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Protein

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

Gene

Cacna1c

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Pore-forming, alpha-1C subunit of the voltage-gated calcium channel that gives rise to L-type calcium currents (Probable) (PubMed:15140941, PubMed:15170217). Mediates influx of calcium ions into the cytoplasm, and thereby triggers calcium release from the sarcoplasm (By similarity). Plays an important role in excitation-contraction coupling in the heart (By similarity). Required for normal heart development and normal regulation of heart rhythm (By similarity). Required for normal contraction of smooth muscle cells in blood vessels and in the intestine. Essential for normal blood pressure regulation via its role in the contraction of arterial smooth muscle cells (By similarity). Long-lasting (L-type) calcium channels belong to the 'high-voltage activated' (HVA) group (By similarity).By similarity1 Publication2 Publications

Activity regulationi

Inhibited by dihydropyridines (DHP), such as isradipine (By similarity). Inhibited by nifedipine (By similarity). Channel activity is regulated by Ca2+ and calmodulin (PubMed:15140941). Binding of STAC1, STAC2 or STAC3 to a region that overlaps with the calmodulin binding site inhibits channel inactivation by Ca2+ and calmodulin (By similarity). Binding of calmodulin or CABP1 at the same regulatory sites results in opposite effects on the channel function (PubMed:15140941). Shear stress and pressure increases calcium channel activity (By similarity).By similarity1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi393CalciumBy similarity1
Sitei393Calcium ion selectivity and permeabilityBy similarity1
Metal bindingi736CalciumBy similarity1
Sitei736Calcium ion selectivity and permeabilityBy similarity1
Metal bindingi1144CalciumBy 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

GO - Biological processi

Keywordsi

Molecular functionCalcium channel, Calmodulin-binding, Ion channel, Voltage-gated channel
Biological processCalcium transport, Ion transport, Transport
LigandCalcium, 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 C1 Publication
Short name:
RBC1 Publication
Voltage-gated calcium channel subunit alpha Cav1.2
Gene namesi
Name:Cacna1c
Synonyms:Cach2, Cacn2, Cacnl1a1, Cchl1a1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2245 Cacna1c

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 154CytoplasmicCuratedAdd BLAST154
Transmembranei155 – 173Helical; Name=S1 of repeat IBy similarityAdd BLAST19
Topological domaini174 – 188ExtracellularCuratedAdd BLAST15
Transmembranei189 – 209Helical; Name=S2 of repeat IBy similarityAdd BLAST21
Topological domaini210 – 218CytoplasmicCurated9
Transmembranei219 – 239Helical; Name=S3 of repeat IBy similarityAdd BLAST21
Topological domaini240 – 262ExtracellularCuratedAdd BLAST23
Transmembranei263 – 281Helical; Name=S4 of repeat IBy similarityAdd BLAST19
Topological domaini282 – 298CytoplasmicCuratedAdd BLAST17
Transmembranei299 – 320Helical; Name=S5 of repeat IBy similarityAdd BLAST22
Topological domaini321 – 380ExtracellularCuratedAdd BLAST60
Intramembranei381 – 402Pore-formingBy similarityAdd BLAST22
Topological domaini403 – 410ExtracellularCurated8
Transmembranei411 – 431Helical; Name=S6 of repeat IBy similarityAdd BLAST21
Topological domaini432 – 554CytoplasmicCuratedAdd BLAST123
Transmembranei555 – 573Helical; Name=S1 of repeat IIBy similarityAdd BLAST19
Topological domaini574 – 584ExtracellularCuratedAdd BLAST11
Transmembranei585 – 605Helical; Name=S2 of repeat IIBy similarityAdd BLAST21
Topological domaini606 – 616CytoplasmicCuratedAdd BLAST11
Transmembranei617 – 636Helical; Name=S3 of repeat IIBy similarityAdd BLAST20
Topological domaini637 – 645ExtracellularCurated9
Transmembranei646 – 664Helical; Name=S4 of repeat IIBy similarityAdd BLAST19
Topological domaini665 – 683CytoplasmicCuratedAdd BLAST19
Transmembranei684 – 703Helical; Name=S5 of repeat IIBy similarityAdd BLAST20
Topological domaini704 – 723ExtracellularCuratedAdd BLAST20
Intramembranei724 – 745Pore-formingBy similarityAdd BLAST22
Topological domaini746 – 755ExtracellularCurated10
Transmembranei756 – 775Helical; Name=S6 of repeat IIBy similarityAdd BLAST20
Topological domaini776 – 930CytoplasmicCuratedAdd BLAST155
Transmembranei931 – 949Helical; Name=S1 of repeat IIIBy similarityAdd BLAST19
Topological domaini950 – 961ExtracellularCuratedAdd BLAST12
Transmembranei962 – 981Helical; Name=S2 of repeat IIIBy similarityAdd BLAST20
Topological domaini982 – 997CytoplasmicCuratedAdd BLAST16
Transmembranei998 – 1016Helical; Name=S3 of repeat IIIBy similarityAdd BLAST19
Topological domaini1017 – 1023ExtracellularCurated7
Transmembranei1024 – 1041Helical; Name=S4 of repeat IIIBy similarityAdd BLAST18
Topological domaini1042 – 1060CytoplasmicCuratedAdd BLAST19
Transmembranei1061 – 1080Helical; Name=S5 of repeat IIIBy similarityAdd BLAST20
Topological domaini1081 – 1130ExtracellularCuratedAdd BLAST50
Intramembranei1131 – 1151Pore-formingBy similarityAdd BLAST21
Topological domaini1152 – 1168ExtracellularCuratedAdd BLAST17
Transmembranei1169 – 1190Helical; Name=S6 of repeat IIIBy similarityAdd BLAST22
Topological domaini1191 – 1248CytoplasmicCuratedAdd BLAST58
Transmembranei1249 – 1270Helical; Name=S1 of repeat IVBy similarityAdd BLAST22
Topological domaini1271 – 1278ExtracellularCurated8
Transmembranei1279 – 1300Helical; Name=S2 of repeat IVBy similarityAdd BLAST22
Topological domaini1301 – 1310CytoplasmicCurated10
Transmembranei1311 – 1330Helical; Name=S3 of repeat IVBy similarityAdd BLAST20
Topological domaini1331 – 1353ExtracellularCuratedAdd BLAST23
Transmembranei1354 – 1372Helical; Name=S4 of repeat IVBy similarityAdd BLAST19
Topological domaini1373 – 1390CytoplasmicCuratedAdd BLAST18
Transmembranei1391 – 1411Helical; Name=S5 of repeat IVBy similarityAdd BLAST21
Topological domaini1412 – 1433ExtracellularCuratedAdd BLAST22
Intramembranei1434 – 1452Pore-formingBy similarityAdd BLAST19
Topological domaini1453 – 1480ExtracellularCuratedAdd BLAST28
Transmembranei1481 – 1505Helical; Name=S6 of repeat IVBy similarityAdd BLAST25
Topological domaini1506 – 2169CytoplasmicCuratedAdd BLAST664

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Membrane, Postsynaptic cell membrane, Synapse

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...) asparagineSequence analysis1
Disulfide bondi328 ↔ 356By similarity
Disulfide bondi346 ↔ 362By similarity
Glycosylationi358N-linked (GlcNAc...) asparagineSequence analysis1
Modified residuei499PhosphoserineBy similarity1
Modified residuei506PhosphothreonineBy similarity1
Modified residuei838PhosphoserineBy similarity1
Modified residuei845PhosphoserineCombined sources1
Glycosylationi1417N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1460 ↔ 1476By similarity
Glycosylationi1468N-linked (GlcNAc...) asparagineSequence analysis1
Modified residuei1516Phosphoserine; by PKASequence analysis1
Modified residuei1699PhosphoserineCombined sources1
Modified residuei1720PhosphoserineCombined sources1
Modified residuei1919Phosphoserine; by PKASequence analysis1
Modified residuei1927Phosphoserine; by PKABy similarity1

Post-translational modificationi

Phosphorylation by PKA activates the channel (By similarity). Elevated levels of blood glucose lead to increased phosphorylation by PKA (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

Detected in hippocampus and brain cortex, on neuronal cell bodies and dendrites, and in post-synaptic density in brain (at protein level) (PubMed:15140941). 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.1 Publication

Developmental stagei

Expressed from embryonic day 16 until the adult stage.

Interactioni

Subunit structurei

Component of a calcium channel complex consisting of a pore-forming alpha subunit (CACNA1C) and ancillary beta, gamma and delta subunits (PubMed:15170217). The channel complex contains alpha, beta, gamma and delta subunits in a 1:1:1:1 ratio, i.e. it contains only one of each type of subunit. CACNA1C channel activity is modulated by ancillary subunits, such as CACNB1, CACNB2, CACNB3, CACNA2D1 and CACNA2D4 (By similarity). Intereracts with the gamma subunits CACNG4, CACNG6, CACNG7 and CACNG8 (By similarity). Interacts with CACNB1 (By similarity). Interacts with CACNB2. Identified in a complex with CACNA2D4 and CACNB3 (By similarity). Interacts with CACNB3 (PubMed:24751537, PubMed:15170217). Interacts with CACNA2D1. Interacts with CACNA2D4. Interacts with CALM1. Interacts (via the N-terminus and the C-terminal C and IQ motifs) with CABP1; this inhibits Ca2+-dependent channel inactivation (PubMed:15140941). 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 (PubMed:15140941). The binding to the cytoplasmic N-terminal domain is calcium independent but is essential for the channel modulation. Interacts (via C-terminal CDB motif) with CABP5; in a calcium-dependent manner. Interacts with CIB1; the interaction increases upon cardiomyocytes hypertrophy (By similarity). Interacts with STAC2 and STAC3; this inhibits channel inactivation (By similarity).By similarity3 Publications

Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

BioGridi246425, 4 interactors
CORUMiP22002
IntActiP22002, 4 interactors
MINTiP22002
STRINGi10116.ENSRNOP00000048790

Chemistry databases

BindingDBiP22002

Structurei

Secondary structure

12169
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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
Regioni77 – 98Calmodulin-bindingBy similarityAdd BLAST22
Regioni458 – 475AID/alpha-interaction domain; mediates interaction with the beta subunit1 PublicationAdd BLAST18
Regioni859 – 906Interaction with STAC2By similarityAdd BLAST48
Regioni1118 – 1207Dihydropyridine bindingBy similarityAdd BLAST90
Regioni1459 – 1527Dihydropyridine bindingBy similarityAdd BLAST69
Regioni1473 – 1515Phenylalkylamine bindingBy similarityAdd BLAST43
Regioni1640 – 1673Calmodulin-bindingBy similarityAdd BLAST34
Regioni1640 – 1667Important for interaction with STAC1, STAC2 and STAC3By similarityAdd BLAST28
Regioni1646 – 1666Calmodulin-binding IQ regionBy similarityAdd BLAST21
Regioni1680 – 1699Important for localization in at the junctional membraneBy similarityAdd BLAST20

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi391 – 394Selectivity filter of repeat IBy similarity4
Motifi734 – 737Selectivity filter of repeat IIBy similarity4
Motifi1142 – 1145Selectivity filter of repeat IIIBy similarity4
Motifi1443 – 1446Selectivity filter of repeat IVBy similarity4

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
InterProiView protein in InterPro
IPR031688 CAC1F_C
IPR031649 GPHH_dom
IPR005821 Ion_trans_dom
IPR014873 VDCC_a1su_IQ
IPR005451 VDCC_L_a1csu
IPR005446 VDCC_L_a1su
IPR002077 VDCCAlpha1
IPR027359 Volt_channel_dom_sf
PfamiView protein in Pfam
PF08763 Ca_chan_IQ, 1 hit
PF16885 CAC1F_C, 1 hit
PF16905 GPHH, 1 hit
PF00520 Ion_trans, 4 hits
PRINTSiPR00167 CACHANNEL
PR01630 LVDCCALPHA1
PR01635 LVDCCALPHA1C
SMARTiView protein in SMART
SM01062 Ca_chan_IQ, 1 hit

Sequences (5+)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket
Note: Additional isoforms seem to exist.

This entry has 5 described isoforms and 3 potential isoforms that are computationally mapped.Show allAlign All

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

Computationally mapped potential isoform sequencesi

There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A0G2QC25A0A0G2QC25_RAT
Voltage-dependent L-type calcium ch...
Cacna1c
2,006Annotation score:
F1MA84F1MA84_RAT
Voltage-dependent L-type calcium ch...
Cacna1c
1,981Annotation score:
E9PT56E9PT56_RAT
Voltage-dependent L-type calcium ch...
Cacna1c
1,901Annotation score:

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

Similar proteinsi

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
CORUMiP22002
IntActiP22002, 4 interactors
MINTiP22002
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

Miscellaneous databases

EvolutionaryTraceiP22002
PROiPR:P22002

Family and domain databases

Gene3Di1.20.120.350, 4 hits
InterProiView protein in InterPro
IPR031688 CAC1F_C
IPR031649 GPHH_dom
IPR005821 Ion_trans_dom
IPR014873 VDCC_a1su_IQ
IPR005451 VDCC_L_a1csu
IPR005446 VDCC_L_a1su
IPR002077 VDCCAlpha1
IPR027359 Volt_channel_dom_sf
PfamiView protein in Pfam
PF08763 Ca_chan_IQ, 1 hit
PF16885 CAC1F_C, 1 hit
PF16905 GPHH, 1 hit
PF00520 Ion_trans, 4 hits
PRINTSiPR00167 CACHANNEL
PR01630 LVDCCALPHA1
PR01635 LVDCCALPHA1C
SMARTiView protein in SMART
SM01062 Ca_chan_IQ, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiCAC1C_RAT
AccessioniPrimary (citable) accession number: P22002
Secondary accession number(s): P27733
, P27734, Q62816, Q63271, Q64178
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: August 1, 1991
Last modified: September 12, 2018
This is version 171 of the entry and version 1 of the sequence. See 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
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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