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Q01815

- CAC1C_MOUSE

UniProt

Q01815 - CAC1C_MOUSE

Protein

Voltage-dependent L-type calcium channel subunit alpha-1C

Gene

Cacna1c

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 147 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    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.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei363 – 3631Calcium ion selectivity and permeabilityBy similarity
    Sitei706 – 7061Calcium ion selectivity and permeabilityBy similarity
    Sitei1115 – 11151Calcium ion selectivity and permeabilityBy similarity
    Sitei1416 – 14161Calcium ion selectivity and permeabilityBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Calcium bindingi1505 – 151612By similarityAdd
    BLAST

    GO - Molecular functioni

    1. enzyme binding Source: BHF-UCL
    2. high voltage-gated calcium channel activity Source: RefGenome
    3. metal ion binding Source: UniProtKB-KW
    4. protein binding Source: BHF-UCL
    5. voltage-gated calcium channel activity Source: MGI

    GO - Biological processi

    1. adult walking behavior Source: MGI
    2. calcium ion-dependent exocytosis Source: MGI
    3. calcium ion import Source: RefGenome
    4. calcium ion transport Source: MGI
    5. cellular calcium ion homeostasis Source: MGI
    6. glucose homeostasis Source: MGI
    7. growth hormone secretion Source: MGI
    8. insulin secretion Source: MGI
    9. membrane depolarization during action potential Source: RefGenome
    10. regulation of blood pressure Source: MGI
    11. regulation of organ growth Source: MGI
    12. regulation of vasoconstriction Source: MGI
    13. smooth muscle contraction Source: MGI
    14. smooth muscle contraction involved in micturition Source: MGI
    15. synaptic transmission Source: MGI
    16. visual learning Source: MGI

    Keywords - Molecular functioni

    Calcium channel, Ion channel, Voltage-gated channel

    Keywords - Biological processi

    Calcium transport, Ion transport, Transport

    Keywords - Ligandi

    Calcium, Metal-binding

    Protein family/group databases

    TCDBi1.A.1.11.6. the voltage-gated ion channel (vic) superfamily.

    Names & Taxonomyi

    Protein namesi
    Recommended 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 namesi
    Name:Cacna1c
    Synonyms:Cach2, Cacn2, Cacnl1a1, Cchl1a1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 6

    Organism-specific databases

    MGIiMGI:103013. Cacna1c.

    Subcellular locationi

    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

    GO - Cellular componenti

    1. caveolar macromolecular signaling complex Source: MGI
    2. dendritic shaft Source: MGI
    3. membrane Source: MGI
    4. neuronal cell body Source: MGI
    5. plasma membrane Source: MGI
    6. T-tubule Source: MGI
    7. voltage-gated calcium channel complex Source: MGI
    8. Z disc Source: MGI

    Keywords - Cellular componenti

    Cell membrane, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 21392139Voltage-dependent L-type calcium channel subunit alpha-1CPRO_0000053929Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi153 – 1531N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi328 – 3281N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1388 – 13881N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1439 – 14391N-linked (GlcNAc...)Sequence Analysis
    Modified residuei1487 – 14871Phosphoserine; by PKASequence Analysis
    Modified residuei1889 – 18891Phosphoserine; by PKASequence Analysis
    Modified residuei1897 – 18971Phosphoserine; by PKASequence Analysis

    Post-translational modificationi

    Phosphorylation by PKA activates the channel.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    PaxDbiQ01815.
    PRIDEiQ01815.

    PTM databases

    PhosphoSiteiQ01815.

    Expressioni

    Tissue specificityi

    High expression in heart, followed by brain and spinal cord. Expressed in retina in rod bipolar cells.1 Publication

    Gene expression databases

    ArrayExpressiQ01815.
    BgeeiQ01815.
    GenevestigatoriQ01815.

    Interactioni

    Subunit structurei

    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. Interacts with CIB1; the interaction increases upon cardiomyocytes hypertrophy.By similarity2 Publications

    Protein-protein interaction databases

    BioGridi198432. 4 interactions.
    IntActiQ01815. 4 interactions.
    MINTiMINT-103522.

    Structurei

    3D structure databases

    ProteinModelPortaliQ01815.
    SMRiQ01815. Positions 128-416, 419-447, 519-808, 891-1165, 1221-1480, 1560-1640.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 124124CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini144 – 16017ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini182 – 19312CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini213 – 23220ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini252 – 27019CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini291 – 38090ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini406 – 524119CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini544 – 55815ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini579 – 5868CytoplasmicSequence Analysis
    Topological domaini606 – 61510ExtracellularSequence Analysis
    Topological domaini635 – 65319CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini674 – 72855ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini754 – 900147CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini920 – 93516ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini956 – 96712CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini987 – 9937ExtracellularSequence Analysis
    Topological domaini1013 – 103119CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini1052 – 114190ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1167 – 121953CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini1239 – 125315ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1274 – 12818CytoplasmicSequence Analysis
    Topological domaini1301 – 132424ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1344 – 136219CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini1383 – 145169ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1477 – 2139663CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei125 – 14319Helical; Name=S1 of repeat ISequence AnalysisAdd
    BLAST
    Transmembranei161 – 18121Helical; Name=S2 of repeat ISequence AnalysisAdd
    BLAST
    Transmembranei194 – 21219Helical; Name=S3 of repeat ISequence AnalysisAdd
    BLAST
    Transmembranei233 – 25119Helical; Name=S4 of repeat ISequence AnalysisAdd
    BLAST
    Transmembranei271 – 29020Helical; Name=S5 of repeat ISequence AnalysisAdd
    BLAST
    Transmembranei381 – 40525Helical; Name=S6 of repeat ISequence AnalysisAdd
    BLAST
    Transmembranei525 – 54319Helical; Name=S1 of repeat IISequence AnalysisAdd
    BLAST
    Transmembranei559 – 57820Helical; Name=S2 of repeat IISequence AnalysisAdd
    BLAST
    Transmembranei587 – 60519Helical; Name=S3 of repeat IISequence AnalysisAdd
    BLAST
    Transmembranei616 – 63419Helical; Name=S4 of repeat IISequence AnalysisAdd
    BLAST
    Transmembranei654 – 67320Helical; Name=S5 of repeat IISequence AnalysisAdd
    BLAST
    Transmembranei729 – 75325Helical; Name=S6 of repeat IISequence AnalysisAdd
    BLAST
    Transmembranei901 – 91919Helical; Name=S1 of repeat IIISequence AnalysisAdd
    BLAST
    Transmembranei936 – 95520Helical; Name=S2 of repeat IIISequence AnalysisAdd
    BLAST
    Transmembranei968 – 98619Helical; Name=S3 of repeat IIISequence AnalysisAdd
    BLAST
    Transmembranei994 – 101219Helical; Name=S4 of repeat IIISequence AnalysisAdd
    BLAST
    Transmembranei1032 – 105120Helical; Name=S5 of repeat IIISequence AnalysisAdd
    BLAST
    Transmembranei1142 – 116625Helical; Name=S6 of repeat IIISequence AnalysisAdd
    BLAST
    Transmembranei1220 – 123819Helical; Name=S1 of repeat IVSequence AnalysisAdd
    BLAST
    Transmembranei1254 – 127320Helical; Name=S2 of repeat IVSequence AnalysisAdd
    BLAST
    Transmembranei1282 – 130019Helical; Name=S3 of repeat IVSequence AnalysisAdd
    BLAST
    Transmembranei1325 – 134319Helical; Name=S4 of repeat IVSequence AnalysisAdd
    BLAST
    Transmembranei1363 – 138220Helical; Name=S5 of repeat IVSequence AnalysisAdd
    BLAST
    Transmembranei1452 – 147625Helical; Name=S6 of repeat IVSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati111 – 408298IAdd
    BLAST
    Repeati510 – 756247IIAdd
    BLAST
    Repeati887 – 1169283IIIAdd
    BLAST
    Repeati1206 – 1479274IVAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni428 – 44518Binding to the beta subunitBy similarityAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi654 – 6607Poly-Leu
    Compositional biasi768 – 7747Poly-Glu
    Compositional biasi1147 – 11537Poly-Ile

    Domaini

    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

    Sequence similaritiesi

    Keywords - Domaini

    Repeat, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG1226.
    GeneTreeiENSGT00750000117620.
    HOGENOMiHOG000231529.
    HOVERGENiHBG050763.
    KOiK04850.
    PhylomeDBiQ01815.

    Family and domain databases

    Gene3Di1.20.120.350. 4 hits.
    InterProiIPR027359. Channel_four-helix_dom.
    IPR005821. Ion_trans_dom.
    IPR014873. VDCC_a1su_IQ.
    IPR005451. VDCC_L_a1csu.
    IPR005446. VDCC_L_a1su.
    IPR002077. VDCCAlpha1.
    [Graphical view]
    PfamiPF08763. Ca_chan_IQ. 1 hit.
    PF00520. Ion_trans. 4 hits.
    [Graphical view]
    PRINTSiPR00167. CACHANNEL.
    PR01630. LVDCCALPHA1.
    PR01635. LVDCCALPHA1C.
    SMARTiSM01062. Ca_chan_IQ. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Note: Additional isoforms seem to exist.

    Isoform 1 (identifier: Q01815-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MVNENTRMYV PEENHQGSNY GSPRPAHANM NANAAAGLAP EHIPTPGAAL     50
    SWQAAIDAAR QAKLMGSAGN ATISTVSSTQ RKRQQYGKPK KQGGTTATRP 100
    PRALLCLTLK NPIRRACISI VEWKPFEIII LLTIFANCVA LAIYIPFPED 150
    DSNATNSNLE RVEYLFLIIF TVEAFLKVIA YGLLFHPNAY LRNGWNLLDF 200
    IIVVVGLFSA ILEQATKADG ANALGGKGAG FDVKALRAFR VLRPLRLVSG 250
    VPSLQVVLNS IIKAMVPLLH IALLVLFVII IYAIIGLELF MGKMHKTCYN 300
    QEGIIDVPAE EDPSPCALET GHGRQCQNGT VCKPGWDGPK HGITNFDNFA 350
    FAMLTVFQCI TMEGWTDVLY WMQDAMGYEL PWVYFVSLVI FGSFFVLNLV 400
    LGVLSGEFSK EREKAKARGD FQKLREKQQL EEDLKGYLDW ITQAEDIDPE 450
    NEDEGMDEDK PRNMSMPTSE TESVNTENVA GGDIEGENCG ARLAHRISKS 500
    KFSRYWRRWN RFCRRKCRAA VKSNVFYWLV IFLVFLNTLT IASEHYNQPH 550
    WLTEVQDTAN KALLALFTAE MLLKMYSLGL QAYFVSLFNR FDCFIVCGGI 600
    LETILVETKI MSPLGISVLR CVRLLRIFKI TRYWNSLSNL VASLLNSVRS 650
    IASLLLLLFL FIIIFSLLGM QLFGGKFNFD EMQTRRSTFD NFPQSLLTVF 700
    QILTGEDWNS VMYDGIMAYG GPSFPGMLVC IYFIILFICG NYILLNVFLA 750
    IAVDNLADAE SLTSAQKEEE EEKERKKLAR TASPEKKQEV MEKPAVEESK 800
    EEKIELKSIT ADGESPPTTK INMDDLQPSE NEDKSPHSNP DTAGEEDEEE 850
    PEMPVGPRPR PLSELHLKEK AVPMPEASAF FIFSPNNRFR LQCHRIVNDT 900
    IFTNLILFFI LLSSISLAAE DPVQHTSFRN HILGNADYVF TSIFTLEIIL 950
    KMTAYGAFLH KGSFCRNYFN ILDLLVVSVS LISFGIQSSA INVVKILRVL 1000
    RVLRPLRAIN RAKGLKHVVQ CVFVAIRTIG NIVIVTTLLQ FMFACIGVQL 1050
    FKGKLYTCSD SSKQTEAECK GNYITYKDGE VDHPIIQPRS WENSKFDFDN 1100
    VLAAMMALFT VSTFEGWPEL LYRSIDSHTE DKGPIYNYRV EISIFFIIYI 1150
    IIIAFFMMNI FVGFVIVTFQ EQGEQEYKNC ELDKNQRQCV EYALKARPLR 1200
    RYIPKNQHQY KVWYVVNSTY FEYLMFVLIL LNTICLAMQH YGQSCLFKIA 1250
    MNILNMLFTG LFTVEMILKL IAFKPKGYFS DPWNVFDFLI VIGSIIDVIL 1300
    SETNPAEHTQ CSPSMSAEEN SRISITFFRL FRVMRLVKLL SRGEGIRTLL 1350
    WTFIKSFQAL PYVALLIVML FFIYAVIGMQ VFGKIALNDT TEINRNNNFQ 1400
    TFPQAVLLLF RCATGEAWQD IMLACMPGKK CAPESEPSNS TEGETPCGSS 1450
    FAVFYFISFY MLCAFLIINL FVAVIMDNFD YLTRDWSILG PHHLDEFKRI 1500
    WAEYDPEAKG RIKHLDVVTL LRRIQPPLGF GKLCPHRVAC KRLVSMNMPL 1550
    NSDGTVMFNA TLFALVRTAL RIKTEGNLEQ ANEELRAIIK KIWKRTSMKL 1600
    LDQVVPPAGD DEVTVGKFYA TFLIQEYFRK FKKRKEQGLV GKPSQRNALS 1650
    LQAGLRTLHD IGPEIRRAIS GDLTAEEELD KAMKEAVSAA SEDDIFRRAG 1700
    GLFGNHVTYY QSDSRGNFPQ TFATQRPLHI NKTGNNQADT ESPSHEKLVD 1750
    STFTPSSYSS TGSNANINNA NNTALGRFPH PAGYSSTVST VEGHGPPLSP 1800
    AVRVQEAAWK LSSKRCHSRE SQGATVNQEI FPDETRSVRM SEEAEYCSEP 1850
    SLLSTDMFSY QEDEHRQLTC PEEDKREIQP SPKRSFLRSA SLGRRASFHL 1900
    ECLKRQKDQG GDISQKTALP LHLVHHQALA VAGLSPLLQR SHSPTTFPRP 1950
    CPTPPVTPGS RGRPLRPIPT LRLEGAESSE KLNSSFPSIH CSSWSEETTA 2000
    CSGSSSMARR ARPVSLTVPS QAGAPGRQFH GSASSLVEAV LISEGLGQFA 2050
    QDPKFIEVTT QELADACDMT IEEMENAADN ILSGGAQQSP NGTLLPFVNC 2100
    RDPGQDRAVA PEDESCAYAL GRGRSEEALA DSRSYVSNL 2139
    Length:2,139
    Mass (Da):240,138
    Last modified:November 1, 1996 - v1
    Checksum:iB564C57A8644E165
    GO
    Isoform 2 (identifier: Q01815-2) [UniParc]FASTAAdd to Basket

    Also known as: CACH2D

    The sequence of this isoform differs from the canonical sequence as follows:
         1277-1304: GYFSDPWNVFDFLIVIGSIIDVILSETN → HYFCDAWNTFDALIVVGSIVDIAITEVH
         1305-1315: Missing.

    Show »
    Length:2,128
    Mass (Da):238,944
    Checksum:iDF7AFC8BF97FE15B
    GO
    Isoform 3 (identifier: Q01815-3) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:1,869
    Mass (Da):210,822
    Checksum:iA8DC3D7154C30AE2
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti310 – 3101E → K in AAA62612. (PubMed:7814415)Curated
    Sequence conflicti477 – 4771E → D in AAA62612. (PubMed:7814415)Curated
    Sequence conflicti555 – 5551V → D in AAA62612. (PubMed:7814415)Curated
    Sequence conflicti811 – 8122AD → GS in AAA62612. (PubMed:7814415)Curated
    Sequence conflicti822 – 8221N → H in AAA62612. (PubMed:7814415)Curated
    Sequence conflicti825 – 8251D → A in AAA62612. (PubMed:7814415)Curated
    Sequence conflicti831 – 8311N → P in AAA62612. (PubMed:7814415)Curated
    Sequence conflicti837 – 8415HSNPD → TPTQT in AAA37351. 1 PublicationCurated
    Sequence conflicti934 – 9385GNADY → FYFDI in AAA37351. 1 PublicationCurated
    Sequence conflicti942 – 9421S → T in AAA37351. 1 PublicationCurated
    Sequence conflicti946 – 9461L → I in AAA37351. 1 PublicationCurated
    Sequence conflicti949 – 9491I → A in AAA37351. 1 PublicationCurated
    Sequence conflicti977 – 9782VS → LC in AAA62612. (PubMed:7814415)Curated
    Sequence conflicti1065 – 10651T → A in AAA62612. (PubMed:7814415)Curated
    Sequence conflicti1507 – 15071E → K in AAA62612. (PubMed:7814415)Curated
    Sequence conflicti1525 – 15251Q → H in AAA62612. (PubMed:7814415)Curated
    Sequence conflicti1633 – 16331K → E in AAA62612. (PubMed:7814415)Curated
    Sequence conflicti1959 – 19591G → A in AAA62612. (PubMed:7814415)Curated
    Sequence conflicti1963 – 19642RP → ST in AAA62612. (PubMed:7814415)Curated
    Sequence conflicti1970 – 19701T → H in AAA62612. (PubMed:7814415)Curated
    Sequence conflicti1974 – 19741E → K in AAA62612. (PubMed:7814415)Curated
    Sequence conflicti2086 – 20861A → R in AAA62612. (PubMed:7814415)Curated
    Sequence conflicti2097 – 20971F → L in AAA62612. (PubMed:7814415)Curated
    Sequence conflicti2110 – 21101A → V in AAA62612. (PubMed:7814415)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 264264Missing in isoform 3. 1 PublicationVSP_000896Add
    BLAST
    Alternative sequencei372 – 39120MQDAM…SLVIF → VNDAVGRDWPWIYFVTLIII in isoform 3. 1 PublicationVSP_000897Add
    BLAST
    Alternative sequencei464 – 4641M → RGAPAGLHDQKKGKFAWFSH STETHV in isoform 3. 1 PublicationVSP_000898
    Alternative sequencei932 – 95120Missing in isoform 3. 1 PublicationVSP_000899Add
    BLAST
    Alternative sequencei1277 – 130428GYFSD…LSETN → HYFCDAWNTFDALIVVGSIV DIAITEVH in isoform 2. 1 PublicationVSP_000900Add
    BLAST
    Alternative sequencei1305 – 131511Missing in isoform 2 and isoform 3. 2 PublicationsVSP_000901Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L01776 mRNA. Translation: AAB59633.1.
    M57973 mRNA. Translation: AAA63291.1.
    L06233 mRNA. Translation: AAA37351.1.
    U17869 mRNA. Translation: AAA62612.1.
    CCDSiCCDS71821.1. [Q01815-3]
    PIRiA44467.
    RefSeqiNP_001153005.1. NM_001159533.2. [Q01815-1]
    UniGeneiMm.41628.
    Mm.436656.

    Genome annotation databases

    EnsembliENSMUST00000112825; ENSMUSP00000108444; ENSMUSG00000051331. [Q01815-3]
    GeneIDi12288.
    KEGGimmu:12288.
    UCSCiuc009dls.2. mouse. [Q01815-3]
    uc012erl.1. mouse. [Q01815-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L01776 mRNA. Translation: AAB59633.1 .
    M57973 mRNA. Translation: AAA63291.1 .
    L06233 mRNA. Translation: AAA37351.1 .
    U17869 mRNA. Translation: AAA62612.1 .
    CCDSi CCDS71821.1. [Q01815-3 ]
    PIRi A44467.
    RefSeqi NP_001153005.1. NM_001159533.2. [Q01815-1 ]
    UniGenei Mm.41628.
    Mm.436656.

    3D structure databases

    ProteinModelPortali Q01815.
    SMRi Q01815. Positions 128-416, 419-447, 519-808, 891-1165, 1221-1480, 1560-1640.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 198432. 4 interactions.
    IntActi Q01815. 4 interactions.
    MINTi MINT-103522.

    Chemistry

    BindingDBi Q01815.
    ChEMBLi CHEMBL2529.
    GuidetoPHARMACOLOGYi 529.

    Protein family/group databases

    TCDBi 1.A.1.11.6. the voltage-gated ion channel (vic) superfamily.

    PTM databases

    PhosphoSitei Q01815.

    Proteomic databases

    PaxDbi Q01815.
    PRIDEi Q01815.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000112825 ; ENSMUSP00000108444 ; ENSMUSG00000051331 . [Q01815-3 ]
    GeneIDi 12288.
    KEGGi mmu:12288.
    UCSCi uc009dls.2. mouse. [Q01815-3 ]
    uc012erl.1. mouse. [Q01815-1 ]

    Organism-specific databases

    CTDi 775.
    MGIi MGI:103013. Cacna1c.

    Phylogenomic databases

    eggNOGi COG1226.
    GeneTreei ENSGT00750000117620.
    HOGENOMi HOG000231529.
    HOVERGENi HBG050763.
    KOi K04850.
    PhylomeDBi Q01815.

    Miscellaneous databases

    ChiTaRSi CACNA1C. mouse.
    NextBioi 280766.
    PROi Q01815.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q01815.
    Bgeei Q01815.
    Genevestigatori Q01815.

    Family and domain databases

    Gene3Di 1.20.120.350. 4 hits.
    InterProi IPR027359. Channel_four-helix_dom.
    IPR005821. Ion_trans_dom.
    IPR014873. VDCC_a1su_IQ.
    IPR005451. VDCC_L_a1csu.
    IPR005446. VDCC_L_a1su.
    IPR002077. VDCCAlpha1.
    [Graphical view ]
    Pfami PF08763. Ca_chan_IQ. 1 hit.
    PF00520. Ion_trans. 4 hits.
    [Graphical view ]
    PRINTSi PR00167. CACHANNEL.
    PR01630. LVDCCALPHA1.
    PR01635. LVDCCALPHA1C.
    SMARTi SM01062. Ca_chan_IQ. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. "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.
    6. Cited for: INTERACTION WITH CIB1.

    Entry informationi

    Entry nameiCAC1C_MOUSE
    AccessioniPrimary (citable) accession number: Q01815
    Secondary accession number(s): Q04476, Q61242, Q99242
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1999
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 147 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3