ID   Q0PCR6_MOUSE            Unreviewed;      2169 AA.
AC   Q0PCR6;
DT   19-SEP-2006, integrated into UniProtKB/TrEMBL.
DT   19-SEP-2006, sequence version 1.
DT   02-SEP-2026, entry version 147.
DE   RecName: Full=Voltage-dependent L-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
GN   Name=Cacna1c {ECO:0000313|MGI:MGI:103013};
GN   Synonyms=CaV1.2-a {ECO:0000313|EMBL:BAF03165.1};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090 {ECO:0000313|EMBL:BAF03165.1};
RN   [1] {ECO:0000313|EMBL:BAF03165.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Heart {ECO:0000313|EMBL:BAF03165.1};
RX   PubMed=16787652; DOI=10.1016/j.yjmcc.2006.05.002;
RA   Murakami M., Ohba T., Takahashi Y., Watanabe H., Miyoshi I., Nakayama S.,
RA   Ono K., Ito H., Iijima T.;
RT   "Identification of a cardiac isoform of the murine calcium channel alpha1C
RT   (Cav1.2-a) subunit and its preferential binding with the beta2 subunit.";
RL   J. Mol. Cell. Cardiol. 41:115-125(2006).
RN   [2] {ECO:0007829|PubMed:21183079}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
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. Required for normal contraction of smooth
CC       muscle cells in blood vessels and in the intestine. Essential for
CC       normal blood pressure regulation via its role in the contraction of
CC       arterial smooth muscle cells. Long-lasting (L-type) calcium channels
CC       belong to the 'high-voltage activated' (HVA) group.
CC       {ECO:0000256|ARBA:ARBA00045450}.
CC   -!- FUNCTION: Voltage-sensitive calcium channels (VSCC) mediate the entry
CC       of calcium ions into excitable cells and are also involved in a variety
CC       of calcium-dependent processes, including muscle contraction, hormone
CC       or neurotransmitter release, gene expression, cell motility, cell
CC       division and cell death. {ECO:0000256|RuleBase:RU003808}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Ca(2+)(in) = Ca(2+)(out); Xref=Rhea:RHEA:29671,
CC         ChEBI:CHEBI:29108; Evidence={ECO:0000256|ARBA:ARBA00036634};
CC   -!- SUBCELLULAR LOCATION: Cell membrane, sarcolemma, T-tubule
CC       {ECO:0000256|ARBA:ARBA00024012}. Cell membrane, sarcolemma
CC       {ECO:0000256|ARBA:ARBA00004415}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004415}. Cell projection, dendrite
CC       {ECO:0000256|ARBA:ARBA00004279}. Membrane
CC       {ECO:0000256|RuleBase:RU003808}; Multi-pass membrane protein
CC       {ECO:0000256|RuleBase:RU003808}. Perikaryon
CC       {ECO:0000256|ARBA:ARBA00004484}. Postsynaptic density membrane
CC       {ECO:0000256|ARBA:ARBA00034112}.
CC   -!- SIMILARITY: Belongs to the calcium channel alpha-1 subunit
CC       (TC 1.A.1.11) family. CACNA1C subfamily.
CC       {ECO:0000256|ARBA:ARBA00024028}.
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DR   EMBL; AB259049; BAF03165.1; -; mRNA.
DR   RefSeq; NP_001153005.1; NM_001159533.2.
DR   RefSeq; NP_001153006.1; NM_001159534.2.
DR   RefSeq; NP_001153007.1; NM_001159535.2.
DR   RefSeq; NP_033911.2; NM_009781.4.
DR   SMR; Q0PCR6; -.
DR   jPOST; Q0PCR6; -.
DR   ProteomicsDB; 343167; -.
DR   Antibodypedia; 22118; 528 antibodies from 39 providers.
DR   DNASU; 12288; -.
DR   GeneID; 12288; -.
DR   KEGG; mmu:12288; -.
DR   UCSC; uc009dlu.3; mouse.
DR   AGR; MGI:103013; -.
DR   CTD; 775; -.
DR   MGI; MGI:103013; Cacna1c.
DR   VEuPathDB; HostDB:ENSMUSG00000051331; -.
DR   GeneTree; ENSGT00940000156127; -.
DR   OrthoDB; 431720at2759; -.
DR   BioGRID-ORCS; 12288; 1 hit in 74 CRISPR screens.
DR   Bgee; ENSMUSG00000051331; Expressed in cardiac muscle of left ventricle and 175 other cell types or tissues.
DR   GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR   GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR   GO; GO:0098839; C:postsynaptic density membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030315; C:T-tubule; IEA:UniProtKB-SubCell.
DR   GO; GO:0005891; C:voltage-gated calcium channel complex; IEA:InterPro.
DR   GO; GO:0005245; F:voltage-gated calcium channel activity; IEA:InterPro.
DR   GO; GO:0097553; P:calcium ion transmembrane import into cytosol; IEA:UniProtKB-ARBA.
DR   GO; GO:0007154; P:cell communication; IEA:UniProtKB-ARBA.
DR   GO; GO:0006874; P:intracellular calcium ion homeostasis; IEA:UniProtKB-ARBA.
DR   GO; GO:0008016; P:regulation of heart contraction; IEA:UniProtKB-ARBA.
DR   GO; GO:0042391; P:regulation of membrane potential; IEA:UniProtKB-ARBA.
DR   GO; GO:0023052; P:signaling; IEA:UniProtKB-ARBA.
DR   GO; GO:0003008; P:system process; IEA:UniProtKB-ARBA.
DR   FunFam; 1.10.287.70:FF:000007; Voltage-dependent L-type calcium channel subunit alpha; 1.
DR   FunFam; 1.10.287.70:FF:000009; Voltage-dependent L-type calcium channel subunit alpha; 1.
DR   FunFam; 1.10.287.70:FF:000021; Voltage-dependent L-type calcium channel subunit alpha; 1.
DR   FunFam; 1.20.120.350:FF:000001; Voltage-dependent L-type calcium channel subunit alpha; 1.
DR   FunFam; 1.20.120.350:FF:000006; Voltage-dependent L-type calcium channel subunit alpha; 1.
DR   FunFam; 1.20.120.350:FF:000010; Voltage-dependent L-type calcium channel subunit alpha; 1.
DR   FunFam; 1.20.120.350:FF:000020; Voltage-dependent L-type calcium channel subunit alpha; 1.
DR   FunFam; 1.10.238.10:FF:000063; Voltage-dependent N-type calcium channel subunit alpha; 1.
DR   Gene3D; 1.10.287.70; -; 4.
DR   Gene3D; 6.10.250.2180; -; 1.
DR   Gene3D; 6.10.250.2500; -; 1.
DR   Gene3D; 1.20.120.350; Voltage-gated potassium channels. Chain C; 4.
DR   InterPro; IPR031688; CAC1F_C.
DR   InterPro; IPR031649; GPHH_dom.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR014873; VDCC_a1su_IQ.
DR   InterPro; IPR050599; VDCC_alpha-1_subunit.
DR   InterPro; IPR005451; VDCC_L_a1csu.
DR   InterPro; IPR005446; VDCC_L_a1su.
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; PF08763; Ca_chan_IQ; 1.
DR   Pfam; PF16885; CAC1F_C; 1.
DR   Pfam; PF16905; GPHH; 1.
DR   Pfam; PF00520; Ion_trans; 4.
DR   PRINTS; PR00167; CACHANNEL.
DR   PRINTS; PR01630; LVDCCALPHA1.
DR   PRINTS; PR01635; LVDCCALPHA1C.
DR   SMART; SM01062; Ca_chan_IQ; 1.
DR   SUPFAM; SSF81324; Voltage-gated potassium channels; 4.
PE   1: Evidence at protein level;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PIRSR:PIRSR602077-1};
KW   Calcium channel {ECO:0000256|ARBA:ARBA00022673,
KW   ECO:0000256|RuleBase:RU003808};
KW   Calcium transport {ECO:0000256|ARBA:ARBA00022568,
KW   ECO:0000256|RuleBase:RU003808};
KW   Calmodulin-binding {ECO:0000256|ARBA:ARBA00022860};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180, ECO:0000256|PIRSR:PIRSR602077-
KW   3}; Ion channel {ECO:0000256|ARBA:ARBA00023303};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR602077-1};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Postsynaptic cell membrane {ECO:0000256|ARBA:ARBA00023257};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Synapse {ECO:0000256|ARBA:ARBA00023018};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448};
KW   Voltage-gated channel {ECO:0000256|ARBA:ARBA00022882,
KW   ECO:0000256|RuleBase:RU003808}.
FT   TRANSMEM        158..175
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        195..215
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        227..245
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        298..320
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        379..400
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        412..434
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        555..572
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        592..615
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        684..703
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        756..783
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        926..948
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        968..989
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1047..1076
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1172..1199
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1250..1267
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1279..1301
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1313..1330
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1389..1412
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1482..1506
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1640..1674
FT                   /note="Voltage-dependent calcium channel alpha-1 subunit
FT                   IQ"
FT                   /evidence="ECO:0000259|SMART:SM01062"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          103..128
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          479..511
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          794..891
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1762..1803
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1970..1996
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        110..121
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        495..508
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        813..836
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        873..882
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1762..1771
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1781..1793
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1794..1803
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1977..1987
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         393
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT   BINDING         736
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT   BINDING         1145
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT   CARBOHYD        358
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602077-3"
SQ   SEQUENCE   2169 AA;  243370 MW;  39764022409F63E2 CRC64;
     MIRAFVQPST PPYQPLSSHS SEETERKFKG KVVHEAQLNC FYISPGGSNY GSPRPAHANM
     NANAAAGLAP EHIPTPGAAL SWQAAIDAAR QAKLMGSAGN ATISTVSSTQ RKRQQYGKPK
     KQGGTTATRP PRALLCLTLK NPIRRACISI VEWKPFEIII LLTIFANCVA LAIYIPFPED
     DSNATNSNLE RVEYLFLIIF TVEAFLKVIA YGLLFHPNAY LRNGWNLLDF IIVVVGLFSA
     ILEQATKADG ANALGGKGAG FDVKALRAFR VLRPLRLVSG VPSLQVVLNS IIKAMVPLLH
     IALLVLFVII IYAIIGLELF MGKMHKTCYN QEGIIDVPAE EDPSPCALET GHGRQCQNGT
     VCKPGWDGPK HGITNFDNFA FAMLTVFQCI TMEGWTDVLY WMQDAMGYEL PWVYFVSLVI
     FGSFFVLNLV LGVLSGEFSK EREKAKARGD FQKLREKQQL EEDLKGYLDW ITQAEDIDPE
     NEDEGMDEDK PRNMSMPTSE TESVNTENVA GGDIEGENCG ARLAHRISKS KFSRYWRRWN
     RFCRRKCRAA VKSNVFYWLV IFLVFLNTLT IASEHYNQPH WLTEVQDTAN KALLALFTAE
     MLLKMYSLGL QAYFVSLFNR FDCFIVCGGI LETILVETKI MSPLGISVLR CVRLLRIFKI
     TRYWNSLSNL VASLLNSVRS IASLLLLLFL FIIIFSLLGM QLFGGKFNFD EMQTRRSTFD
     NFPQSLLTVF QILTGEDWNS VMYDGIMAYG GPSFPGMLVC IYFIILFICG NYILLNVFLA
     IAVDNLADAE SLTSAQKEEE EEKERKKLAR TASPEKKQEV MEKPAVEESK EEKIELKSIT
     ADGESPPTTK INMDDLQPSE NEDKSPHSNP DTAGEEDEEE PEMPVGPRPR PLSELHLKEK
     AVPMPEASAF FIFSPNNRFR LQCHRIVNDT IFTNLILFFI LLSSISLAAE DPVQHTSFRN
     HILGNADYVF TSIFTLEIIL KMTAYGAFLH KGSFCRNYFN ILDLLVVSVS LISFGIQSSA
     INVVKILRVL RVLRPLRAIN RAKGLKHVVQ CVFVAIRTIG NIVIVTTLLQ FMFACIGVQL
     FKGKLYTCSD SSKQTEAECK GNYITYKDGE VDHPIIQPRS WENSKFDFDN VLAAMMALFT
     VSTFEGWPEL LYRSIDSHTE DKGPIYNYRV EISIFFIIYI IIIAFFMMNI FVGFVIVTFQ
     EQGEQEYKNC ELDKNQRQCV EYALKARPLR RYIPKNQHQY KVWYVVNSTY FEYLMFVLIL
     LNTICLAMQH YGQSCLFKIA MNILNMLFTG LFTVEMILKL IAFKPKGYFS DPWNVFDFLI
     VIGSIIDVIL SETNPAEHTQ CSPSMSAEEN SRISITFFRL FRVMRLVKLL SRGEGIRTLL
     WTFIKSFQAL PYVALLIVML FFIYAVIGMQ VFGKIALNDT TEINRNNNFQ TFPQAVLLLF
     RCATGEAWQD IMLACMPGKK CAPESEPSNS TEGETPCGSS FAVFYFISFY MLCAFLIINL
     FVAVIMDNFD YLTRDWSILG PHHLDEFKRI WAEYDPEAKG RIKHLDVVTL LRRIQPPLGF
     GKLCPHRVAC KRLVSMNMPL NSDGTVMFNA TLFALVRTAL RIKTEGNLEQ ANEELRAIIK
     KIWKRTSMKL LDQVVPPAGD DEVTVGKFYA TFLIQEYFRK FKKRKEQGLV GKPSQRNALS
     LQAGLRTLHD IGPEIRRAIS GDLTAEEELD KAMKEAVSAA SEDDIFRRAG GLFGNHVTYY
     QSDSRGNFPQ TFATQRPLHI NKTGNNQADT ESPSHEKLVD STFTPSSYSS TGSNANINNA
     NNTALGRFPH PAGYSSTVST VEGHGPPLSP AVRVQEAAWK LSSKRCHSRE SQGATVNQEI
     FPDETRSVRM SEEAEYCSEP SLLSTDMFSY QEDEHRQLTC PEEDKREIQP SPKRSFLRSA
     SLGRRASFHL ECLKRQKDQG GDISQKTALP LHLVHHQALA VAGLSPLLQR SHSPTTFPRP
     CPTPPVTPGS RGRPLRPIPT LRLEGAESSE KLNSSFPSIH CSSWSEETTA CSGSSSMARR
     ARPVSLTVPS QAGAPGRQFH GSASSLVEAV LISEGLGQFA QDPKFIEVTT QELADACDMT
     IEEMENAADN ILSGGAQQSP NGTLLPFVNC RDPGQDRAVA PEDESCAYAL GRGRSEEALA
     DSRSYVSNL
//