CAC1D_MOUSE
ID CAC1D_MOUSE Reviewed; 2179 AA.
AC Q99246; Q7TSD2; Q8R2I9; Q8R2J0;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Voltage-dependent L-type calcium channel subunit alpha-1D;
DE AltName: Full=Calcium channel, L type, alpha-1 polypeptide isoform 2;
DE AltName: Full=Voltage-gated calcium channel subunit alpha Cav1.3;
GN Name=Cacna1d; Synonyms=Cach3, Cacn4, Cacnl1a2, Cchl1a2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), INDUCTION, AND DEVELOPMENTAL
RP STAGE.
RC STRAIN=C57BL/6J; TISSUE=Heart;
RX PubMed=12900400; DOI=10.1074/jbc.m307598200;
RA Xu M., Welling A., Paparisto S., Hofmann F., Klugbauer N.;
RT "Enhanced expression of L-type Cav1.3 calcium channels in murine embryonic
RT hearts from Cav1.2-deficient mice.";
RL J. Biol. Chem. 278:40837-40841(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=BALB/cJ; TISSUE=Brain;
RA Okamoto T., Kobayashi T., Hino O.;
RT "Cloning of the L-type Ca2+ channel alpha1D-subunit from mouse brain and
RT characterization of its expression in the liver.";
RL Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1168-1463 (ISOFORMS 2/3).
RC STRAIN=ICR; TISSUE=Ovary;
RX PubMed=2173707; DOI=10.1016/s0021-9258(17)30522-7;
RA Perez-Reyes E., Wei X., Castellano A., Birnbaumer L.;
RT "Molecular diversity of L-type calcium channels. Evidence for alternative
RT splicing of the transcripts of three non-allelic genes.";
RL J. Biol. Chem. 265:20430-20436(1990).
RN [5]
RP DISRUPTION PHENOTYPE.
RX PubMed=10929716; DOI=10.1016/s0092-8674(00)00013-1;
RA Platzer J., Engel J., Schrott-Fischer A., Stephan K., Bova S., Chen H.,
RA Zheng H., Striessnig J.;
RT "Congenital deafness and sinoatrial node dysfunction in mice lacking class
RT D L-type Ca2+ channels.";
RL Cell 102:89-97(2000).
RN [6]
RP DISRUPTION PHENOTYPE.
RX PubMed=11581302; DOI=10.1172/jci200113310;
RA Namkung Y., Skrypnyk N., Jeong M.J., Lee T., Lee M.S., Kim H.L., Chin H.,
RA Suh P.G., Kim S.S., Shin H.S.;
RT "Requirement for the L-type Ca(2+) channel alpha(1D) subunit in postnatal
RT pancreatic beta cell generation.";
RL J. Clin. Invest. 108:1015-1022(2001).
RN [7]
RP DISRUPTION PHENOTYPE.
RX PubMed=12700358; DOI=10.1073/pnas.0935295100;
RA Mangoni M.E., Couette B., Bourinet E., Platzer J., Reimer D.,
RA Striessnig J., Nargeot J.;
RT "Functional role of L-type Cav1.3 Ca2+ channels in cardiac pacemaker
RT activity.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:5543-5548(2003).
RN [8]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=16354915; DOI=10.1523/jneurosci.3411-05.2005;
RA Brandt A., Khimich D., Moser T.;
RT "Few CaV1.3 channels regulate the exocytosis of a synaptic vesicle at the
RT hair cell ribbon synapse.";
RL J. Neurosci. 25:11577-11585(2005).
RN [9]
RP INTERACTION WITH CABP1 AND CABP4.
RX PubMed=17947313; DOI=10.1113/jphysiol.2007.142307;
RA Cui G., Meyer A.C., Calin-Jageman I., Neef J., Haeseleer F., Moser T.,
RA Lee A.;
RT "Ca2+-binding proteins tune Ca2+-feedback to Cav1.3 channels in mouse
RT auditory hair cells.";
RL J. Physiol. (Lond.) 585:791-803(2007).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Voltage-sensitive calcium channels (VSCC) mediate the entry
CC of calcium ions into excitable cells and are also involved in a variety
CC of calcium-dependent processes, including muscle contraction, hormone
CC or neurotransmitter release, gene expression, cell motility, cell
CC division and cell death. The isoform alpha-1D gives rise to L-type
CC calcium currents. Long-lasting (L-type) calcium channels belong to the
CC 'high-voltage activated' (HVA) group. They are blocked by
CC dihydropyridines (DHP), phenylalkylamines, and by benzothiazepines.
CC {ECO:0000269|PubMed:16354915}.
CC -!- SUBUNIT: Voltage-dependent calcium channels are multisubunit complexes,
CC consisting of alpha-1, alpha-2, beta and delta subunits in a 1:1:1:1
CC ratio. The channel activity is directed by the pore-forming and
CC voltage-sensitive alpha-1 subunit. In many cases, this subunit is
CC sufficient to generate voltage-sensitive calcium channel activity. The
CC auxiliary subunits beta and alpha-2/delta linked by a disulfide bridge
CC regulate the channel activity. Interacts (via IQ domain) with CABP1 and
CC CABP4 in a calcium independent manner. Interacts with RIMBP2 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q99246-2; Sequence=Displayed;
CC Name=2; Synonyms=Cav1.3(1a);
CC IsoId=Q99246-3; Sequence=VSP_027091, VSP_027092;
CC Name=3; Synonyms=Cav1.3(1b);
CC IsoId=Q99246-4; Sequence=VSP_027090, VSP_027091, VSP_027092;
CC -!- TISSUE SPECIFICITY: Expressed in the inner hair cells (IHC) of the
CC cochlea. {ECO:0000269|PubMed:16354915}.
CC -!- DEVELOPMENTAL STAGE: Isoform 2 and isoform 3 are expressed in heart at
CC 12.5 dpc (at protein level). Expressed in the heart at 9.5, 12.5 and
CC 15.5 dpc. Isoform 2 and isoform 3 are expressed in heart at 9.5 and
CC 12.5 dpc. {ECO:0000269|PubMed:12900400}.
CC -!- INDUCTION: Up-regulated in CACNA1C knockout mice.
CC {ECO:0000269|PubMed:12900400}.
CC -!- DOMAIN: Each of the four internal repeats contains five hydrophobic
CC transmembrane segments (S1, S2, S3, S5, S6) and one positively charged
CC transmembrane segment (S4). S4 segments probably represent the voltage-
CC sensor and are characterized by a series of positively charged amino
CC acids at every third position.
CC -!- DISRUPTION PHENOTYPE: deafness, bradycardia and diabetic traits.
CC {ECO:0000269|PubMed:10929716, ECO:0000269|PubMed:11581302,
CC ECO:0000269|PubMed:12700358}.
CC -!- SIMILARITY: Belongs to the calcium channel alpha-1 subunit (TC
CC 1.A.1.11) family. CACNA1D subfamily. {ECO:0000305}.
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DR EMBL; AJ437291; CAD26883.1; -; mRNA.
DR EMBL; AJ437292; CAD26884.1; -; mRNA.
DR EMBL; AB086123; BAC77259.1; -; mRNA.
DR EMBL; AC119886; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC154305; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC154669; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC154690; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CT009536; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; M57975; AAA63292.1; -; mRNA.
DR CCDS; CCDS36846.1; -. [Q99246-4]
DR CCDS; CCDS36847.1; -. [Q99246-3]
DR CCDS; CCDS88609.1; -. [Q99246-2]
DR RefSeq; NP_001077085.1; NM_001083616.2. [Q99246-3]
DR RefSeq; NP_001289566.1; NM_001302637.1. [Q99246-2]
DR RefSeq; NP_083257.2; NM_028981.3. [Q99246-4]
DR AlphaFoldDB; Q99246; -.
DR SMR; Q99246; -.
DR BioGRID; 198433; 12.
DR CORUM; Q99246; -.
DR IntAct; Q99246; 2.
DR STRING; 10090.ENSMUSP00000107869; -.
DR BindingDB; Q99246; -.
DR ChEMBL; CHEMBL3988632; -.
DR DrugCentral; Q99246; -.
DR GuidetoPHARMACOLOGY; 530; -.
DR iPTMnet; Q99246; -.
DR PhosphoSitePlus; Q99246; -.
DR SwissPalm; Q99246; -.
DR MaxQB; Q99246; -.
DR PaxDb; Q99246; -.
DR PRIDE; Q99246; -.
DR ProteomicsDB; 273881; -. [Q99246-2]
DR ProteomicsDB; 273882; -. [Q99246-3]
DR ProteomicsDB; 273883; -. [Q99246-4]
DR ABCD; Q99246; 2 sequenced antibodies.
DR Antibodypedia; 4062; 323 antibodies from 32 providers.
DR DNASU; 12289; -.
DR Ensembl; ENSMUST00000112250; ENSMUSP00000107869; ENSMUSG00000015968. [Q99246-4]
DR Ensembl; ENSMUST00000224198; ENSMUSP00000153250; ENSMUSG00000015968. [Q99246-3]
DR Ensembl; ENSMUST00000238504; ENSMUSP00000158632; ENSMUSG00000015968. [Q99246-2]
DR GeneID; 12289; -.
DR KEGG; mmu:12289; -.
DR UCSC; uc007suu.2; mouse. [Q99246-3]
DR UCSC; uc007suw.2; mouse. [Q99246-2]
DR UCSC; uc007sux.2; mouse. [Q99246-4]
DR CTD; 776; -.
DR MGI; MGI:88293; Cacna1d.
DR VEuPathDB; HostDB:ENSMUSG00000015968; -.
DR eggNOG; KOG2301; Eukaryota.
DR GeneTree; ENSGT00940000154839; -.
DR HOGENOM; CLU_000540_0_1_1; -.
DR InParanoid; Q99246; -.
DR OrthoDB; 172471at2759; -.
DR TreeFam; TF312805; -.
DR Reactome; R-MMU-422356; Regulation of insulin secretion.
DR BioGRID-ORCS; 12289; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Cacna1d; mouse.
DR PRO; PR:Q99246; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q99246; protein.
DR Bgee; ENSMUSG00000015968; Expressed in pituitary gland and 202 other tissues.
DR ExpressionAtlas; Q99246; baseline and differential.
DR Genevisible; Q99246; MM.
DR GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0098683; C:cochlear hair cell ribbon synapse; IDA:SynGO.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0032590; C:dendrite membrane; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IC:MGI.
DR GO; GO:0099059; C:integral component of presynaptic active zone membrane; IDA:SynGO.
DR GO; GO:1990454; C:L-type voltage-gated calcium channel complex; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
DR GO; GO:0042383; C:sarcolemma; ISO:MGI.
DR GO; GO:0005891; C:voltage-gated calcium channel complex; ISO:MGI.
DR GO; GO:0030018; C:Z disc; IDA:BHF-UCL.
DR GO; GO:0051393; F:alpha-actinin binding; ISO:MGI.
DR GO; GO:0030506; F:ankyrin binding; IPI:BHF-UCL.
DR GO; GO:0005262; F:calcium channel activity; ISO:MGI.
DR GO; GO:0008331; F:high voltage-gated calcium channel activity; IDA:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030165; F:PDZ domain binding; ISO:MGI.
DR GO; GO:0005245; F:voltage-gated calcium channel activity; ISO:MGI.
DR GO; GO:0099635; F:voltage-gated calcium channel activity involved in positive regulation of presynaptic cytosolic calcium levels; IDA:SynGO.
DR GO; GO:0086059; F:voltage-gated calcium channel activity involved SA node cell action potential; IMP:MGI.
DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IMP:MGI.
DR GO; GO:0070509; P:calcium ion import; ISO:MGI.
DR GO; GO:0098703; P:calcium ion import across plasma membrane; IBA:GO_Central.
DR GO; GO:0070588; P:calcium ion transmembrane transport; IMP:MGI.
DR GO; GO:0006816; P:calcium ion transport; ISO:MGI.
DR GO; GO:0019722; P:calcium-mediated signaling; ISO:MGI.
DR GO; GO:0061337; P:cardiac conduction; ISS:UniProtKB.
DR GO; GO:0086002; P:cardiac muscle cell action potential involved in contraction; ISO:MGI.
DR GO; GO:0051649; P:establishment of localization in cell; IMP:MGI.
DR GO; GO:0086046; P:membrane depolarization during SA node cell action potential; IMP:MGI.
DR GO; GO:0030001; P:metal ion transport; ISO:MGI.
DR GO; GO:0045762; P:positive regulation of adenylate cyclase activity; IDA:UniProtKB.
DR GO; GO:1904879; P:positive regulation of calcium ion transmembrane transport via high voltage-gated calcium channel; ISO:MGI.
DR GO; GO:0051928; P:positive regulation of calcium ion transport; ISO:MGI.
DR GO; GO:0032793; P:positive regulation of CREB transcription factor activity; ISO:MGI.
DR GO; GO:0035774; P:positive regulation of insulin secretion involved in cellular response to glucose stimulus; ISO:MGI.
DR GO; GO:0060372; P:regulation of atrial cardiac muscle cell membrane repolarization; IMP:BHF-UCL.
DR GO; GO:0051924; P:regulation of calcium ion transport; ISO:MGI.
DR GO; GO:0086091; P:regulation of heart rate by cardiac conduction; IMP:MGI.
DR GO; GO:1901379; P:regulation of potassium ion transmembrane transport; IMP:BHF-UCL.
DR GO; GO:1901016; P:regulation of potassium ion transmembrane transporter activity; IMP:BHF-UCL.
DR GO; GO:0007605; P:sensory perception of sound; IMP:MGI.
DR Gene3D; 1.20.120.350; -; 4.
DR InterPro; IPR031688; CAC1F_C.
DR InterPro; IPR031649; GPHH_dom.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR005452; LVDCC_a1dsu.
DR InterPro; IPR014873; VDCC_a1su_IQ.
DR InterPro; IPR005446; VDCC_L_a1su.
DR InterPro; IPR002077; VDCCAlpha1.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR Pfam; PF08763; Ca_chan_IQ; 1.
DR Pfam; PF16885; CAC1F_C; 2.
DR Pfam; PF16905; GPHH; 1.
DR Pfam; PF00520; Ion_trans; 4.
DR PRINTS; PR00167; CACHANNEL.
DR PRINTS; PR01630; LVDCCALPHA1.
DR PRINTS; PR01636; LVDCCALPHA1D.
DR SMART; SM01062; Ca_chan_IQ; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Calcium channel; Calcium transport;
KW Coiled coil; Disulfide bond; Ion channel; Ion transport; Membrane;
KW Metal-binding; Phosphoprotein; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1..2179
FT /note="Voltage-dependent L-type calcium channel subunit
FT alpha-1D"
FT /id="PRO_0000053935"
FT TOPO_DOM 1..126
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 127..145
FT /note="Helical; Name=S1 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 146..163
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 164..183
FT /note="Helical; Name=S2 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 184..195
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 196..214
FT /note="Helical; Name=S3 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 215..235
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 236..254
FT /note="Helical; Name=S4 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 255..273
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 274..293
FT /note="Helical; Name=S5 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 294..381
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 382..406
FT /note="Helical; Name=S6 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 407..543
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 544..563
FT /note="Helical; Name=S1 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 564..578
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 579..597
FT /note="Helical; Name=S2 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 598..605
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 606..624
FT /note="Helical; Name=S3 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 625..634
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 635..653
FT /note="Helical; Name=S4 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 654..672
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 673..693
FT /note="Helical; Name=S5 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 694..747
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 748..772
FT /note="Helical; Name=S6 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 773..906
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 907..925
FT /note="Helical; Name=S1 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 926..941
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 942..961
FT /note="Helical; Name=S2 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 962..973
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 974..992
FT /note="Helical; Name=S3 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 993..998
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 999..1018
FT /note="Helical; Name=S4 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1019..1037
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1038..1057
FT /note="Helical; Name=S5 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1058..1147
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1148..1168
FT /note="Helical; Name=S6 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1169..1225
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1226..1244
FT /note="Helical; Name=S1 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1245..1259
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1260..1279
FT /note="Helical; Name=S2 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1280..1286
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1287..1308
FT /note="Helical; Name=S3 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1309..1333
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1334..1353
FT /note="Helical; Name=S4 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1354..1372
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1373..1392
FT /note="Helical; Name=S5 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1393..1459
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1460..1484
FT /note="Helical; Name=S6 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1485..2179
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 113..409
FT /note="I"
FT REPEAT 529..775
FT /note="II"
FT REPEAT 893..1175
FT /note="III"
FT REPEAT 1212..1487
FT /note="IV"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 30..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 64..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 429..446
FT /note="Binding to the beta subunit"
FT /evidence="ECO:0000250"
FT REGION 449..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 786..870
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1095..1185
FT /note="Dihydropyridine binding"
FT /evidence="ECO:0000250"
FT REGION 1440..1506
FT /note="Dihydropyridine binding"
FT /evidence="ECO:0000250"
FT REGION 1452..1495
FT /note="Phenylalkylamine binding"
FT /evidence="ECO:0000250"
FT REGION 1704..1789
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1896..1941
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2135..2171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 771..810
FT /evidence="ECO:0000255"
FT COMPBIAS 35..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 462..480
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 786..808
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 809..823
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 824..842
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 843..858
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1716..1731
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1756..1785
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1897..1926
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 364
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT BINDING 725
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT BINDING 1121
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT VAR_SEQ 1..22
FT /note="MMMMMMMKKMQHQRQHQEDHAN -> MNLPTFSSDLILIKSVLSQETDARYK
FT GRVVSAVESTEDFSQAFA (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12900400"
FT /id="VSP_027090"
FT VAR_SEQ 493..513
FT /note="WCWWKRRGAAKTGPSGCRRWG -> C (in isoform 2 and isoform
FT 3)"
FT /evidence="ECO:0000303|PubMed:12900400"
FT /id="VSP_027091"
FT VAR_SEQ 1311..1325
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:12900400"
FT /id="VSP_027092"
FT CONFLICT 445
FT /note="A -> V (in Ref. 1; CAD26883/CAD26884)"
FT /evidence="ECO:0000305"
FT CONFLICT 868
FT /note="I -> T (in Ref. 1; CAD26883/CAD26884)"
FT /evidence="ECO:0000305"
FT CONFLICT 1871
FT /note="E -> G (in Ref. 1; CAD26883/CAD26884)"
FT /evidence="ECO:0000305"
FT CONFLICT 2043
FT /note="Y -> S (in Ref. 2; BAC77259)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2179 AA; 247061 MW; BEED5EF140E75782 CRC64;
MMMMMMMKKM QHQRQHQEDH ANEANYARGT RLPISGEGPT SQPNSSKQTV LSWQAAIDAA
RQAKAAQTMS TSAPPPVGSL SQRKRQQYAK SKKQGNSSNS RPARALFCLS LNNPIRRACI
SIVEWKPFDI FILLAIFANC VALAIYIPFP EDDSNSTNHN LEKVEYAFLI IFTVETFLKI
IAYGLLLHPN AYVRNGWNLL DFVIVIVGLF SVILEQLTKE TEGGNHSSGK SGGFDVKALR
AFRVLRPLRL VSGVPSLQVV LNSIIKAMVP LLHIALLVLF VIIIYAIIGL ELFIGKMHKT
CFFADSDIVA EEDPAPCAFS GNGRQCTANG TECRSGWVGP NGGITNFDNF AFAMLTVFQC
ITMEGWTDVL YWVNDAIGWE WPWVYFVSLI ILGSFFVLNL VLGVLSGEFS KEREKAKARG
DFQKLREKQQ LEEDLKGYLD WITQAEDIDP ENEEEGGEEG KRNTSMPTSE TESVNTENVS
GEGETQGCCG TLWCWWKRRG AAKTGPSGCR RWGQAISKSK LSRRWRRWNR FNRRRCRAAV
KSVTFYWLVI VLVFLNTLTI SSEHYNQPDW LTQIQDIANK VLLALFTCEM LVKMYSLGLQ
AYFVSLFNRF DCFVVCGGIT ETILVELELM SPLGVSVFRC VRLLRIFKVT RHWTSLSNLV
ASLLNSMKSI ASLLLLLFLF IIIFSLLGMQ LFGGKFNFDE TQTKRSTFDN FPQALLTVFQ
ILTGEDWNAV MYDGIMAYGG PSSSGMIVCI YFIILFICGN YILLNVFLAI AVDNLADAES
LNTAQKEEAE EKERKKIARK ESLENKKNNK PEVNQIANSD NKVTIDDYQE DAEDKDPYPP
CDVPVGEEEE EEEEDEPEVP AGPRPRRISE LNMKEKIAPI PEGSAFFILS KTNPIRVGCH
KLINHHIFTN LILVFIMLSS AALAAEDPIR SHSFRNTILG YFDYAFTAIF TVEILLKMTT
FGAFLHKGAF CRNYFNLLDM LVVGVSLVSF GIQSSAISVV KILRVLRVLR PLRAINRAKG
LKHVVQCVFV AIRTIGNIMI VTTLLQFMFA CIGVQLFKGK FYRCTDEAKS NPEECRGLFI
LYKDGDVDSP VVRERIWQNS DFNFDNVLSA MMALFTVSTF EGWPALLYKA IDSNGENVGP
VYNYRVEISI FFIIYIIIVA FFMMNIFVGF VIVTFQEQGE KEYKNCELDK NQRQCVEYAL
KARPLRRYIP KNPYQYKFWY VVNSSPFEYM MFVLIMLNTL CLAMQHYEQS KMFNDAMDIL
NMVFTGVFTV EMVLKVIAFK PKGYFSDAWN TFDSLIVIGS IIDVALSEAD PSESETIPLP
TATPGNSEES NRISITFFRL FRVMRLVKLL SRGEGIRTLL WTFIKSFQAL PYVALLIAML
FFIYAVIGMQ MFGKVAMRDN NQINRNNNFQ TFPQAVLLLF RCATGEAWQE IMLACLPGKL
CDPDSDYNPG EEYTCGSNFA IVYFISFYML CAFLIINLFV AVIMDNFDYL TRDWSILGPH
HLDEFKRIWS EYDPEAKGRI KHLDVVTLLR RIQPPLGFGK LCPHRVACKR LVAMNMPLNS
DGTVMFNATL FALVRTALKI KTEGNLEQAN EELRAVIKKI WKKTSMKLLD QVVPPAGDDE
VTVGKFYATF LIQDYFRKFK KRKEQGLVGK YPAKNTTIAL QAGLRTLHDI GPEIRRAISC
DLQDDEPEDS KPEEEDVFKR NGALLGNHVN HVNSDRRDSL QQTNTTHRPL HVQRPSMPPA
SDTEKPLFPP AGNSGCHNHH NHNSIGKQAP TSTNANLNNA NMSKAAHGKP PSIGNLEHVS
ENGHYSCKHD RELQRRSSIK RTRYYETYIR SESGDEQFPT ICREDPEIHG YFRDPRCLGE
QEYFSSEECC EDDSSPTWSR QNYNYYNRYP GSSMDFERPR GYHHPQGFLE DDDSPTGYDS
RRSPRRRLLP PTPPSHRRSS FNFECLRRQS SQDDVLPSPA LPHRAALPLH LMQQQIMAVA
GLDSSKAQKY SPSHSTRSWA TPPATPPYRD WSPCYTPLIQ VDRSESMDQV NGSLPSLHRS
SWYTDEPDIS YRTFTPASLT VPSSFRNKNS DKQRSADSLV EAVLISEGLG RYARDPKFVS
ATKHEIADAC DLTIDEMESA ASTLLNGSVC PRANGDMGPI SHRQDYELQD FGPGYSDEEP
DPGREEEDLA DEMICITTL
