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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

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 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 domain specific binding Source: RGD
  5. protein phosphatase 2A binding Source: RGD
  6. 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

Enzyme and pathway databases

ReactomeiREACT_232206. Adrenaline,noradrenaline inhibits insulin secretion.

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

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
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-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 – 47421Combined sources

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP22002.

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

        10         20         30         40         50
MIRAFAQPST PPYQPLSSCL SEDTERKFKG KVVHEAQLNC FYISPGGSNY
60 70 80 90 100
GSPRPAHANM NANAAAGLAP EHIPTPGAAL SWLAAIDAAR QAKLMGSAGN
110 120 130 140 150
ATISTVSSTQ RKRQQYGKPK KQGGTTATRP PRALLCLTLK NPIRRACISI
160 170 180 190 200
VEWKPFEIII LLTIFANCVA LAIYIPFPED DSNATNSNLE RVEYLFLIIF
210 220 230 240 250
TVEAFLKVIA YGLLFHPNAY LRNGWNLLDF IIVVVGLFSA ILEQATKADG
260 270 280 290 300
ANALGGKGAG FDVKALRAFR VLRPLRLVSG VPSLQVVLNS IIKAMVPLLH
310 320 330 340 350
IALLVLFVII IYAIIGLELF MGKMHKTCYN QEGIIDVPAE EDPSPCALET
360 370 380 390 400
GHGRQCQNGT VCKPGWDGPK HGITNFDNFA FAMLTVFQCI TMEGWTDVLY
410 420 430 440 450
WMQDAMGYEL PWVYFVSLVI FGSFFVLNLV LGVLSGEFSK EREKAKARGD
460 470 480 490 500
FQKLREKQQL EEDLKGYLDW ITQAEDIDPE NEDEGMDEDK PRNMSMPTSE
510 520 530 540 550
TESVNTENVA GGDIEGENCG ARLAHRISKS KFSRYWRRWN RFCRRKCRAA
560 570 580 590 600
VKSNVFYWLV IFLVFLNTLT IASEHYNQPH WLTEVQDTAN KALLALFTAE
610 620 630 640 650
MLLKMYSLGL QAYFVSLFNR FDCFIVCGGI LETILVETKI MSPLGISCWR
660 670 680 690 700
CVRLLRIFKI TRYWNSLSNL VASLLNSLRS IASLLLLLFL FIIIFSLLGM
710 720 730 740 750
QLFGGKFNFD EMQTRRSTFD NFPQSLLTVF QILTGEDWNS VMYDGIMAYG
760 770 780 790 800
GPSFPGMLVC IYFIILFISP NYILLNLFLA IAVDNLADAE SLTSAQKEEE
810 820 830 840 850
EEKERKKLAR TASPEKKQEV MEKPAVEESK EEKIELKSIT ADGESPPTTK
860 870 880 890 900
INMDDLQPSE NEDKSPHSNP DTAGEEDEEE PEMPVGPRPR PLSELHLKEK
910 920 930 940 950
AVPMPEASAF FIFSPNNRFR LQCHRIVNDT IFTNLILFFI LLSSISLAAE
960 970 980 990 1000
DPVQHTSFRN HILFYFDIVF TTIFTIEIAL KMTAYGAFLH KGSFCRNYFN
1010 1020 1030 1040 1050
ILDLLVVSVS LISFGIQSSA INVVKILRVL RVLRPLRINR AKGLKHVVQC
1060 1070 1080 1090 1100
VFVAIRTIGN IVIVTTLLQF MFACIGVQLF KGKLYTCSDS SKQTEAESKG
1110 1120 1130 1140 1150
NYITYKTGEV DHPIIQPRSW ENSKFDFDNV LAAMMALFTV STFEGWPELL
1160 1170 1180 1190 1200
YRSIDSHTED KGPIYNYRVE ISIFFIIYII IIAFFMMNIF VGFVIVTFQE
1210 1220 1230 1240 1250
QGEQEYKNCE LDKNQRQCVE YALKARPLPR YIPKNQHQYK VWYVVNSTYF
1260 1270 1280 1290 1300
EYLMFVLILL NTICLAMQHY GQSCLFKIAM NILNMLFTGL FTVEMILKLI
1310 1320 1330 1340 1350
AFKPKHYFCD AWNTFDALIV VGSIVDIAIT EVHPAEHTQC SPSMSAEENS
1360 1370 1380 1390 1400
RISITFFRLF RVMRLVKLLS RGEGIRTLLW TFIKSFQALP YVALLIVMLF
1410 1420 1430 1440 1450
FIYAVIGMQV FGKIALNDTT EINRNNNFQT FPQAVLLLFR CATGEAWQDI
1460 1470 1480 1490 1500
MLACMPGKKC APESEPSNST EGETPCGSSF AVFYFISFYM LCAFLIINLF
1510 1520 1530 1540 1550
VAVIMDNFDY LTRDWSILGP HHLDEFKRIW AEYDPEAKGR IKHLDVVTLL
1560 1570 1580 1590 1600
RRIQPPLGFG KLCPHRVACK RLVSMNMPLN SDGTVMFNAT LFALVRTALR
1610 1620 1630 1640 1650
IKTEGNLEQA NEELRAIIKK IWKRTSMKLL DQVVPPAGDD EVTVGKFYAT
1660 1670 1680 1690 1700
FLIQEYFRKF KKRKEQGLVG KPSQRNALSL QAGLRTLHDI GPEIRRAISG
1710 1720 1730 1740 1750
DLTAEEELDK AMKEAVSAAS EDDIFRRAGG LFGNHVSYYQ SDSRSNFPQT
1760 1770 1780 1790 1800
FATQRPLHIN KTGNNQADTE SPSHEKLVDS TFTPSSYSST GSNANINNAN
1810 1820 1830 1840 1850
NTALGRFPHP AGYSSTVSTV EGHGPPLSPA VRVQEAAWKL SSKRCHSRES
1860 1870 1880 1890 1900
QGATVSQDMF PDETRSSVRL SEEVEYCSEP SLLSTDILSY QDDENRQLTC
1910 1920 1930 1940 1950
LEEDKREIQP CPKRSFLRSA SLGRRASFHL ECLKRQKDQG GDISQKTALP
1960 1970 1980 1990 2000
LHLVHHQALA VAGLSPLLQR SHSPSTFPRP RPTPPVTPGS RGRPLQPIPT
2010 2020 2030 2040 2050
LRLEGAESSE KLNSSFPSIH CSSWSEETTA CSGGSSMARR ARPVSLTVPS
2060 2070 2080 2090 2100
QAGAPGRQFH GSASSLVEAV LISEGLGQFA QDPKFIEVTT QELADACDMT
2110 2120 2130 2140 2150
IEEMENAADN ILSGGAQQSP NGTLLPFVNC RDPGQDRAVV PEDESCVYAL
2160
GRGRSEEALP DSRSYVSNL
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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.

Enzyme and pathway databases

Reactomei REACT_232206. Adrenaline,noradrenaline inhibits insulin secretion.

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: November 26, 2014
This is version 140 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