ID   CAC1D_RAT               Reviewed;        2203 AA.
AC   P27732; O09022; O09023; O09024; Q01542; Q62691; Q62815; Q63491; Q63492;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1999, sequence version 2.
DT   24-JAN-2024, entry version 178.
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=Rat brain class D;
DE            Short=RBD;
DE   AltName: Full=Voltage-gated calcium channel subunit alpha Cav1.3;
GN   Name=Cacna1d; Synonyms=Cach3, Cacn4, Cacnl1a2, Cchl1a2;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Insulinoma;
RX   PubMed=7760845; DOI=10.1210/mend.9.1.7760845;
RA   Ihara Y., Yamada Y., Fujii Y., Gonoi T., Yano H., Yasuda K., Inagaki N.,
RA   Seino Y., Seino S.;
RT   "Molecular diversity and functional characterization of voltage-dependent
RT   calcium channels (CACN4) expressed in pancreatic beta-cells.";
RL   Mol. Endocrinol. 9:121-130(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3; 6; 7; 8 AND 13).
RC   TISSUE=Brain;
RX   PubMed=1648940; DOI=10.1016/0896-6273(91)90072-8;
RA   Hui A., Ellinor P.T., Krizanova O., Wang J.-J., Diebold R.J., Schwartz A.;
RT   "Molecular cloning of multiple subtypes of a novel rat brain isoform of the
RT   alpha-1 subunit of the voltage-dependent calcium channel.";
RL   Neuron 7:35-44(1991).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-125.
RX   PubMed=7553731; DOI=10.1007/bf02089942;
RA   Kamp T.J., Mitas M., Fields K.L., Asoh S., Chin H., Marban E.,
RA   Nirenberg M.;
RT   "Transcriptional regulation of the neuronal L-type calcium channel alpha 1D
RT   subunit gene.";
RL   Cell. Mol. Neurobiol. 15:307-326(1995).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1100-1410 (ISOFORMS 4 AND 11).
RC   TISSUE=Kidney;
RX   PubMed=1279681; DOI=10.1073/pnas.89.21.10494;
RA   Yu A.S.L., Hebert S.C., Brenner B.M., Lytton J.;
RT   "Molecular characterization and nephron distribution of a family of
RT   transcripts encoding the pore-forming subunit of Ca2+ channels in the
RT   kidney.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:10494-10498(1992).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1218-1498 (ISOFORM 12).
RC   TISSUE=Osteosarcoma;
RX   PubMed=7479909; DOI=10.1073/pnas.92.24.10914;
RA   Barry E.L.R., Gesek F.A., Froehner S.C., Friedman P.A.;
RT   "Multiple calcium channel transcripts in rat osteosarcoma cells: selective
RT   activation of alpha 1D isoform by parathyroid hormone.";
RL   Proc. Natl. Acad. Sci. U.S.A. 92:10914-10918(1995).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1200-1493 (ISOFORMS 3; 4; 5; 9 AND 10).
RC   TISSUE=Hepatoma;
RX   PubMed=9232351; DOI=10.1016/s0143-4160(97)90088-9;
RA   Brereton H.M., Harland M.L., Froscio M., Petronijevic T., Barritt G.J.;
RT   "Novel variants of voltage-operated calcium channel alpha-1 subunit
RT   transcripts in a rat liver-derived cell line: deletion in the IVS4 voltage
RT   sensing region.";
RL   Cell Calcium 22:39-52(1997).
RN   [7]
RP   NUCLEOTIDE SEQUENCE OF 1307-1479 (ISOFORM 3).
RX   PubMed=1692134; DOI=10.1073/pnas.87.9.3391;
RA   Snutch T.P., Leonard J.P., Gilbert M.M., Lester H.A., Davidson N.;
RT   "Rat brain expresses a heterogeneous family of calcium channels.";
RL   Proc. Natl. Acad. Sci. U.S.A. 87:3391-3395(1990).
RN   [8]
RP   FUNCTION, MUTAGENESIS OF 1656-ILE-GLN-1657, INTERACTION WITH CABP1 AND
RP   CABP4, AND TISSUE SPECIFICITY.
RX   PubMed=17050707; DOI=10.1523/jneurosci.3236-06.2006;
RA   Yang P.S., Alseikhan B.A., Hiel H., Grant L., Mori M.X., Yang W.,
RA   Fuchs P.A., Yue D.T.;
RT   "Switching of Ca2+-dependent inactivation of Ca(v)1.3 channels by calcium
RT   binding proteins of auditory hair cells.";
RL   J. Neurosci. 26:10677-10689(2006).
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:17050707}.
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 with CABP1 and CABP4,
CC       resulting in a near elimination of calcium-dependent inactivation of
CC       the channel. Interacts with RIMBP2 (By similarity). {ECO:0000250}.
CC   -!- INTERACTION:
CC       P27732; O88871: Gabbr2; NbExp=6; IntAct=EBI-8072674, EBI-7090239;
CC       P27732; Q9QX74-7: Shank2; NbExp=2; IntAct=EBI-8072674, EBI-20939146;
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=13;
CC         Comment=The region sequenced in isoforms ROB3 and RKC5 is identical
CC         to CACN4.;
CC       Name=1; Synonyms=CACN4A;
CC         IsoId=P27732-1; Sequence=Displayed;
CC       Name=2; Synonyms=CACN4B;
CC         IsoId=P27732-2; Sequence=VSP_000923, VSP_000924;
CC       Name=3; Synonyms=CACH3A, RB48, RBD-55;
CC         IsoId=P27732-3; Sequence=VSP_000921;
CC       Name=4; Synonyms=Delta-IV-S3, RKC6;
CC         IsoId=P27732-4; Sequence=VSP_000919;
CC       Name=5; Synonyms=Delta-IV-S4;
CC         IsoId=P27732-5; Sequence=VSP_000922;
CC       Name=6; Synonyms=RB9;
CC         IsoId=P27732-6; Sequence=VSP_000920, VSP_000921;
CC       Name=7; Synonyms=RB11;
CC         IsoId=P27732-7; Sequence=VSP_000917;
CC       Name=8; Synonyms=RB34;
CC         IsoId=P27732-8; Sequence=VSP_000916;
CC       Name=9; Synonyms=RH1;
CC         IsoId=P27732-9; Sequence=VSP_000918;
CC       Name=10; Synonyms=RH2;
CC         IsoId=P27732-10; Sequence=VSP_000919, VSP_000922;
CC       Name=11; Synonyms=RKC5;
CC         IsoId=P27732-13; Sequence=Not described;
CC       Name=12; Synonyms=ROB3;
CC         IsoId=P27732-14; Sequence=Not described;
CC       Name=13; Synonyms=Truncated;
CC         IsoId=P27732-12; Sequence=VSP_000925, VSP_000926;
CC   -!- TISSUE SPECIFICITY: Expressed in brain, pancreatic islets and B-
CC       lymphocytes. {ECO:0000269|PubMed:17050707}.
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   -!- SIMILARITY: Belongs to the calcium channel alpha-1 subunit
CC       (TC 1.A.1.11) family. CACNA1D subfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; D38101; BAA07282.1; -; mRNA.
DR   EMBL; D38102; BAA07283.1; -; mRNA.
DR   EMBL; M57682; AAA42015.1; -; mRNA.
DR   EMBL; U14005; AAB60515.1; -; Genomic_DNA.
DR   EMBL; M99221; AAA40895.1; -; mRNA.
DR   EMBL; U31772; AAA89156.1; -; mRNA.
DR   EMBL; U49126; AAB61634.1; -; mRNA.
DR   EMBL; U49127; AAB61635.1; -; mRNA.
DR   EMBL; U49128; AAB61636.1; -; mRNA.
DR   PIR; JH0422; JH0422.
DR   PIR; T42742; T42742.
DR   RefSeq; NP_058994.1; NM_017298.1.
DR   AlphaFoldDB; P27732; -.
DR   SMR; P27732; -.
DR   BioGRID; 248333; 2.
DR   DIP; DIP-60740N; -.
DR   IntAct; P27732; 5.
DR   MINT; P27732; -.
DR   STRING; 10116.ENSRNOP00000043046; -.
DR   BindingDB; P27732; -.
DR   ChEMBL; CHEMBL4132; -.
DR   DrugCentral; P27732; -.
DR   GuidetoPHARMACOLOGY; 530; -.
DR   TCDB; 1.A.1.11.1; the voltage-gated ion channel (vic) superfamily.
DR   GlyCosmos; P27732; 3 sites, No reported glycans.
DR   GlyGen; P27732; 3 sites.
DR   iPTMnet; P27732; -.
DR   PhosphoSitePlus; P27732; -.
DR   PaxDb; 10116-ENSRNOP00000051407; -.
DR   ABCD; P27732; 2 sequenced antibodies.
DR   AGR; RGD:70973; -.
DR   RGD; 70973; Cacna1d.
DR   eggNOG; KOG2301; Eukaryota.
DR   InParanoid; P27732; -.
DR   OrthoDB; 1110761at2759; -.
DR   PhylomeDB; P27732; -.
DR   Reactome; R-RNO-422356; Regulation of insulin secretion.
DR   PRO; PR:P27732; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0016324; C:apical plasma membrane; IDA:RGD.
DR   GO; GO:0009986; C:cell surface; IDA:RGD.
DR   GO; GO:0098683; C:cochlear hair cell ribbon synapse; ISO:RGD.
DR   GO; GO:0032590; C:dendrite membrane; IDA:RGD.
DR   GO; GO:1990454; C:L-type voltage-gated calcium channel complex; ISO:RGD.
DR   GO; GO:0043204; C:perikaryon; IDA:RGD.
DR   GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR   GO; GO:0048787; C:presynaptic active zone membrane; ISO:RGD.
DR   GO; GO:0150001; C:primary dendrite; IDA:RGD.
DR   GO; GO:0042383; C:sarcolemma; IDA:RGD.
DR   GO; GO:0005891; C:voltage-gated calcium channel complex; ISO:RGD.
DR   GO; GO:0030018; C:Z disc; ISO:RGD.
DR   GO; GO:0051393; F:alpha-actinin binding; ISO:RGD.
DR   GO; GO:0030506; F:ankyrin binding; IPI:BHF-UCL.
DR   GO; GO:0005262; F:calcium channel activity; ISO:RGD.
DR   GO; GO:0008331; F:high voltage-gated calcium channel activity; IDA:RGD.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030165; F:PDZ domain binding; IDA:RGD.
DR   GO; GO:0005245; F:voltage-gated calcium channel activity; IDA:BHF-UCL.
DR   GO; GO:0086007; F:voltage-gated calcium channel activity involved in cardiac muscle cell action potential; IC:BHF-UCL.
DR   GO; GO:0099626; F:voltage-gated calcium channel activity involved in regulation of presynaptic cytosolic calcium levels; ISO:RGD.
DR   GO; GO:0086059; F:voltage-gated calcium channel activity involved SA node cell action potential; ISO:RGD.
DR   GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; ISO:RGD.
DR   GO; GO:0070509; P:calcium ion import; IMP:RGD.
DR   GO; GO:0098703; P:calcium ion import across plasma membrane; IBA:GO_Central.
DR   GO; GO:0070588; P:calcium ion transmembrane transport; ISO:RGD.
DR   GO; GO:0006816; P:calcium ion transport; IDA:BHF-UCL.
DR   GO; GO:0019722; P:calcium-mediated signaling; IDA:RGD.
DR   GO; GO:0086002; P:cardiac muscle cell action potential involved in contraction; ISO:RGD.
DR   GO; GO:1904646; P:cellular response to amyloid-beta; IEP:RGD.
DR   GO; GO:0051649; P:establishment of localization in cell; ISO:RGD.
DR   GO; GO:0007507; P:heart development; IEP:RGD.
DR   GO; GO:0086012; P:membrane depolarization during cardiac muscle cell action potential; IC:BHF-UCL.
DR   GO; GO:0086046; P:membrane depolarization during SA node cell action potential; ISO:RGD.
DR   GO; GO:0007613; P:memory; IEP:RGD.
DR   GO; GO:0030001; P:metal ion transport; IMP:RGD.
DR   GO; GO:0021554; P:optic nerve development; IEP:RGD.
DR   GO; GO:0045762; P:positive regulation of adenylate cyclase activity; ISS:UniProtKB.
DR   GO; GO:1904879; P:positive regulation of calcium ion transmembrane transport via high voltage-gated calcium channel; IMP:RGD.
DR   GO; GO:0051928; P:positive regulation of calcium ion transport; ISO:RGD.
DR   GO; GO:0035774; P:positive regulation of insulin secretion involved in cellular response to glucose stimulus; IMP:RGD.
DR   GO; GO:1904181; P:positive regulation of membrane depolarization; IDA:RGD.
DR   GO; GO:0060372; P:regulation of atrial cardiac muscle cell membrane repolarization; ISO:RGD.
DR   GO; GO:0051924; P:regulation of calcium ion transport; IDA:BHF-UCL.
DR   GO; GO:0086091; P:regulation of heart rate by cardiac conduction; ISO:RGD.
DR   GO; GO:1901379; P:regulation of potassium ion transmembrane transport; ISO:RGD.
DR   GO; GO:0032355; P:response to estradiol; IEP:RGD.
DR   GO; GO:0007605; P:sensory perception of sound; ISO:RGD.
DR   Gene3D; 1.10.287.70; -; 4.
DR   Gene3D; 6.10.250.2180; -; 1.
DR   Gene3D; 6.10.250.2500; -; 1.
DR   Gene3D; 1.20.120.350; Voltage-gated potassium channels. Chain C; 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   PANTHER; PTHR45628; VOLTAGE-DEPENDENT CALCIUM CHANNEL TYPE A SUBUNIT ALPHA-1; 1.
DR   PANTHER; PTHR45628:SF11; VOLTAGE-DEPENDENT L-TYPE CALCIUM CHANNEL SUBUNIT ALPHA-1D; 1.
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.
DR   SUPFAM; SSF81324; Voltage-gated potassium channels; 4.
PE   1: Evidence at protein level;
KW   Alternative splicing; Calcium; Calcium channel; Calcium transport;
KW   Disulfide bond; Glycoprotein; Ion channel; Ion transport; Membrane;
KW   Metal-binding; Phosphoprotein; Reference proteome; Repeat; Transmembrane;
KW   Transmembrane helix; Transport; Voltage-gated channel.
FT   CHAIN           1..2203
FT                   /note="Voltage-dependent L-type calcium channel subunit
FT                   alpha-1D"
FT                   /id="PRO_0000053936"
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..582
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        583..602
FT                   /note="Helical; Name=S1 of repeat II"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        603..617
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        618..636
FT                   /note="Helical; Name=S2 of repeat II"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        637..644
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        645..663
FT                   /note="Helical; Name=S3 of repeat II"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        664..673
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        674..692
FT                   /note="Helical; Name=S4 of repeat II"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        693..711
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        712..732
FT                   /note="Helical; Name=S5 of repeat II"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        733..786
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        787..811
FT                   /note="Helical; Name=S6 of repeat II"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        812..945
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        946..964
FT                   /note="Helical; Name=S1 of repeat III"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        965..980
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        981..1000
FT                   /note="Helical; Name=S2 of repeat III"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1001..1012
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1013..1031
FT                   /note="Helical; Name=S3 of repeat III"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1032..1037
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1038..1057
FT                   /note="Helical; Name=S4 of repeat III"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1058..1076
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1077..1096
FT                   /note="Helical; Name=S5 of repeat III"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1097..1186
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1187..1207
FT                   /note="Helical; Name=S6 of repeat III"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1208..1264
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1265..1283
FT                   /note="Helical; Name=S1 of repeat IV"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1284..1298
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1299..1318
FT                   /note="Helical; Name=S2 of repeat IV"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1319..1325
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1326..1347
FT                   /note="Helical; Name=S3 of repeat IV"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1348..1357
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1358..1377
FT                   /note="Helical; Name=S4 of repeat IV"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1378..1396
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1397..1416
FT                   /note="Helical; Name=S5 of repeat IV"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1417..1483
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1484..1508
FT                   /note="Helical; Name=S6 of repeat IV"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1509..2203
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REPEAT          112..408
FT                   /note="I"
FT   REPEAT          528..774
FT                   /note="II"
FT   REPEAT          892..1174
FT                   /note="III"
FT   REPEAT          1211..1486
FT                   /note="IV"
FT   REGION          1..51
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          822..909
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1134..1224
FT                   /note="Dihydropyridine binding"
FT                   /evidence="ECO:0000250"
FT   REGION          1464..1530
FT                   /note="Dihydropyridine binding"
FT                   /evidence="ECO:0000250"
FT   REGION          1476..1519
FT                   /note="Phenylalkylamine binding"
FT                   /evidence="ECO:0000250"
FT   REGION          1734..1766
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1795..1816
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1920..1963
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2176..2195
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        35..51
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        822..847
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        848..862
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        863..881
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        882..897
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1736..1755
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1795..1809
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1921..1950
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         764
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P07293"
FT   BINDING         1160
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P07293"
FT   CARBOHYD        155
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        225
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        329
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         481..492
FT                   /note="Missing (in isoform 8)"
FT                   /evidence="ECO:0000303|PubMed:1648940"
FT                   /id="VSP_000916"
FT   VAR_SEQ         493..512
FT                   /note="Missing (in isoform 7)"
FT                   /evidence="ECO:0000303|PubMed:1648940"
FT                   /id="VSP_000917"
FT   VAR_SEQ         1322..1392
FT                   /note="Missing (in isoform 9)"
FT                   /evidence="ECO:0000303|PubMed:9232351"
FT                   /id="VSP_000918"
FT   VAR_SEQ         1322..1349
FT                   /note="Missing (in isoform 4 and isoform 10)"
FT                   /evidence="ECO:0000303|PubMed:1279681,
FT                   ECO:0000303|PubMed:9232351"
FT                   /id="VSP_000919"
FT   VAR_SEQ         1322..1348
FT                   /note="GYFSDAWNTFDSLIVIGSIIDVALSEA -> HYFTDAWNTFDALIVVGSVVD
FT                   IAITEVN (in isoform 6)"
FT                   /evidence="ECO:0000303|PubMed:1648940"
FT                   /id="VSP_000920"
FT   VAR_SEQ         1349
FT                   /note="D -> DPSDSENIPLPTATPG (in isoform 6 and isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:1648940,
FT                   ECO:0000303|PubMed:9232351"
FT                   /id="VSP_000921"
FT   VAR_SEQ         1354..1368
FT                   /note="Missing (in isoform 10 and isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:9232351"
FT                   /id="VSP_000922"
FT   VAR_SEQ         1642..1668
FT                   /note="DDEVTVGKFYATFLIQDYFRKFKKRKE -> GNSRSGKSKAWWGNTLRRTPR
FT                   SPYRRD (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:7760845"
FT                   /id="VSP_000923"
FT   VAR_SEQ         1669..2203
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:7760845"
FT                   /id="VSP_000924"
FT   VAR_SEQ         1686..1691
FT                   /note="AGLRTL -> MLERML (in isoform 13)"
FT                   /evidence="ECO:0000303|PubMed:1648940"
FT                   /id="VSP_000925"
FT   VAR_SEQ         1692..2203
FT                   /note="Missing (in isoform 13)"
FT                   /evidence="ECO:0000303|PubMed:1648940"
FT                   /id="VSP_000926"
FT   MUTAGEN         1656..1657
FT                   /note="IQ->AA: Loss of calcium-dependent inactivation
FT                   related to the C-terminal lobe of calmodulin."
FT                   /evidence="ECO:0000269|PubMed:17050707"
FT   CONFLICT        124
FT                   /note="D -> N (in Ref. 2; AAA42015)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        183
FT                   /note="S -> Y (in Ref. 2; AAA42015)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        192
FT                   /note="S -> Y (in Ref. 2; AAA42015)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        513
FT                   /note="G -> C (in Ref. 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        522..560
FT                   /note="Missing (in Ref. 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1452
FT                   /note="W -> R (in Ref. 5; AAA89156)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   2203 AA;  250136 MW;  8E746A8D988050C6 CRC64;
     MMMMMMMKKM QHQRQQQEDH ANEANYARGT RLPISGEGPT SQPNSSKQTV LSWQAAIDAA
     RQAKAAQTMS TSAPPPVGSL SQRKRQQYAK SKKQGNSSNS RPARALFCLS LNNPIRRACI
     SIVDWKPFDI FILLAIFANC VALAIYIPFP EDDSNSTNHN LEKVEYAFLI IFTVETFLKI
     IASGLLLHPN ASVRNGWNLL DFVIVIVGLF SVILEQLTKE TEGGNHSSGK SGGFDVKALR
     AFRVLRPLRL VSGVPSLQVV LNSIIKAMVP LLHIALLVLF VIIIYAIIGL ELFIGKMHKT
     CFFADSDIVA EEDPAPCAFS GNGRQCAANG TECRSGWVGP NGGITNFDNF AFAMLTVFQC
     ITMEGWTDVL YWVNDAIGWE WPWVYFVSLI ILGSFFVLNL VLGVLSGEFS KEREKAKARG
     DFQKLREKQQ LEEDLKGYLD WITQAEDIDP ENEEEGGEEG KRNTSMPTSE TESVNTENVS
     GEGETQGCCG SLWCWWKRRG AAKTGPSGCR RWGQAISKSK LRSHGAREAL CVCRCSLESL
     VKLWTSRFSA HLQAAYVRPY SRRWRRWNRF NRRRCRAAVK SVTFYWLVIV LVFLNTLTIS
     SEHYNQPDWL TQIQDIANKV LLALFTCEML VKMYSLGLQA YFVSLFNRFD CFVVCGGITE
     TILVELELMS PLGVSVFRCV RLLRIFKVTR HWTSLSNLVA SLLNSMKSIA SLLLLLFLFI
     IIFSLLGMQL FGGKFNFDET QTKRSTFDNF PQALLTVFQI LTGEDWNAVM YDGIMAYGGP
     SSSGMIVCIY FIILFICGNY ILLKLFLAIA VDNLADAESL NTAQKEEAEE KERKKIARKE
     SLENKKNNKP EVNQIANSDN KVTIDDYQEE AEDKDPYPPC DVPVGEEEEE EEEDEPEVPA
     GPRPRRISEL NMKEKIAPIP EGSAFFILSK TNPIRVGCHK LINHHIFTNL ILVFIMLSSA
     ALAAEDPIRS HSFRNTILGY FDYAFTAIFT VEILLKMTTF GAFLHKGAFC RNYFNLLDML
     VVGVSLVSFG IQSSAISVVK ILRVLRVLRP LRAINRAKGL KHVVQCVFVA IRTIGNIMIV
     TTLLQFMFAC IGVQLFKGKF YRCTDEAKSN PEECRGLFIL YKDGDVDSPV VRERIWQNSD
     FNFDNVLSAM MALFTVSTFE GWPALLYKAI DSNGENVGPV YNYRVEISIF FIIYIIIVAF
     FMMNIFVGFV IVTFQEQGEK EYKNCELDKN QRQCVEYALK ARPLRRYIPK NPYQYKFWYV
     VNSSPFEYMM FVLIMLNTLC LAMQHYEQSK MFNDAMDILN MVFTGVFTVE MVLKVIAFKP
     KGYFSDAWNT FDSLIVIGSI IDVALSEADN SEESNRISIT FFRLFRVMRL VKLLSRGEGI
     RTLLWTFIKS FQALPYVALL IAMLFFIYAV IGMQMFGKVA MRDNNQINRN NNFQTFPQAV
     LLLFRCATGE AWQEIMLACL PGKLCDPDSD YNPGEEYTCG SNFAIVYFIS FYMLCAFLII
     NLFVAVIMDN FDYLTRDWSI LGPHHLDEFK RIWSEYDPEA KGRIKHLDVV TLLRRIQPPL
     GFGKLCPHRV ACKRLVAMNM PLNSDGTVMF NATLFALVRT ALKIKTEGNL EQANEELRAV
     IKKIWKKTSM KLLDQVVPPA GDDEVTVGKF YATFLIQDYF RKFKKRKEQG LVGKYPAKNT
     TIALQAGLRT LHDIGPEIRR AISCDLQDDE PEDSKPEEED VFKRNGALLG NYVNHVNSDR
     RESLQQTNTT HRPLHVQRPS IPPASDTEKP LFPPAGNSVC HNHHNHNSIG KQVPTSTNAN
     LNNANMSKAA HGKRPSIGDL EHVSENGHYS YKHDRELQRR SSIKRTRYYE TYIRSESGDE
     QLPTIFREDP EIHGYFRDPR CFGEQEYFSS EECCEDDSSP TWSRQNYSYY NRYPGSSMDF
     ERPRGYHHPQ GFLEDDDSPI GYDSRRSPRR RLLPPTPPSH RRSSFNFECL RRQNSQDDVL
     PSPALPHRAA LPLHLMQQQI MAVAGLDSSK AQKYSPSHST RSWATPPATP PYRDWTPCYT
     PLIQVDRSES MDQVNGSLPS LHRSSWYTDE PDISYRTFTP ASLTVPSSFR NKNSDKQRSA
     DSLVEAVLIS EGLGRYARDP KFVSATKHEI ADACDLTIDE MESAASTLLN GSVCPRANGD
     MGPISHRQDY ELQDFGPGYS DEEPDPGREE EDLADEMICI TTL
//