Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

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

Gene

CACNA1C

Organism
Oryctolagus cuniculus (Rabbit)
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 (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei393 – 3931Calcium ion selectivity and permeability
Sitei736 – 7361Calcium ion selectivity and permeability
Sitei1145 – 11451Calcium ion selectivity and permeability
Sitei1446 – 14461Calcium ion selectivity and permeability

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi1535 – 154612Add
BLAST

GO - Molecular functioni

  • calmodulin binding Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
  • voltage-gated calcium channel activity Source: UniProtKB

GO - Biological processi

  • calcium ion transmembrane transport Source: UniProtKB
  • calcium ion transmembrane transport via high voltage-gated calcium channel Source: BHF-UCL
  • calcium ion transport into cytosol Source: BHF-UCL
  • cardiac conduction Source: UniProtKB
  • positive regulation of cytosolic calcium ion concentration Source: UniProtKB
  • regulation of membrane repolarization during action potential Source: BHF-UCL
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
Smooth muscle calcium channel blocker receptor
Short name:
CACB-receptor
Voltage-gated calcium channel subunit alpha Cav1.2
Gene namesi
Name:CACNA1C
Synonyms:CACH2, CACN2, CACNL1A1, CCHL1A1
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
Proteomesi
  • UP000001811 Componenti: Unplaced

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 154154CytoplasmicSequence analysisAdd
BLAST
Transmembranei155 – 17319Helical; Name=S1 of repeat IAdd
BLAST
Topological domaini174 – 19017ExtracellularSequence analysisAdd
BLAST
Transmembranei191 – 21121Helical; Name=S2 of repeat IAdd
BLAST
Topological domaini212 – 22312CytoplasmicSequence analysisAdd
BLAST
Transmembranei224 – 24219Helical; Name=S3 of repeat IAdd
BLAST
Topological domaini243 – 26220ExtracellularSequence analysisAdd
BLAST
Transmembranei263 – 28119Helical; Name=S4 of repeat IAdd
BLAST
Topological domaini282 – 30019CytoplasmicSequence analysisAdd
BLAST
Transmembranei301 – 32020Helical; Name=S5 of repeat IAdd
BLAST
Topological domaini321 – 41090ExtracellularSequence analysisAdd
BLAST
Transmembranei411 – 43525Helical; Name=S6 of repeat IAdd
BLAST
Topological domaini436 – 554119CytoplasmicSequence analysisAdd
BLAST
Transmembranei555 – 57319Helical; Name=S1 of repeat IIAdd
BLAST
Topological domaini574 – 58815ExtracellularSequence analysisAdd
BLAST
Transmembranei589 – 60820Helical; Name=S2 of repeat IIAdd
BLAST
Topological domaini609 – 6168CytoplasmicSequence analysis
Transmembranei617 – 63519Helical; Name=S3 of repeat IIAdd
BLAST
Topological domaini636 – 64510ExtracellularSequence analysis
Transmembranei646 – 66419Helical; Name=S4 of repeat IIAdd
BLAST
Topological domaini665 – 68319CytoplasmicSequence analysisAdd
BLAST
Transmembranei684 – 70320Helical; Name=S5 of repeat IIAdd
BLAST
Topological domaini704 – 75855ExtracellularSequence analysisAdd
BLAST
Transmembranei759 – 78325Helical; Name=S6 of repeat IIAdd
BLAST
Topological domaini784 – 930147CytoplasmicSequence analysisAdd
BLAST
Transmembranei931 – 94919Helical; Name=S1 of repeat IIIAdd
BLAST
Topological domaini950 – 96516ExtracellularSequence analysisAdd
BLAST
Transmembranei966 – 98520Helical; Name=S2 of repeat IIIAdd
BLAST
Topological domaini986 – 99712CytoplasmicSequence analysisAdd
BLAST
Transmembranei998 – 101619Helical; Name=S3 of repeat IIIAdd
BLAST
Topological domaini1017 – 10237ExtracellularSequence analysis
Transmembranei1024 – 104219Helical; Name=S4 of repeat IIIAdd
BLAST
Topological domaini1043 – 106119CytoplasmicSequence analysisAdd
BLAST
Transmembranei1062 – 108120Helical; Name=S5 of repeat IIIAdd
BLAST
Topological domaini1082 – 117190ExtracellularSequence analysisAdd
BLAST
Transmembranei1172 – 119625Helical; Name=S6 of repeat IIIAdd
BLAST
Topological domaini1197 – 124953CytoplasmicSequence analysisAdd
BLAST
Transmembranei1250 – 126819Helical; Name=S1 of repeat IVAdd
BLAST
Topological domaini1269 – 128315ExtracellularSequence analysisAdd
BLAST
Transmembranei1284 – 130320Helical; Name=S2 of repeat IVAdd
BLAST
Topological domaini1304 – 13118CytoplasmicSequence analysis
Transmembranei1312 – 133019Helical; Name=S3 of repeat IVAdd
BLAST
Topological domaini1331 – 135424ExtracellularSequence analysisAdd
BLAST
Transmembranei1355 – 137319Helical; Name=S4 of repeat IVAdd
BLAST
Topological domaini1374 – 139219CytoplasmicSequence analysisAdd
BLAST
Transmembranei1393 – 141220Helical; Name=S5 of repeat IVAdd
BLAST
Topological domaini1413 – 148169ExtracellularSequence analysisAdd
BLAST
Transmembranei1482 – 150625Helical; Name=S6 of repeat IVAdd
BLAST
Topological domaini1507 – 2171665CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • integral component of membrane Source: UniProtKB
  • L-type voltage-gated calcium channel complex Source: BHF-UCL
  • plasma membrane Source: UniProtKB
  • postsynaptic density Source: UniProtKB
  • voltage-gated calcium channel complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi168 – 1681C → G: Small reduction of current amplitude. 1 Publication
Mutagenesisi168 – 1681C → K or W: No current. 1 Publication
Mutagenesisi168 – 1681C → S: No effect. 1 Publication
Mutagenesisi168 – 1681C → Y: Slower channel activation and reduction of current amplitude. 1 Publication
Mutagenesisi393 – 3931E → K: Drastic reduction of barium permeability. Reduction of calcium block of lithium currents. 1 Publication
Mutagenesisi393 – 3931E → Q: Attenuates calcium block of inward barium, lithium, or cadmium currents. 1 Publication
Mutagenesisi736 – 7361E → K: Drastic reduction of barium permeability. Reduction of calcium block of lithium currents. 1 Publication
Mutagenesisi736 – 7361E → Q: Attenuates calcium block of inward barium, lithium, or cadmium currents. 1 Publication
Mutagenesisi1145 – 11451E → K: Drastic reduction of barium permeability. Reduction of calcium block of lithium currents. 1 Publication
Mutagenesisi1145 – 11451E → Q: Attenuates calcium block of inward barium, lithium, or cadmium currents. 1 Publication
Mutagenesisi1446 – 14461E → K: Moderate reduction of barium permeability. Reduction of calcium block of lithium currents. 1 Publication
Mutagenesisi1446 – 14461E → Q: Attenuates calcium block of inward barium, lithium, or cadmium currents. 1 Publication

Chemistry

ChEMBLiCHEMBL2830.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 21712171Voltage-dependent L-type calcium channel subunit alpha-1CPRO_0000053930Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi183 – 1831N-linked (GlcNAc...)Sequence analysis
Glycosylationi358 – 3581N-linked (GlcNAc...)Sequence analysis
Modified residuei499 – 4991PhosphoserineBy similarity
Modified residuei506 – 5061PhosphothreonineBy similarity
Modified residuei838 – 8381PhosphoserineBy similarity
Modified residuei845 – 8451PhosphoserineBy similarity
Glycosylationi1418 – 14181N-linked (GlcNAc...)Sequence analysis
Glycosylationi1469 – 14691N-linked (GlcNAc...)Sequence analysis
Modified residuei1517 – 15171Phosphoserine; by PKASequence analysis
Modified residuei1700 – 17001PhosphoserineBy similarity
Modified residuei1721 – 17211PhosphoserineBy similarity
Modified residuei1920 – 19201Phosphoserine; by PKASequence analysis
Modified residuei1928 – 19281Phosphoserine; by PKASequence analysis

Post-translational modificationi

Phosphorylation by PKA activates the channel.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

PTM databases

iPTMnetiP15381.

Expressioni

Tissue specificityi

Expression in cardiac muscle. In lung, expressed in airway and vascular smooth muscle cells.

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 with CABP1 and 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

GO - Molecular functioni

  • calmodulin binding Source: UniProtKB

Protein-protein interaction databases

DIPiDIP-61286N.

Chemistry

BindingDBiP15381.

Structurei

Secondary structure

1
2171
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi451 – 47525Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4DEYX-ray1.95B435-539[»]
ProteinModelPortaliP15381.
SMRiP15381. Positions 1642-1670.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati141 – 438298IAdd
BLAST
Repeati540 – 786247IIAdd
BLAST
Repeati917 – 1199283IIIAdd
BLAST
Repeati1236 – 1509274IVAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni458 – 47518Binding to the beta subunitBy similarityAdd
BLAST
Regioni1119 – 120991Dihydropyridine bindingBy similarityAdd
BLAST
Regioni1460 – 151758Dihydropyridine bindingBy similarityAdd
BLAST
Regioni1474 – 152047Phenylalkylamine bindingBy similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi684 – 6907Poly-Leu
Compositional biasi798 – 8047Poly-Glu
Compositional biasi1177 – 11837Poly-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.

Sequence similaritiesi

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

HOVERGENiHBG050763.
InParanoidiP15381.
KOiK04850.

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. 2 hits.
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 1 (identifier: P15381-1) [UniParc]FASTAAdd to basket

Also known as: CACH2A

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
MLRALVQPAT PAYQPLPSHL SAETESTCKG TVVHEAQLNH FYISPGGSNY
60 70 80 90 100
GSPRPAHANM NANAAAGLAP EHIPTPGAAL SWQAAIDAAR QAKLMGSAGN
110 120 130 140 150
ATISTVSSTQ RKRQQYGKPK KQGSTTATRP 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 QEGVADVPAE DDPSPCALET
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 NEDEGMDEEK 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 LETILVETKV MSPLGISVLR
660 670 680 690 700
CVRLLRIFKI TRYWNSLSNL VASLLNSVRS IASLLLLLFL FIIIFSLLGM
710 720 730 740 750
QLFGGKFNFD EMQTRRSTFD NFPQSLLTVF QILTGEDWNS VMYDGIMAYG
760 770 780 790 800
GPSFPGMLVC IYFIILFICG NYILLNVFLA IAVDNLADAE SLTSAQKEEE
810 820 830 840 850
EEKERKKLAR TASPEKKQEV VGKPALEEAK EEKIELKSIT ADGESPPTTK
860 870 880 890 900
INMDDLQPNE SEDKSPYPNP ETTGEEDEEE 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 RVLRPLRAIN RAKGLKHVVQ
1060 1070 1080 1090 1100
CVFVAIRTIG NIVIVTTLLQ FMFACIGVQL FKGKLYTCSD SSKQTEAECK
1110 1120 1130 1140 1150
GNYITYKDGE VDHPIIQPRS WENSKFDFDN VLAAMMALFT VSTFEGWPEL
1160 1170 1180 1190 1200
LYRSIDSHTE DKGPIYNYRV EISIFFIIYI IIIAFFMMNI FVGFVIVTFQ
1210 1220 1230 1240 1250
EQGEQEYKNC ELDKNQRQCV EYALKARPLR RYIPKNQHQY KVWYVVNSTY
1260 1270 1280 1290 1300
FEYLMFVLIL LNTICLAMQH YGQSCLFKIA MNILNMLFTG LFTVEMILKL
1310 1320 1330 1340 1350
IAFKPKGYFS DPWNVFDFLI VIGSIIDVIL SETNPAEHTQ CSPSMNAEEN
1360 1370 1380 1390 1400
SRISITFFRL FRVMRLVKLL SRGEGIRTLL WTFIKSFQAL PYVALLIVML
1410 1420 1430 1440 1450
FFIYAVIGMQ VFGKIALNDT TEINRNNNFQ TFPQAVLLLF RCATGEAWQD
1460 1470 1480 1490 1500
IMLACMPGKK CAPESEPHNS TEGETPCGSS FAVFYFISFY MLCAFLIINL
1510 1520 1530 1540 1550
FVAVIMDNFD YLTRDWSILG PHHLDEFKRI WAEYDPEAKG RIKHLDVVTL
1560 1570 1580 1590 1600
LRRIQPPLGF GKLCPHRVAC KRLVSMNMPL NSDGTVMFNA TLFALVRTAL
1610 1620 1630 1640 1650
RIKTEGNLEQ ANEELRAIIK KIWKRTSMKL LDQVVPPAGD DEVTVGKFYA
1660 1670 1680 1690 1700
TFLIQEYFRK FKKRKEQGLV GKPSQRNALS LQAGLRTLHD IGPEIRRAIS
1710 1720 1730 1740 1750
GDLTAEEELD KAMKEAVSAA SEDDIFRRAG GLFGNHVSYY QSDSRSAFPQ
1760 1770 1780 1790 1800
TFTTQRPLHI SKAGNNQGDT ESPSHEKLVD STFTPSSYSS TGSNANINNA
1810 1820 1830 1840 1850
NNTALGRLPR PAGYPSTVST VEGHGSPLSP AVRAQEAAWK LSSKRCHSQE
1860 1870 1880 1890 1900
SQIAMACQEG ASQDDNYDVR IGEDAECCSE PSLLSTEMLS YQDDENRQLA
1910 1920 1930 1940 1950
PPEEEKRDIR LSPKKGFLRS ASLGRRASFH LECLKRQKNQ GGDISQKTVL
1960 1970 1980 1990 2000
PLHLVHHQAL AVAGLSPLLQ RSHSPTSLPR PCATPPATPG SRGWPPQPIP
2010 2020 2030 2040 2050
TLRLEGADSS EKLNSSFPSI HCGSWSGENS PCRGDSSAAR RARPVSLTVP
2060 2070 2080 2090 2100
SQAGAQGRQF HGSASSLVEA VLISEGLGQF AQDPKFIEVT TQELADACDL
2110 2120 2130 2140 2150
TIEEMENAAD DILSGGARQS PNGTLLPFVN RRDPGRDRAG QNEQDASGAC
2160 2170
APGCGQSEEA LADRRAGVSS L
Length:2,171
Mass (Da):242,784
Last modified:April 1, 1990 - v1
Checksum:iB64F08F09D71C65D
GO
Isoform 2 (identifier: P15381-2) [UniParc]FASTAAdd to basket

Also known as: CACH2C

The sequence of this isoform differs from the canonical sequence as follows:
     1307-1334: GYFSDPWNVFDFLIVIGSIIDVILSETN → HYFCDAWNTFDALIVVGSIVDIAITEVH

Show »
Length:2,171
Mass (Da):242,759
Checksum:i7F19227123159A9E
GO
Isoform 3 (identifier: P15381-3) [UniParc]FASTAAdd to basket

Also known as: CACH2D

The sequence of this isoform differs from the canonical sequence as follows:
     1335-1345: Missing.

Show »
Length:2,160
Mass (Da):241,615
Checksum:i567DCCDB7351490F
GO
Isoform 4 (identifier: P15381-4) [UniParc]FASTAAdd to basket

Also known as: Lung

The sequence of this isoform differs from the canonical sequence as follows:
     1-46: MLRALVQPATPAYQPLPSHLSAETESTCKGTVVHEAQLNHFYISPG → MVNENTRMYIPEENHQ
     402-421: MQDAMGYELPWVYFVSLVIF → VNDAVGRDWPWIYFVTLIII
     494-494: M → RGTPAGLHAQKKGKFAWFSHSTETHV
     1307-1334: GYFSDPWNVFDFLIVIGSIIDVILSETN → HYFCDAWNTFDALIVVGSIVDIAITEVH

Show »
Length:2,166
Mass (Da):242,485
Checksum:i824857C865A8E5F5
GO
Isoform 5 (identifier: P15381-5) [UniParc]FASTAAdd to basket

Also known as: C141

The sequence of this isoform differs from the canonical sequence as follows:
     1-46: MLRALVQPATPAYQPLPSHLSAETESTCKGTVVHEAQLNHFYISPG → MVNENTRMYIPEENHQ
     66-79: Missing.

Show »
Length:2,127
Mass (Da):238,515
Checksum:iD183FDEC42FB6401
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1346 – 13461N → S in AAA31182 (PubMed:2173707).Curated
Sequence conflicti1468 – 14681H → S in AAA31182 (PubMed:2173707).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 4646MLRAL…YISPG → MVNENTRMYIPEENHQ in isoform 4 and isoform 5. 1 PublicationVSP_000902Add
BLAST
Alternative sequencei66 – 7914Missing in isoform 5. 1 PublicationVSP_000903Add
BLAST
Alternative sequencei402 – 42120MQDAM…SLVIF → VNDAVGRDWPWIYFVTLIII in isoform 4. CuratedVSP_000904Add
BLAST
Alternative sequencei494 – 4941M → RGTPAGLHAQKKGKFAWFSH STETHV in isoform 4. CuratedVSP_000905
Alternative sequencei1307 – 133428GYFSD…LSETN → HYFCDAWNTFDALIVVGSIV DIAITEVH in isoform 2 and isoform 4. 1 PublicationVSP_000906Add
BLAST
Alternative sequencei1335 – 134511Missing in isoform 3. CuratedVSP_000907Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15539 mRNA. Translation: CAA33546.1.
X55763 mRNA. Translation: CAA39289.1.
X60782 mRNA. Translation: CAA43196.1.
M57974 mRNA. Translation: AAA31182.1.
PIRiS05054.
S11339.
RefSeqiNP_001129994.1. NM_001136522.1. [P15381-1]
UniGeneiOcu.1835.
Ocu.3254.

Genome annotation databases

GeneIDi100101555.
KEGGiocu:100101555.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15539 mRNA. Translation: CAA33546.1.
X55763 mRNA. Translation: CAA39289.1.
X60782 mRNA. Translation: CAA43196.1.
M57974 mRNA. Translation: AAA31182.1.
PIRiS05054.
S11339.
RefSeqiNP_001129994.1. NM_001136522.1. [P15381-1]
UniGeneiOcu.1835.
Ocu.3254.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4DEYX-ray1.95B435-539[»]
ProteinModelPortaliP15381.
SMRiP15381. Positions 1642-1670.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-61286N.

Chemistry

BindingDBiP15381.
ChEMBLiCHEMBL2830.

PTM databases

iPTMnetiP15381.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100101555.
KEGGiocu:100101555.

Organism-specific databases

CTDi775.

Phylogenomic databases

HOVERGENiHBG050763.
InParanoidiP15381.
KOiK04850.

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. 2 hits.
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...

Publicationsi

  1. "Primary structure and functional expression of the cardiac dihydropyridine-sensitive calcium channel."
    Mikami A., Imoto K., Tanabe T., Ni Idomme T., Mori Y., Takeshima H., Narumiya S., Numa S.
    Nature 340:230-233(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Heart.
  2. "Primary structure and functional expression of a high voltage activated calcium channel from rabbit lung."
    Biel M., Ruth P., Bosse E., Hullin R., Stuehmer W., Flockerzi V., Hoffmann F.
    FEBS Lett. 269:409-412(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Heart and Lung.
  3. "Tissue-specific expression of high-voltage-activated dihydropyridine-sensitive L-type calcium channels."
    Biel M., Hullin R., Freundner S., Singer D., Dascal N., Flockerzi V., Hofmann F.
    Eur. J. Biochem. 200:81-88(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-98 (ISOFORM 5).
    Tissue: Heart muscle.
  4. "Molecular diversity of L-type calcium channels. Evidence for alternative splicing of the transcripts of three non-allelic genes."
    Perez-Reyes E., Wei X., Castellano A., Birnbaumer L.
    J. Biol. Chem. 265:20430-20436(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1192-1485 (ISOFORM 2).
    Tissue: Heart.
  5. "Molecular determinants of Ca2+ selectivity and ion permeation in L-type Ca2+ channels."
    Yang J., Ellinor P.T., Sather W.A., Zhang J.-F., Tsien R.W.
    Nature 366:158-161(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS, CALCIUM-BINDING.
  6. "A mutation affecting dihydropyridine-sensitive current levels and activation kinetics in Drosophila muscle and mammalian heart calcium channels."
    Ren D., Xu H., Eberl D.F., Chopra M., Hall L.M.
    J. Neurosci. 18:2335-2341(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF CYS-168.
  7. "Cyclic AMP-dependent phosphorylation and regulation of the cardiac dihydropyridine-sensitive Ca channel."
    Yoshida A., Takahashi M., Nishimura S., Takeshima H., Kokubun S.
    FEBS Lett. 309:343-349(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION BY PKA.
  8. "Calcium channel beta-subunit binds to a conserved motif in the I-II cytoplasmic linker of the alpha 1-subunit."
    Pragnell M., de Waard M., Mori Y., Tanabe T., Snutch T.P., Campbell K.P.
    Nature 368:67-70(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: BETA-SUBUNIT BINDING DOMAIN.
  9. "Essential Ca(2+)-binding motif for Ca(2+)-sensitive inactivation of L-type Ca2+ channels."
    de Leon M., Wang Y., Jones L., Perez-Reyes E., Wei X., Soong T.W., Snutch T.P., Yue D.T.
    Science 270:1502-1505(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: EF-HAND MOTIF AND CALCIUM INACTIVATION.
  10. "Dominant negative suppression of Rad leads to QT prolongation and causes ventricular arrhythmias via modulation of L-type Ca2+ channels in the heart."
    Yada H., Murata M., Shimoda K., Yuasa S., Kawaguchi H., Ieda M., Adachi T., Murata M., Ogawa S., Fukuda K.
    Circ. Res. 101:69-77(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.

Entry informationi

Entry nameiCAC1C_RABIT
AccessioniPrimary (citable) accession number: P15381
Secondary accession number(s): Q03716, Q28676, Q99243
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: June 8, 2016
This is version 136 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.