ID CAC1C_CHICK Reviewed; 177 AA. AC O73707; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1998, sequence version 1. DT 24-JAN-2024, entry version 130. DE RecName: Full=Voltage-dependent L-type calcium channel subunit alpha-1C; DE AltName: Full=CHCACHA1C; DE AltName: Full=Voltage-gated calcium channel subunit alpha Cav1.2; DE Flags: Fragment; GN Name=CACNA1C; OS Gallus gallus (Chicken). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae; OC Phasianinae; Gallus. OX NCBI_TaxID=9031; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=White leghorn; TISSUE=Basilar papilla; RX PubMed=9405708; DOI=10.1073/pnas.94.26.14883; RA Kollmar R., Montgomery L.G., Fak J., Henry L.J., Hudspeth A.J.; RT "Predominance of the alpha1D subunit in L-type voltage-gated Ca2+ channels RT of hair cells in the chicken's cochlea."; RL Proc. Natl. Acad. Sci. U.S.A. 94:14883-14888(1997). CC -!- FUNCTION: Pore-forming, alpha-1C subunit of the voltage-gated calcium CC channel that gives rise to L-type calcium currents. Mediates influx of CC calcium ions into the cytoplasm, and thereby triggers calcium release CC from the sarcoplasm. Plays an important role in excitation-contraction CC coupling in the heart. Required for normal heart development and normal CC regulation of heart rhythm (By similarity). Required for normal CC contraction of smooth muscle cells in blood vessels and in the CC intestine. Essential for normal blood pressure regulation via its role CC in the contraction of arterial smooth muscle cells (By similarity). CC Long-lasting (L-type) calcium channels belong to the 'high-voltage CC activated' (HVA) group (By similarity). {ECO:0000250|UniProtKB:P15381, CC ECO:0000250|UniProtKB:Q01815, ECO:0000250|UniProtKB:Q13936}. CC -!- ACTIVITY REGULATION: Inhibited by dihydropyridines (DHP), such as CC isradipine. Channel activity is regulated by Ca(2+) and calmodulin. CC {ECO:0000250|UniProtKB:Q13936}. CC -!- SUBUNIT: Component of a calcium channel complex consisting of a pore- CC forming alpha subunit (CACNA1C) and ancillary beta, gamma and delta CC subunits. The channel complex contains alpha, beta, gamma and delta CC subunits in a 1:1:1:1 ratio, i.e. it contains only one of each type of CC subunit. CACNA1C channel activity is modulated by ancillary subunits, CC such as CACNB2, CACNB3, CACNA2D1 and CACNA2D4. CC {ECO:0000250|UniProtKB:Q13936}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P22002}; CC Multi-pass membrane protein {ECO:0000250|UniProtKB:P22002}. Perikaryon CC {ECO:0000250|UniProtKB:P22002}. Postsynaptic density membrane CC {ECO:0000250|UniProtKB:P22002}. Cell projection, dendrite CC {ECO:0000250|UniProtKB:P22002}. Cell membrane, sarcolemma, T-tubule CC {ECO:0000250|UniProtKB:Q01815}. Note=The interaction between RRAD and CC CACNB2 promotes the expression of CACNA1C at the cell membrane. CC {ECO:0000250|UniProtKB:P15381}. CC -!- DOMAIN: Each of the four internal repeats contains five hydrophobic CC transmembrane segments (S1, S2, S3, S5, S6) and one positively charged CC transmembrane segment (S4). S4 segments probably represent the voltage- CC sensor and are characterized by a series of positively charged amino CC acids at every third position. CC -!- DOMAIN: Binding of intracellular calcium through the EF-hand motif CC inhibits the opening of the channel. {ECO:0000250|UniProtKB:P15381}. CC -!- PTM: Phosphorylation by PKA activates the channel. CC {ECO:0000250|UniProtKB:P15381}. CC -!- SIMILARITY: Belongs to the calcium channel alpha-1 subunit CC (TC 1.A.1.11) family. CACNA1C subfamily. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF027610; AAC08311.1; -; mRNA. DR AlphaFoldDB; O73707; -. DR SMR; O73707; -. DR STRING; 9031.ENSGALP00000066917; -. DR GlyCosmos; O73707; 2 sites, No reported glycans. DR PaxDb; 9031-ENSGALP00000021230; -. DR VEuPathDB; HostDB:geneid_395891; -. DR eggNOG; KOG2301; Eukaryota. DR InParanoid; O73707; -. DR PhylomeDB; O73707; -. DR Proteomes; UP000000539; Unassembled WGS sequence. DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell. DR GO; GO:1990454; C:L-type voltage-gated calcium channel complex; ISS:UniProtKB. DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB. DR GO; GO:0098839; C:postsynaptic density membrane; IEA:UniProtKB-SubCell. DR GO; GO:0042383; C:sarcolemma; ISS:UniProtKB. DR GO; GO:0030315; C:T-tubule; ISS:UniProtKB. DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW. DR GO; GO:0008331; F:high voltage-gated calcium channel activity; ISS:UniProtKB. DR GO; GO:0005245; F:voltage-gated calcium channel activity; ISS:UniProtKB. DR GO; GO:0070588; P:calcium ion transmembrane transport; ISS:UniProtKB. DR GO; GO:0061577; P:calcium ion transmembrane transport via high voltage-gated calcium channel; ISS:UniProtKB. DR GO; GO:0060402; P:calcium ion transport into cytosol; ISS:UniProtKB. DR GO; GO:0061337; P:cardiac conduction; ISS:UniProtKB. DR GO; GO:0010881; P:regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion; ISS:UniProtKB. DR Gene3D; 1.10.287.70; -; 1. DR Gene3D; 1.20.120.350; Voltage-gated potassium channels. Chain C; 1. DR InterPro; IPR005821; Ion_trans_dom. DR InterPro; IPR002077; VDCCAlpha1. DR InterPro; IPR027359; Volt_channel_dom_sf. DR PANTHER; PTHR45628; VOLTAGE-DEPENDENT CALCIUM CHANNEL TYPE A SUBUNIT ALPHA-1; 1. DR PANTHER; PTHR45628:SF10; VOLTAGE-DEPENDENT L-TYPE CALCIUM CHANNEL SUBUNIT ALPHA-1C; 1. DR Pfam; PF00520; Ion_trans; 1. DR PRINTS; PR00167; CACHANNEL. DR SUPFAM; SSF81324; Voltage-gated potassium channels; 1. PE 2: Evidence at transcript level; KW Calcium; Calcium channel; Calcium transport; Calmodulin-binding; KW Cell membrane; Cell projection; Disulfide bond; Glycoprotein; Ion channel; KW Ion transport; Membrane; Phosphoprotein; Postsynaptic cell membrane; KW Reference proteome; Repeat; Synapse; Transmembrane; Transmembrane helix; KW Transport; Voltage-gated channel. FT CHAIN <1..>177 FT /note="Voltage-dependent L-type calcium channel subunit FT alpha-1C" FT /id="PRO_0000053932" FT TRANSMEM 27..45 FT /note="Helical; Name=S4 of repeat IV" FT /evidence="ECO:0000250|UniProtKB:P07293" FT TRANSMEM 64..84 FT /note="Helical; Name=S5 of repeat IV" FT /evidence="ECO:0000250|UniProtKB:P07293" FT INTRAMEM 107..125 FT /note="Pore-forming" FT /evidence="ECO:0000250|UniProtKB:P07293" FT TRANSMEM 154..>177 FT /note="Helical; Name=S6 of repeat IV" FT /evidence="ECO:0000250|UniProtKB:P07293" FT MOTIF 116..119 FT /note="Selectivity filter of repeat IV" FT /evidence="ECO:0000250|UniProtKB:P07293" FT SITE 118 FT /note="Calcium ion selectivity and permeability" FT /evidence="ECO:0000250|UniProtKB:P15381" FT CARBOHYD 90 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 141 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 133..149 FT /evidence="ECO:0000250|UniProtKB:P07293" FT NON_TER 1 FT NON_TER 177 SQ SEQUENCE 177 AA; 19957 MW; 84CB4656D78AAF23 CRC64; ALIVVGSIVD IAITEVNNAE ENSRISITFF RLFRVMRLVK LLSRGEGIRT LLWTFIKSFQ ALPYVALLIV MLFFIYAVIG MQVFGKIALN DTTEINRNNN FQTFPQAVLL LFRCATGEAW QEIMLACLPD KKCDPDSEPA NSTEADHSCG SSFAVFYFIS FYMLCAFLII DLFVAVI //