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Voltage-dependent L-type calcium channel subunit alpha-1D (Calcium channel, L type, alpha-1 polypeptide, isoform 2) (Voltage-gated calcium channel subunit alpha Cav1.3)

 CAC1D_HUMAN             Reviewed;        2161 AA.
Q01668; B0FYA3; Q13916; Q13931; Q71UT1; Q9UDC3;
15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
17-OCT-2006, sequence version 2.
25-OCT-2017, entry version 181.
RecName: Full=Voltage-dependent L-type calcium channel subunit alpha-1D;
AltName: Full=Calcium channel, L type, alpha-1 polypeptide, isoform 2;
AltName: Full=Voltage-gated calcium channel subunit alpha Cav1.3;
Name=CACNA1D; Synonyms=CACH3, CACN4, CACNL1A2, CCHL1A2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM NEURONAL-TYPE).
TISSUE=Neuroblastoma;
PubMed=1309651; DOI=10.1016/0896-6273(92)90109-Q;
Williams M.E., Feldman D.H., McCue A.F., Brenner R., Velicelebi G.,
Ellis S.B., Harpold M.M.;
"Structure and functional expression of alpha 1, alpha 2, and beta
subunits of a novel human neuronal calcium channel subtype.";
Neuron 8:71-84(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA-CELL-TYPE).
TISSUE=Pancreatic islet;
PubMed=1309948; DOI=10.1073/pnas.89.2.584;
Seino S., Chen L., Seino M., Blondel O., Takeda J., Johnson J.H.,
Bell G.I.;
"Cloning of the alpha 1 subunit of a voltage-dependent calcium channel
expressed in pancreatic beta cells.";
Proc. Natl. Acad. Sci. U.S.A. 89:584-588(1992).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM BETA-CELL-TYPE), AND
VARIANT MET-1 INS.
PubMed=7557998; DOI=10.1006/geno.1995.1048;
Yamada Y., Masuda K., Li Q., Ihara Y., Kubota A., Miura T.,
Nakamura K., Fujii Y., Seino S., Seino Y.;
"The structures of the human calcium channel alpha 1 subunit
(CACNL1A2) and beta subunit (CACNLB3) genes.";
Genomics 27:312-319(1995).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, SUBUNIT, SUBCELLULAR
LOCATION, AND ALTERNATIVE SPLICING (ISOFORM 4).
TISSUE=Pancreas;
PubMed=18482979; DOI=10.1074/jbc.M802254200;
Singh A., Gebhart M., Fritsch R., Sinnegger-Brauns M.J., Poggiani C.,
Hoda J.C., Engel J., Romanin C., Striessnig J., Koschak A.;
"Modulation of voltage- and Ca2+-dependent gating of CaV1.3 L-type
calcium channels by alternative splicing of a C-terminal regulatory
domain.";
J. Biol. Chem. 283:20733-20744(2008).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16641997; DOI=10.1038/nature04728;
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
Gibbs R.A.;
"The DNA sequence, annotation and analysis of human chromosome 3.";
Nature 440:1194-1198(2006).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-125.
PubMed=9894156; DOI=10.1038/emm.1998.36;
Kim H.-L., Chang Y.J., Lee S.M., Hong Y.-S.;
"Genomic structure of the regulatory region of the voltage-gated
calcium channel alpha 1D.";
Exp. Mol. Med. 30:246-251(1998).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 747-1039, AND TISSUE SPECIFICITY.
TISSUE=Lung carcinoma;
PubMed=1335101; DOI=10.1016/S0025-6196(12)61144-6;
Oguro-Okano M., Griesmann G.E., Wieben E.D., Slaymaker S.J.,
Snutch T.P., Lennon V.A.;
"Molecular diversity of neuronal-type calcium channels identified in
small cell lung carcinoma.";
Mayo Clin. Proc. 67:1150-1159(1992).
[8]
X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS) OF 502-510 IN COMPLEX WITH HLA.
PubMed=21280120; DOI=10.1002/pro.559;
Loll B., Ruckert C., Hee C.S., Saenger W., Uchanska-Ziegler B.,
Ziegler A.;
"Loss of recognition by cross-reactive T cells and its relation to a
C-terminus-induced conformational reorientation of an HLA-B*2705-bound
peptide.";
Protein Sci. 20:278-290(2011).
[9]
VARIANT SANDD GLY-403 INS, AND CHARACTERIZATION OF VARIANT SANDD
GLY-403 INS.
PubMed=21131953; DOI=10.1038/nn.2694;
Baig S.M., Koschak A., Lieb A., Gebhart M., Dafinger C., Nurnberg G.,
Ali A., Ahmad I., Sinnegger-Brauns M.J., Brandt N., Engel J.,
Mangoni M.E., Farooq M., Khan H.U., Nurnberg P., Striessnig J.,
Bolz H.J.;
"Loss of Ca(v)1.3 (CACNA1D) function in a human channelopathy with
bradycardia and congenital deafness.";
Nat. Neurosci. 14:77-84(2011).
[10]
VARIANTS PASNA ASP-403 AND MET-750, AND CHARACTERIZATION OF VARIANTS
PASNA ASP-403 AND MET-750.
PubMed=23913001; DOI=10.1038/ng.2695;
Scholl U.I., Goh G., Stoelting G., de Oliveira R.C., Choi M.,
Overton J.D., Fonseca A.L., Korah R., Starker L.F., Kunstman J.W.,
Prasad M.L., Hartung E.A., Mauras N., Benson M.R., Brady T.,
Shapiro J.R., Loring E., Nelson-Williams C., Libutti S.K., Mane S.,
Hellman P., Westin G., Aakerstroem G., Bjoerklund P., Carling T.,
Fahlke C., Hidalgo P., Lifton R.P.;
"Somatic and germline CACNA1D calcium channel mutations in
aldosterone-producing adenomas and primary aldosteronism.";
Nat. Genet. 45:1050-1054(2013).
-!- FUNCTION: Voltage-sensitive calcium channels (VSCC) mediate the
entry of calcium ions into excitable cells and are also involved
in a variety of calcium-dependent processes, including muscle
contraction, hormone or neurotransmitter release, gene expression,
cell motility, cell division and cell death. The isoform alpha-1D
gives rise to L-type calcium currents. Long-lasting (L-type)
calcium channels belong to the 'high-voltage activated' (HVA)
group. They are blocked by dihydropyridines (DHP),
phenylalkylamines, benzothiazepines, and by omega-agatoxin-IIIA
(omega-Aga-IIIA). They are however insensitive to omega-conotoxin-
GVIA (omega-CTx-GVIA) and omega-agatoxin-IVA (omega-Aga-IVA).
{ECO:0000269|PubMed:18482979}.
-!- SUBUNIT: Voltage-dependent calcium channels are multisubunit
complexes, consisting of alpha-1, alpha-2, beta and delta subunits
in a 1:1:1:1 ratio. The channel activity is directed by the pore-
forming and voltage-sensitive alpha-1 subunit. In many cases, this
subunit is sufficient to generate voltage-sensitive calcium
channel activity. The auxiliary subunits beta and alpha-2/delta
linked by a disulfide bridge regulate the channel activity.
Channel activity is further modulated, depending on the presence
of specific delta subunit isoforms. Interacts (via IQ domain) with
CABP1 and CABP4 in a calcium independent manner (By similarity).
Interacts with RIMBP2 (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:18482979};
Multi-pass membrane protein {ECO:0000269|PubMed:18482979}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Comment=Additional isoforms seem to exist.;
Name=Neuronal-type;
IsoId=Q01668-1; Sequence=Displayed;
Name=Beta-cell-type;
IsoId=Q01668-2; Sequence=VSP_000913, VSP_000914;
Name=4; Synonyms=Ca(V)1.3(42A);
IsoId=Q01668-4; Sequence=VSP_047921, VSP_047922;
Note=Expressed at 5% to 15% of isoform Neuronal-type in brain
tissues, increased current density.;
Name=3;
IsoId=Q01668-3; Sequence=VSP_046743, VSP_046744;
-!- TISSUE SPECIFICITY: Expressed in pancreatic islets and in brain,
where it has been seen in cerebral cortex, hippocampus, basal
ganglia, habenula and thalamus. Expressed in the small cell lung
carcinoma cell line SCC-9. No expression in skeletal muscle.
{ECO:0000269|PubMed:1335101}.
-!- 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.
-!- POLYMORPHISM: A change from seven to eight ATG trinucleotide
repeats, resulting in an additional N-terminal methionine, has
been found in a patient with non-insulin-dependent diabetes
mellitus (NIDDM). {ECO:0000269|PubMed:7557998}.
-!- DISEASE: Sinoatrial node dysfunction and deafness (SANDD)
[MIM:614896]: A disease characterized by congenital severe to
profound deafness without vestibular dysfunction, associated with
episodic syncope due to intermittent pronounced bradycardia.
{ECO:0000269|PubMed:21131953}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Primary aldosteronism, seizures, and neurologic
abnormalities (PASNA) [MIM:615474]: A disorder characterized by
hypertension, hypokalemia, and high aldosterone levels with low
plasma renin activity and an elevated aldosterone/renin ratio.
Other features include generalized seizures, cerebral palsy,
spasticity, intellectual disability, and developmental delay.
{ECO:0000269|PubMed:23913001}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the calcium channel alpha-1 subunit (TC
1.A.1.11) family. CACNA1D subfamily. {ECO:0000305}.
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EMBL; M76558; AAA58402.1; -; mRNA.
EMBL; M83566; AAA35629.1; -; mRNA.
EMBL; D43747; BAA07804.1; -; Genomic_DNA.
EMBL; EU363339; ABY66526.1; -; mRNA.
EMBL; AC005905; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC012467; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC024149; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC132810; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AF055575; AAD08651.1; -; Genomic_DNA.
CCDS; CCDS2872.1; -. [Q01668-2]
CCDS; CCDS46848.1; -. [Q01668-1]
CCDS; CCDS46849.1; -. [Q01668-3]
PIR; JH0564; JH0564.
RefSeq; NP_000711.1; NM_000720.3. [Q01668-2]
RefSeq; NP_001122311.1; NM_001128839.2. [Q01668-3]
RefSeq; NP_001122312.1; NM_001128840.2. [Q01668-1]
UniGene; Hs.476358; -.
PDB; 3LV3; X-ray; 1.94 A; C=502-510.
PDBsum; 3LV3; -.
ProteinModelPortal; Q01668; -.
SMR; Q01668; -.
BioGrid; 107230; 1.
DIP; DIP-48998N; -.
IntAct; Q01668; 2.
STRING; 9606.ENSP00000288139; -.
BindingDB; Q01668; -.
ChEMBL; CHEMBL4138; -.
DrugBank; DB00381; Amlodipine.
DrugBank; DB00568; Cinnarizine.
DrugBank; DB04920; Clevidipine.
DrugBank; DB04855; Dronedarone.
DrugBank; DB00898; Ethanol.
DrugBank; DB01023; Felodipine.
DrugBank; DB00270; Isradipine.
DrugBank; DB01388; Mibefradil.
DrugBank; DB00622; Nicardipine.
DrugBank; DB01115; Nifedipine.
DrugBank; DB06712; Nilvadipine.
DrugBank; DB00393; Nimodipine.
DrugBank; DB00401; Nisoldipine.
DrugBank; DB01054; Nitrendipine.
DrugBank; DB00421; Spironolactone.
DrugBank; DB00661; Verapamil.
GuidetoPHARMACOLOGY; 530; -.
iPTMnet; Q01668; -.
PhosphoSitePlus; Q01668; -.
DMDM; 116241275; -.
PaxDb; Q01668; -.
PeptideAtlas; Q01668; -.
PRIDE; Q01668; -.
Ensembl; ENST00000288139; ENSP00000288139; ENSG00000157388. [Q01668-2]
Ensembl; ENST00000350061; ENSP00000288133; ENSG00000157388. [Q01668-1]
Ensembl; ENST00000422281; ENSP00000409174; ENSG00000157388. [Q01668-3]
GeneID; 776; -.
KEGG; hsa:776; -.
UCSC; uc003dgu.6; human. [Q01668-1]
CTD; 776; -.
DisGeNET; 776; -.
EuPathDB; HostDB:ENSG00000157388.13; -.
GeneCards; CACNA1D; -.
HGNC; HGNC:1391; CACNA1D.
HPA; HPA020215; -.
MalaCards; CACNA1D; -.
MIM; 114206; gene.
MIM; 614896; phenotype.
MIM; 615474; phenotype.
neXtProt; NX_Q01668; -.
OpenTargets; ENSG00000157388; -.
Orphanet; 85142; Aldosterone-producing adenoma.
Orphanet; 369929; Aldosterone-producing adenoma with seizures and neurological abnormalities.
Orphanet; 324321; Sinoatrial node dysfunction and deafness.
PharmGKB; PA84; -.
eggNOG; KOG2301; Eukaryota.
eggNOG; ENOG410XNP6; LUCA.
GeneTree; ENSGT00830000128247; -.
HOGENOM; HOG000231529; -.
HOVERGEN; HBG050763; -.
InParanoid; Q01668; -.
KO; K04851; -.
OMA; LIQVERP; -.
OrthoDB; EOG091G0TKO; -.
PhylomeDB; Q01668; -.
TreeFam; TF312805; -.
Reactome; R-HSA-400042; Adrenaline,noradrenaline inhibits insulin secretion.
Reactome; R-HSA-419037; NCAM1 interactions.
Reactome; R-HSA-422356; Regulation of insulin secretion.
Reactome; R-HSA-5576892; Phase 0 - rapid depolarisation.
Reactome; R-HSA-5576893; Phase 2 - plateau phase.
ChiTaRS; CACNA1D; human.
GeneWiki; Cav1.3; -.
GenomeRNAi; 776; -.
PRO; PR:Q01668; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000157388; -.
CleanEx; HS_CACNA1D; -.
ExpressionAtlas; Q01668; baseline and differential.
Genevisible; Q01668; HS.
GO; GO:1990454; C:L-type voltage-gated calcium channel complex; IDA:BHF-UCL.
GO; GO:0005886; C:plasma membrane; ISS:BHF-UCL.
GO; GO:0005891; C:voltage-gated calcium channel complex; IDA:UniProtKB.
GO; GO:0030018; C:Z disc; ISS:BHF-UCL.
GO; GO:0051393; F:alpha-actinin binding; IPI:BHF-UCL.
GO; GO:0030506; F:ankyrin binding; ISS:BHF-UCL.
GO; GO:0008331; F:high voltage-gated calcium channel activity; IEA:Ensembl.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0005245; F:voltage-gated calcium channel activity; IDA:UniProtKB.
GO; GO:0086007; F:voltage-gated calcium channel activity involved in cardiac muscle cell action potential; IC:BHF-UCL.
GO; GO:0086059; F:voltage-gated calcium channel activity involved SA node cell action potential; IMP:BHF-UCL.
GO; GO:0007188; P:adenylate cyclase-modulating G-protein coupled receptor signaling pathway; ISS:BHF-UCL.
GO; GO:0070509; P:calcium ion import; IDA:BHF-UCL.
GO; GO:0070588; P:calcium ion transmembrane transport; ISS:BHF-UCL.
GO; GO:0006816; P:calcium ion transport; IDA:UniProtKB.
GO; GO:0061337; P:cardiac conduction; TAS:Reactome.
GO; GO:0086002; P:cardiac muscle cell action potential involved in contraction; IMP:BHF-UCL.
GO; GO:0086012; P:membrane depolarization during cardiac muscle cell action potential; IC:BHF-UCL.
GO; GO:0086046; P:membrane depolarization during SA node cell action potential; IMP:BHF-UCL.
GO; GO:0051928; P:positive regulation of calcium ion transport; IDA:BHF-UCL.
GO; GO:0060372; P:regulation of atrial cardiac muscle cell membrane repolarization; ISS:BHF-UCL.
GO; GO:0086091; P:regulation of heart rate by cardiac conduction; IMP:BHF-UCL.
GO; GO:0050796; P:regulation of insulin secretion; TAS:Reactome.
GO; GO:1901379; P:regulation of potassium ion transmembrane transport; ISS:BHF-UCL.
GO; GO:1901016; P:regulation of potassium ion transmembrane transporter activity; ISS:BHF-UCL.
GO; GO:0007605; P:sensory perception of sound; IMP:BHF-UCL.
InterPro; IPR031688; CAC1F_C.
InterPro; IPR031649; GPHH_dom.
InterPro; IPR005821; Ion_trans_dom.
InterPro; IPR005452; LVDCC_a1dsu.
InterPro; IPR014873; VDCC_a1su_IQ.
InterPro; IPR005446; VDCC_L_a1su.
InterPro; IPR002077; VDCCAlpha1.
PANTHER; PTHR10037:SF139; PTHR10037:SF139; 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; PR01636; LVDCCALPHA1D.
SMART; SM01062; Ca_chan_IQ; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Calcium; Calcium channel;
Calcium transport; Complete proteome; Deafness; Disease mutation;
Disulfide bond; Epilepsy; Glycoprotein; Ion channel; Ion transport;
Membrane; Metal-binding; Phosphoprotein; Polymorphism;
Reference proteome; Repeat; Transmembrane; Transmembrane helix;
Transport; Triplet repeat expansion; Voltage-gated channel.
CHAIN 1 2161 Voltage-dependent L-type calcium channel
subunit alpha-1D.
/FTId=PRO_0000053933.
TOPO_DOM 1 126 Cytoplasmic. {ECO:0000255}.
TRANSMEM 127 145 Helical; Name=S1 of repeat I.
{ECO:0000255}.
TOPO_DOM 146 163 Extracellular. {ECO:0000255}.
TRANSMEM 164 183 Helical; Name=S2 of repeat I.
{ECO:0000255}.
TOPO_DOM 184 195 Cytoplasmic. {ECO:0000255}.
TRANSMEM 196 214 Helical; Name=S3 of repeat I.
{ECO:0000255}.
TOPO_DOM 215 235 Extracellular. {ECO:0000255}.
TRANSMEM 236 254 Helical; Name=S4 of repeat I.
{ECO:0000255}.
TOPO_DOM 255 273 Cytoplasmic. {ECO:0000255}.
TRANSMEM 274 293 Helical; Name=S5 of repeat I.
{ECO:0000255}.
TOPO_DOM 294 381 Extracellular. {ECO:0000255}.
TRANSMEM 382 406 Helical; Name=S6 of repeat I.
{ECO:0000255}.
TOPO_DOM 407 523 Cytoplasmic. {ECO:0000255}.
TRANSMEM 524 543 Helical; Name=S1 of repeat II.
{ECO:0000255}.
TOPO_DOM 544 558 Extracellular. {ECO:0000255}.
TRANSMEM 559 577 Helical; Name=S2 of repeat II.
{ECO:0000255}.
TOPO_DOM 578 585 Cytoplasmic. {ECO:0000255}.
TRANSMEM 586 604 Helical; Name=S3 of repeat II.
{ECO:0000255}.
TOPO_DOM 605 614 Extracellular. {ECO:0000255}.
TRANSMEM 615 633 Helical; Name=S4 of repeat II.
{ECO:0000255}.
TOPO_DOM 634 652 Cytoplasmic. {ECO:0000255}.
TRANSMEM 653 673 Helical; Name=S5 of repeat II.
{ECO:0000255}.
TOPO_DOM 674 727 Extracellular. {ECO:0000255}.
TRANSMEM 728 752 Helical; Name=S6 of repeat II.
{ECO:0000255}.
TOPO_DOM 753 886 Cytoplasmic. {ECO:0000255}.
TRANSMEM 887 905 Helical; Name=S1 of repeat III.
{ECO:0000255}.
TOPO_DOM 906 921 Extracellular. {ECO:0000255}.
TRANSMEM 922 941 Helical; Name=S2 of repeat III.
{ECO:0000255}.
TOPO_DOM 942 953 Cytoplasmic. {ECO:0000255}.
TRANSMEM 954 972 Helical; Name=S3 of repeat III.
{ECO:0000255}.
TOPO_DOM 973 978 Extracellular. {ECO:0000255}.
TRANSMEM 979 998 Helical; Name=S4 of repeat III.
{ECO:0000255}.
TOPO_DOM 999 1017 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1018 1037 Helical; Name=S5 of repeat III.
{ECO:0000255}.
TOPO_DOM 1038 1127 Extracellular. {ECO:0000255}.
TRANSMEM 1128 1148 Helical; Name=S6 of repeat III.
{ECO:0000255}.
TOPO_DOM 1149 1205 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1206 1224 Helical; Name=S1 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1225 1239 Extracellular. {ECO:0000255}.
TRANSMEM 1240 1259 Helical; Name=S2 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1260 1266 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1267 1288 Helical; Name=S3 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1289 1313 Extracellular. {ECO:0000255}.
TRANSMEM 1314 1333 Helical; Name=S4 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1334 1352 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1353 1372 Helical; Name=S5 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1373 1439 Extracellular. {ECO:0000255}.
TRANSMEM 1440 1464 Helical; Name=S6 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1465 2161 Cytoplasmic. {ECO:0000255}.
REPEAT 113 409 I.
REPEAT 509 755 II.
REPEAT 873 1155 III.
REPEAT 1192 1467 IV.
CA_BIND 1493 1504 {ECO:0000250}.
REGION 429 446 Binding to the beta subunit.
{ECO:0000250}.
REGION 1075 1165 Dihydropyridine binding. {ECO:0000250}.
REGION 1420 1486 Dihydropyridine binding. {ECO:0000250}.
REGION 1432 1475 Phenylalkylamine binding. {ECO:0000250}.
COMPBIAS 1 7 Poly-Met.
COMPBIAS 653 659 Poly-Leu.
COMPBIAS 827 838 Poly-Glu.
SITE 364 364 Calcium ion selectivity and permeability.
{ECO:0000250}.
SITE 705 705 Calcium ion selectivity and permeability.
{ECO:0000250}.
SITE 1101 1101 Calcium ion selectivity and permeability.
{ECO:0000250}.
SITE 1406 1406 Calcium ion selectivity and permeability.
{ECO:0000250}.
MOD_RES 1475 1475 Phosphoserine; by PKA. {ECO:0000255}.
CARBOHYD 155 155 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 225 225 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 329 329 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 373 392 MNDAMGFELPWVYFVSLVIF -> VNDAIGWEWPWVYFVSL
IIL (in isoform Beta-cell-type).
{ECO:0000303|PubMed:1309948}.
/FTId=VSP_000913.
VAR_SEQ 493 493 C -> WCWWRRRGAAKAGPSGCRRWG (in isoform
Beta-cell-type).
{ECO:0000303|PubMed:1309948}.
/FTId=VSP_000914.
VAR_SEQ 1291 1305 Missing (in isoform 3).
{ECO:0000303|PubMed:18482979}.
/FTId=VSP_046743.
VAR_SEQ 1642 1647 AGLRTL -> MLERML (in isoform 4).
{ECO:0000305}.
/FTId=VSP_047921.
VAR_SEQ 1648 2161 Missing (in isoform 4). {ECO:0000305}.
/FTId=VSP_047922.
VAR_SEQ 1803 1811 Missing (in isoform 3).
{ECO:0000303|PubMed:18482979}.
/FTId=VSP_046744.
VARIANT 1 1 M -> MM (in a NIDDM patient).
{ECO:0000269|PubMed:7557998}.
/FTId=VAR_001497.
VARIANT 403 403 G -> D (in PASNA; the mutant channel is
activated at less depolarized potentials;
results in increased current density and
impaired channel inactivation).
{ECO:0000269|PubMed:23913001}.
/FTId=VAR_070868.
VARIANT 403 403 G -> GG (in SANDD; the mutant channels
are unable to conduct calcium ions
currents and have abnormal voltage-
dependent gating).
{ECO:0000269|PubMed:21131953}.
/FTId=VAR_069170.
VARIANT 750 750 I -> M (in PASNA; the mutant channel is
activated at less depolarized potentials;
results in increased current density;
dbSNP:rs41276445).
{ECO:0000269|PubMed:23913001}.
/FTId=VAR_070869.
VARIANT 2097 2097 D -> N (in dbSNP:rs41276455).
/FTId=VAR_061103.
CONFLICT 576 576 S -> T (in Ref. 3; BAA07804).
{ECO:0000305}.
CONFLICT 637 637 S -> C (in Ref. 1; AAA58402).
{ECO:0000305}.
CONFLICT 650 650 I -> S (in Ref. 1; AAA58402).
{ECO:0000305}.
CONFLICT 918 918 I -> T (in Ref. 3; BAA07804).
{ECO:0000305}.
CONFLICT 960 960 M -> I (in Ref. 3; BAA07804).
{ECO:0000305}.
CONFLICT 1289 1290 Missing (in Ref. 3; BAA07804).
{ECO:0000305}.
CONFLICT 1346 1346 S -> F (in Ref. 1; AAA58402).
{ECO:0000305}.
CONFLICT 1433 1433 Y -> H (in Ref. 1; AAA58402).
{ECO:0000305}.
SEQUENCE 2161 AA; 245141 MW; 31B0ADFCDB30B575 CRC64;
MMMMMMMKKM QHQRQQQADH ANEANYARGT RLPLSGEGPT 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 YWMNDAMGFE LPWVYFVSLV IFGSFFVLNL VLGVLSGEFS KEREKAKARG
DFQKLREKQQ LEEDLKGYLD WITQAEDIDP ENEEEGGEEG KRNTSMPTSE TESVNTENVS
GEGENRGCCG SLCQAISKSK LSRRWRRWNR FNRRRCRAAV KSVTFYWLVI VLVFLNTLTI
SSEHYNQPDW LTQIQDIANK VLLALFTCEM LVKMYSLGLQ AYFVSLFNRF DCFVVCGGIT
ETILVELEIM SPLGISVFRC VRLLRIFKVT RHWTSLSNLV ASLLNSMKSI ASLLLLLFLF
IIIFSLLGMQ LFGGKFNFDE TQTKRSTFDN FPQALLTVFQ ILTGEDWNAV MYDGIMAYGG
PSSSGMIVCI YFIILFICGN YILLNVFLAI AVDNLADAES LNTAQKEEAE EKERKKIARK
ESLENKKNNK PEVNQIANSD NKVTIDDYRE EDEDKDPYPP 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 IDSNGENIGP IYNHRVEISI FFIIYIIIVA
FFMMNIFVGF VIVTFQEQGE KEYKNCELDK NQRQCVEYAL KARPLRRYIP KNPYQYKFWY
VVNSSPFEYM MFVLIMLNTL CLAMQHYEQS KMFNDAMDIL NMVFTGVFTV EMVLKVIAFK
PKGYFSDAWN TFDSLIVIGS IIDVALSEAD PTESENVPVP TATPGNSEES NRISITFFRL
FRVMRLVKLL SRGEGIRTLL WTFIKSFQAL PYVALLIAML FFIYAVIGMQ MFGKVAMRDN
NQINRNNNFQ TFPQAVLLLF RCATGEAWQE IMLACLPGKL CDPESDYNPG EEYTCGSNFA
IVYFISFYML CAFLIINLFV AVIMDNFDYL TRDWSILGPH HLDEFKRIWS EYDPEAKGRI
KHLDVVTLLR RIQPPLGFGK LCPHRVACKR LVAMNMPLNS DGTVMFNATL FALVRTALKI
KTEGNLEQAN EELRAVIKKI WKKTSMKLLD QVVPPAGDDE VTVGKFYATF LIQDYFRKFK
KRKEQGLVGK YPAKNTTIAL QAGLRTLHDI GPEIRRAISC DLQDDEPEET KREEEDDVFK
RNGALLGNHV NHVNSDRRDS LQQTNTTHRP LHVQRPSIPP ASDTEKPLFP PAGNSVCHNH
HNHNSIGKQV PTSTNANLNN ANMSKAAHGK RPSIGNLEHV SENGHHSSHK HDREPQRRSS
VKRTRYYETY IRSDSGDEQL PTICREDPEI HGYFRDPHCL GEQEYFSSEE CYEDDSSPTW
SRQNYGYYSR YPGRNIDSER PRGYHHPQGF LEDDDSPVCY DSRRSPRRRL LPPTPASHRR
SSFNFECLRR QSSQEEVPSS PIFPHRTALP LHLMQQQIMA VAGLDSSKAQ KYSPSHSTRS
WATPPATPPY RDWTPCYTPL IQVEQSEALD QVNGSLPSLH RSSWYTDEPD ISYRTFTPAS
LTVPSSFRNK NSDKQRSADS LVEAVLISEG LGRYARDPKF VSATKHEIAD ACDLTIDEME
SAASTLLNGN VRPRANGDVG PLSHRQDYEL QDFGPGYSDE EPDPGRDEED LADEMICITT
L


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