CAC1C_CHICK
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 03-AUG-2022, entry version 124.
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 (TC
CC 1.A.1.11) family. CACNA1C subfamily. {ECO:0000305}.
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DR EMBL; AF027610; AAC08311.1; -; mRNA.
DR AlphaFoldDB; O73707; -.
DR SMR; O73707; -.
DR STRING; 9031.ENSGALP00000021230; -.
DR PaxDb; O73707; -.
DR PRIDE; O73707; -.
DR VEuPathDB; HostDB:geneid_395891; -.
DR eggNOG; KOG2301; Eukaryota.
DR InParanoid; O73707; -.
DR OrthoDB; 172471at2759; -.
DR PhylomeDB; O73707; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
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: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:0005891; C:voltage-gated calcium channel complex; IBA:GO_Central.
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:0098703; P:calcium ion import across plasma membrane; IBA:GO_Central.
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; 1.20.120.350; -; 1.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR002077; VDCCAlpha1.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR Pfam; PF00520; Ion_trans; 1.
DR PRINTS; PR00167; CACHANNEL.
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
