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Protein

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

Gene

Cacna1c

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: 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.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei393Calcium ion selectivity and permeabilityBy similarity1
Sitei736Calcium ion selectivity and permeabilityBy similarity1
Sitei1144Calcium ion selectivity and permeabilityBy similarity1
Sitei1445Calcium ion selectivity and permeabilityBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Calcium bindingi1534 – 1545By similarityAdd BLAST12

GO - Molecular functioni

  • alpha-actinin binding Source: BHF-UCL
  • high voltage-gated calcium channel activity Source: RGD
  • ion channel binding Source: BHF-UCL
  • metal ion binding Source: UniProtKB-KW
  • protein domain specific binding Source: RGD
  • protein phosphatase 2A binding Source: RGD
  • translation initiation factor binding Source: RGD
  • voltage-gated calcium channel activity Source: RGD
  • voltage-gated calcium channel activity involved in AV node cell action potential Source: BHF-UCL
  • voltage-gated calcium channel activity involved in cardiac muscle cell action potential Source: BHF-UCL

GO - Biological processi

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

ReactomeiR-RNO-400042. 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
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2245. Cacna1c.

Subcellular locationi

  • Membrane By similarity; Multi-pass membrane protein By similarity
  • Cell membrane By similarity

  • Note: The interaction between RRAD and CACNB2 regulates its trafficking to the cell membrane.By similarity

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 154CytoplasmicSequence analysisAdd BLAST154
Transmembranei155 – 173Helical; Name=S1 of repeat ISequence analysisAdd BLAST19
Topological domaini174 – 190ExtracellularSequence analysisAdd BLAST17
Transmembranei191 – 211Helical; Name=S2 of repeat ISequence analysisAdd BLAST21
Topological domaini212 – 223CytoplasmicSequence analysisAdd BLAST12
Transmembranei224 – 242Helical; Name=S3 of repeat ISequence analysisAdd BLAST19
Topological domaini243 – 262ExtracellularSequence analysisAdd BLAST20
Transmembranei263 – 281Helical; Name=S4 of repeat ISequence analysisAdd BLAST19
Topological domaini282 – 300CytoplasmicSequence analysisAdd BLAST19
Transmembranei301 – 320Helical; Name=S5 of repeat ISequence analysisAdd BLAST20
Topological domaini321 – 410ExtracellularSequence analysisAdd BLAST90
Transmembranei411 – 435Helical; Name=S6 of repeat ISequence analysisAdd BLAST25
Topological domaini436 – 554CytoplasmicSequence analysisAdd BLAST119
Transmembranei555 – 573Helical; Name=S1 of repeat IISequence analysisAdd BLAST19
Topological domaini574 – 588ExtracellularSequence analysisAdd BLAST15
Transmembranei589 – 608Helical; Name=S2 of repeat IISequence analysisAdd BLAST20
Topological domaini609 – 616CytoplasmicSequence analysis8
Transmembranei617 – 635Helical; Name=S3 of repeat IISequence analysisAdd BLAST19
Topological domaini636 – 645ExtracellularSequence analysis10
Transmembranei646 – 664Helical; Name=S4 of repeat IISequence analysisAdd BLAST19
Topological domaini665 – 683CytoplasmicSequence analysisAdd BLAST19
Transmembranei684 – 703Helical; Name=S5 of repeat IISequence analysisAdd BLAST20
Topological domaini704 – 758ExtracellularSequence analysisAdd BLAST55
Transmembranei759 – 783Helical; Name=S6 of repeat IISequence analysisAdd BLAST25
Topological domaini784 – 930CytoplasmicSequence analysisAdd BLAST147
Transmembranei931 – 949Helical; Name=S1 of repeat IIISequence analysisAdd BLAST19
Topological domaini950 – 965ExtracellularSequence analysisAdd BLAST16
Transmembranei966 – 985Helical; Name=S2 of repeat IIISequence analysisAdd BLAST20
Topological domaini986 – 997CytoplasmicSequence analysisAdd BLAST12
Transmembranei998 – 1016Helical; Name=S3 of repeat IIISequence analysisAdd BLAST19
Topological domaini1017 – 1023ExtracellularSequence analysis7
Transmembranei1024 – 1041Helical; Name=S4 of repeat IIISequence analysisAdd BLAST18
Topological domaini1042 – 1060CytoplasmicSequence analysisAdd BLAST19
Transmembranei1061 – 1080Helical; Name=S5 of repeat IIISequence analysisAdd BLAST20
Topological domaini1081 – 1170ExtracellularSequence analysisAdd BLAST90
Transmembranei1171 – 1195Helical; Name=S6 of repeat IIISequence analysisAdd BLAST25
Topological domaini1196 – 1248CytoplasmicSequence analysisAdd BLAST53
Transmembranei1249 – 1267Helical; Name=S1 of repeat IVSequence analysisAdd BLAST19
Topological domaini1268 – 1282ExtracellularSequence analysisAdd BLAST15
Transmembranei1283 – 1302Helical; Name=S2 of repeat IVSequence analysisAdd BLAST20
Topological domaini1303 – 1310CytoplasmicSequence analysis8
Transmembranei1311 – 1329Helical; Name=S3 of repeat IVSequence analysisAdd BLAST19
Topological domaini1330 – 1353ExtracellularSequence analysisAdd BLAST24
Transmembranei1354 – 1372Helical; Name=S4 of repeat IVSequence analysisAdd BLAST19
Topological domaini1373 – 1391CytoplasmicSequence analysisAdd BLAST19
Transmembranei1392 – 1411Helical; Name=S5 of repeat IVSequence analysisAdd BLAST20
Topological domaini1412 – 1480ExtracellularSequence analysisAdd BLAST69
Transmembranei1481 – 1505Helical; Name=S6 of repeat IVSequence analysisAdd BLAST25
Topological domaini1506 – 2169CytoplasmicSequence analysisAdd BLAST664

GO - Cellular componenti

  • dendrite Source: UniProtKB
  • L-type voltage-gated calcium channel complex Source: UniProtKB
  • membrane Source: RGD
  • neuronal cell body Source: UniProtKB
  • plasma membrane Source: RGD
  • postsynaptic density Source: UniProtKB
  • protein complex Source: RGD
  • sarcolemma Source: RGD
  • T-tubule Source: BHF-UCL
  • voltage-gated calcium channel complex Source: RGD
  • Z disc Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL3762.
GuidetoPHARMACOLOGYi529.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000539311 – 2169Voltage-dependent L-type calcium channel subunit alpha-1CAdd BLAST2169

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi183N-linked (GlcNAc...)Sequence analysis1
Glycosylationi358N-linked (GlcNAc...)Sequence analysis1
Modified residuei499PhosphoserineBy similarity1
Modified residuei506PhosphothreonineBy similarity1
Modified residuei838PhosphoserineBy similarity1
Modified residuei845PhosphoserineCombined sources1
Glycosylationi1417N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1468N-linked (GlcNAc...)Sequence analysis1
Modified residuei1516Phosphoserine; by PKASequence analysis1
Modified residuei1699PhosphoserineCombined sources1
Modified residuei1720PhosphoserineCombined sources1
Modified residuei1919Phosphoserine; by PKASequence analysis1
Modified residuei1927Phosphoserine; by PKASequence analysis1

Post-translational modificationi

Phosphorylation by PKA activates the channel (By similarity). Is also phosphorylated in vitro by CaM-kinase II, PKC and CGPK (PubMed:8396138).By similarity1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP22002.
PRIDEiP22002.

PTM databases

iPTMnetiP22002.
PhosphoSitePlusiP22002.

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.

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 similarity3 Publications

Binary interactionsi

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

GO - Molecular functioni

  • alpha-actinin binding Source: BHF-UCL
  • ion channel binding Source: BHF-UCL
  • protein domain specific binding Source: RGD
  • protein phosphatase 2A binding Source: RGD
  • translation initiation factor binding Source: RGD

Protein-protein interaction databases

BioGridi246425. 4 interactors.
IntActiP22002. 4 interactors.
MINTiMINT-5026000.
STRINGi10116.ENSRNOP00000048790.

Chemistry databases

BindingDBiP22002.

Structurei

Secondary structure

12169
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi454 – 474Combined sources21

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP22002.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati141 – 438IAdd BLAST298
Repeati540 – 786IIAdd BLAST247
Repeati917 – 1198IIIAdd BLAST282
Repeati1235 – 1508IVAdd BLAST274

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni458 – 475AID/alpha-interaction domain; mediates interaction with the beta subunit1 PublicationAdd BLAST18
Regioni1118 – 1208Dihydropyridine bindingBy similarityAdd BLAST91
Regioni1459 – 1527Dihydropyridine bindingBy similarityAdd BLAST69
Regioni1473 – 1516Phenylalkylamine bindingBy similarityAdd BLAST44

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi684 – 690Poly-Leu7
Compositional biasi798 – 804Poly-Glu7
Compositional biasi1176 – 1182Poly-Ile7

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

eggNOGiKOG2301. Eukaryota.
ENOG410XNP6. LUCA.
HOVERGENiHBG050763.
InParanoidiP22002.
KOiK04850.
PhylomeDBiP22002.

Family and domain databases

Gene3Di1.20.120.350. 4 hits.
InterProiIPR031688. CAC1F_C.
IPR027359. Channel_four-helix_dom.
IPR031649. GPHH_dom.
IPR005821. Ion_trans_dom.
IPR014873. VDCC_a1su_IQ.
IPR005451. VDCC_L_a1csu.
IPR005446. VDCC_L_a1su.
IPR002077. VDCCAlpha1.
[Graphical view]
PANTHERiPTHR10037:SF188. PTHR10037:SF188. 1 hit.
PfamiPF08763. Ca_chan_IQ. 1 hit.
PF16885. CAC1F_C. 1 hit.
PF16905. GPHH. 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. AlignAdd to basket

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)DescriptionActionsGraphical viewLength
Sequence conflicti83L → Q in AAA18905 (PubMed:1648941).Curated1
Sequence conflicti83L → Q in AAA42016 (PubMed:1648941).Curated1
Sequence conflicti87D → G in AAA18905 (PubMed:1648941).Curated1
Sequence conflicti520G → R in AAA18905 (PubMed:1648941).Curated1
Sequence conflicti648 – 649CW → VL in AAA18905 (PubMed:1648941).Curated2
Sequence conflicti648 – 649CW → VL in AAA42016 (PubMed:1648941).Curated2
Sequence conflicti678L → V in AAA18905 (PubMed:1648941).Curated1
Sequence conflicti678L → V in AAA42016 (PubMed:1648941).Curated1
Sequence conflicti769 – 770SP → CG in AAA18905 (PubMed:1648941).Curated2
Sequence conflicti769 – 770SP → CG in AAA42016 (PubMed:1648941).Curated2
Sequence conflicti777L → V in AAA18905 (PubMed:1648941).Curated1
Sequence conflicti777L → V in AAA42016 (PubMed:1648941).Curated1
Sequence conflicti871D → N in AAA18905 (PubMed:1648941).Curated1
Sequence conflicti1037R → RA in AAA18905 (PubMed:1648941).Curated1
Sequence conflicti1037R → RA in AAA42016 (PubMed:1648941).Curated1
Sequence conflicti1098S → C in AAA18905 (PubMed:1648941).Curated1
Sequence conflicti1098S → C in AAA42016 (PubMed:1648941).Curated1
Sequence conflicti1107T → D in AAA18905 (PubMed:1648941).Curated1
Sequence conflicti1107T → D in AAA42016 (PubMed:1648941).Curated1
Sequence conflicti1229P → R in AAA18905 (PubMed:1648941).Curated1
Sequence conflicti1229P → R in AAA42016 (PubMed:1648941).Curated1
Sequence conflicti1229P → R no nucleotide entry (PubMed:1692134).Curated1
Sequence conflicti1229P → R in AAA89157 (PubMed:7479909).Curated1
Sequence conflicti1306H → D in AAB35528 (PubMed:7485440).Curated1
Sequence conflicti1306H → G in AAA42016 (PubMed:1648941).Curated1
Sequence conflicti1306H → G in AAA89157 (PubMed:7479909).Curated1
Sequence conflicti1329I → L in AAB35528 (PubMed:7485440).Curated1
Sequence conflicti1471E → K in AAA18905 (PubMed:1648941).Curated1
Sequence conflicti1911C → S in AAA18905 (PubMed:1648941).Curated1
Sequence conflicti1911C → S in AAA42016 (PubMed:1648941).Curated1
Sequence conflicti2084K → N in AAA18905 (PubMed:1648941).Curated1
Sequence conflicti2154R → Q in AAA42016 (PubMed:1648941).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0009081 – 46MIRAF…YISPG → MVNENTRMYVPEENHQ in isoform 4 and isoform 5. 1 PublicationAdd BLAST46
Alternative sequenceiVSP_000909810R → RPAR in isoform 5. 1 Publication1
Alternative sequenceiVSP_000910964 – 979FYFDI…TIEIA → GNADYVFTSIFTLEII in isoform 4 and isoform 5. 1 PublicationAdd BLAST16
Alternative sequenceiVSP_0009111306 – 1333HYFCD…ITEVH → GYFSDPSNVFDFLIVIGSII AVILSETN in isoform 1 and isoform 4. 2 PublicationsAdd BLAST28
Alternative sequenceiVSP_0009121334 – 1344Missing in isoform 3. 1 PublicationAdd BLAST11

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.
RefSeqiNP_036649.2. NM_012517.2.
UniGeneiRn.9827.

3D structure databases

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

Protein-protein interaction databases

BioGridi246425. 4 interactors.
IntActiP22002. 4 interactors.
MINTiMINT-5026000.
STRINGi10116.ENSRNOP00000048790.

Chemistry databases

BindingDBiP22002.
ChEMBLiCHEMBL3762.
GuidetoPHARMACOLOGYi529.

PTM databases

iPTMnetiP22002.
PhosphoSitePlusiP22002.

Proteomic databases

PaxDbiP22002.
PRIDEiP22002.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi775.
RGDi2245. Cacna1c.

Phylogenomic databases

eggNOGiKOG2301. Eukaryota.
ENOG410XNP6. LUCA.
HOVERGENiHBG050763.
InParanoidiP22002.
KOiK04850.
PhylomeDBiP22002.

Enzyme and pathway databases

ReactomeiR-RNO-400042. Adrenaline,noradrenaline inhibits insulin secretion.

Miscellaneous databases

EvolutionaryTraceiP22002.
PROiP22002.

Family and domain databases

Gene3Di1.20.120.350. 4 hits.
InterProiIPR031688. CAC1F_C.
IPR027359. Channel_four-helix_dom.
IPR031649. GPHH_dom.
IPR005821. Ion_trans_dom.
IPR014873. VDCC_a1su_IQ.
IPR005451. VDCC_L_a1csu.
IPR005446. VDCC_L_a1su.
IPR002077. VDCCAlpha1.
[Graphical view]
PANTHERiPTHR10037:SF188. PTHR10037:SF188. 1 hit.
PfamiPF08763. Ca_chan_IQ. 1 hit.
PF16885. CAC1F_C. 1 hit.
PF16905. GPHH. 1 hit.
PF00520. Ion_trans. 4 hits.
[Graphical view]
PRINTSiPR00167. CACHANNEL.
PR01630. LVDCCALPHA1.
PR01635. LVDCCALPHA1C.
SMARTiSM01062. Ca_chan_IQ. 1 hit.
[Graphical view]
ProtoNetiSearch...

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 30, 2016
This is version 157 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.