Database: UniProt
Original site: CAC1C_CAVPO 
ID   CAC1C_CAVPO             Reviewed;         169 AA.
AC   O35505;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   28-FEB-2018, entry version 94.
DE   RecName: Full=Voltage-dependent L-type calcium channel subunit alpha-1C;
DE   AltName: Full=Calcium channel, L type, alpha-1 polypeptide, isoform 1, cardiac muscle;
DE   AltName: Full=Voltage-gated calcium channel subunit alpha Cav1.2;
DE   Flags: Fragment;
GN   Name=CACNA1C; Synonyms=CACH2, CACN2, CACNL1A1, CCHL1A1;
OS   Cavia porcellus (Guinea pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia;
OC   Hystricomorpha; Caviidae; Cavia.
OX   NCBI_TaxID=10141;
RN   [1]
RC   TISSUE=Uterus;
RA   Collins P.L., Lundgren D.W., Kulp T.M., Shah P., Chang S.M.,
RA   Chang A.S.;
RT   "Gestational expression of voltage-dependent calcium channel subunits
RT   in guinea pig uterus.";
RL   Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Voltage-sensitive calcium channels (VSCC) mediate the
CC       entry of calcium ions into excitable cells and are also involved
CC       in a variety of calcium-dependent processes, including muscle
CC       contraction, hormone or neurotransmitter release, gene expression,
CC       cell motility, cell division and cell death. The isoform alpha-1C
CC       gives rise to L-type calcium currents. Long-lasting (L-type)
CC       calcium channels belong to the 'high-voltage activated' (HVA)
CC       group. They are blocked by dihydropyridines (DHP),
CC       phenylalkylamines, benzothiazepines, and by omega-agatoxin-IIIA
CC       (omega-Aga-IIIA). They are however insensitive to omega-conotoxin-
CC       GVIA (omega-CTx-GVIA) and omega-agatoxin-IVA (omega-Aga-IVA).
CC       Calcium channels containing the alpha-1C subunit play an important
CC       role in excitation-contraction coupling in the heart. The various
CC       isoforms display marked differences in the sensitivity to DHP
CC       compounds. Binding of calmodulin or CABP1 at the same regulatory
CC       sites results in opposite effects on the channel function.
CC       {ECO:0000250|UniProtKB:Q13936}.
CC   -!- SUBUNIT: Voltage-dependent calcium channels are multisubunit
CC       complexes, consisting of alpha-1, alpha-2, beta and delta subunits
CC       in a 1:1:1:1 ratio. The channel activity is directed by the pore-
CC       forming and voltage-sensitive alpha-1 subunit. In many cases, this
CC       subunit is sufficient to generate voltage-sensitive calcium
CC       channel activity. The auxiliary subunits beta and alpha-2/delta
CC       linked by a disulfide bridge regulate the channel activity.
CC       Interacts (via C-terminal CDB motif) with CABP5; in a calcium-
CC       dependent manner. Interacts with CABP1 and CACNA2D4 (By
CC       similarity). Interacts with CIB1; the interaction increases upon
CC       cardiomyocytes hypertrophy. Interacts with STAC2 and STAC3.
CC       {ECO:0000250|UniProtKB:P22002, ECO:0000250|UniProtKB:Q01815,
CC       ECO:0000250|UniProtKB:Q13936}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P15381};
CC       Multi-pass membrane protein {ECO:0000250|UniProtKB:P15381}. Cell
CC       membrane {ECO:0000250|UniProtKB:P15381}. Note=The interaction
CC       between RRAD and CACNB2 regulates its trafficking to the cell
CC       membrane. {ECO:0000250|UniProtKB:P15381}.
CC   -!- DOMAIN: Each of the four internal repeats contains five
CC       hydrophobic transmembrane segments (S1, S2, S3, S5, S6) and one
CC       positively charged transmembrane segment (S4). S4 segments
CC       probably represent the voltage-sensor and are characterized by a
CC       series of positively charged amino acids at every third position.
CC   -!- DOMAIN: Binding of intracellular calcium through the EF-hand motif
CC       inhibits the opening of the channel.
CC       {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}.
DR   EMBL; AF005938; AAB62890.1; -; mRNA.
DR   ProteinModelPortal; O35505; -.
DR   SMR; O35505; -.
DR   STRING; 10141.ENSCPOP00000009195; -.
DR   BindingDB; O35505; -.
DR   ChEMBL; CHEMBL2366456; -.
DR   eggNOG; KOG2301; Eukaryota.
DR   InParanoid; O35505; -.
DR   Proteomes; UP000005447; Unassembled WGS sequence.
DR   GO; GO:1990454; C:L-type voltage-gated calcium channel complex; 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:0061337; P:cardiac conduction; ISS:UniProtKB.
DR   GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR005452; LVDCC_a1dsu.
DR   InterPro; IPR002077; VDCCAlpha1.
DR   PANTHER; PTHR10037:SF139; PTHR10037:SF139; 2.
DR   Pfam; PF00520; Ion_trans; 1.
PE   2: Evidence at transcript level;
KW   Calcium; Calcium channel; Calcium transport; Cell membrane;
KW   Complete proteome; Disulfide bond; Glycoprotein; Ion channel;
KW   Ion transport; Membrane; Phosphoprotein; Reference proteome; Repeat;
KW   Transmembrane; Transmembrane helix; Transport; Voltage-gated channel.
FT   CHAIN        <1   >169       Voltage-dependent L-type calcium channel
FT                                subunit alpha-1C.
FT                                /FTId=PRO_0000053927.
FT   TRANSMEM     <1     11       Helical; Name=S3 of repeat IV.
FT                                {ECO:0000255}.
FT   TOPO_DOM     12     38       Extracellular. {ECO:0000255}.
FT   TRANSMEM     39     57       Helical; Name=S4 of repeat IV.
FT                                {ECO:0000255}.
FT   TOPO_DOM     58     76       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM     77     96       Helical; Name=S5 of repeat IV.
FT                                {ECO:0000255}.
FT   TOPO_DOM     97    165       Extracellular. {ECO:0000255}.
FT   TRANSMEM    166   >169       Helical; Name=S6 of repeat IV.
FT                                {ECO:0000255}.
FT   REGION       <1     11       Dihydropyridine binding. {ECO:0000250}.
FT   REGION      144   >169       Dihydropyridine binding. {ECO:0000250}.
FT   REGION      158   >169       Phenylalkylamine binding. {ECO:0000250}.
FT   SITE        130    130       Calcium ion selectivity and permeability.
FT                                {ECO:0000250|UniProtKB:P15381}.
FT   CARBOHYD    102    102       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    153    153       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   NON_TER       1      1
FT   NON_TER     169    169
SQ   SEQUENCE   169 AA;  19514 MW;  138E88E510D30CB8 CRC64;
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