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P22002

- CAC1C_RAT

UniProt

P22002 - CAC1C_RAT

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Protein
Voltage-dependent L-type calcium channel subunit alpha-1C
Gene
Cacna1c, Cach2, Cacn2, Cacnl1a1, Cchl1a1
Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 permeability By similarity
Sitei736 – 7361Calcium ion selectivity and permeability By similarity
Sitei1116 – 11161Calcium ion selectivity and permeability By similarity
Sitei1445 – 14451Calcium ion selectivity and permeability By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi1534 – 154512 By similarity
Add
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
Complete GO annotation...

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.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 154154Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei155 – 17319Helical; Name=S1 of repeat I; Reviewed prediction
Add
BLAST
Topological domaini174 – 19017Extracellular Reviewed prediction
Add
BLAST
Transmembranei191 – 21121Helical; Name=S2 of repeat I; Reviewed prediction
Add
BLAST
Topological domaini212 – 22312Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei224 – 24219Helical; Name=S3 of repeat I; Reviewed prediction
Add
BLAST
Topological domaini243 – 26220Extracellular Reviewed prediction
Add
BLAST
Transmembranei263 – 28119Helical; Name=S4 of repeat I; Reviewed prediction
Add
BLAST
Topological domaini282 – 30019Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei301 – 32020Helical; Name=S5 of repeat I; Reviewed prediction
Add
BLAST
Topological domaini321 – 41090Extracellular Reviewed prediction
Add
BLAST
Transmembranei411 – 43525Helical; Name=S6 of repeat I; Reviewed prediction
Add
BLAST
Topological domaini436 – 554119Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei555 – 57319Helical; Name=S1 of repeat II; Reviewed prediction
Add
BLAST
Topological domaini574 – 58815Extracellular Reviewed prediction
Add
BLAST
Transmembranei589 – 60820Helical; Name=S2 of repeat II; Reviewed prediction
Add
BLAST
Topological domaini609 – 6168Cytoplasmic Reviewed prediction
Transmembranei617 – 63519Helical; Name=S3 of repeat II; Reviewed prediction
Add
BLAST
Topological domaini636 – 64510Extracellular Reviewed prediction
Transmembranei646 – 66419Helical; Name=S4 of repeat II; Reviewed prediction
Add
BLAST
Topological domaini665 – 68319Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei684 – 70320Helical; Name=S5 of repeat II; Reviewed prediction
Add
BLAST
Topological domaini704 – 75855Extracellular Reviewed prediction
Add
BLAST
Transmembranei759 – 78325Helical; Name=S6 of repeat II; Reviewed prediction
Add
BLAST
Topological domaini784 – 930147Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei931 – 94919Helical; Name=S1 of repeat III; Reviewed prediction
Add
BLAST
Topological domaini950 – 96516Extracellular Reviewed prediction
Add
BLAST
Transmembranei966 – 98520Helical; Name=S2 of repeat III; Reviewed prediction
Add
BLAST
Topological domaini986 – 99712Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei998 – 101619Helical; Name=S3 of repeat III; Reviewed prediction
Add
BLAST
Topological domaini1017 – 10237Extracellular Reviewed prediction
Transmembranei1024 – 104118Helical; Name=S4 of repeat III; Reviewed prediction
Add
BLAST
Topological domaini1042 – 106019Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei1061 – 108020Helical; Name=S5 of repeat III; Reviewed prediction
Add
BLAST
Topological domaini1081 – 117090Extracellular Reviewed prediction
Add
BLAST
Transmembranei1171 – 119525Helical; Name=S6 of repeat III; Reviewed prediction
Add
BLAST
Topological domaini1196 – 124853Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei1249 – 126719Helical; Name=S1 of repeat IV; Reviewed prediction
Add
BLAST
Topological domaini1268 – 128215Extracellular Reviewed prediction
Add
BLAST
Transmembranei1283 – 130220Helical; Name=S2 of repeat IV; Reviewed prediction
Add
BLAST
Topological domaini1303 – 13108Cytoplasmic Reviewed prediction
Transmembranei1311 – 132919Helical; Name=S3 of repeat IV; Reviewed prediction
Add
BLAST
Topological domaini1330 – 135324Extracellular Reviewed prediction
Add
BLAST
Transmembranei1354 – 137219Helical; Name=S4 of repeat IV; Reviewed prediction
Add
BLAST
Topological domaini1373 – 139119Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei1392 – 141120Helical; Name=S5 of repeat IV; Reviewed prediction
Add
BLAST
Topological domaini1412 – 148069Extracellular Reviewed prediction
Add
BLAST
Transmembranei1481 – 150525Helical; Name=S6 of repeat IV; Reviewed prediction
Add
BLAST
Topological domaini1506 – 2169664Cytoplasmic Reviewed prediction
Add
BLAST

GO - Cellular componenti

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

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-1C
PRO_0000053931Add
BLAST

Amino acid modifications

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

Post-translational modificationi

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

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.1 Publication

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

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.

Miscellaneous databases

EvolutionaryTraceiP22002.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati141 – 438298I
Add
BLAST
Repeati540 – 786247II
Add
BLAST
Repeati917 – 1198282III
Add
BLAST
Repeati1235 – 1508274IV
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni458 – 47518Binding to the beta subunit By similarity
Add
BLAST
Regioni1118 – 120891Dihydropyridine binding By similarity
Add
BLAST
Regioni1459 – 152769Dihydropyridine binding By similarity
Add
BLAST
Regioni1473 – 151644Phenylalkylamine binding By similarity
Add
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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 4646MIRAF…YISPG → MVNENTRMYVPEENHQ in isoform 4 and isoform 5.
VSP_000908Add
BLAST
Alternative sequencei810 – 8101R → RPAR in isoform 5.
VSP_000909
Alternative sequencei964 – 97916FYFDI…TIEIA → GNADYVFTSIFTLEII in isoform 4 and isoform 5.
VSP_000910Add
BLAST
Alternative sequencei1306 – 133328HYFCD…ITEVH → GYFSDPSNVFDFLIVIGSII AVILSETN in isoform 1 and isoform 4.
VSP_000911Add
BLAST
Alternative sequencei1334 – 134411Missing in isoform 3.
VSP_000912Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti83 – 831L → Q in AAA18905. 1 Publication
Sequence conflicti83 – 831L → Q in AAA42016. 1 Publication
Sequence conflicti87 – 871D → G in AAA18905. 1 Publication
Sequence conflicti520 – 5201G → R in AAA18905. 1 Publication
Sequence conflicti648 – 6492CW → VL in AAA18905. 1 Publication
Sequence conflicti648 – 6492CW → VL in AAA42016. 1 Publication
Sequence conflicti678 – 6781L → V in AAA18905. 1 Publication
Sequence conflicti678 – 6781L → V in AAA42016. 1 Publication
Sequence conflicti769 – 7702SP → CG in AAA18905. 1 Publication
Sequence conflicti769 – 7702SP → CG in AAA42016. 1 Publication
Sequence conflicti777 – 7771L → V in AAA18905. 1 Publication
Sequence conflicti777 – 7771L → V in AAA42016. 1 Publication
Sequence conflicti871 – 8711D → N in AAA18905. 1 Publication
Sequence conflicti1037 – 10371R → RA in AAA18905. 1 Publication
Sequence conflicti1037 – 10371R → RA in AAA42016. 1 Publication
Sequence conflicti1098 – 10981S → C in AAA18905. 1 Publication
Sequence conflicti1098 – 10981S → C in AAA42016. 1 Publication
Sequence conflicti1107 – 11071T → D in AAA18905. 1 Publication
Sequence conflicti1107 – 11071T → D in AAA42016. 1 Publication
Sequence conflicti1229 – 12291P → R in AAA18905. 1 Publication
Sequence conflicti1229 – 12291P → R in AAA42016. 1 Publication
Sequence conflicti1229 – 12291P → R no nucleotide entry 1 Publication
Sequence conflicti1229 – 12291P → R in AAA89157. 1 Publication
Sequence conflicti1306 – 13061H → D in AAB35528. 1 Publication
Sequence conflicti1306 – 13061H → G in AAA42016. 1 Publication
Sequence conflicti1306 – 13061H → G in AAA89157. 1 Publication
Sequence conflicti1329 – 13291I → L in AAB35528. 1 Publication
Sequence conflicti1471 – 14711E → K in AAA18905. 1 Publication
Sequence conflicti1911 – 19111C → S in AAA18905. 1 Publication
Sequence conflicti1911 – 19111C → S in AAA42016. 1 Publication
Sequence conflicti2084 – 20841K → N in AAA18905. 1 Publication
Sequence conflicti2154 – 21541R → Q in AAA42016. 1 Publication

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: September 3, 2014
This is version 137 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

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