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

 CAC1C_RAT               Reviewed;        2169 AA.
P22002; P27733; P27734; Q62816; Q63271; Q64178;
01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
01-AUG-1991, sequence version 1.
05-DEC-2018, entry version 173.
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=Rat brain class C {ECO:0000303|PubMed:1648941};
Short=RBC {ECO:0000303|PubMed:1648941};
AltName: Full=Voltage-gated calcium channel subunit alpha Cav1.2;
Name=Cacna1c; Synonyms=Cach2, Cacn2, Cacnl1a1, Cchl1a1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=Aorta;
PubMed=2170396;
Koch W.J., Ellinor P.T., Schwartz A.;
"cDNA cloning of a dihydropyridine-sensitive calcium channel from rat
aorta. Evidence for the existence of alternatively spliced forms.";
J. Biol. Chem. 265:17786-17791(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 4 AND 5), FUNCTION, AND
SUBCELLULAR LOCATION.
TISSUE=Brain;
PubMed=1648941; DOI=10.1016/0896-6273(91)90073-9;
Snutch T.P., Tomlinson W.J., Leonard J.P., Gilbert M.M.;
"Distinct calcium channels are generated by alternative splicing and
are differentially expressed in the mammalian CNS.";
Neuron 7:45-57(1991).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 1168-1413 (ISOFORM 1).
PubMed=1692134; DOI=10.1073/pnas.87.9.3391;
Snutch T.P., Leonard J.P., Gilbert M.M., Lester H.A., Davidson N.;
"Rat brain expresses a heterogeneous family of calcium channels.";
Proc. Natl. Acad. Sci. U.S.A. 87:3391-3395(1990).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1269-1415 (ISOFORMS 1; 2 AND 3).
PubMed=1311102; DOI=10.1073/pnas.89.4.1497;
Diebold R.J., Koch W.J., Ellinor P.T., Wang J.-J., Muthuchamy M.,
Wieczorek D.F., Schwartz A.;
"Mutually exclusive exon splicing of the cardiac calcium channel a1
subunit generates developmentally regulated isoforms in the rat
heart.";
Proc. Natl. Acad. Sci. U.S.A. 89:1497-1501(1992).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 1269-1387.
TISSUE=Myometrium;
PubMed=7485440;
Tezuka N., Ali M., Chwalisz K., Garfield R.E.;
"Changes in transcripts encoding calcium channel subunits of rat
myometrium during pregnancy.";
Am. J. Physiol. 269:C1008-C1017(1995).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 1202-1495 (ISOFORM 3).
TISSUE=Osteosarcoma;
PubMed=7479909; DOI=10.1073/pnas.92.24.10914;
Barry E.L.R., Gesek F.A., Froehner S.C., Friedman P.A.;
"Multiple calcium channel transcripts in rat osteosarcoma cells:
selective activation of alpha 1D isoform by parathyroid hormone.";
Proc. Natl. Acad. Sci. U.S.A. 92:10914-10918(1995).
[7]
PHOSPHORYLATION.
PubMed=8396138;
Hell J.W., Yokoyama C.T., Wong S.T., Warner C., Snutch T.P.,
Catterall W.A.;
"Differential phosphorylation of two size forms of the neuronal class
C L-type calcium channel alpha 1 subunit.";
J. Biol. Chem. 268:19451-19457(1993).
[8]
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).
[9]
INTERACTION WITH CABP1, FUNCTION, ACTIVITY REGULATION, SUBCELLULAR
LOCATION, AND TISSUE SPECIFICITY.
PubMed=15140941; DOI=10.1523/JNEUROSCI.5523-03.2004;
Zhou H., Kim S.-A., Kirk E.A., Tippens A.L., Sun H., Haeseleer F.,
Lee A.;
"Ca2+-binding protein-1 facilitates and forms a postsynaptic complex
with Cav1.2 (L-type) Ca2+ channels.";
J. Neurosci. 24:4698-4708(2004).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-845; SER-1699 AND
SER-1720, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
[11]
INTERACTION WITH CACNB3.
PubMed=24751537; DOI=10.1083/jcb.201304101;
Beguin P., Nagashima K., Mahalakshmi R.N., Vigot R., Matsunaga A.,
Miki T., Ng M.Y., Ng Y.J., Lim C.H., Tay H.S., Hwang L.A., Firsov D.,
Tang B.L., Inagaki N., Mori Y., Seino S., Launey T., Hunziker W.;
"BARP suppresses voltage-gated calcium channel activity and Ca2+-
evoked exocytosis.";
J. Cell Biol. 205:233-249(2014).
[12]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 452-476 IN COMPLEX WITH
CACNB3, FUNCTION, AND REGION.
PubMed=15170217; DOI=10.1038/nature02641;
Chen Y.H., Li M.H., Zhang Y., He L.L., Yamada Y., Fitzmaurice A.,
Shen Y., Zhang H., Tong L., Yang J.;
"Structural basis of the alpha1-beta subunit interaction of voltage-
gated Ca2+ channels.";
Nature 429:675-680(2004).
-!- FUNCTION: Pore-forming, alpha-1C subunit of the voltage-gated
calcium channel that gives rise to L-type calcium currents
(Probable) (PubMed:15140941, PubMed:15170217). 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 (By
similarity). 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 (By similarity).
{ECO:0000250|UniProtKB:P15381, ECO:0000250|UniProtKB:Q01815,
ECO:0000250|UniProtKB:Q13936, ECO:0000269|PubMed:15140941,
ECO:0000269|PubMed:15170217, ECO:0000305|PubMed:1648941}.
-!- ACTIVITY REGULATION: Inhibited by dihydropyridines (DHP), such as
isradipine (By similarity). Inhibited by nifedipine (By
similarity). Channel activity is regulated by Ca(2+) and
calmodulin (PubMed:15140941). 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
(PubMed:15140941). Shear stress and pressure increases calcium
channel activity (By similarity). {ECO:0000250|UniProtKB:P15381,
ECO:0000250|UniProtKB:Q13936, ECO:0000269|PubMed:15140941}.
-!- SUBUNIT: Component of a calcium channel complex consisting of a
pore-forming alpha subunit (CACNA1C) and ancillary beta, gamma and
delta subunits (PubMed:15170217). 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 (By
similarity). Interacts with CACNB3 (PubMed:24751537,
PubMed:15170217). 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 (PubMed:15140941). 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 (PubMed:15140941). 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 STAC2 and STAC3; this
inhibits channel inactivation (By similarity).
{ECO:0000250|UniProtKB:P15381, ECO:0000250|UniProtKB:Q01815,
ECO:0000250|UniProtKB:Q13936, ECO:0000269|PubMed:15140941,
ECO:0000269|PubMed:15170217, ECO:0000269|PubMed:24751537}.
-!- INTERACTION:
P63329:Ppp3ca; NbExp=5; IntAct=EBI-1185084, EBI-7022944;
Q9WUD9:Src; NbExp=4; IntAct=EBI-1185084, EBI-7784541;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15140941,
ECO:0000269|PubMed:15170217, ECO:0000305|PubMed:1648941}; Multi-
pass membrane protein {ECO:0000305}. Cell membrane, sarcolemma
{ECO:0000250|UniProtKB:P15381}; Multi-pass membrane protein
{ECO:0000305}. Perikaryon {ECO:0000269|PubMed:15140941}. Cell
junction, synapse, postsynaptic cell membrane, postsynaptic
density {ECO:0000269|PubMed:15140941}. Cell projection, dendrite
{ECO:0000269|PubMed:15140941}. 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=5;
Comment=Additional isoforms seem to exist.;
Name=2; Synonyms=S3B;
IsoId=P22002-1; Sequence=Displayed;
Name=1; Synonyms=S3A;
IsoId=P22002-2; Sequence=VSP_000911;
Name=3; Synonyms=D1, ROB2;
IsoId=P22002-3; Sequence=VSP_000912;
Name=4; Synonyms=rbC-I;
IsoId=P22002-4; Sequence=VSP_000908, VSP_000910, VSP_000911;
Name=5; Synonyms=rbC-II;
IsoId=P22002-5; Sequence=VSP_000908, VSP_000909, VSP_000910;
-!- TISSUE SPECIFICITY: Detected in hippocampus and brain cortex, on
neuronal cell bodies and dendrites, and in post-synaptic density
in brain (at protein level) (PubMed:15140941). Isoforms 4 and 5
are expressed throughout the central nervous system, with highest
levels in the olfactory bulb and cerebellum. Also expressed in
heart, pituitary, adrenal gland, liver, kidney, and in a much
lesser extent in testes and spleen. {ECO:0000269|PubMed:15140941}.
-!- DEVELOPMENTAL STAGE: Expressed from embryonic day 16 until the
adult stage.
-!- 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 (By similarity).
Elevated levels of blood glucose lead to increased phosphorylation
by PKA (By similarity). Is also phosphorylated in vitro by CaM-
kinase II, PKC and CGPK (PubMed:8396138).
{ECO:0000250|UniProtKB:Q01815, ECO:0000269|PubMed:8396138}.
-!- SIMILARITY: Belongs to the calcium channel alpha-1 subunit (TC
1.A.1.11) family. CACNA1C subfamily. {ECO:0000305}.
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EMBL; M59786; AAA85463.1; -; mRNA.
EMBL; M67515; AAA18905.1; -; mRNA.
EMBL; M67516; AAA42016.1; -; mRNA.
EMBL; M91242; AAA41460.1; -; Genomic_DNA.
EMBL; M91240; AAA41460.1; JOINED; Genomic_DNA.
EMBL; M89924; AAA41460.1; JOINED; Genomic_DNA.
EMBL; M91241; AAA41460.1; JOINED; Genomic_DNA.
EMBL; S80558; AAB35528.1; -; mRNA.
EMBL; U31815; AAA89157.1; -; mRNA.
RefSeq; NP_036649.2; NM_012517.2.
UniGene; Rn.9827; -.
PDB; 1VYT; X-ray; 2.60 A; E/F=452-476.
PDBsum; 1VYT; -.
ProteinModelPortal; P22002; -.
SMR; P22002; -.
BioGrid; 246425; 4.
CORUM; P22002; -.
IntAct; P22002; 4.
MINT; P22002; -.
STRING; 10116.ENSRNOP00000048790; -.
BindingDB; P22002; -.
ChEMBL; CHEMBL3762; -.
GuidetoPHARMACOLOGY; 529; -.
iPTMnet; P22002; -.
PhosphoSitePlus; P22002; -.
PaxDb; P22002; -.
PRIDE; P22002; -.
GeneID; 24239; -.
KEGG; rno:24239; -.
UCSC; RGD:2245; rat. [P22002-1]
CTD; 775; -.
RGD; 2245; Cacna1c.
eggNOG; KOG2301; Eukaryota.
eggNOG; ENOG410XNP6; LUCA.
HOVERGEN; HBG050763; -.
InParanoid; P22002; -.
KO; K04850; -.
PhylomeDB; P22002; -.
EvolutionaryTrace; P22002; -.
PRO; PR:P22002; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0009986; C:cell surface; IDA:RGD.
GO; GO:0030425; C:dendrite; IDA:UniProtKB.
GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
GO; GO:0099055; C:integral component of postsynaptic membrane; IDA:SynGO.
GO; GO:0099056; C:integral component of presynaptic membrane; IDA:SynGO.
GO; GO:1990454; C:L-type voltage-gated calcium channel complex; IDA:UniProtKB.
GO; GO:0016020; C:membrane; IDA:RGD.
GO; GO:0043025; C:neuronal cell body; IDA:UniProtKB.
GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IDA:RGD.
GO; GO:0014069; C:postsynaptic density; IDA:UniProtKB.
GO; GO:0045211; C:postsynaptic membrane; IDA:SynGO.
GO; GO:0042734; C:presynaptic membrane; IDA:SynGO.
GO; GO:0032991; C:protein-containing complex; IDA:RGD.
GO; GO:0042383; C:sarcolemma; IDA:RGD.
GO; GO:0030315; C:T-tubule; IDA:RGD.
GO; GO:0005891; C:voltage-gated calcium channel complex; IDA:RGD.
GO; GO:0030018; C:Z disc; IDA:BHF-UCL.
GO; GO:0051393; F:alpha-actinin binding; ISS:BHF-UCL.
GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
GO; GO:0008331; F:high voltage-gated calcium channel activity; IDA:RGD.
GO; GO:0044325; F:ion channel binding; IPI:BHF-UCL.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0019904; F:protein domain specific binding; IPI:RGD.
GO; GO:0051721; F:protein phosphatase 2A binding; IPI:RGD.
GO; GO:0031369; F:translation initiation factor binding; IPI:RGD.
GO; GO:0005245; F:voltage-gated calcium channel activity; IDA:RGD.
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:0070509; P:calcium ion import; IMP:RGD.
GO; GO:0061577; P:calcium ion transmembrane transport via high voltage-gated calcium channel; IDA:UniProtKB.
GO; GO:0006816; P:calcium ion transport; IMP:RGD.
GO; GO:0060402; P:calcium ion transport into cytosol; ISS:UniProtKB.
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:1904646; P:cellular response to amyloid-beta; IEP:RGD.
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:1904879; P:positive regulation of calcium ion transmembrane transport via high voltage-gated calcium channel; IMP:RGD.
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:0098911; P:regulation of ventricular cardiac muscle cell action potential; ISS: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; 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;
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 2169 Voltage-dependent L-type calcium channel
subunit alpha-1C.
/FTId=PRO_0000053931.
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 1041 Helical; Name=S4 of repeat III.
{ECO:0000250|UniProtKB:P07293}.
TOPO_DOM 1042 1060 Cytoplasmic. {ECO:0000305}.
TRANSMEM 1061 1080 Helical; Name=S5 of repeat III.
{ECO:0000250|UniProtKB:P07293}.
TOPO_DOM 1081 1130 Extracellular. {ECO:0000305}.
INTRAMEM 1131 1151 Pore-forming.
{ECO:0000250|UniProtKB:P07293}.
TOPO_DOM 1152 1168 Extracellular. {ECO:0000305}.
TRANSMEM 1169 1190 Helical; Name=S6 of repeat III.
{ECO:0000250|UniProtKB:P07293}.
TOPO_DOM 1191 1248 Cytoplasmic. {ECO:0000305}.
TRANSMEM 1249 1270 Helical; Name=S1 of repeat IV.
{ECO:0000250|UniProtKB:P07293}.
TOPO_DOM 1271 1278 Extracellular. {ECO:0000305}.
TRANSMEM 1279 1300 Helical; Name=S2 of repeat IV.
{ECO:0000250|UniProtKB:P07293}.
TOPO_DOM 1301 1310 Cytoplasmic. {ECO:0000305}.
TRANSMEM 1311 1330 Helical; Name=S3 of repeat IV.
{ECO:0000250|UniProtKB:P07293}.
TOPO_DOM 1331 1353 Extracellular. {ECO:0000305}.
TRANSMEM 1354 1372 Helical; Name=S4 of repeat IV.
{ECO:0000250|UniProtKB:P07293}.
TOPO_DOM 1373 1390 Cytoplasmic. {ECO:0000305}.
TRANSMEM 1391 1411 Helical; Name=S5 of repeat IV.
{ECO:0000250|UniProtKB:P07293}.
TOPO_DOM 1412 1433 Extracellular. {ECO:0000305}.
INTRAMEM 1434 1452 Pore-forming.
{ECO:0000250|UniProtKB:P07293}.
TOPO_DOM 1453 1480 Extracellular. {ECO:0000305}.
TRANSMEM 1481 1505 Helical; Name=S6 of repeat IV.
{ECO:0000250|UniProtKB:P07293}.
TOPO_DOM 1506 2169 Cytoplasmic. {ECO:0000305}.
REPEAT 141 438 I.
REPEAT 540 786 II.
REPEAT 917 1198 III.
REPEAT 1235 1508 IV.
CA_BIND 1534 1545 {ECO:0000250}.
REGION 77 98 Calmodulin-binding.
{ECO:0000250|UniProtKB:Q13936}.
REGION 458 475 AID/alpha-interaction domain; mediates
interaction with the beta subunit.
{ECO:0000269|PubMed:15170217}.
REGION 859 906 Interaction with STAC2.
{ECO:0000250|UniProtKB:Q13936}.
REGION 1118 1207 Dihydropyridine binding.
{ECO:0000250|UniProtKB:P07293}.
REGION 1459 1527 Dihydropyridine binding.
{ECO:0000250|UniProtKB:P07293}.
REGION 1473 1515 Phenylalkylamine binding.
{ECO:0000250|UniProtKB:P07293}.
REGION 1640 1673 Calmodulin-binding.
{ECO:0000250|UniProtKB:Q13936}.
REGION 1640 1667 Important for interaction with STAC1,
STAC2 and STAC3.
{ECO:0000250|UniProtKB:P15381}.
REGION 1646 1666 Calmodulin-binding IQ region.
{ECO:0000250|UniProtKB:Q13936}.
REGION 1680 1699 Important for localization in at the
junctional membrane.
{ECO:0000250|UniProtKB:P15381}.
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 1142 1145 Selectivity filter of repeat III.
{ECO:0000250|UniProtKB:P07293}.
MOTIF 1443 1446 Selectivity filter of repeat IV.
{ECO:0000250|UniProtKB:P07293}.
COMPBIAS 684 690 Poly-Leu.
COMPBIAS 798 804 Poly-Glu.
COMPBIAS 1176 1182 Poly-Ile.
METAL 393 393 Calcium. {ECO:0000250|UniProtKB:P07293}.
METAL 736 736 Calcium. {ECO:0000250|UniProtKB:P07293}.
METAL 1144 1144 Calcium. {ECO:0000250|UniProtKB:P07293}.
SITE 393 393 Calcium ion selectivity and permeability.
{ECO:0000250|UniProtKB:P15381}.
SITE 736 736 Calcium ion selectivity and permeability.
{ECO:0000250|UniProtKB:P15381}.
SITE 1144 1144 Calcium ion selectivity and permeability.
{ECO:0000250|UniProtKB:P15381}.
SITE 1445 1445 Calcium ion selectivity and permeability.
{ECO:0000250|UniProtKB:P15381}.
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:0000244|PubMed:22673903}.
MOD_RES 1516 1516 Phosphoserine; by PKA. {ECO:0000255}.
MOD_RES 1699 1699 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 1720 1720 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 1919 1919 Phosphoserine; by PKA. {ECO:0000255}.
MOD_RES 1927 1927 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 1417 1417 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1468 1468 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 328 356 {ECO:0000250|UniProtKB:P07293}.
DISULFID 346 362 {ECO:0000250|UniProtKB:P07293}.
DISULFID 1460 1476 {ECO:0000250|UniProtKB:P07293}.
VAR_SEQ 1 46 MIRAFAQPSTPPYQPLSSCLSEDTERKFKGKVVHEAQLNCF
YISPG -> MVNENTRMYVPEENHQ (in isoform 4
and isoform 5).
{ECO:0000303|PubMed:1648941}.
/FTId=VSP_000908.
VAR_SEQ 810 810 R -> RPAR (in isoform 5).
{ECO:0000303|PubMed:1648941}.
/FTId=VSP_000909.
VAR_SEQ 964 979 FYFDIVFTTIFTIEIA -> GNADYVFTSIFTLEII (in
isoform 4 and isoform 5).
{ECO:0000303|PubMed:1648941}.
/FTId=VSP_000910.
VAR_SEQ 1306 1333 HYFCDAWNTFDALIVVGSIVDIAITEVH -> GYFSDPSNV
FDFLIVIGSIIAVILSETN (in isoform 1 and
isoform 4). {ECO:0000303|PubMed:1648941,
ECO:0000303|PubMed:1692134}.
/FTId=VSP_000911.
VAR_SEQ 1334 1344 Missing (in isoform 3).
{ECO:0000303|PubMed:7479909}.
/FTId=VSP_000912.
CONFLICT 83 83 L -> Q (in Ref. 2; AAA18905/AAA42016).
{ECO:0000305}.
CONFLICT 87 87 D -> G (in Ref. 2; AAA18905).
{ECO:0000305}.
CONFLICT 520 520 G -> R (in Ref. 2; AAA18905).
{ECO:0000305}.
CONFLICT 648 649 CW -> VL (in Ref. 2; AAA18905/AAA42016).
{ECO:0000305}.
CONFLICT 678 678 L -> V (in Ref. 2; AAA18905/AAA42016).
{ECO:0000305}.
CONFLICT 769 770 SP -> CG (in Ref. 2; AAA18905/AAA42016).
{ECO:0000305}.
CONFLICT 777 777 L -> V (in Ref. 2; AAA18905/AAA42016).
{ECO:0000305}.
CONFLICT 871 871 D -> N (in Ref. 2; AAA18905).
{ECO:0000305}.
CONFLICT 1037 1037 R -> RA (in Ref. 2; AAA18905/AAA42016).
{ECO:0000305}.
CONFLICT 1098 1098 S -> C (in Ref. 2; AAA18905/AAA42016).
{ECO:0000305}.
CONFLICT 1107 1107 T -> D (in Ref. 2; AAA18905/AAA42016).
{ECO:0000305}.
CONFLICT 1229 1229 P -> R (in Ref. 2; AAA18905/AAA42016, 3;
no nucleotide entry and 6; AAA89157).
{ECO:0000305}.
CONFLICT 1306 1306 H -> D (in Ref. 5; AAB35528).
{ECO:0000305}.
CONFLICT 1306 1306 H -> G (in Ref. 2; AAA42016 and 6;
AAA89157). {ECO:0000305}.
CONFLICT 1329 1329 I -> L (in Ref. 5; AAB35528).
{ECO:0000305}.
CONFLICT 1471 1471 E -> K (in Ref. 2; AAA18905).
{ECO:0000305}.
CONFLICT 1911 1911 C -> S (in Ref. 2; AAA18905/AAA42016).
{ECO:0000305}.
CONFLICT 2084 2084 K -> N (in Ref. 2; AAA18905).
{ECO:0000305}.
CONFLICT 2154 2154 R -> Q (in Ref. 2; AAA42016).
{ECO:0000305}.
HELIX 454 474 {ECO:0000244|PDB:1VYT}.
SEQUENCE 2169 AA; 243482 MW; D3ADBD20E4763B69 CRC64;
MIRAFAQPST PPYQPLSSCL SEDTERKFKG KVVHEAQLNC FYISPGGSNY GSPRPAHANM
NANAAAGLAP EHIPTPGAAL SWLAAIDAAR 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 MSPLGISCWR CVRLLRIFKI
TRYWNSLSNL VASLLNSLRS IASLLLLLFL FIIIFSLLGM QLFGGKFNFD EMQTRRSTFD
NFPQSLLTVF QILTGEDWNS VMYDGIMAYG GPSFPGMLVC IYFIILFISP NYILLNLFLA
IAVDNLADAE SLTSAQKEEE EEKERKKLAR TASPEKKQEV MEKPAVEESK EEKIELKSIT
ADGESPPTTK INMDDLQPSE NEDKSPHSNP DTAGEEDEEE PEMPVGPRPR PLSELHLKEK
AVPMPEASAF FIFSPNNRFR LQCHRIVNDT IFTNLILFFI LLSSISLAAE DPVQHTSFRN
HILFYFDIVF TTIFTIEIAL KMTAYGAFLH KGSFCRNYFN ILDLLVVSVS LISFGIQSSA
INVVKILRVL RVLRPLRINR AKGLKHVVQC VFVAIRTIGN IVIVTTLLQF MFACIGVQLF
KGKLYTCSDS SKQTEAESKG NYITYKTGEV DHPIIQPRSW ENSKFDFDNV LAAMMALFTV
STFEGWPELL YRSIDSHTED KGPIYNYRVE ISIFFIIYII IIAFFMMNIF VGFVIVTFQE
QGEQEYKNCE LDKNQRQCVE YALKARPLPR YIPKNQHQYK VWYVVNSTYF EYLMFVLILL
NTICLAMQHY GQSCLFKIAM NILNMLFTGL FTVEMILKLI AFKPKHYFCD AWNTFDALIV
VGSIVDIAIT EVHPAEHTQC SPSMSAEENS RISITFFRLF RVMRLVKLLS RGEGIRTLLW
TFIKSFQALP YVALLIVMLF FIYAVIGMQV FGKIALNDTT EINRNNNFQT FPQAVLLLFR
CATGEAWQDI MLACMPGKKC APESEPSNST EGETPCGSSF AVFYFISFYM LCAFLIINLF
VAVIMDNFDY LTRDWSILGP HHLDEFKRIW AEYDPEAKGR IKHLDVVTLL RRIQPPLGFG
KLCPHRVACK RLVSMNMPLN SDGTVMFNAT LFALVRTALR IKTEGNLEQA NEELRAIIKK
IWKRTSMKLL DQVVPPAGDD EVTVGKFYAT FLIQEYFRKF KKRKEQGLVG KPSQRNALSL
QAGLRTLHDI GPEIRRAISG DLTAEEELDK AMKEAVSAAS EDDIFRRAGG LFGNHVSYYQ
SDSRSNFPQT FATQRPLHIN KTGNNQADTE SPSHEKLVDS TFTPSSYSST GSNANINNAN
NTALGRFPHP AGYSSTVSTV EGHGPPLSPA VRVQEAAWKL SSKRCHSRES QGATVSQDMF
PDETRSSVRL SEEVEYCSEP SLLSTDILSY QDDENRQLTC LEEDKREIQP CPKRSFLRSA
SLGRRASFHL ECLKRQKDQG GDISQKTALP LHLVHHQALA VAGLSPLLQR SHSPSTFPRP
RPTPPVTPGS RGRPLQPIPT LRLEGAESSE KLNSSFPSIH CSSWSEETTA CSGGSSMARR
ARPVSLTVPS QAGAPGRQFH GSASSLVEAV LISEGLGQFA QDPKFIEVTT QELADACDMT
IEEMENAADN ILSGGAQQSP NGTLLPFVNC RDPGQDRAVV PEDESCVYAL GRGRSEEALP
DSRSYVSNL


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