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Q01815 (CAC1C_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 132. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Voltage-dependent L-type calcium channel subunit alpha-1C
Alternative name(s):
Calcium channel, L type, alpha-1 polypeptide, isoform 1, cardiac muscle
MELC-CC
Mouse brain class C
Short name=MBC
Voltage-gated calcium channel subunit alpha Cav1.2
Gene names
Name:Cacna1c
Synonyms:Cach2, Cacn2, Cacnl1a1, Cchl1a1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length2139 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Voltage-sensitive calcium channels (VSCC) mediate the entry of calcium ions into excitable cells and are also involved in a variety of calcium-dependent processes, including muscle contraction, hormone or neurotransmitter release, gene expression, cell motility, cell division and cell death. The isoform alpha-1C gives rise to L-type calcium currents. Long-lasting (L-type) calcium channels belong to the 'high-voltage activated' (HVA) group. They are blocked by dihydropyridines (DHP), phenylalkylamines, benzothiazepines, and by omega-agatoxin-IIIA (omega-Aga-IIIA). They are however insensitive to omega-conotoxin-GVIA (omega-CTx-GVIA) and omega-agatoxin-IVA (omega-Aga-IVA). Calcium channels containing the alpha-1C subunit play an important role in excitation-contraction coupling in the heart. Binding of calmodulin or CABP1 at the same regulatory sites results in an opposit effects on the channel function By similarity.

Subunit structure

Voltage-dependent calcium channels are multisubunit complexes, consisting of alpha-1, alpha-2, beta and delta subunits in a 1:1:1:1 ratio. The channel activity is directed by the pore-forming and voltage-sensitive alpha-1 subunit. In many cases, this subunit is sufficient to generate voltage-sensitive calcium channel activity. The auxiliary subunits beta and alpha-2/delta linked by a disulfide bridge regulate the channel activity. Interacts (via C-terminal CDB motif) with CABP5; in a calcium-dependent manner. Interacts with CABP1 and CACNA2D4 By similarity. Ref.6

Subcellular location

Membrane; Multi-pass membrane protein. Cell membrane By similarity. Note: The interaction between RRAD and CACNB2 regulates its trafficking to the cell membrane By similarity.

Tissue specificity

High expression in heart, followed by brain and spinal cord. Expressed in retina in rod bipolar cells. Ref.6

Domain

Each of the four internal repeats contains five hydrophobic transmembrane segments (S1, S2, S3, S5, S6) and one positively charged transmembrane segment (S4). S4 segments probably represent the voltage-sensor and are characterized by a series of positively charged amino acids at every third position.

Binding of intracellular calcium through the EF-hand motif inhibits the opening of the channel By similarity.

Post-translational modification

Phosphorylation by PKA activates the channel By similarity.

Sequence similarities

Belongs to the calcium channel alpha-1 subunit (TC 1.A.1.11) family. CACNA1C subfamily. [View classification]

Ontologies

Keywords
   Biological processCalcium transport
Ion transport
Transport
   Cellular componentCell membrane
Membrane
   Coding sequence diversityAlternative splicing
   DomainRepeat
Transmembrane
Transmembrane helix
   LigandCalcium
Metal-binding
   Molecular functionCalcium channel
Ion channel
Voltage-gated channel
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processadult walking behavior

Inferred from genetic interaction PubMed 9882694. Source: MGI

calcium ion-dependent exocytosis

Inferred from mutant phenotype PubMed 12881419. Source: MGI

cellular calcium ion homeostasis

Inferred from mutant phenotype PubMed 15132976. Source: MGI

glucose homeostasis

Inferred from mutant phenotype PubMed 12881419. Source: MGI

growth hormone secretion

Inferred from direct assay Ref.1. Source: MGI

insulin secretion

Inferred from mutant phenotype PubMed 12881419. Source: MGI

regulation of blood pressure

Inferred from mutant phenotype PubMed 14609949. Source: MGI

regulation of organ growth

Inferred from mutant phenotype PubMed 15132976. Source: MGI

regulation of vasoconstriction

Inferred from mutant phenotype PubMed 14609949. Source: MGI

smooth muscle contraction involved in micturition

Inferred from mutant phenotype PubMed 15132976. Source: MGI

synaptic transmission

Inferred from mutant phenotype PubMed 16251435. Source: MGI

visual learning

Inferred from mutant phenotype PubMed 16251435. Source: MGI

   Cellular_componentT-tubule

Traceable author statement PubMed 11784029. Source: MGI

Z disc

Inferred from direct assay PubMed 19383796. Source: MGI

caveolar macromolecular signaling complex

Inferred from direct assay PubMed 16648270. Source: MGI

dendritic shaft

Inferred from direct assay PubMed 15090038. Source: MGI

neuronal cell body

Inferred from direct assay PubMed 15090038. Source: MGI

voltage-gated calcium channel complex

Traceable author statement PubMed 11296258. Source: MGI

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

voltage-gated calcium channel activity

Inferred from direct assay Ref.1PubMed 16267232PubMed 7635187Ref.4. Source: MGI

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform 1 (identifier: Q01815-1)

Also known as: CACH2A;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q01815-2)

Also known as: CACH2D;

The sequence of this isoform differs from the canonical sequence as follows:
     1277-1304: GYFSDPWNVFDFLIVIGSIIDVILSETN → HYFCDAWNTFDALIVVGSIVDIAITEVH
     1305-1315: Missing.
Isoform 3 (identifier: Q01815-3)

Also known as: Truncated;

The sequence of this isoform differs from the canonical sequence as follows:
     1-264: Missing.
     372-391: MQDAMGYELPWVYFVSLVIF → VNDAVGRDWPWIYFVTLIII
     464-464: M → RGAPAGLHDQKKGKFAWFSHSTETHV
     932-951: Missing.
     1305-1315: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 21392139Voltage-dependent L-type calcium channel subunit alpha-1C
PRO_0000053929

Regions

Topological domain1 – 124124Cytoplasmic Potential
Transmembrane125 – 14319Helical; Name=S1 of repeat I; Potential
Topological domain144 – 16017Extracellular Potential
Transmembrane161 – 18121Helical; Name=S2 of repeat I; Potential
Topological domain182 – 19312Cytoplasmic Potential
Transmembrane194 – 21219Helical; Name=S3 of repeat I; Potential
Topological domain213 – 23220Extracellular Potential
Transmembrane233 – 25119Helical; Name=S4 of repeat I; Potential
Topological domain252 – 27019Cytoplasmic Potential
Transmembrane271 – 29020Helical; Name=S5 of repeat I; Potential
Topological domain291 – 38090Extracellular Potential
Transmembrane381 – 40525Helical; Name=S6 of repeat I; Potential
Topological domain406 – 524119Cytoplasmic Potential
Transmembrane525 – 54319Helical; Name=S1 of repeat II; Potential
Topological domain544 – 55815Extracellular Potential
Transmembrane559 – 57820Helical; Name=S2 of repeat II; Potential
Topological domain579 – 5868Cytoplasmic Potential
Transmembrane587 – 60519Helical; Name=S3 of repeat II; Potential
Topological domain606 – 61510Extracellular Potential
Transmembrane616 – 63419Helical; Name=S4 of repeat II; Potential
Topological domain635 – 65319Cytoplasmic Potential
Transmembrane654 – 67320Helical; Name=S5 of repeat II; Potential
Topological domain674 – 72855Extracellular Potential
Transmembrane729 – 75325Helical; Name=S6 of repeat II; Potential
Topological domain754 – 900147Cytoplasmic Potential
Transmembrane901 – 91919Helical; Name=S1 of repeat III; Potential
Topological domain920 – 93516Extracellular Potential
Transmembrane936 – 95520Helical; Name=S2 of repeat III; Potential
Topological domain956 – 96712Cytoplasmic Potential
Transmembrane968 – 98619Helical; Name=S3 of repeat III; Potential
Topological domain987 – 9937Extracellular Potential
Transmembrane994 – 101219Helical; Name=S4 of repeat III; Potential
Topological domain1013 – 103119Cytoplasmic Potential
Transmembrane1032 – 105120Helical; Name=S5 of repeat III; Potential
Topological domain1052 – 114190Extracellular Potential
Transmembrane1142 – 116625Helical; Name=S6 of repeat III; Potential
Topological domain1167 – 121953Cytoplasmic Potential
Transmembrane1220 – 123819Helical; Name=S1 of repeat IV; Potential
Topological domain1239 – 125315Extracellular Potential
Transmembrane1254 – 127320Helical; Name=S2 of repeat IV; Potential
Topological domain1274 – 12818Cytoplasmic Potential
Transmembrane1282 – 130019Helical; Name=S3 of repeat IV; Potential
Topological domain1301 – 132424Extracellular Potential
Transmembrane1325 – 134319Helical; Name=S4 of repeat IV; Potential
Topological domain1344 – 136219Cytoplasmic Potential
Transmembrane1363 – 138220Helical; Name=S5 of repeat IV; Potential
Topological domain1383 – 145169Extracellular Potential
Transmembrane1452 – 147625Helical; Name=S6 of repeat IV; Potential
Topological domain1477 – 2139663Cytoplasmic Potential
Repeat111 – 408298I
Repeat510 – 756247II
Repeat887 – 1169283III
Repeat1206 – 1479274IV
Calcium binding1505 – 151612 By similarity
Region428 – 44518Binding to the beta subunit By similarity
Compositional bias654 – 6607Poly-Leu
Compositional bias768 – 7747Poly-Glu
Compositional bias1147 – 11537Poly-Ile

Sites

Site3631Calcium ion selectivity and permeability By similarity
Site7061Calcium ion selectivity and permeability By similarity
Site11151Calcium ion selectivity and permeability By similarity
Site14161Calcium ion selectivity and permeability By similarity

Amino acid modifications

Modified residue8151Phosphoserine Ref.5
Modified residue14871Phosphoserine; by PKA Potential
Modified residue18891Phosphoserine; by PKA Potential
Modified residue18971Phosphoserine; by PKA Potential
Glycosylation1531N-linked (GlcNAc...) Potential
Glycosylation3281N-linked (GlcNAc...) Potential
Glycosylation13881N-linked (GlcNAc...) Potential
Glycosylation14391N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence1 – 264264Missing in isoform 3.
VSP_000896
Alternative sequence372 – 39120MQDAM…SLVIF → VNDAVGRDWPWIYFVTLIII in isoform 3.
VSP_000897
Alternative sequence4641M → RGAPAGLHDQKKGKFAWFSH STETHV in isoform 3.
VSP_000898
Alternative sequence932 – 95120Missing in isoform 3.
VSP_000899
Alternative sequence1277 – 130428GYFSD…LSETN → HYFCDAWNTFDALIVVGSIV DIAITEVH in isoform 2.
VSP_000900
Alternative sequence1305 – 131511Missing in isoform 2 and isoform 3.
VSP_000901

Experimental info

Sequence conflict3101E → K in AAA62612. Ref.4
Sequence conflict4771E → D in AAA62612. Ref.4
Sequence conflict5551V → D in AAA62612. Ref.4
Sequence conflict811 – 8122AD → GS in AAA62612. Ref.4
Sequence conflict8221N → H in AAA62612. Ref.4
Sequence conflict8251D → A in AAA62612. Ref.4
Sequence conflict8311N → P in AAA62612. Ref.4
Sequence conflict837 – 8415HSNPD → TPTQT in AAA37351. Ref.3
Sequence conflict934 – 9385GNADY → FYFDI in AAA37351. Ref.3
Sequence conflict9421S → T in AAA37351. Ref.3
Sequence conflict9461L → I in AAA37351. Ref.3
Sequence conflict9491I → A in AAA37351. Ref.3
Sequence conflict977 – 9782VS → LC in AAA62612. Ref.4
Sequence conflict10651T → A in AAA62612. Ref.4
Sequence conflict15071E → K in AAA62612. Ref.4
Sequence conflict15251Q → H in AAA62612. Ref.4
Sequence conflict16331K → E in AAA62612. Ref.4
Sequence conflict19591G → A in AAA62612. Ref.4
Sequence conflict1963 – 19642RP → ST in AAA62612. Ref.4
Sequence conflict19701T → H in AAA62612. Ref.4
Sequence conflict19741E → K in AAA62612. Ref.4
Sequence conflict20861A → R in AAA62612. Ref.4
Sequence conflict20971F → L in AAA62612. Ref.4
Sequence conflict21101A → V in AAA62612. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (CACH2A) [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: B564C57A8644E165

FASTA2,139240,138
        10         20         30         40         50         60 
MVNENTRMYV PEENHQGSNY GSPRPAHANM NANAAAGLAP EHIPTPGAAL SWQAAIDAAR 

        70         80         90        100        110        120 
QAKLMGSAGN ATISTVSSTQ RKRQQYGKPK KQGGTTATRP PRALLCLTLK NPIRRACISI 

       130        140        150        160        170        180 
VEWKPFEIII LLTIFANCVA LAIYIPFPED DSNATNSNLE RVEYLFLIIF TVEAFLKVIA 

       190        200        210        220        230        240 
YGLLFHPNAY LRNGWNLLDF IIVVVGLFSA ILEQATKADG ANALGGKGAG FDVKALRAFR 

       250        260        270        280        290        300 
VLRPLRLVSG VPSLQVVLNS IIKAMVPLLH IALLVLFVII IYAIIGLELF MGKMHKTCYN 

       310        320        330        340        350        360 
QEGIIDVPAE EDPSPCALET GHGRQCQNGT VCKPGWDGPK HGITNFDNFA FAMLTVFQCI 

       370        380        390        400        410        420 
TMEGWTDVLY WMQDAMGYEL PWVYFVSLVI FGSFFVLNLV LGVLSGEFSK EREKAKARGD 

       430        440        450        460        470        480 
FQKLREKQQL EEDLKGYLDW ITQAEDIDPE NEDEGMDEDK PRNMSMPTSE TESVNTENVA 

       490        500        510        520        530        540 
GGDIEGENCG ARLAHRISKS KFSRYWRRWN RFCRRKCRAA VKSNVFYWLV IFLVFLNTLT 

       550        560        570        580        590        600 
IASEHYNQPH WLTEVQDTAN KALLALFTAE MLLKMYSLGL QAYFVSLFNR FDCFIVCGGI 

       610        620        630        640        650        660 
LETILVETKI MSPLGISVLR CVRLLRIFKI TRYWNSLSNL VASLLNSVRS IASLLLLLFL 

       670        680        690        700        710        720 
FIIIFSLLGM QLFGGKFNFD EMQTRRSTFD NFPQSLLTVF QILTGEDWNS VMYDGIMAYG 

       730        740        750        760        770        780 
GPSFPGMLVC IYFIILFICG NYILLNVFLA IAVDNLADAE SLTSAQKEEE EEKERKKLAR 

       790        800        810        820        830        840 
TASPEKKQEV MEKPAVEESK EEKIELKSIT ADGESPPTTK INMDDLQPSE NEDKSPHSNP 

       850        860        870        880        890        900 
DTAGEEDEEE PEMPVGPRPR PLSELHLKEK AVPMPEASAF FIFSPNNRFR LQCHRIVNDT 

       910        920        930        940        950        960 
IFTNLILFFI LLSSISLAAE DPVQHTSFRN HILGNADYVF TSIFTLEIIL KMTAYGAFLH 

       970        980        990       1000       1010       1020 
KGSFCRNYFN ILDLLVVSVS LISFGIQSSA INVVKILRVL RVLRPLRAIN RAKGLKHVVQ 

      1030       1040       1050       1060       1070       1080 
CVFVAIRTIG NIVIVTTLLQ FMFACIGVQL FKGKLYTCSD SSKQTEAECK GNYITYKDGE 

      1090       1100       1110       1120       1130       1140 
VDHPIIQPRS WENSKFDFDN VLAAMMALFT VSTFEGWPEL LYRSIDSHTE DKGPIYNYRV 

      1150       1160       1170       1180       1190       1200 
EISIFFIIYI IIIAFFMMNI FVGFVIVTFQ EQGEQEYKNC ELDKNQRQCV EYALKARPLR 

      1210       1220       1230       1240       1250       1260 
RYIPKNQHQY KVWYVVNSTY FEYLMFVLIL LNTICLAMQH YGQSCLFKIA MNILNMLFTG 

      1270       1280       1290       1300       1310       1320 
LFTVEMILKL IAFKPKGYFS DPWNVFDFLI VIGSIIDVIL SETNPAEHTQ CSPSMSAEEN 

      1330       1340       1350       1360       1370       1380 
SRISITFFRL FRVMRLVKLL SRGEGIRTLL WTFIKSFQAL PYVALLIVML FFIYAVIGMQ 

      1390       1400       1410       1420       1430       1440 
VFGKIALNDT TEINRNNNFQ TFPQAVLLLF RCATGEAWQD IMLACMPGKK CAPESEPSNS 

      1450       1460       1470       1480       1490       1500 
TEGETPCGSS FAVFYFISFY MLCAFLIINL FVAVIMDNFD YLTRDWSILG PHHLDEFKRI 

      1510       1520       1530       1540       1550       1560 
WAEYDPEAKG RIKHLDVVTL LRRIQPPLGF GKLCPHRVAC KRLVSMNMPL NSDGTVMFNA 

      1570       1580       1590       1600       1610       1620 
TLFALVRTAL RIKTEGNLEQ ANEELRAIIK KIWKRTSMKL LDQVVPPAGD DEVTVGKFYA 

      1630       1640       1650       1660       1670       1680 
TFLIQEYFRK FKKRKEQGLV GKPSQRNALS LQAGLRTLHD IGPEIRRAIS GDLTAEEELD 

      1690       1700       1710       1720       1730       1740 
KAMKEAVSAA SEDDIFRRAG GLFGNHVTYY QSDSRGNFPQ TFATQRPLHI NKTGNNQADT 

      1750       1760       1770       1780       1790       1800 
ESPSHEKLVD STFTPSSYSS TGSNANINNA NNTALGRFPH PAGYSSTVST VEGHGPPLSP 

      1810       1820       1830       1840       1850       1860 
AVRVQEAAWK LSSKRCHSRE SQGATVNQEI FPDETRSVRM SEEAEYCSEP SLLSTDMFSY 

      1870       1880       1890       1900       1910       1920 
QEDEHRQLTC PEEDKREIQP SPKRSFLRSA SLGRRASFHL ECLKRQKDQG GDISQKTALP 

      1930       1940       1950       1960       1970       1980 
LHLVHHQALA VAGLSPLLQR SHSPTTFPRP CPTPPVTPGS RGRPLRPIPT LRLEGAESSE 

      1990       2000       2010       2020       2030       2040 
KLNSSFPSIH CSSWSEETTA CSGSSSMARR ARPVSLTVPS QAGAPGRQFH GSASSLVEAV 

      2050       2060       2070       2080       2090       2100 
LISEGLGQFA QDPKFIEVTT QELADACDMT IEEMENAADN ILSGGAQQSP NGTLLPFVNC 

      2110       2120       2130 
RDPGQDRAVA PEDESCAYAL GRGRSEEALA DSRSYVSNL

« Hide

Isoform 2 (CACH2D) [UniParc].

Checksum: DF7AFC8BF97FE15B
Show »

FASTA2,128238,944
Isoform 3 (Truncated) [UniParc].

Checksum: A8DC3D7154C30AE2
Show »

FASTA1,869210,822

References

« Hide 'large scale' references
[1]"Expression of a cDNA for a neuronal calcium channel alpha1 subunit enhances secretion from adrenal chromaffin cells."
Ma W.-J., Holz R.W., Uhler M.D.
J. Biol. Chem. 267:22728-22732(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING.
Tissue: Brain.
[2]"Molecular diversity of L-type calcium channels. Evidence for alternative splicing of the transcripts of three non-allelic genes."
Perez-Reyes E., Wei X., Castellano A., Birnbaumer L.
J. Biol. Chem. 265:20430-20436(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1162-1455 (ISOFORMS 1 AND 2).
Strain: ICR.
Tissue: Ovary.
[3]Chaudhari N.
Submitted (JAN-1993) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 762-1070.
[4]"Cloning and expression of a novel truncated calcium channel from non-excitable cells."
Ma Y., Kobrinsky E., Marks A.R.
J. Biol. Chem. 270:483-493(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 265-2139 (ISOFORM 3).
Strain: DBA/2J.
Tissue: Erythroleukemia.
[5]"Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations."
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M.
Mol. Cell. Proteomics 6:283-293(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-815, MASS SPECTROMETRY.
Tissue: Brain cortex.
[6]"Characterization of Ca2+-binding protein 5 knockout mouse retina."
Rieke F., Lee A., Haeseleer F.
Invest. Ophthalmol. Vis. Sci. 49:5126-5135(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CABP5, TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		L01776 mRNA. Translation: AAB59633.1.
M57973 mRNA. Translation: AAA63291.1.
L06233 mRNA. Translation: AAA37351.1.
U17869 mRNA. Translation: AAA62612.1.
IPIIPI00229513.
IPI00277044.
IPI00875159.
PIRA44467.
RefSeqNP_001153005.1. NM_001159533.1.
UniGeneMm.436656.

3D structure databases

ProteinModelPortalQ01815.
SMRQ01815. Positions 162-404, 419-447, 519-754, 891-1165, 1208-1477, 1560-1640.
ModBaseSearch...

Protein-protein interaction databases

IntActQ01815. 2 interactions.
MINTMINT-103522.

Protein family/group databases

TCDB1.A.1.11.6. voltage-gated ion channel (VIC) superfamily.

PTM databases

PhosphoSiteQ01815.

Proteomic databases

PaxDbQ01815.
PRIDEQ01815.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000112825; ENSMUSP00000108444; ENSMUSG00000051331.
GeneID12288.
KEGGmmu:12288.
UCSCuc009dls.2. mouse.
uc012erl.1. mouse.

Organism-specific databases

CTD775.
MGIMGI:103013. Cacna1c.

Phylogenomic databases

eggNOGCOG1226.
GeneTreeENSGT00680000099727.
HOGENOMHOG000231529.
HOVERGENHBG050763.
KOK04850.

Enzyme and pathway databases

ReactomeREACT_127416. Developmental Biology.

Gene expression databases

ArrayExpressQ01815.
BgeeQ01815.
GenevestigatorQ01815.
GermOnlineENSMUSG00000051331. Mus musculus.

Family and domain databases

InterProIPR005821. Ion_trans_dom.
IPR014873. VDCC_a1su_IQ.
IPR005451. VDCC_L_a1csu.
IPR005446. VDCC_L_a1su.
IPR002077. VDCCAlpha1.
[Graphical view]
PANTHERPTHR10037:SF47. PTHR10037:SF47. 1 hit.
PfamPF08763. Ca_chan_IQ. 1 hit.
PF00520. Ion_trans. 4 hits.
[Graphical view]
PRINTSPR00167. CACHANNEL.
PR01630. LVDCCALPHA1.
PR01635. LVDCCALPHA1C.
SMARTSM01062. Ca_chan_IQ. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

BindingDBQ01815.
ChEMBLCHEMBL2529.
ChiTaRSCACNA1C. mouse.
NextBio280766.
SOURCESearch...

Entry information

Entry nameCAC1C_MOUSE
AccessionPrimary (citable) accession number: Q01815
Secondary accession number(s): Q04476, Q61242, Q99242
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: November 1, 1996
Last modified: May 1, 2013
This is version 132 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

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