., Sather W.A., Zhang J.-F., Tsien R.W.;
"Molecular determinants of Ca2+ selectivity and ion permeation in L-
type Ca2+ channels.";
Nature 366:158-161(1993).
[6]
FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF CYS-168.
PubMed=9502794;
Ren D., Xu H., Eberl D.F., Chopra M., Hall L.M.;
"A mutation affecting dihydropyridine-sensitive current levels and
activation kinetics in Drosophila muscle and mammalian heart calcium
channels.";
J. Neurosci. 18:2335-2341(1998).
[7]
PHOSPHORYLATION BY PKA.
PubMed=1325377; DOI=10.1016/0014-5793(92)80804-P;
Yoshida A., Takahashi M., Nishimura S., Takeshima H., Kokubun S.;
"Cyclic AMP-dependent phosphorylation and regulation of the cardiac
dihydropyridine-sensitive Ca channel.";
FEBS Lett. 309:343-349(1992).
[8]
BETA-SUBUNIT BINDING DOMAIN, AND INTERACTION WITH CACNB1.
PubMed=7509046; DOI=10.1038/368067a0;
Pragnell M., de Waard M., Mori Y., Tanabe T., Snutch T.P.,
Campbell K.P.;
"Calcium channel beta-subunit binds to a conserved motif in the I-II
cytoplasmic linker of the alpha 1-subunit.";
Nature 368:67-70(1994).
[9]
EF-HAND MOTIF AND CALCIUM INACTIVATION, AND ACTIVITY REGULATION.
PubMed=7491499; DOI=10.1126/science.270.5241.1502;
de Leon M., Wang Y., Jones L., Perez-Reyes E., Wei X., Soong T.W.,
Snutch T.P., Yue D.T.;
"Essential Ca(2+)-binding motif for Ca(2+)-sensitive inactivation of
L-type Ca2+ channels.";
Science 270:1502-1505(1995).
[10]
FUNCTION, ACTIVITY REGULATION, SUBCELLULAR LOCATION, SUBUNIT, AND
INTERACTION WITH CACNA2D1.
PubMed=9278523;
Felix R., Gurnett C.A., De Waard M., Campbell K.P.;
"Dissection of functional domains of the voltage-dependent Ca2+
channel alpha2delta subunit.";
J. Neurosci. 17:6884-6891(1997).
[11]
INTERACTION WITH CACNB1, FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=15615847; DOI=10.1152/ajpheart.00348.2004;
Cohen R.M., Foell J.D., Balijepalli R.C., Shah V., Hell J.W.,
Kamp T.J.;
"Unique modulation of L-type Ca2+ channels by short auxiliary beta1d
subunit present in cardiac muscle.";
Am. J. Physiol. 288:H2363-H2374(2005).
[12]
SUBCELLULAR LOCATION, INTERACTION WITH CACNB2, AND FUNCTION.
PubMed=17525370; DOI=10.1161/CIRCRESAHA.106.146399;
Yada H., Murata M., Shimoda K., Yuasa S., Kawaguchi H., Ieda M.,
Adachi T., Murata M., Ogawa S., Fukuda K.;
"Dominant negative suppression of Rad leads to QT prolongation and
causes ventricular arrhythmias via modulation of L-type Ca2+ channels
in the heart.";
Circ. Res. 101:69-77(2007).
[13]
FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND INTERACTION WITH CACNB1;
CACNB2; CACNA2D1; CACNG4; CACNG6; CACNG7 AND CACNG8.
PubMed=21127204; DOI=10.1096/fj.10-172353;
Yang L., Katchman A., Morrow J.P., Doshi D., Marx S.O.;
"Cardiac L-type calcium channel (Cav1.2) associates with gamma
subunits.";
FASEB J. 25:928-936(2011).
[14]
FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF 1681-LEU--GLY-1684;
1685-LEU--LEU-1688 AND 1697-ARG--SER-1700.
PubMed=22928916; DOI=10.1042/BJ20120773;
Nakada T., Flucher B.E., Kashihara T., Sheng X., Shibazaki T.,
Horiuchi-Hirose M., Gomi S., Hirose M., Yamada M.;
"The proximal C-terminus of alpha(1C) subunits is necessary for
junctional membrane targeting of cardiac L-type calcium channels.";
Biochem. J. 448:221-231(2012).
[15]
FUNCTION, ACTIVITY REGULATION, SUBCELLULAR LOCATION, AND MUTAGENESIS
OF GLU-393; GLU-736; LEU-775; THR-1066; GLU-1145 AND GLU-1446.
PubMed=23145875; DOI=10.1021/bi301124a;
Gez L.S., Hagalili Y., Shainberg A., Atlas D.;
"Voltage-driven Ca(2+) binding at the L-type Ca(2+) channel triggers
cardiac excitation-contraction coupling prior to Ca(2+) influx.";
Biochemistry 51:9658-9666(2012).
[16]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH STAC2 AND STAC3.
PubMed=25548159; DOI=10.1073/pnas.1423113112;
Polster A., Perni S., Bichraoui H., Beam K.G.;
"Stac adaptor proteins regulate trafficking and function of muscle and
neuronal L-type Ca2+ channels.";
Proc. Natl. Acad. Sci. U.S.A. 112:602-606(2015).
[17]
FUNCTION, ACTIVITY REGULATION, INTERACTION WITH STAC1; STAC2 AND
STAC3, SUBCELLULAR LOCATION, AND MUTAGENESIS OF PHE-1648; ILE-1654;
PHE-1658 AND ARG-1659.
PubMed=29363593; DOI=10.1073/pnas.1715997115;
Campiglio M., Coste de Bagneaux P., Ortner N.J., Tuluc P.,
Van Petegem F., Flucher B.E.;
"STAC proteins associate to the IQ domain of CaV1.2 and inhibit
calcium-dependent inactivation.";
Proc. Natl. Acad. Sci. U.S.A. 115:1376-1381(2018).
[18] {ECO:0000244|PDB:4DEY}
X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 435-539 IN COMPLEX WITH
CACNB2, FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF GLY-449.
PubMed=22649239; DOI=10.1523/JNEUROSCI.5727-11.2012;
Almagor L., Chomsky-Hecht O., Ben-Mocha A., Hendin-Barak D.,
Dascal N., Hirsch J.A.;
"The role of a voltage-dependent Ca2+ channel intracellular linker: a
structure-function analysis.";
J. Neurosci. 32:7602-7613(2012).
-!- FUNCTION: Pore-forming, alpha-1C subunit of the voltage-gated
calcium channel that gives rise to L-type calcium currents
(PubMed:2474130, PubMed:2169433, PubMed:8232554, PubMed:9502794,
PubMed:9278523, PubMed:15615847, PubMed:17525370, PubMed:21127204,
PubMed:22928916, PubMed:23145875, PubMed:29363593,
PubMed:22649239). Mediates influx of calcium ions into the
cytoplasm, and thereby triggers calcium release from the
sarcoplasm (PubMed:23145875). Plays an important role in
excitation-contraction coupling in the heart (PubMed:17525370,
PubMed:22928916, PubMed:23145875). Required for normal heart
development and normal regulation of heart rhythm (By similarity).
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 (By similarity). Long-lasting (L-type) calcium
channels belong to the 'high-voltage activated' (HVA) group
(Probable). {ECO:0000250|UniProtKB:Q01815,
ECO:0000250|UniProtKB:Q13936, ECO:0000269|PubMed:15615847,
ECO:0000269|PubMed:17525370, ECO:0000269|PubMed:21127204,
ECO:0000269|PubMed:2169433, ECO:0000269|PubMed:22649239,
ECO:0000269|PubMed:22928916, ECO:0000269|PubMed:23145875,
ECO:0000269|PubMed:2474130, ECO:0000269|PubMed:29363593,
ECO:0000269|PubMed:8232554, ECO:0000269|PubMed:9278523,
ECO:0000269|PubMed:9502794, ECO:0000305}.
-!- ACTIVITY REGULATION: Inhibited by dihydropyridines (DHP), such as
isradipine (PubMed:2474130, PubMed:9278523). Inhibited by
nifedipine (PubMed:23145875). Channel activity is regulated by
Ca(2+) and calmodulin (PubMed:7491499, PubMed:29363593). Binding
of STAC1, STAC2 or STAC3 to a region that overlaps with the
calmodulin binding site inhibits channel inactivation by Ca(2+)
and calmodulin (PubMed:29363593). Binding of calmodulin or CABP1
at the same regulatory sites results in opposite effects on the
channel function (By similarity). Shear stress and pressure
increases calcium channel activity (By similarity).
{ECO:0000250|UniProtKB:Q13936, ECO:0000269|PubMed:23145875,
ECO:0000269|PubMed:2474130, ECO:0000269|PubMed:29363593,
ECO:0000269|PubMed:7491499, ECO:0000269|PubMed:9278523}.
-!- SUBUNIT: Component of a calcium channel complex consisting of a
pore-forming alpha subunit (CACNA1C) and ancillary beta, gamma and
delta subunits (PubMed:17525370, PubMed:21127204). 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
(Probable). CACNA1C channel activity is modulated by ancillary
subunits, such as CACNB1, CACNB2, CACNB3, CACNA2D1 and CACNA2D4
(PubMed:9278523, PubMed:15615847, PubMed:17525370,
PubMed:21127204). Interacts with CACNB1 (PubMed:7509046,
PubMed:15615847, PubMed:21127204). Interacts with CACNB2
(PubMed:17525370, PubMed:21127204, PubMed:22649239). Identified in
a complex with CACNA2D4 and CACNB3. Interacts with CACNB3 (By
similarity). Interacts with CACNA2D1 (PubMed:9278523,
PubMed:21127204). Intereracts with the gamma subunits CACNG4,
CACNG6, CACNG7 and CACNG8 (PubMed:21127204). Interacts with
CACNA2D4 (By similarity). Interacts with CALM1 (PubMed:29363593).
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. Interacts (via C-terminal
CDB motif) with CABP5; in a calcium-dependent manner. Interacts
with CIB1; the interaction increases upon cardiomyocytes
hypertrophy (By similarity). Interacts with STAC1, STAC2 and
STAC3; this inhibits channel inactivation, probably by hindering
CALM1 binding (PubMed:25548159, PubMed:29363593).
{ECO:0000250|UniProtKB:Q01815, ECO:0000250|UniProtKB:Q13936,
ECO:0000269|PubMed:15615847, ECO:0000269|PubMed:17525370,
ECO:0000269|PubMed:21127204, ECO:0000269|PubMed:22649239,
ECO:0000269|PubMed:25548159, ECO:0000269|PubMed:29363593,
ECO:0000269|PubMed:7509046, ECO:0000269|PubMed:9278523,
ECO:0000305}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15615847,
ECO:0000269|PubMed:17525370, ECO:0000269|PubMed:21127204,
ECO:0000269|PubMed:2169433, ECO:0000269|PubMed:22649239,
ECO:0000269|PubMed:2474130, ECO:0000269|PubMed:25548159,
ECO:0000269|PubMed:8232554, ECO:0000269|PubMed:9278523,
ECO:0000269|PubMed:9502794}; Multi-pass membrane protein
{ECO:0000305}. Cell membrane, sarcolemma
{ECO:0000269|PubMed:22928916, ECO:0000269|PubMed:23145875,
ECO:0000269|PubMed:29363593}; 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
(PubMed:22928916, PubMed:29363593). The interaction between RRAD
and CACNB2 promotes the expression of CACNA1C at the cell membrane
(PubMed:17525370). {ECO:0000269|PubMed:17525370,
ECO:0000269|PubMed:22928916, ECO:0000269|PubMed:29363593}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Comment=Additional isoforms seem to exist.;
Name=1; Synonyms=CACH2A;
IsoId=P15381-1; Sequence=Displayed;
Name=2; Synonyms=CACH2C;
IsoId=P15381-2; Sequence=VSP_000906;
Name=3; Synonyms=CACH2D;
IsoId=P15381-3; Sequence=VSP_000907;
Name=4; Synonyms=Lung;
IsoId=P15381-4; Sequence=VSP_000902, VSP_000904, VSP_000905,
VSP_000906;
Name=5; Synonyms=C141;
IsoId=P15381-5; Sequence=VSP_000902, VSP_000903;
-!- TISSUE SPECIFICITY: Expression in cardiac muscle. In lung,
expressed in airway and vascular smooth muscle cells.
-!- 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:0000269|PubMed:7491499}.
-!- PTM: Phosphorylation by PKA activates the channel
(PubMed:1325377). Elevated levels of blood glucose lead to
increased phosphorylation by PKA (By similarity).
{ECO:0000250|UniProtKB:Q01815, ECO:0000269|PubMed:1325377}.
-!- SIMILARITY: Belongs to the calcium channel alpha-1 subunit (TC
1.A.1.11) family. CACNA1C subfamily. {ECO:0000305}.
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EMBL; X15539; CAA33546.1; -; mRNA.
EMBL; X55763; CAA39289.1; -; mRNA.
EMBL; X60782; CAA43196.1; -; mRNA.
EMBL; M57974; AAA31182.1; -; mRNA.
PIR; S05054; S05054.
PIR; S11339; S11339.
RefSeq; NP_001129994.1; NM_001136522.1. [P15381-1]
UniGene; Ocu.1835; -.
UniGene; Ocu.3254; -.
PDB; 4DEY; X-ray; 1.95 A; B=435-539.
PDBsum; 4DEY; -.
ProteinModelPortal; P15381; -.
SMR; P15381; -.
DIP; DIP-61286N; -.
IntAct; P15381; 3.
BindingDB; P15381; -.
ChEMBL; CHEMBL2830; -.
iPTMnet; P15381; -.
PRIDE; P15381; -.
GeneID; 100101555; -.
KEGG; ocu:100101555; -.
CTD; 775; -.
HOVERGEN; HBG050763; -.
InParanoid; P15381; -.
KO; K04850; -.
Proteomes; UP000001811; Unplaced.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
GO; GO:0005622; C:intracellular; IEA:GOC.
GO; GO:1990454; C:L-type voltage-gated calcium channel complex; IDA:UniProtKB.
GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0014069; C:postsynaptic density; ISS:UniProtKB.
GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW.
GO; GO:0042383; C:sarcolemma; IDA:UniProtKB.
GO; GO:0030315; C:T-tubule; IDA:UniProtKB.
GO; GO:0005891; C:voltage-gated calcium channel complex; ISS:UniProtKB.
GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
GO; GO:0008331; F:high voltage-gated calcium channel activity; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0005245; F:voltage-gated calcium channel activity; IDA:UniProtKB.
GO; GO:0070588; P:calcium ion transmembrane transport; IDA:BHF-UCL.
GO; GO:0061577; P:calcium ion transmembrane transport via high voltage-gated calcium channel; IDA:BHF-UCL.
GO; GO:0060402; P:calcium ion transport into cytosol; IDA:UniProtKB.
GO; GO:0061337; P:cardiac conduction; ISS:UniProtKB.
GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISS:UniProtKB.
GO; GO:0010881; P:regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion; IMP:UniProtKB.
GO; GO:0098903; P:regulation of membrane repolarization during action potential; IDA:BHF-UCL.
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; 2.
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;
3D-structure; 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 2171 Voltage-dependent L-type calcium channel
subunit alpha-1C.
/FTId=PRO_0000053930.
TOPO_DOM 1 154 Cytoplasmic. {ECO:0000305}.
TRANSMEM 155 173 Helical; Name=S1 of repeat I.
{ECO:0000250|UniProtKB:P07293}.
TOPO_DOM 174 188 Extracellular. {ECO:0000305}.
TRANSMEM 189 209 Helical; Name=S2 of repeat I.
{ECO:0000250|UniProtKB:P07293}.
TOPO_DOM 210 218 Cytoplasmic. {ECO:0000305}.
TRANSMEM 219 239 Helical; Name=S3 of repeat I.
{ECO:0000250|UniProtKB:P07293}.
TOPO_DOM 240 262 Extracellular. {ECO:0000305}.
TRANSMEM 263 281 Helical; Name=S4 of repeat I.
{ECO:0000250|UniProtKB:P07293}.
TOPO_DOM 282 298 Cytoplasmic. {ECO:0000305}.
TRANSMEM 299 320 Helical; Name=S5 of repeat I.
{ECO:0000250|UniProtKB:P07293}.
TOPO_DOM 321 380 Extracellular. {ECO:0000305}.
INTRAMEM 381 402 Pore-forming.
{ECO:0000250|UniProtKB:P07293}.
TOPO_DOM 403 410 Extracellular. {ECO:0000305}.
TRANSMEM 411 431 Helical; Name=S6 of repeat I.
{ECO:0000250|UniProtKB:P07293}.
TOPO_DOM 432 554 Cytoplasmic. {ECO:0000305}.
TRANSMEM 555 573 Helical; Name=S1 of repeat II.
{ECO:0000250|UniProtKB:P07293}.
TOPO_DOM 574 584 Extracellular. {ECO:0000305}.
TRANSMEM 585 605 Helical; Name=S2 of repeat II.
{ECO:0000250|UniProtKB:P07293}.
TOPO_DOM 606 616 Cytoplasmic. {ECO:0000305}.
TRANSMEM 617 636 Helical; Name=S3 of repeat II.
{ECO:0000250|UniProtKB:P07293}.
TOPO_DOM 637 645 Extracellular. {ECO:0000305}.
TRANSMEM 646 664 Helical; Name=S4 of repeat II.
{ECO:0000250|UniProtKB:P07293}.
TOPO_DOM 665 683 Cytoplasmic. {ECO:0000305}.
TRANSMEM 684 703 Helical; Name=S5 of repeat II.
{ECO:0000250|UniProtKB:P07293}.
TOPO_DOM 704 723 Extracellular. {ECO:0000305}.
INTRAMEM 724 745 Pore-forming.
{ECO:0000250|UniProtKB:P07293}.
TOPO_DOM 746 755 Extracellular. {ECO:0000305}.
TRANSMEM 756 775 Helical; Name=S6 of repeat II.
{ECO:0000250|UniProtKB:P07293}.
TOPO_DOM 776 930 Cytoplasmic. {ECO:0000305}.
TRANSMEM 931 949 Helical; Name=S1 of repeat III.
{ECO:0000250|UniProtKB:P07293}.
TOPO_DOM 950 961 Extracellular. {ECO:0000305}.
TRANSMEM 962 981 Helical; Name=S2 of repeat III.
{ECO:0000250|UniProtKB:P07293}.
TOPO_DOM 982 997 Cytoplasmic. {ECO:0000305}.
TRANSMEM 998 1016 Helical; Name=S3 of repeat III.
{ECO:0000250|UniProtKB:P07293}.
TOPO_DOM 1017 1023 Extracellular. {ECO:0000305}.
TRANSMEM 1024 1042 Helical; Name=S4 of repeat III.
{ECO:0000250|UniProtKB:P07293}.
TOPO_DOM 1043 1061 Cytoplasmic. {ECO:0000305}.
TRANSMEM 1062 1081 Helical; Name=S5 of repeat III.
{ECO:0000250|UniProtKB:P07293}.
TOPO_DOM 1082 1131 Extracellular. {ECO:0000305}.
INTRAMEM 1132 1152 Pore-forming.
{ECO:0000250|UniProtKB:P07293}.
TOPO_DOM 1153 1169 Extracellular. {ECO:0000305}.
TRANSMEM 1170 1191 Helical; Name=S6 of repeat III.
{ECO:0000250|UniProtKB:P07293}.
TOPO_DOM 1192 1249 Cytoplasmic. {ECO:0000305}.
TRANSMEM 1250 1271 Helical; Name=S1 of repeat IV.
{ECO:0000250|UniProtKB:P07293}.
TOPO_DOM 1272 1279 Extracellular. {ECO:0000305}.
TRANSMEM 1280 1301 Helical; Name=S2 of repeat IV.
{ECO:0000250|UniProtKB:P07293}.
TOPO_DOM 1302 1311 Cytoplasmic. {ECO:0000305}.
TRANSMEM 1312 1331 Helical; Name=S3 of repeat IV.
{ECO:0000250|UniProtKB:P07293}.
TOPO_DOM 1332 1354 Extracellular. {ECO:0000305}.
TRANSMEM 1355 1373 Helical; Name=S4 of repeat IV.
{ECO:0000250|UniProtKB:P07293}.
TOPO_DOM 1374 1391 Cytoplasmic. {ECO:0000305}.
TRANSMEM 1392 1412 Helical; Name=S5 of repeat IV.
{ECO:0000250|UniProtKB:P07293}.
TOPO_DOM 1413 1434 Extracellular. {ECO:0000305}.
INTRAMEM 1435 1453 Pore-forming.
{ECO:0000250|UniProtKB:P07293}.
TOPO_DOM 1454 1481 Extracellular. {ECO:0000305}.
TRANSMEM 1482 1506 Helical; Name=S6 of repeat IV.
{ECO:0000250|UniProtKB:P07293}.
TOPO_DOM 1507 2171 Cytoplasmic. {ECO:0000305}.
REPEAT 141 438 I.
REPEAT 540 786 II.
REPEAT 917 1199 III.
REPEAT 1236 1509 IV.
CA_BIND 1535 1546
REGION 77 98 Calmodulin-binding.
{ECO:0000250|UniProtKB:Q13936}.
REGION 458 475 AID/alpha-interaction domain; mediates
interaction with the beta subunit.
{ECO:0000250|UniProtKB:P22002}.
REGION 859 906 Interaction with STAC2.
{ECO:0000250|UniProtKB:Q13936}.
REGION 1119 1208 Dihydropyridine binding.
{ECO:0000250|UniProtKB:P07293}.
REGION 1460 1528 Dihydropyridine binding.
{ECO:0000250|UniProtKB:P07293}.
REGION 1474 1516 Phenylalkylamine binding.
{ECO:0000250|UniProtKB:P07293}.
REGION 1641 1668 Important for interaction with STAC1,
STAC2 and STAC3.
{ECO:0000269|PubMed:29363593}.
REGION 1647 1667 Calmodulin-binding IQ region.
{ECO:0000250|UniProtKB:Q13936}.
REGION 1681 1700 Important for localization in at the
junctional membrane.
{ECO:0000269|PubMed:22928916}.
MOTIF 391 394 Selectivity filter of repeat I.
{ECO:0000250|UniProtKB:P07293}.
MOTIF 734 737 Selectivity filter of repeat II.
{ECO:0000250|UniProtKB:P07293}.
MOTIF 1143 1146 Selectivity filter of repeat III.
{ECO:0000250|UniProtKB:P07293}.
MOTIF 1444 1447 Selectivity filter of repeat IV.
{ECO:0000250|UniProtKB:P07293}.
COMPBIAS 684 690 Poly-Leu.
COMPBIAS 798 804 Poly-Glu.
COMPBIAS 1177 1183 Poly-Ile.
METAL 393 393 Calcium. {ECO:0000250|UniProtKB:P07293}.
METAL 736 736 Calcium. {ECO:0000250|UniProtKB:P07293}.
METAL 1145 1145 Calcium. {ECO:0000250|UniProtKB:P07293}.
SITE 393 393 Calcium ion selectivity and permeability.
{ECO:0000269|PubMed:8232554}.
SITE 736 736 Calcium ion selectivity and permeability.
{ECO:0000269|PubMed:8232554}.
SITE 1145 1145 Calcium ion selectivity and permeability.
{ECO:0000269|PubMed:8232554}.
SITE 1446 1446 Calcium ion selectivity and permeability.
{ECO:0000269|PubMed:8232554}.
MOD_RES 499 499 Phosphoserine.
{ECO:0000250|UniProtKB:Q01815}.
MOD_RES 506 506 Phosphothreonine.
{ECO:0000250|UniProtKB:Q01815}.
MOD_RES 838 838 Phosphoserine.
{ECO:0000250|UniProtKB:Q01815}.
MOD_RES 845 845 Phosphoserine.
{ECO:0000250|UniProtKB:Q01815}.
MOD_RES 1517 1517 Phosphoserine; by PKA. {ECO:0000255}.
MOD_RES 1700 1700 Phosphoserine.
{ECO:0000250|UniProtKB:Q01815}.
MOD_RES 1721 1721 Phosphoserine.
{ECO:0000250|UniProtKB:Q01815}.
MOD_RES 1920 1920 Phosphoserine; by PKA. {ECO:0000255}.
MOD_RES 1928 1928 Phosphoserine; by PKA.
{ECO:0000250|UniProtKB:Q01815}.
CARBOHYD 183 183 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 358 358 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1418 1418 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1469 1469 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 328 356 {ECO:0000250|UniProtKB:P07293}.
DISULFID 346 362 {ECO:0000250|UniProtKB:P07293}.
DISULFID 1088 1099 {ECO:0000250|UniProtKB:P07293}.
DISULFID 1461 1477 {ECO:0000250|UniProtKB:P07293}.
VAR_SEQ 1 46 MLRALVQPATPAYQPLPSHLSAETESTCKGTVVHEAQLNHF
YISPG -> MVNENTRMYIPEENHQ (in isoform 4
and isoform 5).
{ECO:0000303|PubMed:1652442}.
/FTId=VSP_000902.
VAR_SEQ 66 79 Missing (in isoform 5).
{ECO:0000303|PubMed:1652442}.
/FTId=VSP_000903.
VAR_SEQ 402 421 MQDAMGYELPWVYFVSLVIF -> VNDAVGRDWPWIYFVTL
III (in isoform 4). {ECO:0000305}.
/FTId=VSP_000904.
VAR_SEQ 494 494 M -> RGTPAGLHAQKKGKFAWFSHSTETHV (in
isoform 4). {ECO:0000305}.
/FTId=VSP_000905.
VAR_SEQ 1307 1334 GYFSDPWNVFDFLIVIGSIIDVILSETN -> HYFCDAWNT
FDALIVVGSIVDIAITEVH (in isoform 2 and
isoform 4). {ECO:0000303|PubMed:2173707}.
/FTId=VSP_000906.
VAR_SEQ 1335 1345 Missing (in isoform 3). {ECO:0000305}.
/FTId=VSP_000907.
MUTAGEN 168 168 C->G: Small reduction of current
amplitude. {ECO:0000269|PubMed:9502794}.
MUTAGEN 168 168 C->K,W: No current.
{ECO:0000269|PubMed:9502794}.
MUTAGEN 168 168 C->S: No effect.
{ECO:0000269|PubMed:9502794}.
MUTAGEN 168 168 C->Y: Slower channel activation and
reduction of current amplitude.
{ECO:0000269|PubMed:9502794}.
MUTAGEN 393 393 E->A: Loss of channel activity and
ability to trigger cardiomyocyte
contraction; when associated with A-736;
A-1145 and A-1446.
{ECO:0000269|PubMed:23145875}.
MUTAGEN 393 393 E->K: Drastic reduction of barium
permeability. Reduction of calcium block
of lithium currents.
{ECO:0000269|PubMed:8232554}.
MUTAGEN 393 393 E->Q: Attenuates calcium block of inward
barium, lithium, or cadmium currents.
{ECO:0000269|PubMed:8232554}.
MUTAGEN 449 449 G->R: Decreased rate of channel
inactivation.
{ECO:0000269|PubMed:22649239}.
MUTAGEN 736 736 E->A: Loss of channel activity and
ability to trigger cardiomyocyte
contraction; when associated with A-393;
A-1145 and A-1446.
{ECO:0000269|PubMed:23145875}.
MUTAGEN 736 736 E->K: Drastic reduction of barium
permeability. Reduction of calcium block
of lithium currents.
{ECO:0000269|PubMed:8232554}.
MUTAGEN 736 736 E->Q: Attenuates calcium block of inward
barium, lithium, or cadmium currents.
{ECO:0000269|PubMed:8232554}.
MUTAGEN 775 775 L->P: Loss of nifedipine-sensitivity and
channel activity; when associated with Y-
1066. {ECO:0000269|PubMed:23145875}.
MUTAGEN 1066 1066 T->Y: Loss of nifedipine-sensitivity and
channel activity; when associated with P-
775. {ECO:0000269|PubMed:23145875}.
MUTAGEN 1145 1145 E->A: Loss of channel activity and
ability to trigger cardiomyocyte
contraction; when associated with A-393;
A-736 and A-1446.
{ECO:0000269|PubMed:23145875}.
MUTAGEN 1145 1145 E->K: Drastic reduction of barium
permeability. Reduction of calcium block
of lithium currents.
{ECO:0000269|PubMed:8232554}.
MUTAGEN 1145 1145 E->Q: Attenuates calcium block of inward
barium, lithium, or cadmium currents.
{ECO:0000269|PubMed:8232554}.
MUTAGEN 1446 1446 E->A: Loss of channel activity and
ability to trigger cardiomyocyte
contraction; when associated with A-393;
A-736 and A-1145.
{ECO:0000269|PubMed:23145875}.
MUTAGEN 1446 1446 E->K: Moderate reduction of barium
permeability. Reduction of calcium block
of lithium currents.
{ECO:0000269|PubMed:8232554}.
MUTAGEN 1446 1446 E->Q: Attenuates calcium block of inward
barium, lithium, or cadmium currents.
{ECO:0000269|PubMed:8232554}.
MUTAGEN 1648 1648 F->A: Mildly decreased interaction with
STAC3. {ECO:0000269|PubMed:29363593}.
MUTAGEN 1654 1654 I->A: Strongly decreased interaction with
STAC3. {ECO:0000269|PubMed:29363593}.
MUTAGEN 1658 1658 F->A: Decreased interaction with STAC3.
{ECO:0000269|PubMed:29363593}.
MUTAGEN 1659 1659 R->A: Mildly decreased interaction with
STAC3. {ECO:0000269|PubMed:29363593}.
MUTAGEN 1681 1684 LQAG->AAAA: Strongly reduced channel
clustering at the junctional membrane.
{ECO:0000269|PubMed:22928916}.
MUTAGEN 1685 1688 LRTL->AAAA: Strongly reduced channel
clustering at the junctional membrane.
{ECO:0000269|PubMed:22928916}.
MUTAGEN 1697 1700 RAIS->AAAA: Strongly reduced channel
clustering at the junctional membrane.
{ECO:0000269|PubMed:22928916}.
CONFLICT 1346 1346 N -> S (in Ref. 4; AAA31182).
{ECO:0000305}.
CONFLICT 1468 1468 H -> S (in Ref. 4; AAA31182).
{ECO:0000305}.
HELIX 451 475 {ECO:0000244|PDB:4DEY}.
SEQUENCE 2171 AA; 242784 MW; B64F08F09D71C65D CRC64;
MLRALVQPAT PAYQPLPSHL SAETESTCKG TVVHEAQLNH FYISPGGSNY GSPRPAHANM
NANAAAGLAP EHIPTPGAAL SWQAAIDAAR QAKLMGSAGN ATISTVSSTQ RKRQQYGKPK
KQGSTTATRP PRALLCLTLK NPIRRACISI VEWKPFEIII LLTIFANCVA LAIYIPFPED
DSNATNSNLE RVEYLFLIIF TVEAFLKVIA YGLLFHPNAY LRNGWNLLDF IIVVVGLFSA
ILEQATKADG ANALGGKGAG FDVKALRAFR VLRPLRLVSG VPSLQVVLNS IIKAMVPLLH
IALLVLFVII IYAIIGLELF MGKMHKTCYN QEGVADVPAE DDPSPCALET GHGRQCQNGT
VCKPGWDGPK HGITNFDNFA FAMLTVFQCI TMEGWTDVLY WMQDAMGYEL PWVYFVSLVI
FGSFFVLNLV LGVLSGEFSK EREKAKARGD FQKLREKQQL EEDLKGYLDW ITQAEDIDPE
NEDEGMDEEK PRNMSMPTSE TESVNTENVA GGDIEGENCG ARLAHRISKS KFSRYWRRWN
RFCRRKCRAA VKSNVFYWLV IFLVFLNTLT IASEHYNQPH WLTEVQDTAN KALLALFTAE
MLLKMYSLGL QAYFVSLFNR FDCFIVCGGI LETILVETKV MSPLGISVLR CVRLLRIFKI
TRYWNSLSNL VASLLNSVRS IASLLLLLFL FIIIFSLLGM QLFGGKFNFD EMQTRRSTFD
NFPQSLLTVF QILTGEDWNS VMYDGIMAYG GPSFPGMLVC IYFIILFICG NYILLNVFLA
IAVDNLADAE SLTSAQKEEE EEKERKKLAR TASPEKKQEV VGKPALEEAK EEKIELKSIT
ADGESPPTTK INMDDLQPNE SEDKSPYPNP ETTGEEDEEE PEMPVGPRPR PLSELHLKEK
AVPMPEASAF FIFSPNNRFR LQCHRIVNDT IFTNLILFFI LLSSISLAAE DPVQHTSFRN
HILFYFDIVF TTIFTIEIAL 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 CSPSMNAEEN SRISITFFRL FRVMRLVKLL SRGEGIRTLL
WTFIKSFQAL PYVALLIVML FFIYAVIGMQ VFGKIALNDT TEINRNNNFQ TFPQAVLLLF
RCATGEAWQD IMLACMPGKK CAPESEPHNS 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 GLFGNHVSYY
QSDSRSAFPQ TFTTQRPLHI SKAGNNQGDT ESPSHEKLVD STFTPSSYSS TGSNANINNA
NNTALGRLPR PAGYPSTVST VEGHGSPLSP AVRAQEAAWK LSSKRCHSQE SQIAMACQEG
ASQDDNYDVR IGEDAECCSE PSLLSTEMLS YQDDENRQLA PPEEEKRDIR LSPKKGFLRS
ASLGRRASFH LECLKRQKNQ GGDISQKTVL PLHLVHHQAL AVAGLSPLLQ RSHSPTSLPR
PCATPPATPG SRGWPPQPIP TLRLEGADSS EKLNSSFPSI HCGSWSGENS PCRGDSSAAR
RARPVSLTVP SQAGAQGRQF HGSASSLVEA VLISEGLGQF AQDPKFIEVT TQELADACDL
TIEEMENAAD DILSGGARQS PNGTLLPFVN RRDPGRDRAG QNEQDASGAC APGCGQSEEA
LADRRAGVSS L


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