Protein detail
CAC1C
Voltage-dependent L-type calcium channel subunit alpha-1C (Calcium channel, L type, alpha-1 polypeptide, isoform 1, cardiac muscle) (Voltage-gated calcium channel subunit alpha Cav1.2)
Protein symbol CAC1C | UniProt ID | EVMP score 0.50 |
Frequency 1 | Transmembrane count 24 | Protein classification Disease related genesFDA approved drug targetsHuman disease related genesPredicted membrane proteinsTransportersVoltage-gated ion channels |
EVMP score: annotation confidence score.
Extremely high >= 0.85High >= 0.70Medium >= 0.55Low >= 0.40
Basic Information
Protein Names
Voltage-dependent L-type calcium channel subunit alpha-1C (Calcium channel, L type, alpha-1 polypeptide, isoform 1, cardiac muscle) (Voltage-gated calcium channel subunit alpha Cav1.2)
Protein Class
Disease related genesFDA approved drug targetsHuman disease related genesPredicted membrane proteinsTransportersVoltage-gated ion channels
Protein Function
- Voltage-gated ion channels:Voltage-Gated Calcium Channels
- Transporters:Transporter channels and pores
- Disease related genes
- Human disease related genes:Cardiovascular diseases:Cardiac diseases
- FDA approved drug targets:Small molecule drugs
Transmembrane
125..143; Helical; Name=S1 of repeat I; 159..179; Helical; Name=S2 of repeat I; 189..209; Helical; Name=S3 of repeat I; 233..251; Helical; Name=S4 of repeat I; 269..290; Helical; Name=S5 of repeat I; 381..401; Helical; Name=S6 of repeat I; 525..543; Helical; Name=S1 of repeat II; 555..575; Helical; Name=S2 of repeat II; 587..606; Helical; Name=S3 of repeat II; 616..634; Helical; Name=S4 of repeat II; 654..673; Helical; Name=S5 of repeat II; 726..745; Helical; Name=S6 of repeat II; 901..919; Helical; Name=S1 of repeat III; 932..952; Helical; Name=S2 of repeat III; 988..1006; Helical; Name=S3 of repeat III; 1014..1032; Helical; Name=S4 of repeat III; 1052..1071; Helical; Name=S5 of repeat III; 1160..1181; Helical; Name=S6 of repeat III; 1240..1261; Helical; Name=S1 of repeat IV; 1270..1291; Helical; Name=S2 of repeat IV; 1302..1321; Helical; Name=S3 of repeat IV; 1373..1391; Helical; Name=S4 of repeat IV; 1410..1430; Helical; Name=S5 of repeat IV; 1500..1524; Helical; Name=S6 of repeat IV
Transmembrane Count
24
Ensembl
Entrez Gene Symbol
Gene Synonym
CACH2CACN2CACNL1A1Cav1.2CCHL1A1LQT8TS
Gene Description
Calcium voltage-gated channel subunit alpha1 C
Chromosome
12
Position
1970772-2697950
Frequency
1
EVMP Score
0.50
Fluorescence & Localization
Cell SpecificEndometrial glandular cells
Function & Pathway
Protein Function
- Voltage-gated ion channels:Voltage-Gated Calcium Channels
- Transporters:Transporter channels and pores
- Disease related genes
- Human disease related genes:Cardiovascular diseases:Cardiac diseases
- FDA approved drug targets:Small molecule drugs
Cellular Component
Molecular Function
- GO:0005245 voltage-gated calcium channel activity
- GO:0005515 protein binding
- GO:0005516 calmodulin binding
- GO:0008331 high voltage-gated calcium channel activity
- GO:0046872 metal ion binding
- GO:0051393 alpha-actinin binding
- GO:0086007 voltage-gated calcium channel activity involved in cardiac muscle cell action potential
- GO:0086056 voltage-gated calcium channel activity involved in AV node cell action potential
Biological Process
KEGG
- hsa04010 MAPK signaling pathway
- KEGG:hsa04020 Calcium signaling pathway
- KEGG:hsa04022 cGMP-PKG signaling pathway
- KEGG:hsa04024 cAMP signaling pathway
- KEGG:hsa04260 Cardiac muscle contraction
- KEGG:hsa04261 Adrenergic signaling in cardiomyocytes
- KEGG:hsa04270 Vascular smooth muscle contraction
- KEGG:hsa04713 Circadian entrainment
- KEGG:hsa04720 Long-term potentiation
- KEGG:hsa04723 Retrograde endocannabinoid signaling
- KEGG:hsa04724 Glutamatergic synapse
- KEGG:hsa04725 Cholinergic synapse
- KEGG:hsa04726 Serotonergic synapse
- KEGG:hsa04727 GABAergic synapse
- KEGG:hsa04728 Dopaminergic synapse
- KEGG:hsa04742 Taste transduction
- KEGG:hsa04911 Insulin secretion
- KEGG:hsa04912 GnRH signaling pathway
- KEGG:hsa04921 Oxytocin signaling pathway
- KEGG:hsa04924 Renin secretion
- KEGG:hsa04925 Aldosterone synthesis and secretion
- KEGG:hsa04927 Cortisol synthesis and secretion
- KEGG:hsa04929 GnRH secretion
- KEGG:hsa04930 Type II diabetes mellitus
- KEGG:hsa04934 Cushing syndrome
- KEGG:hsa04935 Growth hormone synthesis, secretion and action
- KEGG:hsa05010 Alzheimer disease
- KEGG:hsa05020 Prion disease
- KEGG:hsa05022 Pathways of neurodegeneration - multiple diseases
- KEGG:hsa05031 Amphetamine addiction
- KEGG:hsa05207 Chemical carcinogenesis - receptor activation
- KEGG:hsa05410 Hypertrophic cardiomyopathy
- KEGG:hsa05412 Arrhythmogenic right ventricular cardiomyopathy
- KEGG:hsa05414 Dilated cardiomyopathy
Reactome
- R-hsa-400042 adrenaline noradrenaline inhibits insulin secretion
- R-hsa-5576891 cardiac conduction
- R-hsa-163685 integration of energy metabolism
- R-hsa-397014 muscle contraction
- R-hsa-419037 ncam1 interactions
- R-hsa-375165 ncam signaling for neurite out growth
- R-hsa-9675108 nervous system development
- R-hsa-5576892 phase 0 rapid depolarisation
- R-hsa-5576893 phase 2 plateau phase
- R-hsa-422356 regulation of insulin secretion
Mediation Categories
Clinical-translation mediationFusion and delivery mediationMetabolism mediationReceptor-signaling mediation
Relations & Evidence
Enzyme-Mediated Modification
13 records.
| Substrate Gene Symbol | Enzyme Gene Symbol | Enzyme UniProt ID | Residue Type | Residue Offset | Modification | Database | References |
|---|---|---|---|---|---|---|---|
| CACNA1C | PRKACA | P17612 | S | 1,897 | phosphorylation | SIGNOR_ProtMapperSIGNORProtMapper | SIGNOR:28119464ProtMapper:28119464 |
| CACNA1C | PRKACA | P17612 | S | 1,898 | phosphorylation | HPRDKEA | KEA:8612821HPRD:8612821HPRD:9247274KEA:9247274 |
| CACNA1C | PRKACA | P17612 | S | 1,535 | phosphorylation | PhosphoSitePhosphoSite_ProtMapperProtMapper | |
| CACNA1C | PRKACA | P17612 | S | 1,981 | phosphorylation | MIMPHPRD_MIMPPhosphoSitePhosphoSite_MIMP | |
| CACNA1C | PRKACA | P17612 | S | 1,645 | phosphorylation | MIMPHPRD_MIMP | |
| CACNA1C | PRKACA | P17612 | S | 1,718 | phosphorylation | MIMPHPRD_MIMP | |
| CACNA1C | PRKACA | P17612 | S | 1,597 | phosphorylation | KEA | KEA:8664319 |
| CACNA1C | PRKACA | P17612 | S | 1,670 | phosphorylation | KEA | KEA:8664319 |
| CACNA1C | PRKD1 | Q15139 | S | 1,981 | phosphorylation | PhosphoSite_MIMPMIMPHPRD_MIMPSIGNORProtMapperSIGNOR_ProtMapperPhosphoSitePhosphoSite_ProtMapper | ProtMapper:22100296SIGNOR:22100296 |
| CACNA1C | SRC | P12931 | Y | 2,217 | phosphorylation | PhosphoSite_MIMPMIMPProtMapperPhosphoSitePhosphoSite_ProtMapper |
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Ligand-Receptor Signaling
31 records.
| Category | Parent | Database | Transmitter | Receiver | Secreted | Plasma Membrane (Transmembrane) | Plasma Membrane (Peripheral) |
|---|---|---|---|---|---|---|---|
| transmembrane | transmembrane_predicted | Phobius | No | No | No | No | No |
Page 4 of 4Previous
Regulatory Interaction Network
4 records.
| Source Protein Symbol | Source UniProt ID | Target Protein Symbol | Target UniProt ID | Is Directed | Is Stimulation | Is Inhibition | Database | References |
|---|---|---|---|---|---|---|---|---|
| KAPCA | P17612 | CAC1C | Q13936 | Yes | Yes | Yes | WangPhosphoSite_MIMPMIMPHPRD_MIMPiPTMnetPhosphoPointSIGNORProtMapperHPRDCui2007PhosphoSite_KEAKEACA1HPRD_KEASIGNOR_ProtMapperPhosphoSiteHPRD-phosPhosphoSite_ProtMapper | KEA:8612821HPRD:8664319CA1:2174428HPRD-phos:9247274PhosphoSite:29123182ProtMapper:8612821HPRD:8612821KEA:9247274KEA:8664319SIGNOR:28119464ProtMapper:9247274CA1:10514522ProtMapper:28119464iPTMnet:8612821HPRD-phos:8612821HPRD:9247274CA1:10984483CA1:7621818 |
| SRC | P12931 | CAC1C | Q13936 | Yes | Yes | No | PhosphoSite_MIMPMIMPiPTMnetSIGNORProtMapperCui2007CA1WangPhosphoSitePhosphoSite_ProtMapper | SIGNOR:17942635CA1:12850569PhosphoSite:17942635 |
| DCC | P43146 | CAC1C | Q13936 | Yes | Yes | No | SIGNOR | SIGNOR:12827203 |
| KPCD1 | Q15139 | CAC1C | Q13936 | Yes | Yes | No | PhosphoSite_MIMPMIMPHPRD_MIMPiPTMnetSIGNORProtMapperSIGNOR_ProtMapperPhosphoSitePhosphoSite_ProtMapper | ProtMapper:22100296PhosphoSite:22100296PhosphoSite:22310722PhosphoSite:31759979SIGNOR:22100296 |
Protein Complex Composition
10 records.
| Component Name | Component Gene Symbols | Component UniProt ID | Stoichiometry | Database | Database IDs | References |
|---|---|---|---|---|---|---|
| Cav1.2 voltage-gated calcium channel complexCACNA2D3-CACNB1 variant | CACNA1CCACNA2D3CACNB1 | Q02641Q13936Q8IZS8 | 1:1:2 | ComplexPortal | intact:EBI-50433483 | 340729541511110427481713147552921629951116382099 |
| Cav1.2 voltage-gated calcium channel complexCACNA2D3-CACNB2 variant | CACNA1CCACNA2D3CACNB2 | Q08289Q13936Q8IZS8 | 1:1:2 | ComplexPortal | intact:EBI-50433579 | 340729541511110427481713147552921629951116382099 |
| Cav1.2 voltage-gated calcium channel complexCACNA2D3-CACNB3 variant | CACNA1CCACNA2D3CACNB3 | P54284Q13936Q8IZS8 | 1:1:2 | ComplexPortal | intact:EBI-50433630 | 340729541511110427481713147552921629951116382099 |
| Cav1.2 voltage-gated calcium channel complexCACNA2D3-CACNB4 variant | CACNA1CCACNA2D3CACNB4 | O00305Q13936Q8IZS8 | 1:1:2 | ComplexPortal | intact:EBI-50433684 | 340729541511110427481713147552921629951116382099 |
| Cav1.2 voltage-gated calcium channel complexCACNA2D4-CACNB1 variant | CACNA1CCACNA2D4CACNB1 | Q02641Q13936Q7Z3S7 | 1:1:2 | ComplexPortal | intact:EBI-50433742 | 340729541511110427481713147552921629951116382099 |
| Cav1.2 voltage-gated calcium channel complexCACNA2D4-CACNB2 variant | CACNA1CCACNA2D4CACNB2 | Q08289Q13936Q7Z3S7 | 1:1:2 | ComplexPortal | intact:EBI-50433807 | 340729541511110427481713147552921629951116382099 |
| Cav1.2 voltage-gated calcium channel complexCACNA2D4-CACNB3 variant | CACNA1CCACNA2D4CACNB3 | P54284Q13936Q7Z3S7 | 1:1:2 | ComplexPortal | intact:EBI-50433858 | 340729541511110427481713147552921629951116382099 |
| Cav1.2 voltage-gated calcium channel complexCACNA2D4-CACNB4 variant | CACNA1CCACNA2D4CACNB4 | O00305Q13936Q7Z3S7 | 1:1:2 | ComplexPortal | intact:EBI-50433909 | 340729541511110427481713147552921629951116382099 |
| CACNA1CCACNA1DCACNA1FCACNA1S | O60840Q01668Q13698Q13936 | 0:0:0:0 | KEGG-MEDICUS | |||
| CACNA1CCALM1 | P0DP23Q13936 | 3:3 | PDB | PDB:6u39PDB:2be6PDB:6u3bPDB:6u3dPDB:2lqcPDB:6daePDB:2f3zPDB:6dafPDB:3oxqPDB:2f3yPDB:3g43PDB:6dadPDB:6u3aPDB:7l8v |
Isolation & Detection Technology
0 records.
Sequence, Structure & Domains
Sequences
Length
2,221
Mass
248,977
Sequence
MVNENTRMYIPEENHQGSNYGSPRPAHANMNANAAAGLAPEHIPTPGAALSWQAAIDAARQAKLMGSAGNATISTVSSTQRKRQQYGKPKKQGSTTATRPPRALLCLTLKNPIRRACISIVEWKPFEIIILLTIFANCVALAIYIPFPEDDSNATNSNLERVEYLFLIIFTVEAFLKVIAYGLLFHPNAYLRNGWNLLDFIIVVVGLFSAILEQATKADGANALGGKGAGFDVKALRAFRVLRPLRLVSGVPSLQVVLNSIIKAMVPLLHIALLVLFVIIIYAIIGLELFMGKMHKTCYNQEGIADVPAEDDPSPCALETGHGRQCQNGTVCKPGWDGPKHGITNFDNFAFAMLTVFQCITMEGWTDVLYWVNDAVGRDWPWIYFVTLIIIGSFFVLNLVLGVLSGEFSKEREKAKARGDFQKLREKQQLEEDLKGYLDWITQAEDIDPENEDEGMDEEKPRNMSMPTSETESVNTENVAGGDIEGENCGARLAHRISKSKFSRYWRRWNRFCRRKCRAAVKSNVFYWLVIFLVFLNTLTIASEHYNQPNWLTEVQDTANKALLALFTAEMLLKMYSLGLQAYFVSLFNRFDCFVVCGGILETILVETKIMSPLGISVLRCVRLLRIFKITRYWNSLSNLVASLLNSVRSIASLLLLLFLFIIIFSLLGMQLFGGKFNFDEMQTRRSTFDNFPQSLLTVFQILTGEDWNSVMYDGIMAYGGPSFPGMLVCIYFIILFICGNYILLNVFLAIAVDNLADAESLTSAQKEEEEEKERKKLARTASPEKKQELVEKPAVGESKEEKIELKSITADGESPPATKINMDDLQPNENEDKSPYPNPETTGEEDEEEPEMPVGPRPRPLSELHLKEKAVPMPEASAFFIFSSNNRFRLQCHRIVNDTIFTNLILFFILLSSISLAAEDPVQHTSFRNHILFYFDIVFTTIFTIEIALKILGNADYVFTSIFTLEIILKMTAYGAFLHKGSFCRNYFNILDLLVVSVSLISFGIQSSAINVVKILRVLRVLRPLRAINRAKGLKHVVQCVFVAIRTIGNIVIVTTLLQFMFACIGVQLFKGKLYTCSDSSKQTEAECKGNYITYKDGEVDHPIIQPRSWENSKFDFDNVLAAMMALFTVSTFEGWPELLYRSIDSHTEDKGPIYNYRVEISIFFIIYIIIIAFFMMNIFVGFVIVTFQEQGEQEYKNCELDKNQRQCVEYALKARPLRRYIPKNQHQYKVWYVVNSTYFEYLMFVLILLNTICLAMQHYGQSCLFKIAMNILNMLFTGLFTVEMILKLIAFKPKGYFSDPWNVFDFLIVIGSIIDVILSETNHYFCDAWNTFDALIVVGSIVDIAITEVNPAEHTQCSPSMNAEENSRISITFFRLFRVMRLVKLLSRGEGIRTLLWTFIKSFQALPYVALLIVMLFFIYAVIGMQVFGKIALNDTTEINRNNNFQTFPQAVLLLFRCATGEAWQDIMLACMPGKKCAPESEPSNSTEGETPCGSSFAVFYFISFYMLCAFLIINLFVAVIMDNFDYLTRDWSILGPHHLDEFKRIWAEYDPEAKGRIKHLDVVTLLRRIQPPLGFGKLCPHRVACKRLVSMNMPLNSDGTVMFNATLFALVRTALRIKTEGNLEQANEELRAIIKKIWKRTSMKLLDQVVPPAGDDEVTVGKFYATFLIQEYFRKFKKRKEQGLVGKPSQRNALSLQAGLRTLHDIGPEIRRAISGDLTAEEELDKAMKEAVSAASEDDIFRRAGGLFGNHVSYYQSDGRSAFPQTFTTQRPLHINKAGSSQGDTESPSHEKLVDSTFTPSSYSSTGSNANINNANNTALGRLPRPAGYPSTVSTVEGHGPPLSPAIRVQEVAWKLSSNRERHVPMCEDLELRRDSGSAGTQAHCLLLRKANPSRCHSRESQAAMAGQEETSQDETYEVKMNHDTEACSEPSLLSTEMLSYQDDENRQLTLPEEDKRDIRQSPKRGFLRSASLGRRASFHLECLKRQKDRGGDISQKTVLPLHLVHHQALAVAGLSPLLQRSHSPASFPRPFATPPATPGSRGWPPQPVPTLRLEGVESSEKLNSSFPSIHCGSWAETTPGGGGSSAARRVRPVSLMVPSQAGAPGRQFHGSASSLVEAVLISEGLGQFAQDPKFIEVTTQELADACDMTIEEMESAADNILSGGAPQSPNGALLPFVNCRDAGQDRAGGEEDAGCVRARGRPSEEELQDSRVYVSSL
Alternative Products
Event=Alternative splicing; Named isoforms=37; Comment=Additional isoforms seem to exist. Exons 8A, 21, 22, 31, 32, 33, 40B, 43A, 41A and 45 are alternatively spliced in a variety of combinations. Experimental confirmation may be lacking for some isoforms.; Name=1; Synonyms=HFCC, Fibroblast; IsoId=Q13936-1; Sequence=Displayed; Name=2; IsoId=Q13936-2; Sequence=VSP_000894; Name=3; IsoId=Q13936-3; Sequence=VSP_000886; Name=4; IsoId=Q13936-4; Sequence=VSP_000887; Name=5; IsoId=Q13936-5; Sequence=VSP_000888; Name=6; IsoId=Q13936-6; Sequence=VSP_000889; Name=7; IsoId=Q13936-7; Sequence=VSP_000890; Name=8; IsoId=Q13936-8; Sequence=VSP_000891; Name=9; IsoId=Q13936-9; Sequence=VSP_000892; Name=10; IsoId=Q13936-10; Sequence=VSP_000893; Name=11; Synonyms=Alpha-1C.90; IsoId=Q13936-11; Sequence=VSP_000895; Name=12; Synonyms=Alpha-1C.70; IsoId=Q13936-12; Sequence=VSP_000888, VSP_000889, VSP_000895; Name=13; Synonyms=Alpha-1C.127; IsoId=Q13936-13; Sequence=VSP_000888, VSP_000890, VSP_000893, VSP_000895; Name=14; Synonyms=Alpha-1C.126; IsoId=Q13936-14; Sequence=VSP_000888, VSP_000889, VSP_022504, VSP_000893, VSP_000895; Name=15; Synonyms=Alpha-1C.125; IsoId=Q13936-15; Sequence=VSP_000888, VSP_000889, VSP_022503, VSP_000893, VSP_000895; Name=16; IsoId=Q13936-16; Sequence=VSP_000885, VSP_000886, VSP_000888, VSP_000890; Name=17; IsoId=Q13936-17; Sequence=VSP_000885, VSP_000886, VSP_000888, VSP_000890, VSP_000895; Name=18; Synonyms=HHT-1; IsoId=Q13936-18; Sequence=VSP_000885, VSP_000886, VSP_000888, VSP_000890, VSP_000894; Name=19; Synonyms=Alpha-1C.76; IsoId=Q13936-19; Sequence=VSP_000887, VSP_000889, VSP_000891, VSP_000895; Name=20; Synonyms=Alpha-1C.77; IsoId=Q13936-20; Sequence=VSP_000887, VSP_000889, VSP_000895; Name=21; Synonyms=Alpha-1C.69; IsoId=Q13936-21; Sequence=VSP_000887, VSP_000890, VSP_000895; Name=22; Synonyms=Alpha-1C.78; IsoId=Q13936-22; Sequence=VSP_000888, VSP_000890, VSP_000895; Name=23; Synonyms=Alpha-1C.105; IsoId=Q13936-23; Sequence=VSP_000886, VSP_000887, VSP_000889, VSP_000895; Name=24; Synonyms=Alpha-1C.71; IsoId=Q13936-24; Sequence=VSP_000888, VSP_000889, VSP_000893, VSP_000895; Name=25; Synonyms=Alpha-1C.73; IsoId=Q13936-25; Sequence=VSP_000888, VSP_000889, VSP_000891, VSP_000893, VSP_000895; Name=26; Synonyms=Alpha-1C.86; IsoId=Q13936-26; Sequence=VSP_000887, VSP_000889, VSP_000892, VSP_000895; Name=27; Synonyms=Alpha-1C.72; IsoId=Q13936-27; Sequence=VSP_000887, VSP_000889, VSP_000893, VSP_000895; Name=28; IsoId=Q13936-28; Sequence=VSP_000885, VSP_000886, VSP_000888, VSP_000889, VSP_000891, VSP_000894; Name=29; Synonyms=Alpha-1C.74; IsoId=Q13936-29; Sequence=VSP_000887, VSP_000889, VSP_000891, VSP_000893, VSP_000895; Name=30; Synonyms=Alpha-1C.87; IsoId=Q13936-30; Sequence=VSP_000889, VSP_000895; Name=31; Synonyms=Alpha-1C.88; IsoId=Q13936-31; Sequence=VSP_000888, VSP_000895; Name=32; Synonyms=Alpha-1C.89; IsoId=Q13936-32; Sequence=VSP_000887, VSP_000891, VSP_000895; Name=33; Synonyms=Alpha-1C.85; IsoId=Q13936-33; Sequence=VSP_000887, VSP_000889; Name=34; Synonyms=Alpha-1C,long-NT; IsoId=Q13936-34; Sequence=VSP_035146; Name=35; IsoId=Q13936-35; Sequence=VSP_035877, VSP_000888, VSP_000890, VSP_000895; Name=36; IsoId=Q13936-36; Sequence=VSP_000886, VSP_000888, VSP_000890; Name=37; IsoId=Q13936-37; Sequence=VSP_000886, VSP_000888, VSP_000890, VSP_000895
Alternative Sequence
1..29; Missing (in isoform 16, isoform 17, isoform 18 and isoform 28); 1..16; MVNENTRMYIPEENHQ -> MLRAFVQPGTPAYQPLPSHLSANTEVKFKGTLVHEAQLNYFYISPG (in isoform 34); 306..308; Missing (in isoform 35); 372..391; VNDAVGRDWPWIYFVTLIII -> MQDAMGYELPWVYFVSLVIF (in isoform 3, isoform 16, isoform 17, isoform 18, isoform 23, isoform 28, isoform 36 and isoform 37); 932..951; Missing (in isoform 4, isoform 19, isoform 20, isoform 21, isoform 23, isoform 26, isoform 27, isoform 29, isoform 32 and isoform 33); 952..971; Missing (in isoform 5, isoform 12, isoform 13, isoform 14, isoform 15, isoform 16, isoform 17, isoform 18, isoform 22, isoform 24, isoform 25, isoform 28, isoform 31, isoform 35, isoform 36 and isoform 37); 1297..1324; Missing (in isoform 6, isoform 12, isoform 14, isoform 15, isoform 19, isoform 20, isoform 23, isoform 24, isoform 25, isoform 26, isoform 27, isoform 28, isoform 29, isoform 30 and isoform 33); 1325..1352; Missing (in isoform 7, isoform 13, isoform 16, isoform 17, isoform 18, isoform 21, isoform 22, isoform 35, isoform 36 and isoform 37); 1351..1363; Missing (in isoform 15); 1353..1363; Missing (in isoform 8, isoform 19, isoform 25, isoform 28, isoform 29 and isoform 32); 1363; M -> MGPSCSHPPLAVLTAPPVADGFQ (in isoform 14); 1618..1699; LRIKTEGNLEQANEELRAIIKKIWKRTSMKLLDQVVPPAGDDEVTVGKFYATFLIQEYFRKFKKRKEQGLVGKPSQRNALSL -> LREAELSSQVQYQAKEASLLERRRKSSHPKSSTKPNKLLSSGGSTGWVEDARALEGQVLARGCGWLGSLEERERGPHHPPLGF (in isoform 9 and isoform 26); 1623; E -> EEGPSPSEAHQGAEDPFRPA (in isoform 10, isoform 13, isoform 14, isoform 15, isoform 24, isoform 25, isoform 27 and isoform 29); 1864..1898; Missing (in isoform 11, isoform 12, isoform 13, isoform 14, isoform 15, isoform 17, isoform 19, isoform 20, isoform 21, isoform 22, isoform 23, isoform 24, isoform 25, isoform 26, isoform 27, isoform 29, isoform 30, isoform 31, isoform 32, isoform 35 and isoform 37); 1864..1897; ERHVPMCEDLELRRDSGSAGTQAHCLLLRKANPS -> MHCCDMLDGGTFPPALGPRRAPPCLHQQLQGSLAGLREDTPCIVPGHASLCCSSRVGEWLPAGCTAPQHA (in isoform 2, isoform 18 and isoform 28)
3D Structural Models
Turn
119..122; 339..342; 444..446; 510..513; 580..585; 674..676; 705..707; 728..730; 777..782; 977..981; 1010..1012; 1029..1031; 1033..1036; 1049..1051; 1072..1074; 1149..1151; 1173..1175; 1481..1483; 1574..1576; 1654..1656
Helix
48..65; 113..116; 126..142; 148..150; 154..181; 194..216; 233..236; 237..242; 245..250; 252..262; 266..268; 269..289; 351..360; 365..375; 382..392; 395..418; 429..443; 514..521; 528..541; 552..576; 587..607; 612..614; 617..630; 635..646; 648..673; 692..704; 708..718; 724..727; 731..747; 749..776; 891..897; 900..902; 903..913; 915..918; 929..933; 954..974; 990..1006; 1014..1017; 1020..1023; 1025..1028; 1037..1048; 1052..1071; 1086..1088; 1097..1099; 1121..1132; 1137..1145; 1160..1162; 1163..1172; 1176..1194; 1206..1214; 1228..1236; 1239..1255; 1256..1259; 1265..1300; 1302..1321; 1330..1348; 1374..1376; 1377..1382; 1383..1388; 1394..1407; 1411..1430; 1450..1461; 1466..1471; 1500..1524; 1527..1530; 1534..1537; 1539..1550; 1562..1566; 1569..1571; 1586..1593; 1609..1651; 1659..1661; 1666..1680; 1973..1975
Beta Strand
185..187; 290..292; 296..298; 301..304; 305..307; 309..311; 315..317; 321..323; 327..329; 332..334; 344..348; 378..381; 523..525; 609..611; 680..683; 689..691; 720..723; 925..928; 1077..1080; 1091..1096; 1103..1108; 1111..1113; 1133..1136; 1156..1158; 1195..1198; 1200..1202; 1439..1445; 1447..1449; 1474..1477; 1489..1491; 1554..1557; 1558..1560; 1579..1581; 1583..1585; 1597..1599; 1601..1603
3D Structure
Electron microscopy (12); NMR spectroscopy (3); X-ray crystallography (17)
Domain & Motif Annotations
Compositional Bias
80..91; Basic residues; 465..478; Polar residues; 783..792; Basic and acidic residues; 843..852; Acidic residues; 1799..1811; Polar residues; 1812..1822; Low complexity
Repeat
111..408; I; 510..756; II; 887..1189; III; 1226..1527; IV
Motif
361..364; Selectivity filter of repeat I; 704..707; Selectivity filter of repeat II; 1133..1136; Selectivity filter of repeat III; 1462..1465; Selectivity filter of repeat IV
Domain (CC)
Each of the four internal repeats contains five hydrophobic transmembrane segments (S1, S2, S3, S5, S6) and one positively charged transmembrane segment (S4). S4 segments probably represent the voltage-sensor and are characterized by a series of positively charged amino acids at every third position.; DOMAIN: Binding of intracellular calcium through the EF-hand motif inhibits the opening of the channel.
Region
1..20; Disordered; 47..68; Calmodulin-binding; 73..98; Disordered; 428..445; AID/alpha-interaction domain; mediates interaction with the beta subunit; 449..481; Disordered; 764..861; Disordered; 829..876; Interaction with STAC2; 1109..1198; Dihydropyridine binding; 1478..1546; Dihydropyridine binding; 1492..1534; Phenylalkylamine binding; 1659..1686; Important for interaction with STAC1, STAC2 and STAC3; 1665..1685; Calmodulin-binding IQ region; 1699..1718; Important for localization in at the junctional membrane; 1778..1847; Disordered; 2029..2063; Disordered; 2186..2221; Disordered
Protein Families
- Calcium channel alpha-1 subunit (TC 1.A.1.11) family
- CACNA1C subfamily
Sequence Similarities
Belongs to the calcium channel alpha-1 subunit (TC 1.A.1.11) family. CACNA1C subfamily.
Clinical Relevance
Disease Involvement
AutismAutism spectrum disorderBrugada syndromeDisease variantEpilepsyFDA approved drug targetsIntellectual disabilityLong QT syndrome
Related Diseases
Biomarker
Phase 3; Terminated; Investigative
Drug Targets
FDA approved drug targets
Drugs
AMLODIPINE BESYLATEAZD1305CELECOXIBPHLOROGLUCINOLCLEVIDIPINEFELODIPINEGABAPENTIN ENACARBILSULOCTIDILNITRENDIPINEARVERAPAMILDEHYDRATED ALCOHOLNILVADIPINEBENIDIPINEDRONEDARONE HYDROCHLORIDEIBUTILIDENIMODIPINEPREGABALINCALCIUM CHANNEL BLOCKERIMAGABALINNULLATENOLOLBEPRIDIL HYDROCHLORIDEATAGABALINVERAPAMILLERCANIDIPINE HYDROCHLORIDEAZELNIDIPINEDILTIAZEM MALATEDILTIAZEM HYDROCHLORIDENISOLDIPINEVALPROIC ACIDCINNARIZINETERODILINE HYDROCHLORIDENICARDIPINEISRADIPINENICARDIPINE HYDROCHLORIDEMEPIRODIPINELACIDIPINENIFEDIPINEMANIDIPINEAMLODIPINE MALEATEELPETRIGINELEVAMLODIPINE MALEATEGABAPENTINHALOPERIDOL DECANOATECILNIDIPINEAMLODIPINE BENZOATECITALOPRAMRAUWOLFIA SERPENTINA (USP)
Interaction Protein
ENSG00000072110ENSG00000100151ENSG00000157782
Interaction Count
3
Interaction Dataset
intact_biogrid