Cacna1c
entrez
12288
canonical
uniprot
Q01815
canonical
ensembl
ENSMUSG00000051331
resolver
ensp
ENSMUSP00000077433
resolver
ensp
ENSMUSP00000108410
resolver
ensp
ENSMUSP00000108413
resolver
ensp
ENSMUSP00000108444
resolver
ensp
ENSMUSP00000140056
resolver
ensp
ENSMUSP00000140341
resolver
ensp
ENSMUSP00000140415
resolver
ensp
ENSMUSP00000140886
resolver
ensp
ENSMUSP00000140961
resolver
ensp
ENSMUSP00000141015
resolver
ensp
ENSMUSP00000141033
resolver
ensp
ENSMUSP00000151863
resolver
enst
ENSMUST00000112790
resolver
enst
ENSMUST00000112793
resolver
enst
ENSMUST00000186889
resolver
enst
ENSMUST00000187474
resolver
enst
ENSMUST00000187940
resolver
enst
ENSMUST00000188106
resolver
enst
ENSMUST00000190285
resolver
genesymbol
Cacna1c
resolver
genesymbol_syn
CaV1.2-a
resolver
genesymbol_syn
Cach2
resolver
genesymbol_syn
Cacn2
resolver
genesymbol_syn
Cacnl1a1
resolver
genesymbol_syn
Cchl1a1
resolver
uniprot
A0A087WQ62
resolver
uniprot
A0A087WS40
resolver
uniprot
A0A087WSA3
resolver
uniprot
A0A087WSE7
resolver
uniprot
A0A087WSG2
resolver
uniprot
C7TQ57
resolver
uniprot
C7TQ58
resolver
uniprot
C7TQ59
resolver
uniprot
C7TQ60
resolver
uniprot
C7TQ61
resolver
uniprot
C7TQ62
resolver
uniprot
F7C376
resolver
uniprot
F8WJL1
resolver
uniprot
Q04476
resolver
uniprot
Q0PCR6
resolver
uniprot
Q61242
resolver
uniprot
Q99242
resolver
uniprot_entry
A0A087WQ62_MOUSE
resolver
uniprot_entry
A0A087WS40_MOUSE
resolver
uniprot_entry
A0A087WSA3_MOUSE
resolver
uniprot_entry
A0A087WSE7_MOUSE
resolver
uniprot_entry
A0A087WSG2_MOUSE
resolver
uniprot_entry
C7TQ57_MOUSE
resolver
uniprot_entry
C7TQ58_MOUSE
resolver
uniprot_entry
C7TQ59_MOUSE
resolver
uniprot_entry
C7TQ60_MOUSE
resolver
uniprot_entry
C7TQ61_MOUSE
resolver
uniprot_entry
C7TQ62_MOUSE
resolver
uniprot_entry
CAC1C_MOUSE
resolver
uniprot_entry
F7C376_MOUSE
resolver
uniprot_entry
F8WJL1_MOUSE
resolver
uniprot_entry
Q0PCR6_MOUSE
resolver
uniprot_sec
Q04476
resolver
uniprot_sec
Q61242
resolver
uniprot_sec
Q99242
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by dihydropyridines (DHP), such as isradipine (PubMed:14609949, PubMed:21216955). Inhibited by nifedipine. Selectively inhibited by the snake venom calciseptine (By similarity). Inhibited by pinaverium bromide (PIN) (By similarity). Channel activity is regulated by Ca(2+) and calmodulin. Binding of STAC1, STAC2 or STAC3 to a region that overlaps with the calmodulin binding site inhibits channel inactivation by Ca(2+) 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). {ECO:0000250|UniProtKB:P15381, ECO:0000250|UniProtKB:Q13936, ECO:0000269|PubMed:14609949, ECO:0000269|PubMed:21216955}.
uniprot
proteins
amino_acid_sequence
MVNENTRMYVPEENHQGSNYGSPRPAHANMNANAAAGLAPEHIPTPGAALSWQAAIDAARQAKLMGSAGNATISTVSSTQRKRQQYGKPKKQGGTTATRPPRALLCLTLKNPIRRACISIVEWKPFEIIILLTIFANCVALAIYIPFPEDDSNATNSNLERVEYLFLIIFTVEAFLKVIAYGLLFHPNAYLRNGWNLLDFIIVVVGLFSAILEQATKADGANALGGKGAGFDVKALRAFRVLRPLRLVSGVPSLQVVLNSIIKAMVPLLHIALLVLFVIIIYAIIGLELFMGKMHKTCYNQEGIIDVPAEEDPSPCALETGHGRQCQNGTVCKPGWDGPKHGITNFDNFAFAMLTVFQCITMEGWTDVLYWMQDAMGYELPWVYFVSLVIFGSFFVLNLVLGVLSGEFSKEREKAKARGDFQKLREKQQLEEDLKGYLDWITQAEDIDPENEDEGMDEDKPRNMSMPTSETESVNTENVAGGDIEGENCGARLAHRISKSKFSRYWRRWNRFCRRKCRAAVKSNVFYWLVIFLVFLNTLTIASEHYNQPHWLTEVQDTANKALLALFTAEMLLKMYSLGLQAYFVSLFNRFDCFIVCGGILETILVETKIMSPLGISVLRCVRLLRIFKITRYWNSLSNLVASLLNSVRSIASLLLLLFLFIIIFSLLGMQLFGGKFNFDEMQTRRSTFDNFPQSLLTVFQILTGEDWNSVMYDGIMAYGGPSFPGMLVCIYFIILFICGNYILLNVFLAIAVDNLADAESLTSAQKEEEEEKERKKLARTASPEKKQEVMEKPAVEESKEEKIELKSITADGESPPTTKINMDDLQPSENEDKSPHSNPDTAGEEDEEEPEMPVGPRPRPLSELHLKEKAVPMPEASAFFIFSPNNRFRLQCHRIVNDTIFTNLILFFILLSSISLAAEDPVQHTSFRNHILGNADYVFTSIFTLEIILKMTAYGAFLHKGSFCRNYFNILDLLVVSVSLISFGIQSSAINVVKILRVLRVLRPLRAINRAKGLKHVVQCVFVAIRTIGNIVIVTTLLQFMFACIGVQLFKGKLYTCSDSSKQTEAECKGNYITYKDGEVDHPIIQPRSWENSKFDFDNVLAAMMALFTVSTFEGWPELLYRSIDSHTEDKGPIYNYRVEISIFFIIYIIIIAFFMMNIFVGFVIVTFQEQGEQEYKNCELDKNQRQCVEYALKARPLRRYIPKNQHQYKVWYVVNSTYFEYLMFVLILLNTICLAMQHYGQSCLFKIAMNILNMLFTGLFTVEMILKLIAFKPKGYFSDPWNVFDFLIVIGSIIDVILSETNPAEHTQCSPSMSAEENSRISITFFRLFRVMRLVKLLSRGEGIRTLLWTFIKSFQALPYVALLIVMLFFIYAVIGMQVFGKIALNDTTEINRNNNFQTFPQAVLLLFRCATGEAWQDIMLACMPGKKCAPESEPSNSTEGETPCGSSFAVFYFISFYMLCAFLIINLFVAVIMDNFDYLTRDWSILGPHHLDEFKRIWAEYDPEAKGRIKHLDVVTLLRRIQPPLGFGKLCPHRVACKRLVSMNMPLNSDGTVMFNATLFALVRTALRIKTEGNLEQANEELRAIIKKIWKRTSMKLLDQVVPPAGDDEVTVGKFYATFLIQEYFRKFKKRKEQGLVGKPSQRNALSLQAGLRTLHDIGPEIRRAISGDLTAEEELDKAMKEAVSAASEDDIFRRAGGLFGNHVTYYQSDSRGNFPQTFATQRPLHINKTGNNQADTESPSHEKLVDSTFTPSSYSSTGSNANINNANNTALGRFPHPAGYSSTVSTVEGHGPPLSPAVRVQEAAWKLSSKRCHSRESQGATVNQEIFPDETRSVRMSEEAEYCSEPSLLSTDMFSYQEDEHRQLTCPEEDKREIQPSPKRSFLRSASLGRRASFHLECLKRQKDQGGDISQKTALPLHLVHHQALAVAGLSPLLQRSHSPTTFPRPCPTPPVTPGSRGRPLRPIPTLRLEGAESSEKLNSSFPSIHCSSWSEETTACSGSSSMARRARPVSLTVPSQAGAPGRQFHGSASSLVEAVLISEGLGQFAQDPKFIEVTTQELADACDMTIEEMENAADNILSGGAQQSPNGTLLPFVNCRDPGQDRAVAPEDESCAYALGRGRSEEALADSRSYVSNL
uniprot
proteins
function
FUNCTION: 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, PubMed:10973973). 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). {ECO:0000250|UniProtKB:P15381, ECO:0000269|PubMed:10973973, ECO:0000269|PubMed:14609949, ECO:0000269|PubMed:18586882, ECO:0000269|PubMed:21216955, ECO:0000269|PubMed:25368181, ECO:0000269|PubMed:28119464, ECO:0000305}.
uniprot
proteins
mass_dalton
240138
uniprot
proteins
mutagenesis
MUTAGEN 1670; /note="S->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."; /evidence="ECO:0000269|PubMed:25368181"; MUTAGEN 1794..1796; /note="HGP->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."; /evidence="ECO:0000269|PubMed:21216955"; MUTAGEN 1797..2139; /note="Missing: 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."; /evidence="ECO:0000269|PubMed:21216955"; MUTAGEN 1897; /note="S->A: Loss of phosphorylation site. Abolishes increased vasoconstriction in response to elevated blood glucose."; /evidence="ECO:0000269|PubMed:28119464
uniprot
proteins
post_translational_modification
PTM: Phosphorylation by PKA at Ser-1897 activates the channel (PubMed:28119464). Elevated levels of blood glucose lead to increased phosphorylation by PKA. {ECO:0000269|PubMed:28119464}.
uniprot
proteins
protein_family
CACNA1C subfamily
uniprot
proteins
protein_family
Calcium channel alpha-1 subunit (TC 1.A.1.11) family
uniprot
proteins
pubmed
10973973
uniprot
proteins
pubmed
1385406
uniprot
proteins
pubmed
14609949
uniprot
proteins
pubmed
18586882
uniprot
proteins
pubmed
20639889
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
21216955
uniprot
proteins
pubmed
2173707
uniprot
proteins
pubmed
22355118
uniprot
proteins
pubmed
25368181
uniprot
proteins
pubmed
28119464
uniprot
proteins
pubmed
28363979
uniprot
proteins
pubmed
7814415
uniprot
proteins
sequence_length
2139
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14609949, ECO:0000269|PubMed:18586882, ECO:0000269|PubMed:21216955}; Multi-pass membrane protein {ECO:0000305}. Cell membrane, sarcolemma {ECO:0000269|PubMed:25368181, ECO:0000269|PubMed:28119464}; Multi-pass membrane protein {ECO:0000305}. Perikaryon {ECO:0000250|UniProtKB:P22002}. Postsynaptic density membrane {ECO:0000250|UniProtKB:P22002}. Cell projection, dendrite {ECO:0000250|UniProtKB:P22002}. Cell membrane, sarcolemma, T-tubule {ECO:0000269|PubMed:22355118}. Note=Colocalizes with ryanodine receptors in distinct clusters at the junctional membrane, where the sarcolemma and the sarcoplasmic reticulum are in close contact. The interaction between RRAD and CACNB2 promotes the expression of CACNA1C at the cell membrane. Localized in T-tubules, as shown in SERCA2-knockout cardiomyocytes (PubMed:22355118). {ECO:0000250|UniProtKB:P15381, ECO:0000269|PubMed:22355118}.
uniprot
proteins
transmembrane_region
TRANSMEM 125..143; /note="Helical; Name=S1 of repeat I"; /evidence="ECO:0000250|UniProtKB:P07293"; TRANSMEM 159..179; /note="Helical; Name=S2 of repeat I"; /evidence="ECO:0000250|UniProtKB:P07293"; TRANSMEM 189..209; /note="Helical; Name=S3 of repeat I"; /evidence="ECO:0000250|UniProtKB:P07293"; TRANSMEM 233..251; /note="Helical; Name=S4 of repeat I"; /evidence="ECO:0000250|UniProtKB:P07293"; TRANSMEM 269..290; /note="Helical; Name=S5 of repeat I"; /evidence="ECO:0000250|UniProtKB:P07293"; TRANSMEM 381..401; /note="Helical; Name=S6 of repeat I"; /evidence="ECO:0000250|UniProtKB:P07293"; TRANSMEM 525..543; /note="Helical; Name=S1 of repeat II"; /evidence="ECO:0000250|UniProtKB:P07293"; TRANSMEM 555..575; /note="Helical; Name=S2 of repeat II"; /evidence="ECO:0000250|UniProtKB:P07293"; TRANSMEM 587..606; /note="Helical; Name=S3 of repeat II"; /evidence="ECO:0000250|UniProtKB:P07293"; TRANSMEM 616..634; /note="Helical; Name=S4 of repeat II"; /evidence="ECO:0000250|UniProtKB:P07293"; TRANSMEM 654..673; /note="Helical; Name=S5 of repeat II"; /evidence="ECO:0000250|UniProtKB:P07293"; TRANSMEM 726..745; /note="Helical; Name=S6 of repeat II"; /evidence="ECO:0000250|UniProtKB:P07293"; TRANSMEM 901..919; /note="Helical; Name=S1 of repeat III"; /evidence="ECO:0000250|UniProtKB:P07293"; TRANSMEM 932..951; /note="Helical; Name=S2 of repeat III"; /evidence="ECO:0000250|UniProtKB:P07293"; TRANSMEM 968..986; /note="Helical; Name=S3 of repeat III"; /evidence="ECO:0000250|UniProtKB:P07293"; TRANSMEM 994..1012; /note="Helical; Name=S4 of repeat III"; /evidence="ECO:0000250|UniProtKB:P07293"; TRANSMEM 1032..1051; /note="Helical; Name=S5 of repeat III"; /evidence="ECO:0000250|UniProtKB:P07293"; TRANSMEM 1140..1161; /note="Helical; Name=S6 of repeat III"; /evidence="ECO:0000250|UniProtKB:P07293"; TRANSMEM 1220..1241; /note="Helical; Name=S1 of repeat IV"; /evidence="ECO:0000250|UniProtKB:P07293"; TRANSMEM 1250..1271; /note="Helical; Name=S2 of repeat IV"; /evidence="ECO:0000250|UniProtKB:P07293"; TRANSMEM 1282..1301; /note="Helical; Name=S3 of repeat IV"; /evidence="ECO:0000250|UniProtKB:P07293"; TRANSMEM 1325..1343; /note="Helical; Name=S4 of repeat IV"; /evidence="ECO:0000250|UniProtKB:P07293"; TRANSMEM 1362..1382; /note="Helical; Name=S5 of repeat IV"; /evidence="ECO:0000250|UniProtKB:P07293"; TRANSMEM 1452..1476; /note="Helical; Name=S6 of repeat IV"; /evidence="ECO:0000250|UniProtKB:P07293
uniprot
proteins