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Reviewed, UniProtKB/Swiss-Prot Q13936 (CAC1C_HUMAN)

Last modified February 9, 2010. Version 122. Feed History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Voltage-dependent L-type calcium channel subunit alpha-1C
Alternative name(s):
    Voltage-gated calcium channel subunit alpha Cav1.2
    Calcium channel, L type, alpha-1 polypeptide, isoform 1, cardiac muscle
Gene names
Name: CACNA1C
Synonyms: CACH2, CACN2, CACNL1A1, CCHL1A1
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length2221 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

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General annotation (Comments)

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-1C 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). Calcium channels containing the alpha-1C subunit play an important role in excitation-contraction coupling in the heart. The various isoforms display marked differences in the sensitivity to DHP compounds. Binding of calmodulin or CABP1 at the same regulatory sites results in an opposit effects on the channel function. Ref.2 Ref.4 Ref.6 Ref.7 Ref.8 Ref.9

Subunit structure

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. Interacts with CACNA2D4. Interacts (via the N-terminus and the C-terminal C and IQ motifs) with CABP1. The binding via the C motif is calcium independent whereas the binding via IQ requires the presence of calcium and is mutually exclusive with calmodulin binding. The binding to the cytoplasmic N-terminal domain is calcium independent but is essential for the channel modulation. Interacts (via C-terminal CDB motif) with CABP5; in a calcium-dependent manner By similarity. Ref.18 Ref.19 Ref.20

Subcellular location

Membrane; Multi-pass membrane protein. Cell membrane By similarity. Note: The interaction between RRAD and CACNB2 regulates its trafficking to the cell membrane By similarity.

Tissue specificity

Expressed in brain, heart, jejunum, ovary, pancreatic beta-cells and vascular smooth muscle. Overall expression is reduced in atherosclerotic vascular smooth muscle. Ref.2 Ref.8 Ref.9

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.

Binding of intracellular calcium through the EF-hand motif inhibits the opening of the channel By similarity.

Post-translational modification

Phosphorylation by PKA activates the channel By similarity.

Involvement in disease

Defects in CACNA1C are the cause of Timothy syndrome (TS) [MIM:601005]. TS is a disorder characterized by multiorgan dysfunction including lethal arrhythmias, webbing of fingers and toes, congenital heart disease, immune deficiency, intermittent hypoglycemia, cognitive abnormalities and autism. Ref.22 Ref.23

Defects in CACNA1C are the cause of Brugada syndrome type 3 (BRS3) [MIM:611875]. BRS3 is a heart disease characterized by the association of Brugada syndrome with shortened QT intervals. Brugada syndrome is a tachyarrhythmia characterized by right bundle branch block and ST segment elevation on an electrocardiogram (ECG). It can cause the ventricles to beat so fast that the blood is prevented from circulating efficiently in the body. When this situation occurs (called ventricular fibrillation), the individual will faint and may die in a few minutes if the heart is not reset. Ref.24

Sequence similarities

Belongs to the calcium channel alpha-1 subunit (TC 1.A.1.11) family. [View classification]

Sequence caution

The sequence AAA02500.2 differs from that shown. Reason: Frameshift at position 1845.

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Binary interactions

With

Entry

#Exp.

IntAct

Notes

CABP1Q9NZU72EBI-1038838,EBI-907894
CALM1P621581EBI-1038838,EBI-397435

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Alternative products

This entry describes 35 isoforms produced by alternative splicing. [Align] [Select]

Note: 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.
Isoform 1 (identifier: Q13936-1)

Also known as: HFCC; Fibroblast;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q13936-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1864-1897: ERHVPMCEDLELRRDSGSAGTQAHCLLLRKANPS → MHCCDMLDGG...PAGCTAPQHA
Isoform 3 (identifier: Q13936-3)

The sequence of this isoform differs from the canonical sequence as follows:
     372-391: VNDAVGRDWPWIYFVTLIII → MQDAMGYELPWVYFVSLVIF
Note: Contains exon 8a.
Isoform 4 (identifier: Q13936-4)

The sequence of this isoform differs from the canonical sequence as follows:
     932-951: Missing.
Note: Lacks exon 21.
Isoform 5 (identifier: Q13936-5)

The sequence of this isoform differs from the canonical sequence as follows:
     952-971: Missing.
Note: Lacks exon 22.
Isoform 6 (identifier: Q13936-6)

The sequence of this isoform differs from the canonical sequence as follows:
     1297-1324: Missing.
Note: Lacks exon 31.
Isoform 7 (identifier: Q13936-7)

The sequence of this isoform differs from the canonical sequence as follows:
     1325-1352: Missing.
Note: Lacks exon 32.
Isoform 8 (identifier: Q13936-8)

The sequence of this isoform differs from the canonical sequence as follows:
     1353-1363: Missing.
Note: Lacks exon 33.
Isoform 9 (identifier: Q13936-9)

The sequence of this isoform differs from the canonical sequence as follows:
     1618-1699: LRIKTEGNLE...KPSQRNALSL → LRETELSSQV...RGPHHPPLGF
Note: Contains exon 40B and 43A.
Isoform 10 (identifier: Q13936-10)

The sequence of this isoform differs from the canonical sequence as follows:
     1623-1623: E → EEGPSPSEAHQGAEDPFRPA
Note: Contains exon 41A.
Isoform 11 (identifier: Q13936-11)

Also known as: Alpha-1C.90;

The sequence of this isoform differs from the canonical sequence as follows:
     1864-1898: Missing.
Note: Lacks exon 45.
Isoform 12 (identifier: Q13936-12)

Also known as: Alpha-1C.70;

The sequence of this isoform differs from the canonical sequence as follows:
     952-971: Missing.
     1297-1324: Missing.
     1864-1898: Missing.
Isoform 13 (identifier: Q13936-13)

Also known as: Alpha-1C.127;

The sequence of this isoform differs from the canonical sequence as follows:
     952-971: Missing.
     1325-1352: Missing.
     1623-1623: E → EEGPSPSEAHQGAEDPFRPA
     1864-1898: Missing.
Isoform 14 (identifier: Q13936-14)

Also known as: Alpha-1C.126;

The sequence of this isoform differs from the canonical sequence as follows:
     952-971: Missing.
     1297-1324: Missing.
     1363-1363: M → MGPSCSHPPLAVLTAPPVADGFQ
     1623-1623: E → EEGPSPSEAHQGAEDPFRPA
     1864-1898: Missing.
Isoform 15 (identifier: Q13936-15)

Also known as: Alpha-1C.125;

The sequence of this isoform differs from the canonical sequence as follows:
     952-971: Missing.
     1297-1324: Missing.
     1351-1363: Missing.
     1623-1623: E → EEGPSPSEAHQGAEDPFRPA
     1864-1898: Missing.
Isoform 16 (identifier: Q13936-16)

The sequence of this isoform differs from the canonical sequence as follows:
     1-29: Missing.
     372-391: VNDAVGRDWPWIYFVTLIII → MQDAMGYELPWVYFVSLVIF
     952-971: Missing.
     1325-1352: Missing.
Isoform 17 (identifier: Q13936-17)

The sequence of this isoform differs from the canonical sequence as follows:
     1-29: Missing.
     372-391: VNDAVGRDWPWIYFVTLIII → MQDAMGYELPWVYFVSLVIF
     952-971: Missing.
     1325-1352: Missing.
     1864-1898: Missing.
Isoform 18 (identifier: Q13936-18)

Also known as: HHT-1;

The sequence of this isoform differs from the canonical sequence as follows:
     1-29: Missing.
     372-391: VNDAVGRDWPWIYFVTLIII → MQDAMGYELPWVYFVSLVIF
     952-971: Missing.
     1325-1352: Missing.
     1864-1897: ERHVPMCEDLELRRDSGSAGTQAHCLLLRKANPS → MHCCDMLDGG...PAGCTAPQHA
Isoform 19 (identifier: Q13936-19)

Also known as: Alpha-1C.76;

The sequence of this isoform differs from the canonical sequence as follows:
     932-951: Missing.
     1297-1324: Missing.
     1353-1363: Missing.
     1864-1898: Missing.
Isoform 20 (identifier: Q13936-20)

Also known as: Alpha-1C.77;

The sequence of this isoform differs from the canonical sequence as follows:
     932-951: Missing.
     1297-1324: Missing.
     1864-1898: Missing.
Note: Predominant isoform in atherosclerotic vascular smooth muscle cells.
Isoform 21 (identifier: Q13936-21)

Also known as: Alpha-1C.69;

The sequence of this isoform differs from the canonical sequence as follows:
     932-951: Missing.
     1325-1352: Missing.
     1864-1898: Missing.
Isoform 22 (identifier: Q13936-22)

Also known as: Alpha-1C.78;

The sequence of this isoform differs from the canonical sequence as follows:
     952-971: Missing.
     1325-1352: Missing.
     1864-1898: Missing.
Isoform 23 (identifier: Q13936-23)

Also known as: Alpha-1C.105;

The sequence of this isoform differs from the canonical sequence as follows:
     372-391: VNDAVGRDWPWIYFVTLIII → MQDAMGYELPWVYFVSLVIF
     932-951: Missing.
     1297-1324: Missing.
     1864-1898: Missing.
Isoform 24 (identifier: Q13936-24)

Also known as: Alpha-1C.71;

The sequence of this isoform differs from the canonical sequence as follows:
     952-971: Missing.
     1297-1324: Missing.
     1623-1623: E → EEGPSPSEAHQGAEDPFRPA
     1864-1898: Missing.
Isoform 25 (identifier: Q13936-25)

Also known as: Alpha-1C.73;

The sequence of this isoform differs from the canonical sequence as follows:
     952-971: Missing.
     1297-1324: Missing.
     1353-1363: Missing.
     1623-1623: E → EEGPSPSEAHQGAEDPFRPA
     1864-1898: Missing.
Isoform 26 (identifier: Q13936-26)

Also known as: Alpha-1C.86;

The sequence of this isoform differs from the canonical sequence as follows:
     932-951: Missing.
     1297-1324: Missing.
     1618-1699: LRIKTEGNLE...KPSQRNALSL → LRETELSSQV...RGPHHPPLGF
     1864-1898: Missing.
Note: Not inhibited by calcium.
Isoform 27 (identifier: Q13936-27)

Also known as: Alpha-1C.72;

The sequence of this isoform differs from the canonical sequence as follows:
     932-951: Missing.
     1297-1324: Missing.
     1623-1623: E → EEGPSPSEAHQGAEDPFRPA
     1864-1898: Missing.
Isoform 28 (identifier: Q13936-28)

The sequence of this isoform differs from the canonical sequence as follows:
     1-29: Missing.
     372-391: VNDAVGRDWPWIYFVTLIII → MQDAMGYELPWVYFVSLVIF
     952-971: Missing.
     1297-1324: Missing.
     1353-1363: Missing.
     1864-1897: ERHVPMCEDLELRRDSGSAGTQAHCLLLRKANPS → MHCCDMLDGG...PAGCTAPQHA
Isoform 29 (identifier: Q13936-29)

Also known as: Alpha-1C.74;

The sequence of this isoform differs from the canonical sequence as follows:
     932-951: Missing.
     1297-1324: Missing.
     1353-1363: Missing.
     1623-1623: E → EEGPSPSEAHQGAEDPFRPA
     1864-1898: Missing.
Isoform 30 (identifier: Q13936-30)

Also known as: Alpha-1C.87;

The sequence of this isoform differs from the canonical sequence as follows:
     1297-1324: Missing.
     1864-1898: Missing.
Isoform 31 (identifier: Q13936-31)

Also known as: Alpha-1C.88;

The sequence of this isoform differs from the canonical sequence as follows:
     952-971: Missing.
     1864-1898: Missing.
Isoform 32 (identifier: Q13936-32)

Also known as: Alpha-1C.89;

The sequence of this isoform differs from the canonical sequence as follows:
     932-951: Missing.
     1353-1363: Missing.
     1864-1898: Missing.
Isoform 33 (identifier: Q13936-33)

Also known as: Alpha-1C.85;

The sequence of this isoform differs from the canonical sequence as follows:
     932-951: Missing.
     1297-1324: Missing.
Isoform 34 (identifier: Q13936-34)

Also known as: Alpha-1C,long-NT;

The sequence of this isoform differs from the canonical sequence as follows:
     1-16: MVNENTRMYIPEENHQ → MLRAFVQPGTPAYQPLPSHLSANTEVKFKGTLVHEAQLNYFYISPG
Note: Enhanced by PKC activator.
Isoform 35 (identifier: Q13936-35)

The sequence of this isoform differs from the canonical sequence as follows:
     306-308: Missing.
     952-971: Missing.
     1325-1352: Missing.
     1864-1898: Missing.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 22212221Voltage-dependent L-type calcium channel subunit alpha-1C
PRO_0000053928

Regions

Topological domain1 – 124124Cytoplasmic Potential
Transmembrane125 – 14319S1 of repeat I Potential
Topological domain144 – 16017Extracellular Potential
Transmembrane161 – 18121S2 of repeat I Potential
Topological domain182 – 19312Cytoplasmic Potential
Transmembrane194 – 21219S3 of repeat I Potential
Topological domain213 – 23220Extracellular Potential
Transmembrane233 – 25119S4 of repeat I Potential
Topological domain252 – 27019Cytoplasmic Potential
Transmembrane271 – 29020S5 of repeat I Potential
Topological domain291 – 38090Extracellular Potential
Transmembrane381 – 40525S6 of repeat I Potential
Topological domain406 – 524119Cytoplasmic Potential
Transmembrane525 – 54319S1 of repeat II Potential
Topological domain544 – 55815Extracellular Potential
Transmembrane559 – 57820S2 of repeat II Potential
Topological domain579 – 5868Cytoplasmic Potential
Transmembrane587 – 60519S3 of repeat II Potential
Topological domain606 – 61510Extracellular Potential
Transmembrane616 – 63419S4 of repeat II Potential
Topological domain635 – 65319Cytoplasmic Potential
Transmembrane654 – 67320S5 of repeat II Potential
Topological domain674 – 72855Extracellular Potential
Transmembrane729 – 75325S6 of repeat II Potential
Topological domain754 – 900147Cytoplasmic Potential
Transmembrane901 – 91919S1 of repeat III Potential
Topological domain920 – 93516Extracellular Potential
Transmembrane936 – 95520S2 of repeat III Potential
Topological domain956 – 98732Cytoplasmic Potential
Transmembrane988 – 100619S3 of repeat III Potential
Topological domain1007 – 10137Extracellular Potential
Transmembrane1014 – 103219S4 of repeat III Potential
Topological domain1033 – 105119Cytoplasmic Potential
Transmembrane1052 – 107120S5 of repeat III Potential
Topological domain1072 – 116190Extracellular Potential
Transmembrane1162 – 118625S6 of repeat III Potential
Topological domain1187 – 123953Cytoplasmic Potential
Transmembrane1240 – 125819S1 of repeat IV Potential
Topological domain1259 – 127315Extracellular Potential
Transmembrane1274 – 129320S2 of repeat IV Potential
Topological domain1294 – 13018Cytoplasmic Potential
Transmembrane1302 – 132019S3 of repeat IV Potential
Topological domain1321 – 137252Extracellular Potential
Transmembrane1373 – 139119S4 of repeat IV Potential
Topological domain1392 – 141019Cytoplasmic Potential
Transmembrane1411 – 143020S5 of repeat IV Potential
Topological domain1431 – 149969Extracellular Potential
Transmembrane1500 – 152425S6 of repeat IV Potential
Topological domain1525 – 2221697Cytoplasmic Potential
Repeat111 – 408298I
Repeat510 – 756247II
Repeat887 – 1189303III
Repeat1226 – 1527302IV
Calcium binding1553 – 156412 By similarity
Region428 – 44518Binding to the beta subunit By similarity
Region1109 – 119991Dihydropyridine binding By similarity
Region1478 – 154669Dihydropyridine binding By similarity
Region1492 – 153544Phenylalkylamine binding By similarity
Compositional bias654 – 6607Poly-Leu
Compositional bias768 – 7747Poly-Glu
Compositional bias1167 – 11737Poly-Ile
Compositional bias2084 – 20874Poly-Gly

Sites

Site3631Calcium ion selectivity and permeability
Site7061Calcium ion selectivity and permeability
Site11351Calcium ion selectivity and permeability
Site14641Calcium ion selectivity and permeability

Amino acid modifications

Modified residue8151Phosphoserine By similarity
Modified residue15351Phosphoserine; by PKA Potential
Modified residue19731Phosphoserine; by PKA Potential
Modified residue19811Phosphoserine; by PKA Potential
Glycosylation1531N-linked (GlcNAc...) Potential
Glycosylation3281N-linked (GlcNAc...) Potential
Glycosylation14361N-linked (GlcNAc...) Potential
Glycosylation14871N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence1 – 2929Missing in isoform 16, isoform 17, isoform 18 and isoform 28.
VSP_000885
Alternative sequence1 – 1616MVNEN…EENHQ → MLRAFVQPGTPAYQPLPSHL SANTEVKFKGTLVHEAQLNY FYISPG in isoform 34.
VSP_035146
Alternative sequence306 – 3083Missing in isoform 35.
VSP_035877
Alternative sequence372 – 39120VNDAV…TLIII → MQDAMGYELPWVYFVSLVIF in isoform 3, isoform 16, isoform 17, isoform 18, isoform 23 and isoform 28.
VSP_000886
Alternative sequence932 – 95120Missing in isoform 4, isoform 19, isoform 20, isoform 21, isoform 23, isoform 26, isoform 27, isoform 29, isoform 32 and isoform 33.
VSP_000887
Alternative sequence952 – 97120Missing 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 and isoform 35.
VSP_000888
Alternative sequence1297 – 132428Missing 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.
VSP_000889
Alternative sequence1325 – 135228Missing in isoform 7, isoform 13, isoform 16, isoform 17, isoform 18, isoform 21, isoform 22 and isoform 35.
VSP_000890
Alternative sequence1351 – 136313Missing in isoform 15.
VSP_022503
Alternative sequence1353 – 136311Missing in isoform 8, isoform 19, isoform 25, isoform 28, isoform 29 and isoform 32.
VSP_000891
Alternative sequence13631M → MGPSCSHPPLAVLTAPPVAD GFQ in isoform 14.
VSP_022504
Alternative sequence1618 – 169982LRIKT…NALSL → LRETELSSQVQYQAKEASLL ERRRKSSHPKSSTKPNKLLS SGGSTGWVEDARALEGQVLA RGCGWLGSLEERERGPHHPP LGF in isoform 9 and isoform 26.
VSP_000892
Alternative sequence16231E → EEGPSPSEAHQGAEDPFRPA in isoform 10, isoform 13, isoform 14, isoform 15, isoform 24, isoform 25, isoform 27 and isoform 29.
VSP_000893
Alternative sequence1864 – 189835Missing 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 and isoform 35.
VSP_000895
Alternative sequence1864 – 189734ERHVP…KANPS → MHCCDMLDGGTFPPALGPRR APPCLHQQLQGSLAGLREDT PCIVPGHASLCCSSRVGEWL PAGCTAPQHA in isoform 2, isoform 18 and isoform 28.
VSP_000894
Natural variant391A → V in BRS3; loss of function. Ref.24
VAR_044039
Natural variant841Q → R: dbSNP rs1051345. Ref.2 Ref.5 Ref.10
VAR_045987
Natural variant3911I → L: dbSNP rs1051356.
VAR_045988
Natural variant4021G → S in TS. Ref.23
VAR_026741
Natural variant4061G → R in TS; causes a nearly complete loss of voltage-dependent channel inactivation. Ref.22
VAR_026742
Natural variant4901G → R in BRS3; loss of function. Ref.24
VAR_044040
Natural variant7521A → T
VAR_001495
Natural variant18681P → L: dbSNP rs10848683.
VAR_059223
Natural variant18691M → V: dbSNP rs10774053. Ref.5 Ref.10 Ref.1
VAR_059224
Natural variant18931K → R: dbSNP rs10774054. Ref.5 Ref.10 Ref.1
VAR_061102
Natural variant21691A → T
VAR_001496

Experimental info

Mutagenesis3631E → K: Loss of selectivity for divalent over monovalent cations.
Mutagenesis9541G → F: Affects voltage-dependent inhibition by dihydropyridines; when associated with I-958. Ref.4
Mutagenesis9581Y → I: Affects voltage-dependent inhibition by dihydropyridines; when associated with F-954. Ref.4
Mutagenesis11351E → K: Loss of selectivity for divalent over monovalent cations.
Mutagenesis14641E → K: Loss of selectivity for divalent over monovalent cations.
Sequence conflict11571N → K in AAA58409. Ref.15
Sequence conflict12441L → P in AAA74590. Ref.16
Sequence conflict13841L → P in AAA74590. Ref.16
Sequence conflict14591R → K in CAA81219. Ref.3
Sequence conflict22051A → G in AAA17030. Ref.1
Sequence conflict22051A → R in AAA02501. Ref.2
Sequence conflict22051A → R in AAA51900. Ref.5
Sequence conflict22051A → R in AAA51901. Ref.5
Sequence conflict22051A → R in AAM70049. Ref.8
Sequence conflict22051A → R in AAA51899. Ref.10
Sequence conflict22051A → R in AC007618. Ref.11

Secondary structure

1 ...... 2221
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (HFCC) (Fibroblast) [UniParc].

Last modified November 25, 2008. Version 3.
Checksum: 61AFCF7AF4C86769

FASTA2,221248,892
        10         20         30         40         50         60 
MVNENTRMYI PEENHQGSNY GSPRPAHANM NANAAAGLAP EHIPTPGAAL SWQAAIDAAR 

        70         80         90        100        110        120 
QAKLMGSAGN ATISTVSSTQ RKRQQYGKPK KQGSTTATRP PRALLCLTLK NPIRRACISI 

       130        140        150        160        170        180 
VEWKPFEIII LLTIFANCVA LAIYIPFPED DSNATNSNLE RVEYLFLIIF TVEAFLKVIA 

       190        200        210        220        230        240 
YGLLFHPNAY LRNGWNLLDF IIVVVGLFSA ILEQATKADG ANALGGKGAG FDVKALRAFR 

       250        260        270        280        290        300 
VLRPLRLVSG VPSLQVVLNS IIKAMVPLLH IALLVLFVII IYAIIGLELF MGKMHKTCYN 

       310        320        330        340        350        360 
QEGIADVPAE DDPSPCALET GHGRQCQNGT VCKPGWDGPK HGITNFDNFA FAMLTVFQCI 

       370        380        390        400        410        420 
TMEGWTDVLY WVNDAVGRDW PWIYFVTLII IGSFFVLNLV LGVLSGEFSK EREKAKARGD 

       430        440        450        460        470        480 
FQKLREKQQL EEDLKGYLDW ITQAEDIDPE NEDEGMDEEK PRNMSMPTSE TESVNTENVA 

       490        500        510        520        530        540 
GGDIEGENCG ARLAHRISKS KFSRYWRRWN RFCRRKCRAA VKSNVFYWLV IFLVFLNTLT 

       550        560        570        580        590        600 
IASEHYNQPN WLTEVQDTAN KALLALFTAE MLLKMYSLGL QAYFVSLFNR FDCFVVCGGI 

       610        620        630        640        650        660 
LETILVETKI MSPLGISVLR CVRLLRIFKI TRYWNSLSNL VASLLNSVRS IASLLLLLFL 

       670        680        690        700        710        720 
FIIIFSLLGM QLFGGKFNFD EMQTRRSTFD NFPQSLLTVF QILTGEDWNS VMYDGIMAYG 

       730        740        750        760        770        780 
GPSFPGMLVC IYFIILFICG NYILLNVFLA IAVDNLADAE SLTSAQKEEE EEKERKKLAR 

       790        800        810        820        830        840 
TASPEKKQEL VEKPAVGESK EEKIELKSIT ADGESPPATK INMDDLQPNE NEDKSPYPNP 

       850        860        870        880        890        900 
ETTGEEDEEE PEMPVGPRPR PLSELHLKEK AVPMPEASAF FIFSSNNRFR LQCHRIVNDT 

       910        920        930        940        950        960 
IFTNLILFFI LLSSISLAAE DPVQHTSFRN HILFYFDIVF TTIFTIEIAL KILGNADYVF 

       970        980        990       1000       1010       1020 
TSIFTLEIIL KMTAYGAFLH KGSFCRNYFN ILDLLVVSVS LISFGIQSSA INVVKILRVL 

      1030       1040       1050       1060       1070       1080 
RVLRPLRAIN RAKGLKHVVQ CVFVAIRTIG NIVIVTTLLQ FMFACIGVQL FKGKLYTCSD 

      1090       1100       1110       1120       1130       1140 
SSKQTEAECK GNYITYKDGE VDHPIIQPRS WENSKFDFDN VLAAMMALFT VSTFEGWPEL 

      1150       1160       1170       1180       1190       1200 
LYRSIDSHTE DKGPIYNYRV EISIFFIIYI IIIAFFMMNI FVGFVIVTFQ EQGEQEYKNC 

      1210       1220       1230       1240       1250       1260 
ELDKNQRQCV EYALKARPLR RYIPKNQHQY KVWYVVNSTY FEYLMFVLIL LNTICLAMQH 

      1270       1280       1290       1300       1310       1320 
YGQSCLFKIA MNILNMLFTG LFTVEMILKL IAFKPKGYFS DPWNVFDFLI VIGSIIDVIL 

      1330       1340       1350       1360       1370       1380 
SETNHYFCDA WNTFDALIVV GSIVDIAITE VNPAEHTQCS PSMNAEENSR ISITFFRLFR 

      1390       1400       1410       1420       1430       1440 
VMRLVKLLSR GEGIRTLLWT FIKSFQALPY VALLIVMLFF IYAVIGMQVF GKIALNDTTE 

      1450       1460       1470       1480       1490       1500 
INRNNNFQTF PQAVLLLFRC ATGEAWQDIM LACMPGKKCA PESEPSNSTE GETPCGSSFA 

      1510       1520       1530       1540       1550       1560 
VFYFISFYML CAFLIINLFV AVIMDNFDYL TRDWSILGPH HLDEFKRIWA EYDPEAKGRI 

      1570       1580       1590       1600       1610       1620 
KHLDVVTLLR RIQPPLGFGK LCPHRVACKR LVSMNMPLNS DGTVMFNATL FALVRTALRI 

      1630       1640       1650       1660       1670       1680 
KTEGNLEQAN EELRAIIKKI WKRTSMKLLD QVVPPAGDDE VTVGKFYATF LIQEYFRKFK 

      1690       1700       1710       1720       1730       1740 
KRKEQGLVGK PSQRNALSLQ AGLRTLHDIG PEIRRAISGD LTAEEELDKA MKEAVSAASE 

      1750       1760       1770       1780       1790       1800 
DDIFRRAGGL FGNHVSYYQS DGRSAFPQTF TTQRPLHINK AGSSQGDTES PSHEKLVDST 

      1810       1820       1830       1840       1850       1860 
FTPSSYSSTG SNANINNANN TALGRLPRPA GYPSTVSTVE GHGPPLSPAI RVQEVAWKLS 

      1870       1880       1890       1900       1910       1920 
SNRERHVPMC EDLELRRDSG SAGTQAHCLL LRKANPSRCH SRESQAAMAG QEETSQDETY 

      1930       1940       1950       1960       1970       1980 
EVKMNHDTEA CSEPSLLSTE MLSYQDDENR QLTLPEEDKR DIRQSPKRGF LRSASLGRRA 

      1990       2000       2010       2020       2030       2040 
SFHLECLKRQ KDRGGDISQK TVLPLHLVHH QALAVAGLSP LLQRSHSPAS FPRPFATPPA 

      2050       2060       2070       2080       2090       2100 
TPGSRGWPPQ PVPTLRLEGV ESSEKLNSSF PSIHCGSWAE TTPGGGGSSA ARRVRPVSLM 

      2110       2120       2130       2140       2150       2160 
VPSQAGAPGR QFHGSASSLV EAVLISEGLG QFAQDPKFIE VTTQELADAC DMTIEEMESA 

      2170       2180       2190       2200       2210       2220 
ADNILSGGAP QSPNGALLPF VNCRDAGQDR AGGEEDAGCV RARGAPSEEE LQDSRVYVSS 


L

« Hide

Isoform 2.

Checksum: C0BCB40B243CFD41
Show »

FASTA2,257252,422
Isoform 3.

Checksum: A14D8E1A74A4F9AF
Show »

FASTA2,221248,910
Isoform 4.

Checksum: F6EA78FDB611A310
Show »

FASTA2,201246,502
Isoform 5.

Checksum: 56CFB4D070A5EF23
Show »

FASTA2,201246,639
Isoform 6.

Checksum: 69BB718AB73EB11D
Show »

FASTA2,193245,735
Isoform 7.

Checksum: 21AE64FE1EFDC425
Show »

FASTA2,193245,783
Isoform 8.

Checksum: CB572FDEFBEDF3DC
Show »

FASTA2,210247,722
Isoform 9.

Checksum: 66B452787D807261
Show »

FASTA2,222248,552
Isoform 10.

Checksum: F78D8E4C44FB3786
Show »

FASTA2,240250,853
Isoform 11 (Alpha-1C.90).

Checksum: F70378F0FFDC1A4D
Show »

FASTA2,186244,962
Isoform 12 (Alpha-1C.70).

Checksum: 3FD73905F439D369
Show »

FASTA2,138239,553
Isoform 13 (Alpha-1C.127).

Checksum: 0E897EBBE8CE80B3
Show »

FASTA2,157241,562
Isoform 14 (Alpha-1C.126).

Checksum: 27FC888216441CBC
Show »

FASTA2,179243,657
Isoform 15 (Alpha-1C.125).

Checksum: C4853F45ABBB5029
Show »

FASTA2,144240,131
Isoform 16.

Checksum: DEF42A539FF14497
Show »

FASTA2,144240,252
Isoform 17.

Checksum: DA8DB8B593C24297
Show »

FASTA2,109236,322
Isoform 18 (HHT-1).

Checksum: A276926FE2CACCDF
Show »

FASTA2,180243,782
Isoform 19 (Alpha-1C.76).

Checksum: 909275719F6E9E1A
Show »

FASTA2,127238,246
Isoform 20 (Alpha-1C.77).

Checksum: C84441D29A7A8BC4
Show »

FASTA2,138239,416
Isoform 21 (Alpha-1C.69).

Checksum: 4BE678B026838D86
Show »

FASTA2,138239,464
Isoform 22 (Alpha-1C.78).

Checksum: BC75006748C0D52B
Show »

FASTA2,138239,601
Isoform 23 (Alpha-1C.105).

Checksum: 436A052B62394E78
Show »

FASTA2,138239,434
Isoform 24 (Alpha-1C.71).

Checksum: DB702050CF536648
Show »

FASTA2,157241,514
Isoform 25 (Alpha-1C.73).

Checksum: B5A40FA59B52D8F8
Show »

FASTA2,146240,345
Isoform 26 (Alpha-1C.86).

Checksum: 849CA0B200ABD3BC
Show »

FASTA2,139239,076
Isoform 27 (Alpha-1C.72).

Checksum: DD04DEA2A12B1F77
Show »

FASTA2,157241,377
Isoform 28.

Checksum: 4C012EE14BEAB4C6
Show »

FASTA2,169242,565
Isoform 29 (Alpha-1C.74).

Checksum: B175938ED91C729C
Show »

FASTA2,146240,207
Isoform 30 (Alpha-1C.87).

Checksum: E4FB149EC28ABB24
Show »

FASTA2,158241,805
Isoform 31 (Alpha-1C.88).

Checksum: 16F37BBC4916E1F2
Show »

FASTA2,166242,709
Isoform 32 (Alpha-1C.89).

Checksum: E9F05B4D54FC4180
Show »

FASTA2,155241,403
Isoform 33 (Alpha-1C.85).

Checksum: F59FA0716379E381
Show »

FASTA2,173243,345
Isoform 34 (Alpha-1C,long-NT).

Checksum: 3547C5B23A501120
Show »

FASTA2,251252,006
Isoform 35.

Checksum: E4B3CF875A7F2449
Show »

FASTA2,135239,290

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References

« Hide 'large scale' references
[1]"Molecular diversity of L-type Ca2+ channel transcripts in human fibroblasts."
Soldatov N.M.
Proc. Natl. Acad. Sci. U.S.A. 89:4628-4632(1992) [PubMed: 1316612] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORM 1), VARIANTS VAL-1869 AND ARG-1893.
Tissue: Fetal fibroblast.
[2]"Cloning, chromosomal localization, and functional expression of the alpha-1 subunit of the L-type voltage-dependent calcium channel from normal human heart."
Schultz D., Mikala G., Yatani A., Engle D.B., Iles D.E., Segers B., Sinke R.J., Weghuis D.O., Kloeckner U., Wakamori M., Wang J.-J., Melvin D., Varadi G., Schwartz A.
Proc. Natl. Acad. Sci. U.S.A. 90:6228-6232(1993) [PubMed: 8392192] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 18), NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1822-1863, FUNCTION, TISSUE SPECIFICITY, VARIANT ARG-84.
Tissue: Heart.
[3]"Genomic structure of human L-type Ca2+ channel."
Soldatov N.M.
Genomics 22:77-87(1994) [PubMed: 7959794] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], NUCLEOTIDE SEQUENCE [MRNA] OF 1112-1803 (ISOFORMS 24/27), NUCLEOTIDE SEQUENCE [MRNA] OF 1364-1972 (ISOFORMS 11/12/19/20/21/22/23/30/31/32).
Tissue: Hippocampus and Lung fibroblast.
[4]"Different voltage-dependent inhibition by dihydropyridines of human Ca2+ channel splice variants."
Soldatov N.M., Bouron A., Reuter H.
J. Biol. Chem. 270:10540-10543(1995) [PubMed: 7737988] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 12; 19 AND 20), ALTERNATIVE SPLICING, FUNCTION, MUTAGENESIS OF GLY-954 AND TYR-958.
Tissue: Fibroblast.
[5]"Properties of three COOH-terminal splice variants of a human cardiac L-type Ca2+-channel alpha1-subunit."
Kloeckner U., Mikala G., Eisfeld J., Iles D.E., Strobeck M., Mershon J.L., Schwartz A., Varadi G.
Am. J. Physiol. 272:H1372-H1381(1997) [PubMed: 9087614] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 16 AND 17), ALTERNATIVE SPLICING, VARIANTS ARG-84; VAL-1869 AND ARG-1893.
Tissue: Heart.
[6]"Molecular structures involved in L-type calcium channel inactivation. Role of the carboxyl-terminal region encoded by exons 40-42 in alpha1C subunit in the kinetics and Ca2+ dependence of inactivation."
Soldatov N.M., Zuelke R.D., Bouron A., Reuter H.
J. Biol. Chem. 272:3560-3566(1997) [PubMed: 9013606] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 26 AND 27), ALTERNATIVE SPLICING, FUNCTION.
Tissue: Hippocampus.
[7]"Ca2+ channel sensitivity towards the blocker isradipine is affected by alternative splicing of the human alpha1C subunit gene."
Zuehlke R.D., Bouron A., Soldatov N.M., Reuter H.
FEBS Lett. 427:220-224(1998) [PubMed: 9607315] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 21; 22 AND 23), FUNCTION.
[8]"Alpha(1C) (Ca(V)1.2) L-type calcium channel mediates mechanosensitive calcium regulation."
Lyford G.L., Strege P.R., Shepard A., Ou Y., Ermilov L., Miller S.M., Gibbons S.J., Rae J.L., Szurszewski J.H., Farrugia G.
Am. J. Physiol. 283:C1001-C1008(2002) [PubMed: 12176756] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 12), FUNCTION, TISSUE SPECIFICITY.
Tissue: Intestinal smooth muscle.
[9]"Atherosclerosis-related molecular alteration of the human CaV1.2 calcium channel alpha1C subunit."
Tiwari S., Zhang Y., Heller J., Abernethy D.R., Soldatov N.M.
Proc. Natl. Acad. Sci. U.S.A. 103:17024-17029(2006) [PubMed: 17071743] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 13; 14; 15; 24 AND 25), FUNCTION, TISSUE SPECIFICITY.
[10]"Functional expression of splice variants of human l-type calcium channel (isoform 1 gene)."
Soldatov N.
Submitted (JUN-1994) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 11; 28; 29; 30; 31; 32 AND 33), ALTERNATIVE SPLICING, VARIANTS ARG-84; VAL-1869 AND ARG-1893.
[11]"The finished DNA sequence of human chromosome 12."
Scherer S.E., Muzny D.M., 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. expand/collapse author list , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
Nature 440:346-351(2006) [PubMed: 16541075] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[12]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 35).
Tissue: Brain.
[13]"A novel long N-terminal isoform of human L-type Ca2+ channel is up-regulated by protein kinase C."
Blumenstein Y., Kanevsky N., Sahar G., Barzilai R., Ivanina T., Dascal N.
J. Biol. Chem. 277:3419-3423(2002) [PubMed: 11741969] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-180 (ISOFORM 34).
[14]"Molecular diversity of L-type calcium channels. Evidence for alternative splicing of the transcripts of three non-allelic genes."
Perez-Reyes E., Wei X., Castellano A., Birnbaumer L.
J. Biol. Chem. 265:20430-20436(1990) [PubMed: 2173707] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1182-1503 (ISOFORMS 6/12/20/23/24), NUCLEOTIDE SEQUENCE [MRNA] OF 1182-1503 (ISOFORMS 7/13/16/17/18/21/22).
Tissue: Heart.
[15]"Assignment of the human gene for the alpha 1 subunit of the cardiac DHP-sensitive Ca2+ channel (CCHL1A1) to chromosome 12p12-pter."
Powers P.A., Gregg R.G., Lalley P.A., Liao M., Hogan K.
Genomics 10:835-839(1991) [PubMed: 1653763] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1140-1206.
Tissue: Heart.
[16]"Mapping of a human brain voltage-gated calcium channel to human chromosome 12p13-pter."
Sun W., McPherson J.D., Hoang D.Q., Wasmuth J.J., Evans G.A., Montal M.
Genomics 14:1092-1094(1992) [PubMed: 1335957] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1196-1421.
Tissue: Brain.
[17]"Molecular localization of ion selectivity sites within the pore of a human L-type cardiac calcium channel."
Tang S., Mikala G., Bahinski A., Yatani A., Varadi G., Schwartz A.
J. Biol. Chem. 268:13026-13029(1993) [PubMed: 8099908] [Abstract]
Cited for: MUTAGENESIS, CALCIUM-BINDING.
[18]"Molecular cloning and characterization of the human voltage-gated calcium channel alpha(2)delta-4 subunit."
Qin N., Yagel S., Momplaisir M.-L., Codd E.E., D'Andrea M.R.
Mol. Pharmacol. 62:485-496(2002) [PubMed: 12181424] [Abstract]
Cited for: INTERACTION WITH CACNA2D4.
[19]"Ca2+-binding protein-1 facilitates and forms a postsynaptic complex with Cav1.2 (L-type) Ca2+ channels."
Zhou H., Kim S.-A., Kirk E.A., Tippens A.L., Sun H., Haeseleer F., Lee A.
J. Neurosci. 24:4698-4708(2004) [PubMed: 15140941] [Abstract]
Cited for: INTERACTION WITH CABP1.
[20]"Molecular mechanism for divergent regulation of Cav1.2 Ca2+ channels by calmodulin and Ca2+-binding protein-1."
Zhou H., Yu K., McCoy K.L., Lee A.
J. Biol. Chem. 280:29612-29619(2005) [PubMed: 15980432] [Abstract]
Cited for: INTERACTION WITH CABP1.
[21]"Structure of a complex between a voltage-gated calcium channel beta-subunit and an alpha-subunit domain."
Van Petegem F., Clark K.A., Chatelain F.C., Minor D.L. Jr.
Nature 429:671-675(2004) [PubMed: 15141227] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 428-445 IN COMPLEX WITH CACNB2.
[22]"Ca(V)1.2 calcium channel dysfunction causes a multisystem disorder including arrhythmia and autism."
Splawski I., Timothy K.W., Sharpe L.M., Decher N., Kumar P., Bloise R., Napolitano C., Schwartz P.J., Joseph R.M., Condouris K., Tager-Flusberg H., Priori S.G., Sanguinetti M.C., Keating M.T.
Cell 119:19-31(2004) [PubMed: 15454078] [Abstract]
Cited for: VARIANT TS ARG-406, CHARACTERIZATION OF VARIANT TS ARG-406.
[23]"Severe arrhythmia disorder caused by cardiac L-type calcium channel mutations."
Splawski I., Timothy K.W., Decher N., Kumar P., Sachse F.B., Beggs A.H., Sanguinetti M.C., Keating M.T.
Proc. Natl. Acad. Sci. U.S.A. 102:8089-8096(2005) [PubMed: 15863612] [Abstract]
Cited for: VARIANT TS SER-402.
[24]"Loss-of-function mutations in the cardiac calcium channel underlie a new clinical entity characterized by ST-segment elevation, short QT intervals, and sudden cardiac death."
Antzelevitch C., Pollevick G.D., Cordeiro J.M., Casis O., Sanguinetti M.C., Aizawa Y., Guerchicoff A., Pfeiffer R., Oliva A., Wollnik B., Gelber P., Bonaros E.P. Jr., Burashnikov E., Wu Y., Sargent J.D., Schickel S., Oberheiden R., Bhatia A. expand/collapse author list , Hsu L.F., Haissaguerre M., Schimpf R., Borggrefe M., Wolpert C.
Circulation 115:442-449(2007) [PubMed: 17224476] [Abstract]
Cited for: VARIANTS BRS3 VAL-39 AND ARG-490, CHARACTERIZATION OF VARIANTS BRS3 VAL-39 AND ARG-490.
+Additional computationally mapped references.

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Web resources

GeneReviews

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M92269 Genomic DNA. Translation: AAA17030.1.
M92270 Genomic DNA. No translation available.
M92271 Genomic DNA. No translation available.
M92272 Genomic DNA. No translation available.
M92273 Genomic DNA. No translation available.
M92274 Genomic DNA. No translation available.
M92275 Genomic DNA. No translation available.
L04568 Genomic DNA. Translation: AAA02500.2. Frameshift.
L04569 mRNA. Translation: AAA02501.1.
L29529 mRNA. Translation: AAA51899.1.
Z26256 Genomic DNA. No translation available.
Z26257 Genomic DNA. No translation available.
Z26258 Genomic DNA. No translation available.
Z26259 Genomic DNA. No translation available.
Z26260 Genomic DNA. No translation available.
Z26261 Genomic DNA. No translation available.
Z26262 Genomic DNA. No translation available.
Z26263 Genomic DNA. No translation available.
Z26264 Genomic DNA. No translation available.
Z26265 Genomic DNA. No translation available.
Z26266 Genomic DNA. No translation available.
Z26267 Genomic DNA. No translation available.
Z26268 Genomic DNA. No translation available.
Z26269 Genomic DNA. No translation available.
Z26271 Genomic DNA. No translation available.
Z26272 Genomic DNA. No translation available.
Z26273 Genomic DNA. No translation available.
Z26274 Genomic DNA. No translation available.
Z26275 Genomic DNA. No translation available.
Z26276 Genomic DNA. No translation available.
Z26277 Genomic DNA. No translation available.
Z26278 Genomic DNA. No translation available.
Z26279 Genomic DNA. No translation available.
Z26280 Genomic DNA. No translation available.
Z26281 Genomic DNA. No translation available.
Z26282 Genomic DNA. No translation available.
Z26283 Genomic DNA. No translation available.
Z26284 Genomic DNA. No translation available.
Z26286 Genomic DNA. No translation available.
Z26287 Genomic DNA. No translation available.
Z26288 Genomic DNA. No translation available.
Z26294 mRNA. Translation: CAA81218.1.
Z26295 mRNA. Translation: CAA81219.1.
Z26308 Genomic DNA. No translation available.
Z34809 mRNA. Translation: CAA84340.1.
Z34810 mRNA. Translation: CAA84341.1.
Z34811 mRNA. Translation: CAA84342.1.
Z34812 mRNA. Translation: CAA84343.1.
Z34813 mRNA. Translation: CAA84344.1.
Z34814 mRNA. Translation: CAA84345.1.
Z34815 mRNA. Translation: CAA84346.1.
Z34816 mRNA. Translation: CAA84347.1.
Z34817 mRNA. Translation: CAA84348.1.
Z34818 mRNA. Translation: CAA84349.1.
Z34819 mRNA. Translation: CAA84350.1.
Z34820 mRNA. Translation: CAA84351.1.
Z34821 mRNA. Translation: CAA84352.1.
Z34822 mRNA. Translation: CAA84353.1.
L29530 Genomic DNA. No translation available.
L29531 Genomic DNA. No translation available.
L29532 Genomic DNA. No translation available.
L29533 Genomic DNA. No translation available.
L29534 mRNA. Translation: AAA51900.1.
L29535 Genomic DNA. No translation available.
L29536 mRNA. Translation: AAA51901.1.
L29537 Genomic DNA. No translation available.
L29538 Genomic DNA. No translation available.
L29539 Genomic DNA. No translation available.
Z74996 mRNA. Translation: CAA99284.1.
AJ224873 mRNA. Translation: CAA12174.1.
AF465484 mRNA. Translation: AAM70049.1.
AY830711 mRNA. Translation: AAX37354.1.
AY830712 mRNA. Translation: AAX37355.1.
AY830713 mRNA. Translation: AAX37356.1.
AC005293 Genomic DNA. No translation available.
AC005342 Genomic DNA. No translation available.
AC005344 Genomic DNA. No translation available.
AC005414 Genomic DNA. No translation available.
AC005866 Genomic DNA. No translation available.
AC006051 Genomic DNA. No translation available.
AC007618 Genomic DNA. No translation available.
AC092471 Genomic DNA. No translation available.
BC146846 mRNA. Translation: AAI46847.1.
AY604867 mRNA. Translation: AAT02226.1.
M57971 mRNA. Translation: AAA62832.1.
M57972 mRNA. Translation: AAB59461.1.
M61130 Genomic DNA. Translation: AAA58409.1.
M91370 Genomic DNA. Translation: AAA74590.1.
IPIIPI00016709.
IPI00216095.
IPI00607583.
IPI00744784.
IPI00789111.
IPI00789708.
IPI00793099.
IPI00793792.
IPI00794300.
IPI00794357.
IPI00794799.
IPI00797606.
IPI00798235.
IPI00827513.
IPI00827543.
IPI00827553.
IPI00827578.
IPI00827633.
IPI00827681.
IPI00827766.
IPI00827775.
IPI00827851.
IPI00827855.
IPI00827887.
IPI00827942.
IPI00827956.
IPI00827998.
IPI00828000.
IPI00828035.
IPI00828116.
IPI00828128.
IPI00828174.
IPI00828206.
IPI00828210.
IPI00900275.
PIRA23660.
A44363.
A45290.
B23660.
C23660.
I54168.
RefSeqNP_000710.5.
NP_001123299.1.
NP_001123301.1.
NP_001123302.1.
NP_001123303.1.
NP_001123304.1.
NP_001123305.1.
NP_001123306.1.
NP_001123307.1.
NP_001123308.1.
NP_001123309.1.
NP_001123310.1.
NP_001123311.1.
NP_001123312.1.
NP_001123313.1.
NP_001123314.1.
NP_001123315.1.
NP_001123316.1.
NP_001123318.1.
UniGeneHs.118262

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1T0JX-ray2.00C428-445[»]
2BE6X-ray2.00D/E/F1659-1692[»]
2F3YX-ray1.45B1665-1685[»]
2F3ZX-ray1.60B1665-1685[»]
3G43X-ray2.10E/F1609-1682[»]
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-29589N.
IntActQ13936. 4 interactions.
STRINGQ13936.

Protein family/group databases

TCDB1.A.1.11.4. voltage-gated ion channel (VIC) superfamily.

PTM databases

PhosphoSiteQ13936.

Proteomic databases

PRIDEQ13936.

Genome annotation databases

EnsemblENST00000402845; ENSP00000385724; ENSG00000151067; Homo sapiens. [Genome view]
GeneID775.
KEGGhsa:775.
UCSCuc001qjz.2. human.
uc001qkb.2. human.
uc001qkc.2. human.
uc001qkd.2. human.
uc001qke.2. human.
uc001qkf.2. human.
uc001qkg.2. human.
uc001qkh.2. human.
uc001qki.1. human.
uc001qkj.1. human.
uc001qkk.1. human.
uc001qkl.2. human.
uc001qkm.1. human.
uc001qkn.2. human.
uc001qko.2. human.
uc001qkp.2. human.
uc001qkq.2. human.
uc001qkr.2. human.
uc001qks.2. human.
uc001qkt.2. human.
uc001qku.2. human.
uc009zdu.1. human.
uc009zdw.1. human.

Organism-specific databases

CTD775.
GeneCardsGC12P002032.
GC12P002033.
GC12P002034.
HGNCHGNC:1390. CACNA1C.
MIM114205. gene.
601005. phenotype.
611875. phenotype.
Orphanet768. Long QT syndrome, familial.
65283. Timothy syndrome.
PharmGKBPA83.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG18750.
HOVERGENQ13936.

Enzyme and pathway databases

ReactomeREACT_1505. Integration of energy metabolism.
REACT_15380. Diabetes pathways.

Gene expression databases

ArrayExpressQ13936.
BgeeQ13936.
GenevestigatorQ13936.

Family and domain databases

InterProIPR005821. Ion_trans.
IPR014873. VDCC_a1su_IQ.
IPR005451. VDCC_L_a1csu.
IPR005446. VDCC_L_a1su.
IPR002077. VDCCAlpha1.
[Graphical view]
PfamPF08763. Ca_chan_IQ. 1 hit.
PF00520. Ion_trans. 5 hits.
[Graphical view]
PRINTSPR00167. CACHANNEL.
PR01630. LVDCCALPHA1.
PR01635. LVDCCALPHA1C.
ProtoNetSearch...

Other Resources

DrugBankDB00308. Ibutilide.
DB00270. Isradipine.
DB00653. Magnesium Sulfate.
DB01388. Mibefradil.
DB00622. Nicardipine.
DB00661. Verapamil.
SOURCESearch...

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Entry information

Entry nameCAC1C_HUMAN
AccessionPrimary (citable) accession number: Q13936
Secondary accession number(s): B2RUT3 expand/collapse secondary AC list , Q13917, Q13918, Q13919, Q13920, Q13921, Q13922, Q13923, Q13924, Q13925, Q13926, Q13927, Q13928, Q13929, Q13930, Q13932, Q13933, Q14743, Q14744, Q15877, Q4VMI7, Q4VMI8, Q4VMI9, Q6PKM7, Q8N6C0, Q99025, Q99241, Q99875
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: November 25, 2008
Last modified: February 9, 2010
This is version 122 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

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SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents