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P22002

- CAC1C_RAT

UniProt

P22002 - CAC1C_RAT

Protein

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

Gene

Cacna1c

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 138 (01 Oct 2014)
      Sequence version 1 (01 Aug 1991)
      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.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei393 – 3931Calcium ion selectivity and permeabilityBy similarity
    Sitei736 – 7361Calcium ion selectivity and permeabilityBy similarity
    Sitei1116 – 11161Calcium ion selectivity and permeabilityBy similarity
    Sitei1445 – 14451Calcium ion selectivity and permeabilityBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Calcium bindingi1534 – 154512By similarityAdd
    BLAST

    GO - Molecular functioni

    1. high voltage-gated calcium channel activity Source: RGD
    2. ion channel binding Source: BHF-UCL
    3. metal ion binding Source: UniProtKB-KW
    4. protein binding Source: UniProtKB
    5. protein domain specific binding Source: RGD
    6. protein phosphatase 2A binding Source: RGD
    7. voltage-gated calcium channel activity Source: RGD

    GO - Biological processi

    1. calcium ion import Source: RGD
    2. calcium ion transport Source: RGD
    3. membrane depolarization during action potential Source: RefGenome

    Keywords - Molecular functioni

    Calcium channel, Ion channel, Voltage-gated channel

    Keywords - Biological processi

    Calcium transport, Ion transport, Transport

    Keywords - Ligandi

    Calcium, Metal-binding

    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
    Rat brain class C
    Short name:
    RBC
    Voltage-gated calcium channel subunit alpha Cav1.2
    Gene namesi
    Name:Cacna1c
    Synonyms:Cach2, Cacn2, Cacnl1a1, Cchl1a1
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi2245. 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. dendrite Source: UniProtKB
    2. membrane Source: RGD
    3. neuronal cell body Source: UniProtKB
    4. plasma membrane Source: RGD
    5. postsynaptic density Source: UniProtKB
    6. protein complex Source: RGD
    7. sarcolemma Source: RGD
    8. T-tubule Source: BHF-UCL
    9. voltage-gated calcium channel complex Source: RGD
    10. Z disc Source: BHF-UCL

    Keywords - Cellular componenti

    Cell membrane, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 21692169Voltage-dependent L-type calcium channel subunit alpha-1CPRO_0000053931Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi183 – 1831N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi358 – 3581N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1417 – 14171N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1468 – 14681N-linked (GlcNAc...)Sequence Analysis
    Modified residuei1516 – 15161Phosphoserine; by PKASequence Analysis
    Modified residuei1919 – 19191Phosphoserine; by PKASequence Analysis
    Modified residuei1927 – 19271Phosphoserine; by PKASequence Analysis

    Post-translational modificationi

    Phosphorylation by PKA activates the channel Probable. Is also phosphorylated in vitro by CaM-kinase II, PKC and CGPK.1 PublicationCurated

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    PaxDbiP22002.
    PRIDEiP22002.

    PTM databases

    PhosphoSiteiP22002.

    Expressioni

    Tissue specificityi

    Isoforms 4 and 5 are expressed throughout the central nervous system, with highest levels in the olfactory bulb and cerebellum. Also expressed in heart, pituitary, adrenal gland, liver, kidney, and in a much lesser extent in testes and spleen.

    Developmental stagei

    Expressed from embryonic day 16 until the adult stage.

    Gene expression databases

    GenevestigatoriP22002.

    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 C and IQ motifs) with CABP1. The binding via the C motif is calcium independent whereas the binding via IQ requires the presence of calcium and is mutually exclusive with calmodulin binding. Interacts with CACNA2D4 By similarity. Interacts (via C-terminal CDB motif) with CABP5; in a calcium-dependent manner. Interacts with CIB1; the interaction increases upon cardiomyocytes hypertrophy By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Ppp3caP633295EBI-1185084,EBI-7022944
    SrcQ9WUD94EBI-1185084,EBI-7784541

    Protein-protein interaction databases

    BioGridi246425. 4 interactions.
    IntActiP22002. 4 interactions.
    MINTiMINT-5026000.

    Structurei

    Secondary structure

    1
    2169
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi454 – 47421

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1VYTX-ray2.60E/F452-476[»]
    ProteinModelPortaliP22002.
    SMRiP22002. Positions 1641-1669.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP22002.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 154154CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini174 – 19017ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini212 – 22312CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini243 – 26220ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini282 – 30019CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini321 – 41090ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini436 – 554119CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini574 – 58815ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini609 – 6168CytoplasmicSequence Analysis
    Topological domaini636 – 64510ExtracellularSequence Analysis
    Topological domaini665 – 68319CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini704 – 75855ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini784 – 930147CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini950 – 96516ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini986 – 99712CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini1017 – 10237ExtracellularSequence Analysis
    Topological domaini1042 – 106019CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini1081 – 117090ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1196 – 124853CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini1268 – 128215ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1303 – 13108CytoplasmicSequence Analysis
    Topological domaini1330 – 135324ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1373 – 139119CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini1412 – 148069ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1506 – 2169664CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei155 – 17319Helical; Name=S1 of repeat ISequence AnalysisAdd
    BLAST
    Transmembranei191 – 21121Helical; Name=S2 of repeat ISequence AnalysisAdd
    BLAST
    Transmembranei224 – 24219Helical; Name=S3 of repeat ISequence AnalysisAdd
    BLAST
    Transmembranei263 – 28119Helical; Name=S4 of repeat ISequence AnalysisAdd
    BLAST
    Transmembranei301 – 32020Helical; Name=S5 of repeat ISequence AnalysisAdd
    BLAST
    Transmembranei411 – 43525Helical; Name=S6 of repeat ISequence AnalysisAdd
    BLAST
    Transmembranei555 – 57319Helical; Name=S1 of repeat IISequence AnalysisAdd
    BLAST
    Transmembranei589 – 60820Helical; Name=S2 of repeat IISequence AnalysisAdd
    BLAST
    Transmembranei617 – 63519Helical; Name=S3 of repeat IISequence AnalysisAdd
    BLAST
    Transmembranei646 – 66419Helical; Name=S4 of repeat IISequence AnalysisAdd
    BLAST
    Transmembranei684 – 70320Helical; Name=S5 of repeat IISequence AnalysisAdd
    BLAST
    Transmembranei759 – 78325Helical; Name=S6 of repeat IISequence AnalysisAdd
    BLAST
    Transmembranei931 – 94919Helical; Name=S1 of repeat IIISequence AnalysisAdd
    BLAST
    Transmembranei966 – 98520Helical; Name=S2 of repeat IIISequence AnalysisAdd
    BLAST
    Transmembranei998 – 101619Helical; Name=S3 of repeat IIISequence AnalysisAdd
    BLAST
    Transmembranei1024 – 104118Helical; Name=S4 of repeat IIISequence AnalysisAdd
    BLAST
    Transmembranei1061 – 108020Helical; Name=S5 of repeat IIISequence AnalysisAdd
    BLAST
    Transmembranei1171 – 119525Helical; Name=S6 of repeat IIISequence AnalysisAdd
    BLAST
    Transmembranei1249 – 126719Helical; Name=S1 of repeat IVSequence AnalysisAdd
    BLAST
    Transmembranei1283 – 130220Helical; Name=S2 of repeat IVSequence AnalysisAdd
    BLAST
    Transmembranei1311 – 132919Helical; Name=S3 of repeat IVSequence AnalysisAdd
    BLAST
    Transmembranei1354 – 137219Helical; Name=S4 of repeat IVSequence AnalysisAdd
    BLAST
    Transmembranei1392 – 141120Helical; Name=S5 of repeat IVSequence AnalysisAdd
    BLAST
    Transmembranei1481 – 150525Helical; Name=S6 of repeat IVSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati141 – 438298IAdd
    BLAST
    Repeati540 – 786247IIAdd
    BLAST
    Repeati917 – 1198282IIIAdd
    BLAST
    Repeati1235 – 1508274IVAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni458 – 47518Binding to the beta subunitBy similarityAdd
    BLAST
    Regioni1118 – 120891Dihydropyridine bindingBy similarityAdd
    BLAST
    Regioni1459 – 152769Dihydropyridine bindingBy similarityAdd
    BLAST
    Regioni1473 – 151644Phenylalkylamine bindingBy similarityAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi684 – 6907Poly-Leu
    Compositional biasi798 – 8047Poly-Glu
    Compositional biasi1176 – 11827Poly-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.
    HOVERGENiHBG050763.
    InParanoidiP22002.
    KOiK04850.
    PhylomeDBiP22002.

    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 (5)i

    Sequence statusi: Complete.

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Note: Additional isoforms seem to exist.

    Isoform 2 (identifier: P22002-1) [UniParc]FASTAAdd to Basket

    Also known as: S3B

    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

    MIRAFAQPST PPYQPLSSCL SEDTERKFKG KVVHEAQLNC FYISPGGSNY     50
    GSPRPAHANM NANAAAGLAP EHIPTPGAAL SWLAAIDAAR QAKLMGSAGN 100
    ATISTVSSTQ RKRQQYGKPK KQGGTTATRP PRALLCLTLK NPIRRACISI 150
    VEWKPFEIII LLTIFANCVA LAIYIPFPED DSNATNSNLE RVEYLFLIIF 200
    TVEAFLKVIA YGLLFHPNAY LRNGWNLLDF IIVVVGLFSA ILEQATKADG 250
    ANALGGKGAG FDVKALRAFR VLRPLRLVSG VPSLQVVLNS IIKAMVPLLH 300
    IALLVLFVII IYAIIGLELF MGKMHKTCYN QEGIIDVPAE EDPSPCALET 350
    GHGRQCQNGT VCKPGWDGPK HGITNFDNFA FAMLTVFQCI TMEGWTDVLY 400
    WMQDAMGYEL PWVYFVSLVI FGSFFVLNLV LGVLSGEFSK EREKAKARGD 450
    FQKLREKQQL EEDLKGYLDW ITQAEDIDPE NEDEGMDEDK PRNMSMPTSE 500
    TESVNTENVA GGDIEGENCG ARLAHRISKS KFSRYWRRWN RFCRRKCRAA 550
    VKSNVFYWLV IFLVFLNTLT IASEHYNQPH WLTEVQDTAN KALLALFTAE 600
    MLLKMYSLGL QAYFVSLFNR FDCFIVCGGI LETILVETKI MSPLGISCWR 650
    CVRLLRIFKI TRYWNSLSNL VASLLNSLRS IASLLLLLFL FIIIFSLLGM 700
    QLFGGKFNFD EMQTRRSTFD NFPQSLLTVF QILTGEDWNS VMYDGIMAYG 750
    GPSFPGMLVC IYFIILFISP NYILLNLFLA IAVDNLADAE SLTSAQKEEE 800
    EEKERKKLAR TASPEKKQEV MEKPAVEESK EEKIELKSIT ADGESPPTTK 850
    INMDDLQPSE NEDKSPHSNP DTAGEEDEEE PEMPVGPRPR PLSELHLKEK 900
    AVPMPEASAF FIFSPNNRFR LQCHRIVNDT IFTNLILFFI LLSSISLAAE 950
    DPVQHTSFRN HILFYFDIVF TTIFTIEIAL KMTAYGAFLH KGSFCRNYFN 1000
    ILDLLVVSVS LISFGIQSSA INVVKILRVL RVLRPLRINR AKGLKHVVQC 1050
    VFVAIRTIGN IVIVTTLLQF MFACIGVQLF KGKLYTCSDS SKQTEAESKG 1100
    NYITYKTGEV DHPIIQPRSW ENSKFDFDNV LAAMMALFTV STFEGWPELL 1150
    YRSIDSHTED KGPIYNYRVE ISIFFIIYII IIAFFMMNIF VGFVIVTFQE 1200
    QGEQEYKNCE LDKNQRQCVE YALKARPLPR YIPKNQHQYK VWYVVNSTYF 1250
    EYLMFVLILL NTICLAMQHY GQSCLFKIAM NILNMLFTGL FTVEMILKLI 1300
    AFKPKHYFCD AWNTFDALIV VGSIVDIAIT EVHPAEHTQC SPSMSAEENS 1350
    RISITFFRLF RVMRLVKLLS RGEGIRTLLW TFIKSFQALP YVALLIVMLF 1400
    FIYAVIGMQV FGKIALNDTT EINRNNNFQT FPQAVLLLFR CATGEAWQDI 1450
    MLACMPGKKC APESEPSNST EGETPCGSSF AVFYFISFYM LCAFLIINLF 1500
    VAVIMDNFDY LTRDWSILGP HHLDEFKRIW AEYDPEAKGR IKHLDVVTLL 1550
    RRIQPPLGFG KLCPHRVACK RLVSMNMPLN SDGTVMFNAT LFALVRTALR 1600
    IKTEGNLEQA NEELRAIIKK IWKRTSMKLL DQVVPPAGDD EVTVGKFYAT 1650
    FLIQEYFRKF KKRKEQGLVG KPSQRNALSL QAGLRTLHDI GPEIRRAISG 1700
    DLTAEEELDK AMKEAVSAAS EDDIFRRAGG LFGNHVSYYQ SDSRSNFPQT 1750
    FATQRPLHIN KTGNNQADTE SPSHEKLVDS TFTPSSYSST GSNANINNAN 1800
    NTALGRFPHP AGYSSTVSTV EGHGPPLSPA VRVQEAAWKL SSKRCHSRES 1850
    QGATVSQDMF PDETRSSVRL SEEVEYCSEP SLLSTDILSY QDDENRQLTC 1900
    LEEDKREIQP CPKRSFLRSA SLGRRASFHL ECLKRQKDQG GDISQKTALP 1950
    LHLVHHQALA VAGLSPLLQR SHSPSTFPRP RPTPPVTPGS RGRPLQPIPT 2000
    LRLEGAESSE KLNSSFPSIH CSSWSEETTA CSGGSSMARR ARPVSLTVPS 2050
    QAGAPGRQFH GSASSLVEAV LISEGLGQFA QDPKFIEVTT QELADACDMT 2100
    IEEMENAADN ILSGGAQQSP NGTLLPFVNC RDPGQDRAVV PEDESCVYAL 2150
    GRGRSEEALP DSRSYVSNL 2169
    Length:2,169
    Mass (Da):243,482
    Last modified:August 1, 1991 - v1
    Checksum:iD3ADBD20E4763B69
    GO
    Isoform 1 (identifier: P22002-2) [UniParc]FASTAAdd to Basket

    Also known as: S3A

    The sequence of this isoform differs from the canonical sequence as follows:
         1306-1333: HYFCDAWNTFDALIVVGSIVDIAITEVH → GYFSDPSNVFDFLIVIGSIIAVILSETN

    Show »
    Length:2,169
    Mass (Da):243,364
    Checksum:i1539479E670D0D2A
    GO
    Isoform 3 (identifier: P22002-3) [UniParc]FASTAAdd to Basket

    Also known as: D1, ROB2

    The sequence of this isoform differs from the canonical sequence as follows:
         1334-1344: Missing.

    Show »
    Length:2,158
    Mass (Da):242,313
    Checksum:i498718087DA7DC10
    GO
    Isoform 4 (identifier: P22002-4) [UniParc]FASTAAdd to Basket

    Also known as: rbC-I

    The sequence of this isoform differs from the canonical sequence as follows:
         1-46: MIRAFAQPSTPPYQPLSSCLSEDTERKFKGKVVHEAQLNCFYISPG → MVNENTRMYVPEENHQ
         964-979: FYFDIVFTTIFTIEIA → GNADYVFTSIFTLEII
         1306-1333: HYFCDAWNTFDALIVVGSIVDIAITEVH → GYFSDPSNVFDFLIVIGSIIAVILSETN

    Show »
    Length:2,139
    Mass (Da):240,045
    Checksum:i8A3C3354E8BDB60D
    GO
    Isoform 5 (identifier: P22002-5) [UniParc]FASTAAdd to Basket

    Also known as: rbC-II

    The sequence of this isoform differs from the canonical sequence as follows:
         1-46: MIRAFAQPSTPPYQPLSSCLSEDTERKFKGKVVHEAQLNCFYISPG → MVNENTRMYVPEENHQ
         810-810: R → RPAR
         964-979: FYFDIVFTTIFTIEIA → GNADYVFTSIFTLEII

    Show »
    Length:2,142
    Mass (Da):240,488
    Checksum:i4207AD0217F19CB2
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti83 – 831L → Q in AAA18905. (PubMed:1648941)Curated
    Sequence conflicti83 – 831L → Q in AAA42016. (PubMed:1648941)Curated
    Sequence conflicti87 – 871D → G in AAA18905. (PubMed:1648941)Curated
    Sequence conflicti520 – 5201G → R in AAA18905. (PubMed:1648941)Curated
    Sequence conflicti648 – 6492CW → VL in AAA18905. (PubMed:1648941)Curated
    Sequence conflicti648 – 6492CW → VL in AAA42016. (PubMed:1648941)Curated
    Sequence conflicti678 – 6781L → V in AAA18905. (PubMed:1648941)Curated
    Sequence conflicti678 – 6781L → V in AAA42016. (PubMed:1648941)Curated
    Sequence conflicti769 – 7702SP → CG in AAA18905. (PubMed:1648941)Curated
    Sequence conflicti769 – 7702SP → CG in AAA42016. (PubMed:1648941)Curated
    Sequence conflicti777 – 7771L → V in AAA18905. (PubMed:1648941)Curated
    Sequence conflicti777 – 7771L → V in AAA42016. (PubMed:1648941)Curated
    Sequence conflicti871 – 8711D → N in AAA18905. (PubMed:1648941)Curated
    Sequence conflicti1037 – 10371R → RA in AAA18905. (PubMed:1648941)Curated
    Sequence conflicti1037 – 10371R → RA in AAA42016. (PubMed:1648941)Curated
    Sequence conflicti1098 – 10981S → C in AAA18905. (PubMed:1648941)Curated
    Sequence conflicti1098 – 10981S → C in AAA42016. (PubMed:1648941)Curated
    Sequence conflicti1107 – 11071T → D in AAA18905. (PubMed:1648941)Curated
    Sequence conflicti1107 – 11071T → D in AAA42016. (PubMed:1648941)Curated
    Sequence conflicti1229 – 12291P → R in AAA18905. (PubMed:1648941)Curated
    Sequence conflicti1229 – 12291P → R in AAA42016. (PubMed:1648941)Curated
    Sequence conflicti1229 – 12291P → R no nucleotide entry (PubMed:1692134)Curated
    Sequence conflicti1229 – 12291P → R in AAA89157. (PubMed:7479909)Curated
    Sequence conflicti1306 – 13061H → D in AAB35528. (PubMed:7485440)Curated
    Sequence conflicti1306 – 13061H → G in AAA42016. (PubMed:1648941)Curated
    Sequence conflicti1306 – 13061H → G in AAA89157. (PubMed:7479909)Curated
    Sequence conflicti1329 – 13291I → L in AAB35528. (PubMed:7485440)Curated
    Sequence conflicti1471 – 14711E → K in AAA18905. (PubMed:1648941)Curated
    Sequence conflicti1911 – 19111C → S in AAA18905. (PubMed:1648941)Curated
    Sequence conflicti1911 – 19111C → S in AAA42016. (PubMed:1648941)Curated
    Sequence conflicti2084 – 20841K → N in AAA18905. (PubMed:1648941)Curated
    Sequence conflicti2154 – 21541R → Q in AAA42016. (PubMed:1648941)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 4646MIRAF…YISPG → MVNENTRMYVPEENHQ in isoform 4 and isoform 5. 1 PublicationVSP_000908Add
    BLAST
    Alternative sequencei810 – 8101R → RPAR in isoform 5. 1 PublicationVSP_000909
    Alternative sequencei964 – 97916FYFDI…TIEIA → GNADYVFTSIFTLEII in isoform 4 and isoform 5. 1 PublicationVSP_000910Add
    BLAST
    Alternative sequencei1306 – 133328HYFCD…ITEVH → GYFSDPSNVFDFLIVIGSII AVILSETN in isoform 1 and isoform 4. 2 PublicationsVSP_000911Add
    BLAST
    Alternative sequencei1334 – 134411Missing in isoform 3. 1 PublicationVSP_000912Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M59786 mRNA. Translation: AAA85463.1.
    M67515 mRNA. Translation: AAA18905.1.
    M67516 mRNA. Translation: AAA42016.1.
    M91242
    , M91240, M89924, M91241 Genomic DNA. Translation: AAA41460.1.
    S80558 mRNA. Translation: AAB35528.1.
    U31815 mRNA. Translation: AAA89157.1.
    RefSeqiNP_036649.2. NM_012517.2.
    UniGeneiRn.9827.

    Genome annotation databases

    GeneIDi24239.
    KEGGirno:24239.
    UCSCiRGD:2245. rat. [P22002-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M59786 mRNA. Translation: AAA85463.1 .
    M67515 mRNA. Translation: AAA18905.1 .
    M67516 mRNA. Translation: AAA42016.1 .
    M91242
    , M91240 , M89924 , M91241 Genomic DNA. Translation: AAA41460.1 .
    S80558 mRNA. Translation: AAB35528.1 .
    U31815 mRNA. Translation: AAA89157.1 .
    RefSeqi NP_036649.2. NM_012517.2.
    UniGenei Rn.9827.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1VYT X-ray 2.60 E/F 452-476 [» ]
    ProteinModelPortali P22002.
    SMRi P22002. Positions 1641-1669.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 246425. 4 interactions.
    IntActi P22002. 4 interactions.
    MINTi MINT-5026000.

    Chemistry

    BindingDBi P22002.
    ChEMBLi CHEMBL2095177.
    GuidetoPHARMACOLOGYi 529.

    PTM databases

    PhosphoSitei P22002.

    Proteomic databases

    PaxDbi P22002.
    PRIDEi P22002.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 24239.
    KEGGi rno:24239.
    UCSCi RGD:2245. rat. [P22002-1 ]

    Organism-specific databases

    CTDi 775.
    RGDi 2245. Cacna1c.

    Phylogenomic databases

    eggNOGi COG1226.
    HOVERGENi HBG050763.
    InParanoidi P22002.
    KOi K04850.
    PhylomeDBi P22002.

    Miscellaneous databases

    EvolutionaryTracei P22002.
    NextBioi 602705.
    PROi P22002.

    Gene expression databases

    Genevestigatori P22002.

    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. "cDNA cloning of a dihydropyridine-sensitive calcium channel from rat aorta. Evidence for the existence of alternatively spliced forms."
      Koch W.J., Ellinor P.T., Schwartz A.
      J. Biol. Chem. 265:17786-17791(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
      Tissue: Aorta.
    2. "Distinct calcium channels are generated by alternative splicing and are differentially expressed in the mammalian CNS."
      Snutch T.P., Tomlinson W.J., Leonard J.P., Gilbert M.M.
      Neuron 7:45-57(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 4 AND 5).
      Tissue: Brain.
    3. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1168-1413 (ISOFORM 1).
    4. "Mutually exclusive exon splicing of the cardiac calcium channel a1 subunit generates developmentally regulated isoforms in the rat heart."
      Diebold R.J., Koch W.J., Ellinor P.T., Wang J.-J., Muthuchamy M., Wieczorek D.F., Schwartz A.
      Proc. Natl. Acad. Sci. U.S.A. 89:1497-1501(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1269-1415 (ISOFORMS 1; 2 AND 3).
    5. "Changes in transcripts encoding calcium channel subunits of rat myometrium during pregnancy."
      Tezuka N., Ali M., Chwalisz K., Garfield R.E.
      Am. J. Physiol. 269:C1008-C1017(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1269-1387.
      Tissue: Myometrium.
    6. "Multiple calcium channel transcripts in rat osteosarcoma cells: selective activation of alpha 1D isoform by parathyroid hormone."
      Barry E.L.R., Gesek F.A., Froehner S.C., Friedman P.A.
      Proc. Natl. Acad. Sci. U.S.A. 92:10914-10918(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1202-1495 (ISOFORM 3).
      Tissue: Osteosarcoma.
    7. "Differential phosphorylation of two size forms of the neuronal class C L-type calcium channel alpha 1 subunit."
      Hell J.W., Yokoyama C.T., Wong S.T., Warner C., Snutch T.P., Catterall W.A.
      J. Biol. Chem. 268:19451-19457(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION.
    8. "Ca2+-binding protein-1 facilitates and forms a postsynaptic complex with Cav1.2 (L-type) Ca2+ channels."
      Zhou H., Kim S.-A., Kirk E.A., Tippens A.L., Sun H., Haeseleer F., Lee A.
      J. Neurosci. 24:4698-4708(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CABP1.
    9. "Structural basis of the alpha1-beta subunit interaction of voltage-gated Ca2+ channels."
      Chen Y.H., Li M.H., Zhang Y., He L.L., Yamada Y., Fitzmaurice A., Shen Y., Zhang H., Tong L., Yang J.
      Nature 429:675-680(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 452-476.

    Entry informationi

    Entry nameiCAC1C_RAT
    AccessioniPrimary (citable) accession number: P22002
    Secondary accession number(s): P27733
    , P27734, Q62816, Q63271, Q64178
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1991
    Last sequence update: August 1, 1991
    Last modified: October 1, 2014
    This is version 138 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3