Cacna1c
entrez
24239
canonical
uniprot
P22002
canonical
ensembl
ENSRNOG00000007090
resolver
ensp
ENSRNOP00000094626
resolver
ensp
ENSRNOP00000094898
resolver
ensp
ENSRNOP00000101938
resolver
ensp
ENSRNOP00000108236
resolver
enst
ENSRNOT00000106776
resolver
enst
ENSRNOT00000113714
resolver
enst
ENSRNOT00000121801
resolver
enst
ENSRNOT00000126089
resolver
genesymbol
Cacna1c
resolver
genesymbol_syn
Cach2
resolver
genesymbol_syn
Cacn2
resolver
genesymbol_syn
Cacnl1a1
resolver
genesymbol_syn
Cchl1a1
resolver
uniprot
A0A8I6ANR4
resolver
uniprot
A0A8I6GKU9
resolver
uniprot
A0ABK0LBJ7
resolver
uniprot
A0ABK0LXC5
resolver
uniprot
A0SLC4
resolver
uniprot
F1LMN0
resolver
uniprot
F1M5G9
resolver
uniprot
P27733
resolver
uniprot
P27734
resolver
uniprot
Q62816
resolver
uniprot
Q63271
resolver
uniprot
Q64178
resolver
uniprot
Q71QJ6
resolver
uniprot
Q8VHT2
resolver
uniprot
Q8VHT3
resolver
uniprot_entry
A0A8I6ANR4_RAT
resolver
uniprot_entry
A0A8I6GKU9_RAT
resolver
uniprot_entry
A0ABK0LBJ7_RAT
resolver
uniprot_entry
A0ABK0LXC5_RAT
resolver
uniprot_entry
A0SLC4_RAT
resolver
uniprot_entry
CAC1C_RAT
resolver
uniprot_entry
Q71QJ6_RAT
resolver
uniprot_entry
Q8VHT2_RAT
resolver
uniprot_entry
Q8VHT3_RAT
resolver
uniprot_sec
F1LMN0
resolver
uniprot_sec
F1M5G9
resolver
uniprot_sec
P27733
resolver
uniprot_sec
P27734
resolver
uniprot_sec
Q62816
resolver
uniprot_sec
Q63271
resolver
uniprot_sec
Q64178
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by dihydropyridines (DHP), such as isradipine (By similarity). Inhibited by nifedipine (By similarity). Channel activity is regulated by Ca(2+) and calmodulin (PubMed:15140941). 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 (PubMed:15140941). Shear stress and pressure increases calcium channel activity (By similarity). {ECO:0000250|UniProtKB:P15381, ECO:0000250|UniProtKB:Q13936, ECO:0000269|PubMed:15140941}.
uniprot
proteins
amino_acid_sequence
MIRAFAQPSTPPYQPLSSCLSEDTERKFKGKVVHEAQLNCFYISPGGSNYGSPRPAHANMNANAAAGLAPEHIPTPGAALSWLAAIDAARQAKLMGSAGNATISTVSSTQRKRQQYGKPKKQGGTTATRPPRALLCLTLKNPIRRACISIVEWKPFEIIILLTIFANCVALAIYIPFPEDDSNATNSNLERVEYLFLIIFTVEAFLKVIAYGLLFHPNAYLRNGWNLLDFIIVVVGLFSAILEQATKADGANALGGKGAGFDVKALRAFRVLRPLRLVSGVPSLQVVLNSIIKAMVPLLHIALLVLFVIIIYAIIGLELFMGKMHKTCYNQEGIIDVPAEEDPSPCALETGHGRQCQNGTVCKPGWDGPKHGITNFDNFAFAMLTVFQCITMEGWTDVLYWMQDAMGYELPWVYFVSLVIFGSFFVLNLVLGVLSGEFSKEREKAKARGDFQKLREKQQLEEDLKGYLDWITQAEDIDPENEDEGMDEDKPRNMSMPTSETESVNTENVAGGDIEGENCGARLAHRISKSKFSRYWRRWNRFCRRKCRAAVKSNVFYWLVIFLVFLNTLTIASEHYNQPHWLTEVQDTANKALLALFTAEMLLKMYSLGLQAYFVSLFNRFDCFIVCGGILETILVETKIMSPLGISCWRCVRLLRIFKITRYWNSLSNLVASLLNSLRSIASLLLLLFLFIIIFSLLGMQLFGGKFNFDEMQTRRSTFDNFPQSLLTVFQILTGEDWNSVMYDGIMAYGGPSFPGMLVCIYFIILFISPNYILLNLFLAIAVDNLADAESLTSAQKEEEEEKERKKLARTASPEKKQEVMEKPAVEESKEEKIELKSITADGESPPTTKINMDDLQPSENEDKSPHSNPDTAGEEDEEEPEMPVGPRPRPLSELHLKEKAVPMPEASAFFIFSPNNRFRLQCHRIVNDTIFTNLILFFILLSSISLAAEDPVQHTSFRNHILFYFDIVFTTIFTIEIALKMTAYGAFLHKGSFCRNYFNILDLLVVSVSLISFGIQSSAINVVKILRVLRVLRPLRINRAKGLKHVVQCVFVAIRTIGNIVIVTTLLQFMFACIGVQLFKGKLYTCSDSSKQTEAESKGNYITYKTGEVDHPIIQPRSWENSKFDFDNVLAAMMALFTVSTFEGWPELLYRSIDSHTEDKGPIYNYRVEISIFFIIYIIIIAFFMMNIFVGFVIVTFQEQGEQEYKNCELDKNQRQCVEYALKARPLPRYIPKNQHQYKVWYVVNSTYFEYLMFVLILLNTICLAMQHYGQSCLFKIAMNILNMLFTGLFTVEMILKLIAFKPKHYFCDAWNTFDALIVVGSIVDIAITEVHPAEHTQCSPSMSAEENSRISITFFRLFRVMRLVKLLSRGEGIRTLLWTFIKSFQALPYVALLIVMLFFIYAVIGMQVFGKIALNDTTEINRNNNFQTFPQAVLLLFRCATGEAWQDIMLACMPGKKCAPESEPSNSTEGETPCGSSFAVFYFISFYMLCAFLIINLFVAVIMDNFDYLTRDWSILGPHHLDEFKRIWAEYDPEAKGRIKHLDVVTLLRRIQPPLGFGKLCPHRVACKRLVSMNMPLNSDGTVMFNATLFALVRTALRIKTEGNLEQANEELRAIIKKIWKRTSMKLLDQVVPPAGDDEVTVGKFYATFLIQEYFRKFKKRKEQGLVGKPSQRNALSLQAGLRTLHDIGPEIRRAISGDLTAEEELDKAMKEAVSAASEDDIFRRAGGLFGNHVSYYQSDSRSNFPQTFATQRPLHINKTGNNQADTESPSHEKLVDSTFTPSSYSSTGSNANINNANNTALGRFPHPAGYSSTVSTVEGHGPPLSPAVRVQEAAWKLSSKRCHSRESQGATVSQDMFPDETRSSVRLSEEVEYCSEPSLLSTDILSYQDDENRQLTCLEEDKREIQPCPKRSFLRSASLGRRASFHLECLKRQKDQGGDISQKTALPLHLVHHQALAVAGLSPLLQRSHSPSTFPRPRPTPPVTPGSRGRPLQPIPTLRLEGAESSEKLNSSFPSIHCSSWSEETTACSGGSSMARRARPVSLTVPSQAGAPGRQFHGSASSLVEAVLISEGLGQFAQDPKFIEVTTQELADACDMTIEEMENAADNILSGGAQQSPNGTLLPFVNCRDPGQDRAVVPEDESCVYALGRGRSEEALPDSRSYVSNL
uniprot
proteins
function
FUNCTION: Pore-forming, alpha-1C subunit of the voltage-gated calcium channel that gives rise to L-type calcium currents (Probable) (PubMed:15140941, PubMed:15170217). 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 (By similarity). Required for normal heart development and normal regulation of heart rhythm (By similarity). 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 (By similarity). Long-lasting (L-type) calcium channels belong to the 'high-voltage activated' (HVA) group (By similarity). {ECO:0000250|UniProtKB:P15381, ECO:0000250|UniProtKB:Q01815, ECO:0000250|UniProtKB:Q13936, ECO:0000269|PubMed:15140941, ECO:0000269|PubMed:15170217, ECO:0000305|PubMed:1648941}.
uniprot
proteins
mass_dalton
243482
uniprot
proteins
post_translational_modification
PTM: Phosphorylation by PKA at Ser-1927 activates the channel (By similarity). Elevated levels of blood glucose lead to increased phosphorylation by PKA (By similarity). Is also phosphorylated in vitro by CaM-kinase II, PKC and CGPK (PubMed:8396138). {ECO:0000250|UniProtKB:Q01815, ECO:0000269|PubMed:8396138}.
uniprot
proteins
protein_family
CACNA1C subfamily
uniprot
proteins
protein_family
Calcium channel alpha-1 subunit (TC 1.A.1.11) family
uniprot
proteins
pubmed
1311102
uniprot
proteins
pubmed
15140941
uniprot
proteins
pubmed
15170217
uniprot
proteins
pubmed
1648941
uniprot
proteins
pubmed
1692134
uniprot
proteins
pubmed
2170396
uniprot
proteins
pubmed
22673903
uniprot
proteins
pubmed
24751537
uniprot
proteins
pubmed
7479909
uniprot
proteins
pubmed
7485440
uniprot
proteins
pubmed
8396138
uniprot
proteins
pubmed
9278523
uniprot
proteins
sequence_length
2169
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15140941, ECO:0000269|PubMed:15170217, ECO:0000305|PubMed:1648941}; Multi-pass membrane protein {ECO:0000305}. Cell membrane, sarcolemma {ECO:0000250|UniProtKB:P15381}; Multi-pass membrane protein {ECO:0000305}. Perikaryon {ECO:0000269|PubMed:15140941}. Postsynaptic density membrane {ECO:0000269|PubMed:15140941}. Cell projection, dendrite {ECO:0000269|PubMed:15140941}. Cell membrane, sarcolemma, T-tubule {ECO:0000250|UniProtKB:Q01815}. 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. {ECO:0000250|UniProtKB:P15381}.
uniprot
proteins
transmembrane_region
TRANSMEM 155..173; /note="Helical; Name=S1 of repeat I"; /evidence="ECO:0000250|UniProtKB:P07293"; TRANSMEM 189..209; /note="Helical; Name=S2 of repeat I"; /evidence="ECO:0000250|UniProtKB:P07293"; TRANSMEM 219..239; /note="Helical; Name=S3 of repeat I"; /evidence="ECO:0000250|UniProtKB:P07293"; TRANSMEM 263..281; /note="Helical; Name=S4 of repeat I"; /evidence="ECO:0000250|UniProtKB:P07293"; TRANSMEM 299..320; /note="Helical; Name=S5 of repeat I"; /evidence="ECO:0000250|UniProtKB:P07293"; TRANSMEM 411..431; /note="Helical; Name=S6 of repeat I"; /evidence="ECO:0000250|UniProtKB:P07293"; TRANSMEM 555..573; /note="Helical; Name=S1 of repeat II"; /evidence="ECO:0000250|UniProtKB:P07293"; TRANSMEM 585..605; /note="Helical; Name=S2 of repeat II"; /evidence="ECO:0000250|UniProtKB:P07293"; TRANSMEM 617..636; /note="Helical; Name=S3 of repeat II"; /evidence="ECO:0000250|UniProtKB:P07293"; TRANSMEM 646..664; /note="Helical; Name=S4 of repeat II"; /evidence="ECO:0000250|UniProtKB:P07293"; TRANSMEM 684..703; /note="Helical; Name=S5 of repeat II"; /evidence="ECO:0000250|UniProtKB:P07293"; TRANSMEM 756..775; /note="Helical; Name=S6 of repeat II"; /evidence="ECO:0000250|UniProtKB:P07293"; TRANSMEM 931..949; /note="Helical; Name=S1 of repeat III"; /evidence="ECO:0000250|UniProtKB:P07293"; TRANSMEM 962..981; /note="Helical; Name=S2 of repeat III"; /evidence="ECO:0000250|UniProtKB:P07293"; TRANSMEM 998..1016; /note="Helical; Name=S3 of repeat III"; /evidence="ECO:0000250|UniProtKB:P07293"; TRANSMEM 1024..1041; /note="Helical; Name=S4 of repeat III"; /evidence="ECO:0000250|UniProtKB:P07293"; TRANSMEM 1061..1080; /note="Helical; Name=S5 of repeat III"; /evidence="ECO:0000250|UniProtKB:P07293"; TRANSMEM 1169..1190; /note="Helical; Name=S6 of repeat III"; /evidence="ECO:0000250|UniProtKB:P07293"; TRANSMEM 1249..1270; /note="Helical; Name=S1 of repeat IV"; /evidence="ECO:0000250|UniProtKB:P07293"; TRANSMEM 1279..1300; /note="Helical; Name=S2 of repeat IV"; /evidence="ECO:0000250|UniProtKB:P07293"; TRANSMEM 1311..1330; /note="Helical; Name=S3 of repeat IV"; /evidence="ECO:0000250|UniProtKB:P07293"; TRANSMEM 1354..1372; /note="Helical; Name=S4 of repeat IV"; /evidence="ECO:0000250|UniProtKB:P07293"; TRANSMEM 1391..1411; /note="Helical; Name=S5 of repeat IV"; /evidence="ECO:0000250|UniProtKB:P07293"; TRANSMEM 1481..1505; /note="Helical; Name=S6 of repeat IV"; /evidence="ECO:0000250|UniProtKB:P07293
uniprot
proteins