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Protein

Voltage-dependent L-type calcium channel subunit alpha-1C

Gene

Cacna1c

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Pore-forming, alpha-1C subunit of the voltage-gated calcium channel that gives rise to L-type calcium currents (PubMed:14609949, PubMed:18586882, PubMed:21216955, PubMed:25368181, PubMed:28119464). Mediates influx of calcium ions into the cytoplasm, and thereby triggers calcium release from the sarcoplasm (By similarity). Plays an important role in excitation-contraction coupling in the heart. Required for normal heart development and normal regulation of heart rhythm (PubMed:21216955). Required for normal contraction of smooth muscle cells in blood vessels and in the intestine. Essential for normal blood pressure regulation via its role in the contraction of arterial smooth muscle cells (PubMed:14609949, PubMed:28119464). Long-lasting (L-type) calcium channels belong to the 'high-voltage activated' (HVA) group (Probable).By similarityCurated5 Publications

Activity regulationi

Inhibited by dihydropyridines (DHP), such as isradipine (PubMed:14609949, PubMed:21216955). Inhibited by nifedipine. Channel activity is regulated by Ca2+ and calmodulin. Binding of STAC1, STAC2 or STAC3 to a region that overlaps with the calmodulin binding site inhibits channel inactivation by Ca2+ and calmodulin (By similarity). Binding of calmodulin or CABP1 at the same regulatory sites results in opposite effects on the channel function. Shear stress and pressure increases calcium channel activity (By similarity).By similarity2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi363CalciumBy similarity1
Sitei363Calcium ion selectivity and permeabilityBy similarity1
Metal bindingi706CalciumBy similarity1
Sitei706Calcium ion selectivity and permeabilityBy similarity1
Metal bindingi1115CalciumBy similarity1
Sitei1115Calcium ion selectivity and permeabilityBy similarity1
Sitei1416Calcium ion selectivity and permeabilityBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Calcium bindingi1505 – 1516By similarityAdd BLAST12

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionCalcium channel, Calmodulin-binding, Ion channel, Voltage-gated channel
Biological processCalcium transport, Ion transport, Transport
LigandCalcium, Metal-binding

Enzyme and pathway databases

ReactomeiR-MMU-422356 Regulation of insulin secretion
R-MMU-5576892 Phase 0 - rapid depolarisation
R-MMU-5576893 Phase 2 - plateau phase

Protein family/group databases

TCDBi1.A.1.11.6 the voltage-gated ion channel (vic) superfamily

Names & Taxonomyi

Protein namesi
Recommended name:
Voltage-dependent L-type calcium channel subunit alpha-1C
Alternative name(s):
Calcium channel, L type, alpha-1 polypeptide, isoform 1, cardiac muscle
MELC-CC
Mouse brain class C
Short name:
MBC
Voltage-gated calcium channel subunit alpha Cav1.2
Gene namesi
Name:Cacna1c
Synonyms:Cach2, Cacn2, Cacnl1a1, Cchl1a1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 6

Organism-specific databases

MGIiMGI:103013 Cacna1c

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 124CytoplasmicCuratedAdd BLAST124
Transmembranei125 – 143Helical; Name=S1 of repeat IBy similarityAdd BLAST19
Topological domaini144 – 158ExtracellularCuratedAdd BLAST15
Transmembranei159 – 179Helical; Name=S2 of repeat IBy similarityAdd BLAST21
Topological domaini180 – 188CytoplasmicCurated9
Transmembranei189 – 209Helical; Name=S3 of repeat IBy similarityAdd BLAST21
Topological domaini210 – 232ExtracellularCuratedAdd BLAST23
Transmembranei233 – 251Helical; Name=S4 of repeat IBy similarityAdd BLAST19
Topological domaini252 – 268CytoplasmicCuratedAdd BLAST17
Transmembranei269 – 290Helical; Name=S5 of repeat IBy similarityAdd BLAST22
Topological domaini291 – 350ExtracellularCuratedAdd BLAST60
Intramembranei351 – 372Pore-formingBy similarityAdd BLAST22
Topological domaini373 – 380ExtracellularCurated8
Transmembranei381 – 401Helical; Name=S6 of repeat IBy similarityAdd BLAST21
Topological domaini402 – 524CytoplasmicCuratedAdd BLAST123
Transmembranei525 – 543Helical; Name=S1 of repeat IIBy similarityAdd BLAST19
Topological domaini544 – 554ExtracellularCuratedAdd BLAST11
Transmembranei555 – 575Helical; Name=S2 of repeat IIBy similarityAdd BLAST21
Topological domaini576 – 586CytoplasmicCuratedAdd BLAST11
Transmembranei587 – 606Helical; Name=S3 of repeat IIBy similarityAdd BLAST20
Topological domaini607 – 615ExtracellularCurated9
Transmembranei616 – 634Helical; Name=S4 of repeat IIBy similarityAdd BLAST19
Topological domaini635 – 653CytoplasmicCuratedAdd BLAST19
Transmembranei654 – 673Helical; Name=S5 of repeat IIBy similarityAdd BLAST20
Topological domaini674 – 693ExtracellularCuratedAdd BLAST20
Intramembranei694 – 715Pore-formingBy similarityAdd BLAST22
Topological domaini716 – 725ExtracellularCurated10
Transmembranei726 – 745Helical; Name=S6 of repeat IIBy similarityAdd BLAST20
Topological domaini746 – 900CytoplasmicCuratedAdd BLAST155
Transmembranei901 – 919Helical; Name=S1 of repeat IIIBy similarityAdd BLAST19
Topological domaini920 – 931ExtracellularCuratedAdd BLAST12
Transmembranei932 – 951Helical; Name=S2 of repeat IIIBy similarityAdd BLAST20
Topological domaini952 – 967CytoplasmicCuratedAdd BLAST16
Transmembranei968 – 986Helical; Name=S3 of repeat IIIBy similarityAdd BLAST19
Topological domaini987 – 993ExtracellularCurated7
Transmembranei994 – 1012Helical; Name=S4 of repeat IIIBy similarityAdd BLAST19
Topological domaini1013 – 1031CytoplasmicCuratedAdd BLAST19
Transmembranei1032 – 1051Helical; Name=S5 of repeat IIIBy similarityAdd BLAST20
Topological domaini1052 – 1101ExtracellularCuratedAdd BLAST50
Intramembranei1102 – 1122Pore-formingBy similarityAdd BLAST21
Topological domaini1123 – 1139ExtracellularCuratedAdd BLAST17
Transmembranei1140 – 1161Helical; Name=S6 of repeat IIIBy similarityAdd BLAST22
Topological domaini1162 – 1219CytoplasmicCuratedAdd BLAST58
Transmembranei1220 – 1241Helical; Name=S1 of repeat IVBy similarityAdd BLAST22
Topological domaini1242 – 1249ExtracellularCurated8
Transmembranei1250 – 1271Helical; Name=S2 of repeat IVBy similarityAdd BLAST22
Topological domaini1272 – 1281CytoplasmicCurated10
Transmembranei1282 – 1301Helical; Name=S3 of repeat IVBy similarityAdd BLAST20
Topological domaini1302 – 1324ExtracellularCuratedAdd BLAST23
Transmembranei1325 – 1343Helical; Name=S4 of repeat IVBy similarityAdd BLAST19
Topological domaini1344 – 1361CytoplasmicCuratedAdd BLAST18
Transmembranei1362 – 1382Helical; Name=S5 of repeat IVBy similarityAdd BLAST21
Topological domaini1383 – 1404ExtracellularCuratedAdd BLAST22
Intramembranei1405 – 1423Pore-formingBy similarityAdd BLAST19
Topological domaini1424 – 1451ExtracellularCuratedAdd BLAST28
Transmembranei1452 – 1476Helical; Name=S6 of repeat IVBy similarityAdd BLAST25
Topological domaini1477 – 2139CytoplasmicCuratedAdd BLAST663

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Membrane, Postsynaptic cell membrane, Synapse

Pathology & Biotechi

Disruption phenotypei

Mutant embryos appear normal and have normal heartbeat at 12.5 dpc. All are dead by 14.5 dpc.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi1670S → A: Expected to abolish a phosphorylation site. Decreased channel activity. No effect on phosphorylation at S-1897. Causes heart hypertrophy and decreased exercise tolerance in adult mice. 1 Publication1
Mutagenesisi1794 – 1796HGP → LSK: Strongly decreased channel activity due to decreased expression at the cell membrane, leading to hypertrophy of the right heart ventricle, heart failure and perinatal death; when associated with 1797-P--L-2139 DEL. 1 Publication3
Mutagenesisi1797 – 2139Missing : Strongly decreased channel activity due to decreased expression at the cell membrane, leading to hypertrophy of the right heart ventricle, heart failure and perinatal death; when associated with 1794-L--K-1796. 1 PublicationAdd BLAST343
Mutagenesisi1897S → A: Loss of phosphorylation site. Abolishes increased vasoconstriction in response to elevated blood glucose. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL2529
GuidetoPHARMACOLOGYi529

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000539291 – 2139Voltage-dependent L-type calcium channel subunit alpha-1CAdd BLAST2139

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi153N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi298 ↔ 326By similarity
Disulfide bondi316 ↔ 332By similarity
Glycosylationi328N-linked (GlcNAc...) asparagineSequence analysis1
Modified residuei469PhosphoserineCombined sources1
Modified residuei476PhosphothreonineCombined sources1
Modified residuei808PhosphoserineCombined sources1
Modified residuei815PhosphoserineCombined sources1
Disulfide bondi1058 ↔ 1069By similarity
Glycosylationi1388N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1431 ↔ 1447By similarity
Glycosylationi1439N-linked (GlcNAc...) asparagineSequence analysis1
Modified residuei1487Phosphoserine; by PKASequence analysis1
Modified residuei1670PhosphoserineCombined sources1 Publication1
Modified residuei1691PhosphoserineCombined sources1
Modified residuei1889Phosphoserine; by PKASequence analysis1
Modified residuei1897Phosphoserine; by PKA2 Publications1

Post-translational modificationi

Phosphorylation by PKA activates the channel. Elevated levels of blood glucose lead to increased phosphorylation by PKA.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ01815
PeptideAtlasiQ01815
PRIDEiQ01815

PTM databases

iPTMnetiQ01815
PhosphoSitePlusiQ01815
SwissPalmiQ01815

Expressioni

Tissue specificityi

Detected in embryonic heart (PubMed:10973973, PubMed:21216955). Detected in retina in rod bipolar cells (PubMed:18586882). Detected in tibialis artery (at protein level) (PubMed:14609949). Detected in smooth muscle cells from tibialis artery and in mesenteric artery (PubMed:14609949). High expression in heart, followed by brain and spinal cord (PubMed:1385406).5 Publications

Gene expression databases

BgeeiENSMUSG00000051331 Expressed in 195 organ(s), highest expression level in heart
ExpressionAtlasiQ01815 baseline and differential
GenevisibleiQ01815 MM

Interactioni

Subunit structurei

Component of a calcium channel complex consisting of a pore-forming alpha subunit (CACNA1C) and ancillary beta, gamma and delta subunits. The channel complex contains alpha, beta, gamma and delta subunits in a 1:1:1:1 ratio, i.e. it contains only one of each type of subunit. CACNA1C channel activity is modulated by ancillary subunits, such as CACNB1, CACNB2, CACNB3, CACNA2D1 and CACNA2D4 (By similarity). Intereracts with the gamma subunits CACNG4, CACNG6, CACNG7 and CACNG8 (By similarity). Interacts with CACNB1 (By similarity). Interacts with CACNB2. Identified in a complex with CACNA2D4 and CACNB3. Interacts with CACNB3. Interacts with CACNA2D1. Interacts with CACNA2D4. Interacts with CALM1. Interacts (via the N-terminus and the C-terminal C and IQ motifs) with CABP1; this inhibits Ca2+-dependent channel inactivation. 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 (By similarity). The binding to the cytoplasmic N-terminal domain is calcium independent but is essential for the channel modulation (By similarity). Interacts (via C-terminal CDB motif) with CABP5; in a calcium-dependent manner (PubMed:18586882). Interacts with CIB1; the interaction increases upon cardiomyocytes hypertrophy (PubMed:20639889). Interacts with STAC2 and STAC3; this inhibits channel inactivation (By similarity).By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Cav3P516374EBI-644904,EBI-298576

GO - Molecular functioni

Protein-protein interaction databases

BioGridi198432, 4 interactors
ComplexPortaliCPX-3194 Cardiac muscle VGCC complex
CORUMiQ01815
DIPiDIP-32232N
IntActiQ01815, 93 interactors
MINTiQ01815

Chemistry databases

BindingDBiQ01815

Structurei

3D structure databases

ProteinModelPortaliQ01815
SMRiQ01815
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati111 – 408IAdd BLAST298
Repeati510 – 756IIAdd BLAST247
Repeati887 – 1169IIIAdd BLAST283
Repeati1206 – 1479IVAdd BLAST274

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni47 – 68Calmodulin-bindingBy similarityAdd BLAST22
Regioni428 – 445AID/alpha-interaction domain; mediates interaction with the beta subunitBy similarityAdd BLAST18
Regioni829 – 876Interaction with STAC2By similarityAdd BLAST48
Regioni1089 – 1178Dihydropyridine bindingBy similarityAdd BLAST90
Regioni1430 – 1498Dihydropyridine bindingBy similarityAdd BLAST69
Regioni1444 – 1486Phenylalkylamine bindingBy similarityAdd BLAST43
Regioni1611 – 1644Calmodulin-bindingBy similarityAdd BLAST34
Regioni1611 – 1638Important for interaction with STAC1, STAC2 and STAC3By similarityAdd BLAST28
Regioni1617 – 1637Calmodulin-binding IQ regionBy similarityAdd BLAST21
Regioni1651 – 1670Important for localization in at the junctional membraneBy similarityAdd BLAST20

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi361 – 364Selectivity filter of repeat IBy similarity4
Motifi704 – 707Selectivity filter of repeat IIBy similarity4
Motifi1113 – 1116Selectivity filter of repeat IIIBy similarity4
Motifi1414 – 1417Selectivity filter of repeat IVBy similarity4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi654 – 660Poly-Leu7
Compositional biasi768 – 774Poly-Glu7
Compositional biasi1147 – 1153Poly-Ile7

Domaini

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

Sequence similaritiesi

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00830000128247
HOGENOMiHOG000231529
HOVERGENiHBG050763
InParanoidiQ01815
KOiK04850
PhylomeDBiQ01815

Family and domain databases

Gene3Di1.20.120.350, 4 hits
InterProiView protein in InterPro
IPR031688 CAC1F_C
IPR031649 GPHH_dom
IPR005821 Ion_trans_dom
IPR014873 VDCC_a1su_IQ
IPR005451 VDCC_L_a1csu
IPR005446 VDCC_L_a1su
IPR002077 VDCCAlpha1
IPR027359 Volt_channel_dom_sf
PfamiView protein in Pfam
PF08763 Ca_chan_IQ, 1 hit
PF16885 CAC1F_C, 1 hit
PF16905 GPHH, 1 hit
PF00520 Ion_trans, 4 hits
PRINTSiPR00167 CACHANNEL
PR01630 LVDCCALPHA1
PR01635 LVDCCALPHA1C
SMARTiView protein in SMART
SM01062 Ca_chan_IQ, 1 hit

Sequences (3+)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket
Note: Additional isoforms seem to exist.

This entry has 3 described isoforms and 19 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: Q01815-1) [UniParc]FASTAAdd to basket
Also known as: CACH2A

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.

« Hide
        10         20         30         40         50
MVNENTRMYV PEENHQGSNY GSPRPAHANM NANAAAGLAP EHIPTPGAAL
60 70 80 90 100
SWQAAIDAAR QAKLMGSAGN ATISTVSSTQ RKRQQYGKPK KQGGTTATRP
110 120 130 140 150
PRALLCLTLK NPIRRACISI VEWKPFEIII LLTIFANCVA LAIYIPFPED
160 170 180 190 200
DSNATNSNLE RVEYLFLIIF TVEAFLKVIA YGLLFHPNAY LRNGWNLLDF
210 220 230 240 250
IIVVVGLFSA ILEQATKADG ANALGGKGAG FDVKALRAFR VLRPLRLVSG
260 270 280 290 300
VPSLQVVLNS IIKAMVPLLH IALLVLFVII IYAIIGLELF MGKMHKTCYN
310 320 330 340 350
QEGIIDVPAE EDPSPCALET GHGRQCQNGT VCKPGWDGPK HGITNFDNFA
360 370 380 390 400
FAMLTVFQCI TMEGWTDVLY WMQDAMGYEL PWVYFVSLVI FGSFFVLNLV
410 420 430 440 450
LGVLSGEFSK EREKAKARGD FQKLREKQQL EEDLKGYLDW ITQAEDIDPE
460 470 480 490 500
NEDEGMDEDK PRNMSMPTSE TESVNTENVA GGDIEGENCG ARLAHRISKS
510 520 530 540 550
KFSRYWRRWN RFCRRKCRAA VKSNVFYWLV IFLVFLNTLT IASEHYNQPH
560 570 580 590 600
WLTEVQDTAN KALLALFTAE MLLKMYSLGL QAYFVSLFNR FDCFIVCGGI
610 620 630 640 650
LETILVETKI MSPLGISVLR CVRLLRIFKI TRYWNSLSNL VASLLNSVRS
660 670 680 690 700
IASLLLLLFL FIIIFSLLGM QLFGGKFNFD EMQTRRSTFD NFPQSLLTVF
710 720 730 740 750
QILTGEDWNS VMYDGIMAYG GPSFPGMLVC IYFIILFICG NYILLNVFLA
760 770 780 790 800
IAVDNLADAE SLTSAQKEEE EEKERKKLAR TASPEKKQEV MEKPAVEESK
810 820 830 840 850
EEKIELKSIT ADGESPPTTK INMDDLQPSE NEDKSPHSNP DTAGEEDEEE
860 870 880 890 900
PEMPVGPRPR PLSELHLKEK AVPMPEASAF FIFSPNNRFR LQCHRIVNDT
910 920 930 940 950
IFTNLILFFI LLSSISLAAE DPVQHTSFRN HILGNADYVF TSIFTLEIIL
960 970 980 990 1000
KMTAYGAFLH KGSFCRNYFN ILDLLVVSVS LISFGIQSSA INVVKILRVL
1010 1020 1030 1040 1050
RVLRPLRAIN RAKGLKHVVQ CVFVAIRTIG NIVIVTTLLQ FMFACIGVQL
1060 1070 1080 1090 1100
FKGKLYTCSD SSKQTEAECK GNYITYKDGE VDHPIIQPRS WENSKFDFDN
1110 1120 1130 1140 1150
VLAAMMALFT VSTFEGWPEL LYRSIDSHTE DKGPIYNYRV EISIFFIIYI
1160 1170 1180 1190 1200
IIIAFFMMNI FVGFVIVTFQ EQGEQEYKNC ELDKNQRQCV EYALKARPLR
1210 1220 1230 1240 1250
RYIPKNQHQY KVWYVVNSTY FEYLMFVLIL LNTICLAMQH YGQSCLFKIA
1260 1270 1280 1290 1300
MNILNMLFTG LFTVEMILKL IAFKPKGYFS DPWNVFDFLI VIGSIIDVIL
1310 1320 1330 1340 1350
SETNPAEHTQ CSPSMSAEEN SRISITFFRL FRVMRLVKLL SRGEGIRTLL
1360 1370 1380 1390 1400
WTFIKSFQAL PYVALLIVML FFIYAVIGMQ VFGKIALNDT TEINRNNNFQ
1410 1420 1430 1440 1450
TFPQAVLLLF RCATGEAWQD IMLACMPGKK CAPESEPSNS TEGETPCGSS
1460 1470 1480 1490 1500
FAVFYFISFY MLCAFLIINL FVAVIMDNFD YLTRDWSILG PHHLDEFKRI
1510 1520 1530 1540 1550
WAEYDPEAKG RIKHLDVVTL LRRIQPPLGF GKLCPHRVAC KRLVSMNMPL
1560 1570 1580 1590 1600
NSDGTVMFNA TLFALVRTAL RIKTEGNLEQ ANEELRAIIK KIWKRTSMKL
1610 1620 1630 1640 1650
LDQVVPPAGD DEVTVGKFYA TFLIQEYFRK FKKRKEQGLV GKPSQRNALS
1660 1670 1680 1690 1700
LQAGLRTLHD IGPEIRRAIS GDLTAEEELD KAMKEAVSAA SEDDIFRRAG
1710 1720 1730 1740 1750
GLFGNHVTYY QSDSRGNFPQ TFATQRPLHI NKTGNNQADT ESPSHEKLVD
1760 1770 1780 1790 1800
STFTPSSYSS TGSNANINNA NNTALGRFPH PAGYSSTVST VEGHGPPLSP
1810 1820 1830 1840 1850
AVRVQEAAWK LSSKRCHSRE SQGATVNQEI FPDETRSVRM SEEAEYCSEP
1860 1870 1880 1890 1900
SLLSTDMFSY QEDEHRQLTC PEEDKREIQP SPKRSFLRSA SLGRRASFHL
1910 1920 1930 1940 1950
ECLKRQKDQG GDISQKTALP LHLVHHQALA VAGLSPLLQR SHSPTTFPRP
1960 1970 1980 1990 2000
CPTPPVTPGS RGRPLRPIPT LRLEGAESSE KLNSSFPSIH CSSWSEETTA
2010 2020 2030 2040 2050
CSGSSSMARR ARPVSLTVPS QAGAPGRQFH GSASSLVEAV LISEGLGQFA
2060 2070 2080 2090 2100
QDPKFIEVTT QELADACDMT IEEMENAADN ILSGGAQQSP NGTLLPFVNC
2110 2120 2130
RDPGQDRAVA PEDESCAYAL GRGRSEEALA DSRSYVSNL
Length:2,139
Mass (Da):240,138
Last modified:November 1, 1996 - v1
Checksum:iB564C57A8644E165
GO
Isoform 2 (identifier: Q01815-2) [UniParc]FASTAAdd to basket
Also known as: CACH2D

The sequence of this isoform differs from the canonical sequence as follows:
     1277-1304: GYFSDPWNVFDFLIVIGSIIDVILSETN → HYFCDAWNTFDALIVVGSIVDIAITEVH
     1305-1315: Missing.

Show »
Length:2,128
Mass (Da):238,944
Checksum:iDF7AFC8BF97FE15B
GO
Isoform 3 (identifier: Q01815-3) [UniParc]FASTAAdd to basket
Also known as: Truncated

The sequence of this isoform differs from the canonical sequence as follows:
     1-264: Missing.
     372-391: MQDAMGYELPWVYFVSLVIF → VNDAVGRDWPWIYFVTLIII
     464-464: M → RGAPAGLHDQKKGKFAWFSHSTETHV
     932-951: Missing.
     1305-1315: Missing.

Show »
Length:1,869
Mass (Da):210,822
Checksum:iA8DC3D7154C30AE2
GO

Computationally mapped potential isoform sequencesi

There are 19 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
F7C376F7C376_MOUSE
Voltage-dependent L-type calcium ch...
Cacna1c
2,222Annotation score:
Q0PCR6Q0PCR6_MOUSE
Voltage-dependent L-type calcium ch...
Cacna1c CaV1.2-a
2,169Annotation score:
F8WJL1F8WJL1_MOUSE
Voltage-dependent L-type calcium ch...
Cacna1c
2,139Annotation score:
C7TQ57C7TQ57_MOUSE
Voltage-dependent L-type calcium ch...
Cacna1c
2,169Annotation score:
A0A087WSE7A0A087WSE7_MOUSE
Voltage-dependent L-type calcium ch...
Cacna1c
2,194Annotation score:
A0A087WS40A0A087WS40_MOUSE
Voltage-dependent L-type calcium ch...
Cacna1c
2,153Annotation score:
C7TQ59C7TQ59_MOUSE
Voltage-dependent L-type calcium ch...
Cacna1c
2,169Annotation score:
A0A087WQJ4A0A087WQJ4_MOUSE
Voltage-dependent L-type calcium ch...
Cacna1c
2,156Annotation score:
A0A087WPP1A0A087WPP1_MOUSE
Voltage-dependent L-type calcium ch...
Cacna1c
2,167Annotation score:
A0A087WRM3A0A087WRM3_MOUSE
Voltage-dependent L-type calcium ch...
Cacna1c
2,187Annotation score:
There are more potential isoformsShow all

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti310E → K in AAA62612 (PubMed:7814415).Curated1
Sequence conflicti477E → D in AAA62612 (PubMed:7814415).Curated1
Sequence conflicti555V → D in AAA62612 (PubMed:7814415).Curated1
Sequence conflicti811 – 812AD → GS in AAA62612 (PubMed:7814415).Curated2
Sequence conflicti822N → H in AAA62612 (PubMed:7814415).Curated1
Sequence conflicti825D → A in AAA62612 (PubMed:7814415).Curated1
Sequence conflicti831N → P in AAA62612 (PubMed:7814415).Curated1
Sequence conflicti837 – 841HSNPD → TPTQT in AAA37351 (Ref. 3) Curated5
Sequence conflicti934 – 938GNADY → FYFDI in AAA37351 (Ref. 3) Curated5
Sequence conflicti942S → T in AAA37351 (Ref. 3) Curated1
Sequence conflicti946L → I in AAA37351 (Ref. 3) Curated1
Sequence conflicti949I → A in AAA37351 (Ref. 3) Curated1
Sequence conflicti977 – 978VS → LC in AAA62612 (PubMed:7814415).Curated2
Sequence conflicti1065T → A in AAA62612 (PubMed:7814415).Curated1
Sequence conflicti1507E → K in AAA62612 (PubMed:7814415).Curated1
Sequence conflicti1525Q → H in AAA62612 (PubMed:7814415).Curated1
Sequence conflicti1633K → E in AAA62612 (PubMed:7814415).Curated1
Sequence conflicti1959G → A in AAA62612 (PubMed:7814415).Curated1
Sequence conflicti1963 – 1964RP → ST in AAA62612 (PubMed:7814415).Curated2
Sequence conflicti1970T → H in AAA62612 (PubMed:7814415).Curated1
Sequence conflicti1974E → K in AAA62612 (PubMed:7814415).Curated1
Sequence conflicti2086A → R in AAA62612 (PubMed:7814415).Curated1
Sequence conflicti2097F → L in AAA62612 (PubMed:7814415).Curated1
Sequence conflicti2110A → V in AAA62612 (PubMed:7814415).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0008961 – 264Missing in isoform 3. 1 PublicationAdd BLAST264
Alternative sequenceiVSP_000897372 – 391MQDAM…SLVIF → VNDAVGRDWPWIYFVTLIII in isoform 3. 1 PublicationAdd BLAST20
Alternative sequenceiVSP_000898464M → RGAPAGLHDQKKGKFAWFSH STETHV in isoform 3. 1 Publication1
Alternative sequenceiVSP_000899932 – 951Missing in isoform 3. 1 PublicationAdd BLAST20
Alternative sequenceiVSP_0009001277 – 1304GYFSD…LSETN → HYFCDAWNTFDALIVVGSIV DIAITEVH in isoform 2. 1 PublicationAdd BLAST28
Alternative sequenceiVSP_0009011305 – 1315Missing in isoform 2 and isoform 3. 2 PublicationsAdd BLAST11

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L01776 mRNA Translation: AAB59633.1
M57973 mRNA Translation: AAA63291.1
L06233 mRNA Translation: AAA37351.1
U17869 mRNA Translation: AAA62612.1
CCDSiCCDS71821.1 [Q01815-3]
CCDS80590.1 [Q01815-1]
PIRiA44467
RefSeqiNP_001153005.1, NM_001159533.2 [Q01815-1]
UniGeneiMm.41628
Mm.436656

Genome annotation databases

EnsembliENSMUST00000075591; ENSMUSP00000075021; ENSMUSG00000051331 [Q01815-1]
ENSMUST00000078320; ENSMUSP00000077433; ENSMUSG00000051331 [Q01815-1]
ENSMUST00000112825; ENSMUSP00000108444; ENSMUSG00000051331 [Q01815-3]
GeneIDi12288
KEGGimmu:12288
UCSCiuc009dls.3 mouse [Q01815-3]
uc012erl.2 mouse [Q01815-1]

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L01776 mRNA Translation: AAB59633.1
M57973 mRNA Translation: AAA63291.1
L06233 mRNA Translation: AAA37351.1
U17869 mRNA Translation: AAA62612.1
CCDSiCCDS71821.1 [Q01815-3]
CCDS80590.1 [Q01815-1]
PIRiA44467
RefSeqiNP_001153005.1, NM_001159533.2 [Q01815-1]
UniGeneiMm.41628
Mm.436656

3D structure databases

ProteinModelPortaliQ01815
SMRiQ01815
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198432, 4 interactors
ComplexPortaliCPX-3194 Cardiac muscle VGCC complex
CORUMiQ01815
DIPiDIP-32232N
IntActiQ01815, 93 interactors
MINTiQ01815

Chemistry databases

BindingDBiQ01815
ChEMBLiCHEMBL2529
GuidetoPHARMACOLOGYi529

Protein family/group databases

TCDBi1.A.1.11.6 the voltage-gated ion channel (vic) superfamily

PTM databases

iPTMnetiQ01815
PhosphoSitePlusiQ01815
SwissPalmiQ01815

Proteomic databases

MaxQBiQ01815
PeptideAtlasiQ01815
PRIDEiQ01815

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000075591; ENSMUSP00000075021; ENSMUSG00000051331 [Q01815-1]
ENSMUST00000078320; ENSMUSP00000077433; ENSMUSG00000051331 [Q01815-1]
ENSMUST00000112825; ENSMUSP00000108444; ENSMUSG00000051331 [Q01815-3]
GeneIDi12288
KEGGimmu:12288
UCSCiuc009dls.3 mouse [Q01815-3]
uc012erl.2 mouse [Q01815-1]

Organism-specific databases

CTDi775
MGIiMGI:103013 Cacna1c

Phylogenomic databases

GeneTreeiENSGT00830000128247
HOGENOMiHOG000231529
HOVERGENiHBG050763
InParanoidiQ01815
KOiK04850
PhylomeDBiQ01815

Enzyme and pathway databases

ReactomeiR-MMU-422356 Regulation of insulin secretion
R-MMU-5576892 Phase 0 - rapid depolarisation
R-MMU-5576893 Phase 2 - plateau phase

Miscellaneous databases

ChiTaRSiCacna1c mouse
PROiPR:Q01815
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000051331 Expressed in 195 organ(s), highest expression level in heart
ExpressionAtlasiQ01815 baseline and differential
GenevisibleiQ01815 MM

Family and domain databases

Gene3Di1.20.120.350, 4 hits
InterProiView protein in InterPro
IPR031688 CAC1F_C
IPR031649 GPHH_dom
IPR005821 Ion_trans_dom
IPR014873 VDCC_a1su_IQ
IPR005451 VDCC_L_a1csu
IPR005446 VDCC_L_a1su
IPR002077 VDCCAlpha1
IPR027359 Volt_channel_dom_sf
PfamiView protein in Pfam
PF08763 Ca_chan_IQ, 1 hit
PF16885 CAC1F_C, 1 hit
PF16905 GPHH, 1 hit
PF00520 Ion_trans, 4 hits
PRINTSiPR00167 CACHANNEL
PR01630 LVDCCALPHA1
PR01635 LVDCCALPHA1C
SMARTiView protein in SMART
SM01062 Ca_chan_IQ, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiCAC1C_MOUSE
AccessioniPrimary (citable) accession number: Q01815
Secondary accession number(s): Q04476, Q61242, Q99242
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: November 1, 1996
Last modified: September 12, 2018
This is version 187 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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Main funding by: National Institutes of Health

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