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CACNA1C Membrane Protein Introduction

Introduction of CACNA1C

Calcium channels, voltage-dependent, L-form, α1C subunit (also known as Cav1.2) are proteins encoded by the CACNA1C gene in humans. CACNA1C is a subunit of the L-type voltage-dependent calcium channel. This gene encodes the alpha-1 subunit of a voltage-dependent calcium channel. Calcium channels mediate the flow of calcium ions into cells during membrane polarization. The alpha-1 subunit consists of 24 transmembrane regions that form pores through which ions enter the cell. The calcium channel consists of a complex of alpha-1, alpha-2/delta and beta subunits in a ratio of 1:1:1. The S3-S4 connector of CACNA1C determines the gating phenotype of the channel and the gating dynamics of the regulation.

Basic Information of CACNA1C
Protein Name Voltage-dependent L-type calcium channel subunit alpha-1C
Gene Name CACNA1C
Aliases CACH2, CACN2, CACNL1A1, CCHL1A1
Organism Homo sapiens (Human)
UniProt ID Q13936
Transmembrane Times 24
Length (aa) 2221
Sequence MVNENTRMYIPEENHQGSNYGSPRPAHANMNANAAAGLAPEHIPTPGAALSWQAAIDAARQAKLMGSAGNATISTVSSTQRKRQQYGKPKKQGSTTATRPPRALLCLTLKNPIRRACISIVEWKPFEIIILLTIFANCVALAIYIPFPEDDSNATNSNLERVEYLFLIIFTVEAFLKVIAYGLLFHPNAYLRNGWNLLDFIIVVVGLFSAILEQATKADGANALGGKGAGFDVKALRAFRVLRPLRLVSGVPSLQVVLNSIIKAMVPLLHIALLVLFVIIIYAIIGLELFMGKMHKTCYNQEGIADVPAEDDPSPCALETGHGRQCQNGTVCKPGWDGPKHGITNFDNFAFAMLTVFQCITMEGWTDVLYWVNDAVGRDWPWIYFVTLIIIGSFFVLNLVLGVLSGEFSKEREKAKARGDFQKLREKQQLEEDLKGYLDWITQAEDIDPENEDEGMDEEKPRNMSMPTSETESVNTENVAGGDIEGENCGARLAHRISKSKFSRYWRRWNRFCRRKCRAAVKSNVFYWLVIFLVFLNTLTIASEHYNQPNWLTEVQDTANKALLALFTAEMLLKMYSLGLQAYFVSLFNRFDCFVVCGGILETILVETKIMSPLGISVLRCVRLLRIFKITRYWNSLSNLVASLLNSVRSIASLLLLLFLFIIIFSLLGMQLFGGKFNFDEMQTRRSTFDNFPQSLLTVFQILTGEDWNSVMYDGIMAYGGPSFPGMLVCIYFIILFICGNYILLNVFLAIAVDNLADAESLTSAQKEEEEEKERKKLARTASPEKKQELVEKPAVGESKEEKIELKSITADGESPPATKINMDDLQPNENEDKSPYPNPETTGEEDEEEPEMPVGPRPRPLSELHLKEKAVPMPEASAFFIFSSNNRFRLQCHRIVNDTIFTNLILFFILLSSISLAAEDPVQHTSFRNHILFYFDIVFTTIFTIEIALKILGNADYVFTSIFTLEIILKMTAYGAFLHKGSFCRNYFNILDLLVVSVSLISFGIQSSAINVVKILRVLRVLRPLRAINRAKGLKHVVQCVFVAIRTIGNIVIVTTLLQFMFACIGVQLFKGKLYTCSDSSKQTEAECKGNYITYKDGEVDHPIIQPRSWENSKFDFDNVLAAMMALFTVSTFEGWPELLYRSIDSHTEDKGPIYNYRVEISIFFIIYIIIIAFFMMNIFVGFVIVTFQEQGEQEYKNCELDKNQRQCVEYALKARPLRRYIPKNQHQYKVWYVVNSTYFEYLMFVLILLNTICLAMQHYGQSCLFKIAMNILNMLFTGLFTVEMILKLIAFKPKGYFSDPWNVFDFLIVIGSIIDVILSETNHYFCDAWNTFDALIVVGSIVDIAITEVNPAEHTQCSPSMNAEENSRISITFFRLFRVMRLVKLLSRGEGIRTLLWTFIKSFQALPYVALLIVMLFFIYAVIGMQVFGKIALNDTTEINRNNNFQTFPQAVLLLFRCATGEAWQDIMLACMPGKKCAPESEPSNSTEGETPCGSSFAVFYFISFYMLCAFLIINLFVAVIMDNFDYLTRDWSILGPHHLDEFKRIWAEYDPEAKGRIKHLDVVTLLRRIQPPLGFGKLCPHRVACKRLVSMNMPLNSDGTVMFNATLFALVRTALRIKTEGNLEQANEELRAIIKKIWKRTSMKLLDQVVPPAGDDEVTVGKFYATFLIQEYFRKFKKRKEQGLVGKPSQRNALSLQAGLRTLHDIGPEIRRAISGDLTAEEELDKAMKEAVSAASEDDIFRRAGGLFGNHVSYYQSDGRSAFPQTFTTQRPLHINKAGSSQGDTESPSHEKLVDSTFTPSSYSSTGSNANINNANNTALGRLPRPAGYPSTVSTVEGHGPPLSPAIRVQEVAWKLSSNRERHVPMCEDLELRRDSGSAGTQAHCLLLRKANPSRCHSRESQAAMAGQEETSQDETYEVKMNHDTEACSEPSLLSTEMLSYQDDENRQLTLPEEDKRDIRQSPKRGFLRSASLGRRASFHLECLKRQKDRGGDISQKTVLPLHLVHHQALAVAGLSPLLQRSHSPASFPRPFATPPATPGSRGWPPQPVPTLRLEGVESSEKLNSSFPSIHCGSWAETTPGGGGSSAARRVRPVSLMVPSQAGAPGRQFHGSASSLVEAVLISEGLGQFAQDPKFIEVTTQELADACDMTIEEMESAADNILSGGAPQSPNGALLPFVNCRDAGQDRAGGEEDAGCVRARGRPSEEELQDSRVYVSSL

Function of CACNA1C Membrane Protein

CACNA1C is widely expressed in smooth muscle, pancreatic cells, fibroblasts, and neurons. Of particular importance, however, is its expression in the heart, which mediates L-type currents that cause calcium-induced calcium release from the ER store via the ryanodine receptor. It depolarizes at -30 mV, helping to determine the shape of the action potential in the myocardium and smooth muscle. CACNA1C binds to dihydropyridine and is inhibited by dihydropyridine. In the cerebral arteries, high levels of calcium in the mitochondria increase the activity of nuclear factor kappa BNF-κB, and the transcription and functional Cav1.2 expression of CACNA1c are increased.

Structure of CACNA1C membrane protein.Fig.1 Structure of CACNA1C membrane protein.

Application of CACNA1C Membrane Protein in Literature

  1. Soldatov N.M., et al. Molecular diversity of L-type Ca2+ channel transcripts in human fibroblasts. Proc Natl Acad Sci U S A. 1992, 89(10): 4628-32. PubMed ID: 1316612

    This article suggests that the fourth diversity region is located at the C-terminal region and comprises insertions and deletions may give rise to multiple subforms of HFCC with altered electrophysiological properties.

  2. Schultz D., et al. Cloning, chromosomal localization, and functional expression of the alpha 1 subunit of the L-type voltage-dependent calcium channel from normal human heart. Proc Natl Acad Sci U S A. 1993, 90(13): 6228-32. PubMed ID: 8392192

    This article focuses on the cloned alpha 1 subunit was expressed in Xenopus oocytes and single-channel analyses revealed native-like pharmacology and channel properties.

  3. Soldatov N.M., et al. Genomic structure of human L-type Ca2+ channel. Genomics. 1994, 22(1): 77-87. PubMed ID: 7959794

    This article suggests that isoforms of the L-type Ca2+ channel gene exist in the human genome.

  4. Soldatov N.M., et al. Different voltage-dependent inhibition by dihydropyridines of human Ca2+ channel splice variants. J Biol Chem. 1995, 270(18): 10540-3. PubMed ID: 7737988

    This article comes up with a new insight into the molecular mechanisms of Ca2+ channel inhibition by this important class of drugs.

  5. Zühlke R.D., et al. Ca2+ channel sensitivity towards the blocker isradipine is affected by alternative splicing of the human alpha1C subunit gene. FEBS Lett. 1998, 427(2): 220-4. PubMed ID: 9607315

    Authors in this group observe up to 10-fold differences in IC50 values for isradipine, as well as changes in the voltage dependence of DHP action.

CACNA1C Preparation Options

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