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Voltage-dependent L-type calcium channel subunit alpha-1S (Calcium channel, L type, alpha-1 polypeptide, isoform 3, skeletal muscle) (Dihydropyridine receptor alpha-1S subunit) (DHPR) (Voltage-gated calcium channel subunit alpha Cav1.1)

 CAC1S_RABIT             Reviewed;        1873 AA.
P07293;
01-APR-1988, integrated into UniProtKB/Swiss-Prot.
01-APR-1988, sequence version 1.
30-AUG-2017, entry version 147.
RecName: Full=Voltage-dependent L-type calcium channel subunit alpha-1S;
AltName: Full=Calcium channel, L type, alpha-1 polypeptide, isoform 3, skeletal muscle;
AltName: Full=Dihydropyridine receptor alpha-1S subunit {ECO:0000303|PubMed:15201141, ECO:0000303|PubMed:1660150, ECO:0000303|PubMed:25667046};
Short=DHPR {ECO:0000303|PubMed:10388749, ECO:0000303|PubMed:25667046};
AltName: Full=Voltage-gated calcium channel subunit alpha Cav1.1;
Name=CACNA1S; Synonyms=CACH1, CACNL1A3;
Oryctolagus cuniculus (Rabbit).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae;
Oryctolagus.
NCBI_TaxID=9986;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, TISSUE
SPECIFICITY, DIHYDROPYRIDINE BINDING, SUBUNIT, AND SUBCELLULAR
LOCATION.
TISSUE=Skeletal muscle;
PubMed=3037387; DOI=10.1038/328313a0;
Tanabe T., Takeshima H., Mikami A., Flockerzi V., Takahashi H.,
Kangawa K., Kojima M., Matsuo H., Hirose T., Numa S.;
"Primary structure of the receptor for calcium channel blockers from
skeletal muscle.";
Nature 328:313-318(1987).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Skeletal muscle;
PubMed=2458626; DOI=10.1126/science.2458626;
Ellis S.B., Williams M.E., Ways N.R., Brenner R., Sharp A.H.,
Leung A.T., Campbell K.P., McKenna E., Koch W.J., Hui A., Schwartz A.,
Harpold M.M.;
"Sequence and expression of mRNAs encoding the alpha 1 and alpha 2
subunits of a DHP-sensitive calcium channel.";
Science 241:1661-1664(1988).
[3]
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).
[4]
PHENYLALKYLAMINE-BINDING REGION.
PubMed=2174553; DOI=10.1073/pnas.87.23.9108;
Striessnig J., Glossmann H., Catterall W.A.;
"Identification of a phenylalkylamine binding region within the alpha
1 subunit of skeletal muscle Ca2+ channels.";
Proc. Natl. Acad. Sci. U.S.A. 87:9108-9112(1990).
[5]
DIHYDROPYRIDINE-BINDING REGION.
PubMed=1656465; DOI=10.1073/pnas.88.20.9203;
Nakayama H., Taki M., Striessnig J., Glossmann H., Catterall W.A.,
Kanaoka Y.;
"Identification of 1,4-dihydropyridine binding regions within the
alpha 1 subunit of skeletal muscle Ca2+ channels by photoaffinity
labeling with diazipine.";
Proc. Natl. Acad. Sci. U.S.A. 88:9203-9207(1991).
[6]
DIHYDROPYRIDINE-BINDING REGION.
PubMed=1660150; DOI=10.1073/pnas.88.23.10769;
Striessnig J., Murphy B.J., Catterall W.A.;
"Dihydropyridine receptor of L-type Ca2+ channels: identification of
binding domains for [3H](+)-PN200-110 and [3H]azidopine within the
alpha 1 subunit.";
Proc. Natl. Acad. Sci. U.S.A. 88:10769-10773(1991).
[7]
PHOSPHORYLATION AT SER-687 AND SER-1617.
PubMed=2844809;
Roehrkasten A., Meyer H.E., Nastainczyk W., Sieber M., Hofmann F.;
"CAMP-dependent protein kinase rapidly phosphorylates serine-687 of
the skeletal muscle receptor for calcium channel blockers.";
J. Biol. Chem. 263:15325-15329(1988).
[8]
PHOSPHORYLATION BY PKA.
PubMed=2549550; DOI=10.1073/pnas.86.17.6816;
Nunoki K., Florio V., Catterall W.A.;
"Activation of purified calcium channels by stoichiometric protein
phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 86:6816-6820(1989).
[9]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=9465115;
Grabner M., Dirksen R.T., Beam K.G.;
"Tagging with green fluorescent protein reveals a distinct subcellular
distribution of L-type and non-L-type Ca2+ channels expressed in
dysgenic myotubes.";
Proc. Natl. Acad. Sci. U.S.A. 95:1903-1908(1998).
[10]
INTERACTION WITH RYR1, AND DOMAIN.
PubMed=10388749; DOI=10.1016/S0006-3495(99)76881-5;
Dulhunty A.F., Laver D.R., Gallant E.M., Casarotto M.G., Pace S.M.,
Curtis S.;
"Activation and inhibition of skeletal RyR channels by a part of the
skeletal DHPR II-III loop: effects of DHPR Ser687 and FKBP12.";
Biophys. J. 77:189-203(1999).
[11]
FUNCTION, MUTAGENESIS OF ARG-1086, SUBCELLULAR LOCATION, AND DOMAIN.
PubMed=15201141; DOI=10.1152/ajpcell.00173.2004;
Weiss R.G., O'Connell K.M., Flucher B.E., Allen P.D., Grabner M.,
Dirksen R.T.;
"Functional analysis of the R1086H malignant hyperthermia mutation in
the DHPR reveals an unexpected influence of the III-IV loop on
skeletal muscle EC coupling.";
Am. J. Physiol. 287:C1094-C1102(2004).
[12]
STRUCTURE BY NMR OF 671-690, AND DOMAIN.
PubMed=10766780; DOI=10.1074/jbc.275.16.11631;
Casarotto M.G., Gibson F., Pace S.M., Curtis S.M., Mulcair M.,
Dulhunty A.F.;
"A structural requirement for activation of skeletal ryanodine
receptors by peptides of the dihydropyridine receptor II-III loop.";
J. Biol. Chem. 275:11631-11637(2000).
[13]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 34-415 IN COMPLEX WITH
CACNB2, AND SUBUNIT.
PubMed=15134636; DOI=10.1016/S0896-6273(04)00250-8;
Opatowsky Y., Chen C.-C., Campbell K.P., Hirsch J.A.;
"Structural analysis of the voltage-dependent calcium channel beta
subunit functional core and its complex with the alpha1 interaction
domain.";
Neuron 42:387-399(2004).
[14]
STRUCTURE BY ELECTRON MICROSCOPY (15 ANGSTROMS), SUBUNIT, TISSUE
SPECIFICITY, SUBCELLULAR LOCATION, AND TOPOLOGY.
TISSUE=Skeletal muscle {ECO:0000303|PubMed:25667046};
PubMed=25667046; DOI=10.1038/srep08370;
Hu H., Wang Z., Wei R., Fan G., Wang Q., Zhang K., Yin C.C.;
"The molecular architecture of dihydropyrindine receptor/L-type Ca2+
channel complex.";
Sci. Rep. 5:8370-8370(2015).
[15] {ECO:0000244|PDB:3JBR}
STRUCTURE BY ELECTRON MICROSCOPY (4.20 ANGSTROMS) IN COMPLEX WITH
CACNG1; CACNB2 AND CACNA2D1, SUBUNIT, SUBCELLULAR LOCATION, TOPOLOGY,
TISSUE SPECIFICITY, IDENTIFICATION BY MASS SPECTROMETRY, AND DOMAIN.
TISSUE=Skeletal muscle {ECO:0000303|PubMed:26680202};
PubMed=26680202; DOI=10.1126/science.aad2395;
Wu J., Yan Z., Li Z., Yan C., Lu S., Dong M., Yan N.;
"Structure of the voltage-gated calcium channel Cav1.1 complex.";
Science 350:2395-2395(2015).
[16] {ECO:0000244|PDB:5GJV, ECO:0000244|PDB:5GJW}
STRUCTURE BY ELECTRON MICROSCOPY (3.60 ANGSTROMS) IN COMPLEX WITH
CALCIUM; CACNB1; CACNG1 AND CACNA2D1, SUBUNIT, SUBCELLULAR LOCATION,
TOPOLOGY, TISSUE SPECIFICITY, IDENTIFICATION BY MASS SPECTROMETRY,
DOMAIN, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-257.
TISSUE=Skeletal muscle {ECO:0000303|PubMed:27580036};
PubMed=27580036; DOI=10.1038/nature19321;
Wu J., Yan Z., Li Z., Qian X., Lu S., Dong M., Zhou Q., Yan N.;
"Structure of the voltage-gated calcium channel Cav1.1 at 3.6A
resolution.";
Nature 537:191-196(2016).
-!- FUNCTION: Pore-forming, alpha-1S subunit of the voltage-gated
calcium channel that gives rise to L-type calcium currents in
skeletal muscle (PubMed:9465115, PubMed:15201141). Calcium
channels containing the alpha-1S subunit play an important role in
excitation-contraction coupling in skeletal muscle via their
interaction with RYR1, which triggers Ca(2+) release from the
sarcplasmic reticulum and ultimately results in muscle contraction
(PubMed:9465115 PubMed:15201141). Long-lasting (L-type) calcium
channels belong to the 'high-voltage activated' (HVA) group.
{ECO:0000269|PubMed:15201141, ECO:0000269|PubMed:9465115,
ECO:0000305}.
-!- ENZYME REGULATION: Channel activity is blocked by dihydropyridines
(DHP), phenylalkylamines, benzothiazepines, and by omega-agatoxin-
IIIA (omega-Aga-IIIA). It is however insensitive to omega-
conotoxin-GVIA (omega-CTx-GVIA) and omega-agatoxin-IVA (omega-Aga-
IVA). {ECO:0000305|PubMed:1656465, ECO:0000305|PubMed:1660150,
ECO:0000305|PubMed:2174553, ECO:0000305|PubMed:3037387}.
-!- SUBUNIT: Component of a calcium channel complex consisting of a
pore-forming alpha subunit (CACNA1S) and the ancillary subunits
CACNB1 or CACNB2, CACNG1 and CACNA2D1 (PubMed:3037387,
PubMed:15134636, PubMed:25667046, PubMed:26680202,
PubMed:27580036). The channel complex contains alpha, beta, gamma
and delta subunits in a 1:1:1:1 ratio, i.e. it contains either
CACNB1 or CACNB2 (PubMed:15134636, PubMed:25667046,
PubMed:26680202, PubMed:27580036). CACNA1S channel activity is
modulated by the auxiliary subunits (CACNB1 or CACNB2, CACNG1 and
CACNA2D1). Interacts with DYSF and JSRP1 (By similarity).
Interacts with RYR1 (PubMed:10388749). Interacts with CALM (By
similarity). {ECO:0000250|UniProtKB:Q02789,
ECO:0000250|UniProtKB:Q13698, ECO:0000269|PubMed:10388749,
ECO:0000269|PubMed:15134636, ECO:0000269|PubMed:25667046,
ECO:0000269|PubMed:26680202, ECO:0000269|PubMed:27580036,
ECO:0000269|PubMed:3037387}.
-!- INTERACTION:
Q96RG2:PASK (xeno); NbExp=2; IntAct=EBI-8613624, EBI-1042651;
-!- SUBCELLULAR LOCATION: Cell membrane, sarcolemma
{ECO:0000269|PubMed:15201141, ECO:0000269|PubMed:25667046,
ECO:0000269|PubMed:26680202, ECO:0000269|PubMed:27580036,
ECO:0000269|PubMed:9465115, ECO:0000305|PubMed:3037387}; Multi-
pass membrane protein {ECO:0000269|PubMed:25667046,
ECO:0000269|PubMed:26680202, ECO:0000269|PubMed:27580036,
ECO:0000305|PubMed:3037387}. Note=Detected on T-tubules
(extensions of the sarcolemma). {ECO:0000269|PubMed:25667046}.
-!- TISSUE SPECIFICITY: Detected in skeletal muscle T-tubules (at
protein level). {ECO:0000269|PubMed:25667046,
ECO:0000269|PubMed:26680202, ECO:0000269|PubMed:27580036,
ECO:0000269|PubMed:3037387}.
-!- 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.
{ECO:0000269|PubMed:26680202, ECO:0000269|PubMed:27580036}.
-!- DOMAIN: The loop between repeats II and III interacts with the
ryanodine receptor, and is therefore important for calcium release
from the endoplasmic reticulum necessary for muscle contraction.
{ECO:0000305|PubMed:10388749, ECO:0000305|PubMed:10766780,
ECO:0000305|PubMed:15201141}.
-!- PTM: The alpha-1S subunit is found in two isoforms in the skeletal
muscle: a minor form of 212 kDa containing the complete amino acid
sequence, and a major form of 190 kDa derived from the full-length
form by post-translational proteolysis close to Phe-1690.
{ECO:0000305|PubMed:3037387}.
-!- PTM: Both the minor and major forms are phosphorylated in vitro by
PKA. Phosphorylation by PKA activates the calcium channel.
{ECO:0000269|PubMed:2549550, ECO:0000269|PubMed:2844809}.
-!- SIMILARITY: Belongs to the calcium channel alpha-1 subunit (TC
1.A.1.11) family. CACNA1S subfamily. {ECO:0000305}.
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EMBL; X05921; CAA29355.1; -; mRNA.
EMBL; M23919; AAA31159.1; -; mRNA.
PIR; A30063; A30063.
RefSeq; NP_001095190.1; NM_001101720.1.
UniGene; Ocu.1826; -.
PDB; 1DU1; NMR; -; A=671-690.
PDB; 1JZP; NMR; -; A=671-690.
PDB; 1T3L; X-ray; 2.20 A; B=357-374.
PDB; 3JBR; EM; 4.20 A; A=1-1395, A=1521-1873.
PDB; 5GJV; EM; 3.60 A; A=1-1873.
PDB; 5GJW; EM; 3.90 A; A=1-1873.
PDBsum; 1DU1; -.
PDBsum; 1JZP; -.
PDBsum; 1T3L; -.
PDBsum; 3JBR; -.
PDBsum; 5GJV; -.
PDBsum; 5GJW; -.
DisProt; DP00228; -.
ProteinModelPortal; P07293; -.
SMR; P07293; -.
DIP; DIP-61879N; -.
IntAct; P07293; 4.
MINT; MINT-8146707; -.
ChEMBL; CHEMBL4169; -.
TCDB; 1.A.1.11.2; the voltage-gated ion channel (vic) superfamily.
iPTMnet; P07293; -.
SwissPalm; P07293; -.
PRIDE; P07293; -.
GeneID; 100009585; -.
KEGG; ocu:100009585; -.
CTD; 779; -.
HOGENOM; HOG000231529; -.
HOVERGEN; HBG050763; -.
InParanoid; P07293; -.
KO; K04857; -.
EvolutionaryTrace; P07293; -.
PRO; PR:P07293; -.
Proteomes; UP000001811; Unplaced.
GO; GO:1990454; C:L-type voltage-gated calcium channel complex; IDA:UniProtKB.
GO; GO:0030315; C:T-tubule; IDA:UniProtKB.
GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
GO; GO:0044325; F:ion channel binding; IPI:CAFA.
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:UniProtKB.
GO; GO:0071313; P:cellular response to caffeine; IDA:UniProtKB.
GO; GO:0060314; P:regulation of ryanodine-sensitive calcium-release channel activity; IMP:CAFA.
InterPro; IPR031688; CAC1F_C.
InterPro; IPR031649; GPHH_dom.
InterPro; IPR005821; Ion_trans_dom.
InterPro; IPR014873; VDCC_a1su_IQ.
InterPro; IPR005450; VDCC_L_a1ssu.
InterPro; IPR005446; VDCC_L_a1su.
InterPro; IPR002077; VDCCAlpha1.
PANTHER; PTHR10037:SF238; PTHR10037:SF238; 1.
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; PR01634; LVDCCALPHA1S.
SMART; SM01062; Ca_chan_IQ; 1.
1: Evidence at protein level;
3D-structure; Calcium; Calcium channel; Calcium transport;
Calmodulin-binding; Cell membrane; Complete proteome;
Direct protein sequencing; Disulfide bond; Glycoprotein; Ion channel;
Ion transport; Membrane; Metal-binding; Phosphoprotein; Polymorphism;
Reference proteome; Repeat; Transmembrane; Transmembrane helix;
Transport; Voltage-gated channel.
CHAIN 1 1873 Voltage-dependent L-type calcium channel
subunit alpha-1S.
/FTId=PRO_0000053945.
TOPO_DOM 1 51 Cytoplasmic.
{ECO:0000269|PubMed:27580036}.
TRANSMEM 52 70 Helical; Name=S1 of repeat I.
{ECO:0000269|PubMed:27580036}.
TOPO_DOM 71 85 Extracellular.
{ECO:0000269|PubMed:27580036}.
TRANSMEM 86 106 Helical; Name=S2 of repeat I.
{ECO:0000269|PubMed:27580036}.
TOPO_DOM 107 115 Cytoplasmic.
{ECO:0000269|PubMed:27580036}.
TRANSMEM 116 136 Helical; Name=S3 of repeat I.
{ECO:0000269|PubMed:27580036}.
TOPO_DOM 137 160 Extracellular.
{ECO:0000269|PubMed:27580036}.
TRANSMEM 161 179 Helical; Name=S4 of repeat I.
{ECO:0000269|PubMed:27580036}.
TOPO_DOM 180 196 Cytoplasmic.
{ECO:0000269|PubMed:27580036}.
TRANSMEM 197 218 Helical; Name=S5 of repeat I.
{ECO:0000269|PubMed:27580036}.
TOPO_DOM 219 279 Extracellular.
{ECO:0000269|PubMed:27580036}.
INTRAMEM 280 301 Pore-forming.
{ECO:0000269|PubMed:26680202,
ECO:0000269|PubMed:27580036}.
TOPO_DOM 302 309 Extracellular.
{ECO:0000269|PubMed:27580036}.
TRANSMEM 310 330 Helical; Name=S6 of repeat I.
{ECO:0000269|PubMed:27580036}.
TOPO_DOM 331 432 Cytoplasmic.
{ECO:0000269|PubMed:27580036}.
TRANSMEM 433 451 Helical; Name=S1 of repeat II.
{ECO:0000269|PubMed:27580036}.
TOPO_DOM 452 462 Extracellular.
{ECO:0000269|PubMed:27580036}.
TRANSMEM 463 483 Helical; Name=S2 of repeat II.
{ECO:0000269|PubMed:27580036}.
TOPO_DOM 484 494 Cytoplasmic.
{ECO:0000269|PubMed:27580036}.
TRANSMEM 495 514 Helical; Name=S3 of repeat II.
{ECO:0000269|PubMed:27580036}.
TOPO_DOM 515 523 Extracellular.
{ECO:0000269|PubMed:27580036}.
TRANSMEM 524 542 Helical; Name=S4 of repeat II.
{ECO:0000269|PubMed:27580036}.
TOPO_DOM 543 561 Cytoplasmic.
{ECO:0000269|PubMed:27580036}.
TRANSMEM 562 581 Helical; Name=S5 of repeat II.
{ECO:0000269|PubMed:27580036}.
TOPO_DOM 582 601 Extracellular.
{ECO:0000269|PubMed:27580036}.
INTRAMEM 602 623 Pore-forming.
{ECO:0000269|PubMed:26680202,
ECO:0000269|PubMed:27580036}.
TOPO_DOM 624 633 Extracellular.
{ECO:0000269|PubMed:27580036}.
TRANSMEM 634 653 Helical; Name=S6 of repeat II.
{ECO:0000269|PubMed:27580036}.
TOPO_DOM 654 799 Cytoplasmic.
{ECO:0000269|PubMed:27580036}.
TRANSMEM 800 818 Helical; Name=S1 of repeat III.
{ECO:0000269|PubMed:27580036}.
TOPO_DOM 819 830 Extracellular.
{ECO:0000269|PubMed:27580036}.
TRANSMEM 831 850 Helical; Name=S2 of repeat III.
{ECO:0000269|PubMed:27580036}.
TOPO_DOM 851 866 Cytoplasmic.
{ECO:0000269|PubMed:27580036}.
TRANSMEM 867 885 Helical; Name=S3 of repeat III.
{ECO:0000269|PubMed:27580036}.
TOPO_DOM 886 892 Extracellular.
{ECO:0000269|PubMed:27580036}.
TRANSMEM 893 911 Helical; Name=S4 of repeat III.
{ECO:0000269|PubMed:27580036}.
TOPO_DOM 912 930 Cytoplasmic.
{ECO:0000269|PubMed:27580036}.
TRANSMEM 931 950 Helical; Name=S5 of repeat III.
{ECO:0000269|PubMed:27580036}.
TOPO_DOM 951 1000 Extracellular.
{ECO:0000269|PubMed:27580036}.
INTRAMEM 1001 1021 Pore-forming.
{ECO:0000269|PubMed:26680202,
ECO:0000269|PubMed:27580036}.
TOPO_DOM 1022 1038 Extracellular.
{ECO:0000269|PubMed:27580036}.
TRANSMEM 1039 1060 Helical; Name=S6 of repeat III.
{ECO:0000269|PubMed:27580036}.
TOPO_DOM 1061 1118 Cytoplasmic.
{ECO:0000269|PubMed:27580036}.
TRANSMEM 1119 1140 Helical; Name=S1 of repeat IV.
{ECO:0000269|PubMed:27580036}.
TOPO_DOM 1141 1148 Extracellular.
{ECO:0000269|PubMed:27580036}.
TRANSMEM 1149 1170 Helical; Name=S2 of repeat IV.
{ECO:0000269|PubMed:27580036}.
TOPO_DOM 1171 1180 Cytoplasmic.
{ECO:0000269|PubMed:27580036}.
TRANSMEM 1181 1200 Helical; Name=S3 of repeat IV.
{ECO:0000269|PubMed:27580036}.
TOPO_DOM 1201 1231 Extracellular.
{ECO:0000269|PubMed:27580036}.
TRANSMEM 1232 1250 Helical; Name=S4 of repeat IV.
{ECO:0000269|PubMed:27580036}.
TOPO_DOM 1251 1268 Cytoplasmic.
{ECO:0000269|PubMed:27580036}.
TRANSMEM 1269 1289 Helical; Name=S5 of repeat IV.
{ECO:0000269|PubMed:27580036}.
TOPO_DOM 1290 1311 Extracellular.
{ECO:0000269|PubMed:27580036}.
INTRAMEM 1312 1330 Pore-forming.
{ECO:0000269|PubMed:26680202,
ECO:0000269|PubMed:27580036}.
TOPO_DOM 1331 1356 Extracellular.
{ECO:0000269|PubMed:27580036}.
TRANSMEM 1357 1381 Helical; Name=S6 of repeat IV.
{ECO:0000269|PubMed:27580036}.
TOPO_DOM 1382 1873 Cytoplasmic.
{ECO:0000269|PubMed:27580036}.
REPEAT 38 337 I. {ECO:0000305}.
REPEAT 418 664 II. {ECO:0000305}.
REPEAT 786 1068 III. {ECO:0000305}.
REPEAT 1105 1384 IV. {ECO:0000305}.
CA_BIND 1410 1421 {ECO:0000250}.
REGION 357 374 Binding to the beta subunit.
{ECO:0000269|PubMed:27580036}.
REGION 988 1077 Dihydropyridine binding.
{ECO:0000269|PubMed:1656465,
ECO:0000269|PubMed:1660150}.
REGION 1337 1403 Dihydropyridine binding.
{ECO:0000269|PubMed:1656465}.
REGION 1349 1391 Phenylalkylamine binding.
{ECO:0000269|PubMed:2174553}.
REGION 1522 1542 Interaction with calmodulin.
{ECO:0000250|UniProtKB:Q13698}.
MOTIF 290 293 Selectivity filter of repeat I.
{ECO:0000305|PubMed:26680202,
ECO:0000305|PubMed:27580036}.
MOTIF 612 615 Selectivity filter of repeat II.
{ECO:0000305|PubMed:26680202,
ECO:0000305|PubMed:27580036}.
MOTIF 1012 1015 Selectivity filter of repeat III.
{ECO:0000305|PubMed:26680202,
ECO:0000305|PubMed:27580036}.
MOTIF 1321 1324 Selectivity filter of repeat IV.
{ECO:0000305|PubMed:26680202,
ECO:0000305|PubMed:27580036}.
COMPBIAS 562 568 Poly-Leu.
METAL 292 292 Calcium. {ECO:0000244|PDB:5GJW,
ECO:0000269|PubMed:27580036}.
METAL 614 614 Calcium. {ECO:0000244|PDB:5GJV,
ECO:0000269|PubMed:27580036}.
METAL 1014 1014 Calcium. {ECO:0000244|PDB:5GJV,
ECO:0000269|PubMed:27580036}.
SITE 1690 1691 Cleavage. {ECO:0000305}.
MOD_RES 393 393 Phosphoserine.
{ECO:0000250|UniProtKB:Q02789}.
MOD_RES 397 397 Phosphoserine.
{ECO:0000250|UniProtKB:Q02789}.
MOD_RES 687 687 Phosphoserine; by PKA.
{ECO:0000269|PubMed:2844809}.
MOD_RES 1392 1392 Phosphoserine; by PKA. {ECO:0000255}.
MOD_RES 1575 1575 Phosphoserine.
{ECO:0000250|UniProtKB:Q02485}.
MOD_RES 1579 1579 Phosphothreonine.
{ECO:0000250|UniProtKB:Q02485}.
MOD_RES 1617 1617 Phosphoserine; by PKA.
{ECO:0000269|PubMed:2844809}.
CARBOHYD 79 79 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 257 257 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:5GJV}.
DISULFID 226 254 {ECO:0000244|PDB:5GJV,
ECO:0000244|PDB:5GJW,
ECO:0000269|PubMed:27580036}.
DISULFID 245 261 {ECO:0000244|PDB:5GJV,
ECO:0000244|PDB:5GJW,
ECO:0000269|PubMed:27580036}.
DISULFID 957 968 {ECO:0000244|PDB:5GJV,
ECO:0000244|PDB:5GJW,
ECO:0000269|PubMed:27580036}.
DISULFID 1338 1352 {ECO:0000244|PDB:5GJV,
ECO:0000244|PDB:5GJW,
ECO:0000269|PubMed:27580036}.
VARIANT 165 165 R -> K.
VARIANT 258 258 G -> D.
VARIANT 1870 1870 P -> L.
MUTAGEN 1086 1086 R->H: Shifts the threshold potential to
more negative values and lowers the
concentration threshold for channel
activation by caffeine.
{ECO:0000269|PubMed:15201141}.
CONFLICT 694 694 T -> R (in Ref. 2; AAA31159).
{ECO:0000305}.
CONFLICT 1808 1808 T -> M (in Ref. 2; AAA31159).
{ECO:0000305}.
CONFLICT 1815 1815 A -> V (in Ref. 2; AAA31159).
{ECO:0000305}.
CONFLICT 1835 1835 A -> E (in Ref. 2; AAA31159).
{ECO:0000305}.
HELIX 359 372 {ECO:0000244|PDB:1T3L}.
HELIX 672 677 {ECO:0000244|PDB:1DU1}.
TURN 678 681 {ECO:0000244|PDB:1DU1}.
SEQUENCE 1873 AA; 212029 MW; 047B10D1946B0796 CRC64;
MEPSSPQDEG LRKKQPKKPL PEVLPRPPRA LFCLTLQNPL RKACISIVEW KPFETIILLT
IFANCVALAV YLPMPEDDNN SLNLGLEKLE YFFLTVFSIE AAMKIIAYGF LFHQDAYLRS
GWNVLDFIIV FLGVFTAILE QVNVIQSNTA PMSSKGAGLD VKALRAFRVL RPLRLVSGVP
SLQVVLNSIF KAMLPLFHIA LLVLFMVIIY AIIGLELFKG KMHKTCYYIG TDIVATVENE
KPSPCARTGS GRPCTINGSE CRGGWPGPNH GITHFDNFGF SMLTVYQCIT MEGWTDVLYW
VNDAIGNEWP WIYFVTLILL GSFFILNLVL GVLSGEFTKE REKAKSRGTF QKLREKQQLE
EDLRGYMSWI TQGEVMDVED LREGKLSLEE GGSDTESLYE IEGLNKIIQF IRHWRQWNRV
FRWKCHDLVK SRVFYWLVIL IVALNTLSIA SEHHNQPLWL THLQDIANRV LLSLFTIEML
LKMYGLGLRQ YFMSIFNRFD CFVVCSGILE LLLVESGAMT PLGISVLRCI RLLRLFKITK
YWTSLSNLVA SLLNSIRSIA SLLLLLFLFI IIFALLGMQL FGGRYDFEDT EVRRSNFDNF
PQALISVFQV LTGEDWNSVM YNGIMAYGGP SYPGVLVCIY FIILFVCGNY ILLNVFLAIA
VDNLAEAESL TSAQKAKAEE RKRRKMSRGL PDKTEEEKSV MAKKLEQKPK GEGIPTTAKL
KVDEFESNVN EVKDPYPSAD FPGDDEEDEP EIPVSPRPRP LAELQLKEKA VPIPEASSFF
IFSPTNKVRV LCHRIVNATW FTNFILLFIL LSSAALAAED PIRAESVRNQ ILGYFDIAFT
SVFTVEIVLK MTTYGAFLHK GSFCRNYFNI LDLLVVAVSL ISMGLESSTI SVVKILRVLR
VLRPLRAINR AKGLKHVVQC VFVAIRTIGN IVLVTTLLQF MFACIGVQLF KGKFFSCNDL
SKMTEEECRG YYYVYKDGDP TQMELRPRQW IHNDFHFDNV LSAMMSLFTV STFEGWPQLL
YRAIDSNEED MGPVYNNRVE MAIFFIIYII LIAFFMMNIF VGFVIVTFQE QGETEYKNCE
LDKNQRQCVQ YALKARPLRC YIPKNPYQYQ VWYVVTSSYF EYLMFALIML NTICLGMQHY
HQSEEMNHIS DILNVAFTII FTLEMILKLL AFKARGYFGD PWNVFDFLIV IGSIIDVILS
EIDTFLASSG GLYCLGGGCG NVDPDESARI SSAFFRLFRV MRLIKLLSRA EGVRTLLWTF
IKSFQALPYV ALLIVMLFFI YAVIGMQMFG KIALVDGTQI NRNNNFQTFP QAVLLLFRCA
TGEAWQEILL ACSYGKLCDP ESDYAPGEEY TCGTNFAYYY FISFYMLCAF LIINLFVAVI
MDNFDYLTRD WSILGPHHLD EFKAIWAEYD PEAKGRIKHL DVVTLLRRIQ PPLGFGKFCP
HRVACKRLVG MNMPLNSDGT VTFNATLFAL VRTALKIKTE GNFEQANEEL RAIIKKIWKR
TSMKLLDQVI PPIGDDEVTV GKFYATFLIQ EHFRKFMKRQ EEYYGYRPKK DTVQIQAGLR
TIEEEAAPEI RRTISGDLTA EEELERAMVE AAMEERIFRR TGGLFGQVDT FLERTNSLPP
VMANQRPLQF AEIEMEELES PVFLEDFPQD ARTNPLARAN TNNANANVAY GNSNHSNNQM
FSSVHCEREF PGEAETPAAG RGALSHSHRA LGPHSKPCAG KLNGQLVQPG MPINQAPPAP
CQQPSTDPPE RGQRRTSLTG SLQDEAPQRR SSEGSTPRRP APATALLIQE ALVRGGLDTL
AADAGFVTAT SQALADACQM EPEEVEVAAT ELLKARESVQ GMASVPGSLS RRSSLGSLDQ
VQGSQETLIP PRP


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