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Q01668

- CAC1D_HUMAN

UniProt

Q01668 - CAC1D_HUMAN

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Protein

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

Gene

CACNA1D

Organism
Homo sapiens (Human)
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-1D 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).1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei364 – 3641Calcium ion selectivity and permeabilityBy similarity
Sitei705 – 7051Calcium ion selectivity and permeabilityBy similarity
Sitei1101 – 11011Calcium ion selectivity and permeabilityBy similarity
Sitei1406 – 14061Calcium ion selectivity and permeabilityBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi1493 – 150412By similarityAdd
BLAST

GO - Molecular functioni

  1. alpha-actinin binding Source: BHF-UCL
  2. ankyrin binding Source: BHF-UCL
  3. high voltage-gated calcium channel activity Source: Ensembl
  4. metal ion binding Source: UniProtKB-KW
  5. voltage-gated calcium channel activity Source: UniProtKB
  6. voltage-gated calcium channel activity involved in cardiac muscle cell action potential Source: BHF-UCL
  7. voltage-gated calcium channel activity involved SA node cell action potential Source: BHF-UCL

GO - Biological processi

  1. adenylate cyclase-modulating G-protein coupled receptor signaling pathway Source: BHF-UCL
  2. axon guidance Source: Reactome
  3. calcium ion import Source: BHF-UCL
  4. calcium ion transmembrane transport Source: BHF-UCL
  5. calcium ion transport Source: UniProtKB
  6. energy reserve metabolic process Source: Reactome
  7. membrane depolarization during action potential Source: RefGenome
  8. membrane depolarization during cardiac muscle cell action potential Source: BHF-UCL
  9. membrane repolarization during SA node cell action potential Source: BHF-UCL
  10. positive regulation of calcium ion transport Source: BHF-UCL
  11. regulation of atrial cardiac muscle cell membrane repolarization Source: BHF-UCL
  12. regulation of heart rate by cardiac conduction Source: BHF-UCL
  13. regulation of insulin secretion Source: Reactome
  14. regulation of potassium ion transmembrane transport Source: BHF-UCL
  15. regulation of potassium ion transmembrane transporter activity Source: BHF-UCL
  16. sensory perception of sound Source: BHF-UCL
  17. small molecule metabolic process Source: Reactome
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_18312. NCAM1 interactions.
REACT_18325. Regulation of insulin secretion.
REACT_18339. Adrenaline,noradrenaline inhibits insulin secretion.

Names & Taxonomyi

Protein namesi
Recommended name:
Voltage-dependent L-type calcium channel subunit alpha-1D
Alternative name(s):
Calcium channel, L type, alpha-1 polypeptide, isoform 2
Voltage-gated calcium channel subunit alpha Cav1.3
Gene namesi
Name:CACNA1D
Synonyms:CACH3, CACN4, CACNL1A2, CCHL1A2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:1391. CACNA1D.

Subcellular locationi

Membrane 1 Publication; Multi-pass membrane protein 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 126126CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei127 – 14519Helical; Name=S1 of repeat ISequence AnalysisAdd
BLAST
Topological domaini146 – 16318ExtracellularSequence AnalysisAdd
BLAST
Transmembranei164 – 18320Helical; Name=S2 of repeat ISequence AnalysisAdd
BLAST
Topological domaini184 – 19512CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei196 – 21419Helical; Name=S3 of repeat ISequence AnalysisAdd
BLAST
Topological domaini215 – 23521ExtracellularSequence AnalysisAdd
BLAST
Transmembranei236 – 25419Helical; Name=S4 of repeat ISequence AnalysisAdd
BLAST
Topological domaini255 – 27319CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei274 – 29320Helical; Name=S5 of repeat ISequence AnalysisAdd
BLAST
Topological domaini294 – 38188ExtracellularSequence AnalysisAdd
BLAST
Transmembranei382 – 40625Helical; Name=S6 of repeat ISequence AnalysisAdd
BLAST
Topological domaini407 – 523117CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei524 – 54320Helical; Name=S1 of repeat IISequence AnalysisAdd
BLAST
Topological domaini544 – 55815ExtracellularSequence AnalysisAdd
BLAST
Transmembranei559 – 57719Helical; Name=S2 of repeat IISequence AnalysisAdd
BLAST
Topological domaini578 – 5858CytoplasmicSequence Analysis
Transmembranei586 – 60419Helical; Name=S3 of repeat IISequence AnalysisAdd
BLAST
Topological domaini605 – 61410ExtracellularSequence Analysis
Transmembranei615 – 63319Helical; Name=S4 of repeat IISequence AnalysisAdd
BLAST
Topological domaini634 – 65219CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei653 – 67321Helical; Name=S5 of repeat IISequence AnalysisAdd
BLAST
Topological domaini674 – 72754ExtracellularSequence AnalysisAdd
BLAST
Transmembranei728 – 75225Helical; Name=S6 of repeat IISequence AnalysisAdd
BLAST
Topological domaini753 – 886134CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei887 – 90519Helical; Name=S1 of repeat IIISequence AnalysisAdd
BLAST
Topological domaini906 – 92116ExtracellularSequence AnalysisAdd
BLAST
Transmembranei922 – 94120Helical; Name=S2 of repeat IIISequence AnalysisAdd
BLAST
Topological domaini942 – 95312CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei954 – 97219Helical; Name=S3 of repeat IIISequence AnalysisAdd
BLAST
Topological domaini973 – 9786ExtracellularSequence Analysis
Transmembranei979 – 99820Helical; Name=S4 of repeat IIISequence AnalysisAdd
BLAST
Topological domaini999 – 101719CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei1018 – 103720Helical; Name=S5 of repeat IIISequence AnalysisAdd
BLAST
Topological domaini1038 – 112790ExtracellularSequence AnalysisAdd
BLAST
Transmembranei1128 – 114821Helical; Name=S6 of repeat IIISequence AnalysisAdd
BLAST
Topological domaini1149 – 120557CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei1206 – 122419Helical; Name=S1 of repeat IVSequence AnalysisAdd
BLAST
Topological domaini1225 – 123915ExtracellularSequence AnalysisAdd
BLAST
Transmembranei1240 – 125920Helical; Name=S2 of repeat IVSequence AnalysisAdd
BLAST
Topological domaini1260 – 12667CytoplasmicSequence Analysis
Transmembranei1267 – 128822Helical; Name=S3 of repeat IVSequence AnalysisAdd
BLAST
Topological domaini1289 – 131325ExtracellularSequence AnalysisAdd
BLAST
Transmembranei1314 – 133320Helical; Name=S4 of repeat IVSequence AnalysisAdd
BLAST
Topological domaini1334 – 135219CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei1353 – 137220Helical; Name=S5 of repeat IVSequence AnalysisAdd
BLAST
Topological domaini1373 – 143967ExtracellularSequence AnalysisAdd
BLAST
Transmembranei1440 – 146425Helical; Name=S6 of repeat IVSequence AnalysisAdd
BLAST
Topological domaini1465 – 2161697CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. plasma membrane Source: BHF-UCL
  2. voltage-gated calcium channel complex Source: UniProtKB
  3. Z disc Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Involvement in diseasei

Sinoatrial node dysfunction and deafness (SANDD) [MIM:614896]: A disease characterized by congenital severe to profound deafness without vestibular dysfunction, associated with episodic syncope due to intermittent pronounced bradycardia.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti403 – 4031G → GG in SANDD; the mutant channels are unable to conduct calcium ions currents and have abnormal voltage-dependent gating. 1 Publication
VAR_069170
Primary aldosteronism, seizures, and neurologic abnormalities (PASNA) [MIM:615474]: A disorder characterized by hypertension, hypokalemia, and high aldosterone levels with low plasma renin activity and an elevated aldosterone/renin ratio. Other features include generalized seizures, cerebral palsy, spasticity, intellectual disability, and developmental delay.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti403 – 4031G → D in PASNA; the mutant channel is activated at less depolarized potentials; results in increased current density and impaired channel inactivation. 1 Publication
VAR_070868
Natural varianti750 – 7501I → M in PASNA; the mutant channel is activated at less depolarized potentials; results in increased current density. 1 Publication
VAR_070869

Keywords - Diseasei

Deafness, Disease mutation, Epilepsy

Organism-specific databases

MIMi614896. phenotype.
615474. phenotype.
Orphaneti85142. Aldosterone-producing adenoma.
369929. Aldosterone-producing adenoma with seizures and neurological abnormalities.
324321. Sinoatrial node dysfunction and deafness.
PharmGKBiPA84.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 21612161Voltage-dependent L-type calcium channel subunit alpha-1DPRO_0000053933Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi155 – 1551N-linked (GlcNAc...)Sequence Analysis
Glycosylationi225 – 2251N-linked (GlcNAc...)Sequence Analysis
Glycosylationi329 – 3291N-linked (GlcNAc...)Sequence Analysis
Modified residuei1475 – 14751Phosphoserine; by PKASequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiQ01668.
PRIDEiQ01668.

PTM databases

PhosphoSiteiQ01668.

Expressioni

Tissue specificityi

Expressed in pancreatic islets and in brain, where it has been seen in cerebral cortex, hippocampus, basal ganglia, habenula and thalamus. Expressed in the small cell lung carcinoma cell line SCC-9. No expression in skeletal muscle.1 Publication

Gene expression databases

BgeeiQ01668.
CleanExiHS_CACNA1D.
ExpressionAtlasiQ01668. baseline and differential.
GenevestigatoriQ01668.

Organism-specific databases

HPAiHPA020215.

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. Channel activity is further modulated, depending on the presence of specific delta subunit isoforms. Interacts (via IQ domain) with CABP1 and CABP4 in a calcium independent manner (By similarity). Interacts with RIMBP2 (By similarity).By similarity

Protein-protein interaction databases

BioGridi107230. 1 interaction.
DIPiDIP-48998N.
IntActiQ01668. 1 interaction.
STRINGi9606.ENSP00000288139.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3LV3X-ray1.94C502-510[»]
ProteinModelPortaliQ01668.
SMRiQ01668. Positions 164-405, 420-448, 519-753, 882-1152, 1201-1465, 1548-1628.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati113 – 409297IAdd
BLAST
Repeati509 – 755247IIAdd
BLAST
Repeati873 – 1155283IIIAdd
BLAST
Repeati1192 – 1467276IVAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni429 – 44618Binding to the beta subunitBy similarityAdd
BLAST
Regioni1075 – 116591Dihydropyridine bindingBy similarityAdd
BLAST
Regioni1420 – 148667Dihydropyridine bindingBy similarityAdd
BLAST
Regioni1432 – 147544Phenylalkylamine bindingBy similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1 – 77Poly-Met
Compositional biasi653 – 6597Poly-Leu
Compositional biasi827 – 83812Poly-GluAdd
BLAST

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.

Sequence similaritiesi

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1226.
GeneTreeiENSGT00760000118827.
HOGENOMiHOG000231529.
HOVERGENiHBG050763.
InParanoidiQ01668.
KOiK04851.
OMAiFSDAWNT.
OrthoDBiEOG7T1RBQ.
PhylomeDBiQ01668.
TreeFamiTF312805.

Family and domain databases

Gene3Di1.20.120.350. 5 hits.
InterProiIPR027359. Channel_four-helix_dom.
IPR005821. Ion_trans_dom.
IPR005452. LVDCC_a1dsu.
IPR014873. VDCC_a1su_IQ.
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.
PR01636. LVDCCALPHA1D.
SMARTiSM01062. Ca_chan_IQ. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

Note: Additional isoforms seem to exist.

Isoform Neuronal-type (identifier: Q01668-1) [UniParc]FASTAAdd to Basket

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
MMMMMMMKKM QHQRQQQADH ANEANYARGT RLPLSGEGPT SQPNSSKQTV
60 70 80 90 100
LSWQAAIDAA RQAKAAQTMS TSAPPPVGSL SQRKRQQYAK SKKQGNSSNS
110 120 130 140 150
RPARALFCLS LNNPIRRACI SIVEWKPFDI FILLAIFANC VALAIYIPFP
160 170 180 190 200
EDDSNSTNHN LEKVEYAFLI IFTVETFLKI IAYGLLLHPN AYVRNGWNLL
210 220 230 240 250
DFVIVIVGLF SVILEQLTKE TEGGNHSSGK SGGFDVKALR AFRVLRPLRL
260 270 280 290 300
VSGVPSLQVV LNSIIKAMVP LLHIALLVLF VIIIYAIIGL ELFIGKMHKT
310 320 330 340 350
CFFADSDIVA EEDPAPCAFS GNGRQCTANG TECRSGWVGP NGGITNFDNF
360 370 380 390 400
AFAMLTVFQC ITMEGWTDVL YWMNDAMGFE LPWVYFVSLV IFGSFFVLNL
410 420 430 440 450
VLGVLSGEFS KEREKAKARG DFQKLREKQQ LEEDLKGYLD WITQAEDIDP
460 470 480 490 500
ENEEEGGEEG KRNTSMPTSE TESVNTENVS GEGENRGCCG SLCQAISKSK
510 520 530 540 550
LSRRWRRWNR FNRRRCRAAV KSVTFYWLVI VLVFLNTLTI SSEHYNQPDW
560 570 580 590 600
LTQIQDIANK VLLALFTCEM LVKMYSLGLQ AYFVSLFNRF DCFVVCGGIT
610 620 630 640 650
ETILVELEIM SPLGISVFRC VRLLRIFKVT RHWTSLSNLV ASLLNSMKSI
660 670 680 690 700
ASLLLLLFLF IIIFSLLGMQ LFGGKFNFDE TQTKRSTFDN FPQALLTVFQ
710 720 730 740 750
ILTGEDWNAV MYDGIMAYGG PSSSGMIVCI YFIILFICGN YILLNVFLAI
760 770 780 790 800
AVDNLADAES LNTAQKEEAE EKERKKIARK ESLENKKNNK PEVNQIANSD
810 820 830 840 850
NKVTIDDYRE EDEDKDPYPP CDVPVGEEEE EEEEDEPEVP AGPRPRRISE
860 870 880 890 900
LNMKEKIAPI PEGSAFFILS KTNPIRVGCH KLINHHIFTN LILVFIMLSS
910 920 930 940 950
AALAAEDPIR SHSFRNTILG YFDYAFTAIF TVEILLKMTT FGAFLHKGAF
960 970 980 990 1000
CRNYFNLLDM LVVGVSLVSF GIQSSAISVV KILRVLRVLR PLRAINRAKG
1010 1020 1030 1040 1050
LKHVVQCVFV AIRTIGNIMI VTTLLQFMFA CIGVQLFKGK FYRCTDEAKS
1060 1070 1080 1090 1100
NPEECRGLFI LYKDGDVDSP VVRERIWQNS DFNFDNVLSA MMALFTVSTF
1110 1120 1130 1140 1150
EGWPALLYKA IDSNGENIGP IYNHRVEISI FFIIYIIIVA FFMMNIFVGF
1160 1170 1180 1190 1200
VIVTFQEQGE KEYKNCELDK NQRQCVEYAL KARPLRRYIP KNPYQYKFWY
1210 1220 1230 1240 1250
VVNSSPFEYM MFVLIMLNTL CLAMQHYEQS KMFNDAMDIL NMVFTGVFTV
1260 1270 1280 1290 1300
EMVLKVIAFK PKGYFSDAWN TFDSLIVIGS IIDVALSEAD PTESENVPVP
1310 1320 1330 1340 1350
TATPGNSEES NRISITFFRL FRVMRLVKLL SRGEGIRTLL WTFIKSFQAL
1360 1370 1380 1390 1400
PYVALLIAML FFIYAVIGMQ MFGKVAMRDN NQINRNNNFQ TFPQAVLLLF
1410 1420 1430 1440 1450
RCATGEAWQE IMLACLPGKL CDPESDYNPG EEYTCGSNFA IVYFISFYML
1460 1470 1480 1490 1500
CAFLIINLFV AVIMDNFDYL TRDWSILGPH HLDEFKRIWS EYDPEAKGRI
1510 1520 1530 1540 1550
KHLDVVTLLR RIQPPLGFGK LCPHRVACKR LVAMNMPLNS DGTVMFNATL
1560 1570 1580 1590 1600
FALVRTALKI KTEGNLEQAN EELRAVIKKI WKKTSMKLLD QVVPPAGDDE
1610 1620 1630 1640 1650
VTVGKFYATF LIQDYFRKFK KRKEQGLVGK YPAKNTTIAL QAGLRTLHDI
1660 1670 1680 1690 1700
GPEIRRAISC DLQDDEPEET KREEEDDVFK RNGALLGNHV NHVNSDRRDS
1710 1720 1730 1740 1750
LQQTNTTHRP LHVQRPSIPP ASDTEKPLFP PAGNSVCHNH HNHNSIGKQV
1760 1770 1780 1790 1800
PTSTNANLNN ANMSKAAHGK RPSIGNLEHV SENGHHSSHK HDREPQRRSS
1810 1820 1830 1840 1850
VKRTRYYETY IRSDSGDEQL PTICREDPEI HGYFRDPHCL GEQEYFSSEE
1860 1870 1880 1890 1900
CYEDDSSPTW SRQNYGYYSR YPGRNIDSER PRGYHHPQGF LEDDDSPVCY
1910 1920 1930 1940 1950
DSRRSPRRRL LPPTPASHRR SSFNFECLRR QSSQEEVPSS PIFPHRTALP
1960 1970 1980 1990 2000
LHLMQQQIMA VAGLDSSKAQ KYSPSHSTRS WATPPATPPY RDWTPCYTPL
2010 2020 2030 2040 2050
IQVEQSEALD QVNGSLPSLH RSSWYTDEPD ISYRTFTPAS LTVPSSFRNK
2060 2070 2080 2090 2100
NSDKQRSADS LVEAVLISEG LGRYARDPKF VSATKHEIAD ACDLTIDEME
2110 2120 2130 2140 2150
SAASTLLNGN VRPRANGDVG PLSHRQDYEL QDFGPGYSDE EPDPGRDEED
2160
LADEMICITT L
Length:2,161
Mass (Da):245,141
Last modified:October 17, 2006 - v2
Checksum:i31B0ADFCDB30B575
GO
Isoform Beta-cell-type (identifier: Q01668-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     373-392: MNDAMGFELPWVYFVSLVIF → VNDAIGWEWPWVYFVSLIIL
     493-493: C → WCWWRRRGAAKAGPSGCRRWG

Show »
Length:2,181
Mass (Da):247,566
Checksum:i93C3A848E89B5A76
GO
Isoform 4 (identifier: Q01668-4) [UniParc]FASTAAdd to Basket

Also known as: Ca(V)1.3(42A)

The sequence of this isoform differs from the canonical sequence as follows:
     1642-1647: AGLRTL → MLERML
     1648-2161: Missing.

Note: Expressed at 5% to 15% of isoform Neuronal-type in brain tissues, increased current density.

Show »
Length:1,647
Mass (Da):187,035
Checksum:iD90F644342325721
GO
Isoform 3 (identifier: Q01668-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1291-1305: Missing.
     1803-1811: Missing.

Show »
Length:2,137
Mass (Da):242,417
Checksum:i0247ED997C1E6128
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti576 – 5761S → T in BAA07804. (PubMed:7557998)Curated
Sequence conflicti637 – 6371S → C in AAA58402. (PubMed:1309651)Curated
Sequence conflicti650 – 6501I → S in AAA58402. (PubMed:1309651)Curated
Sequence conflicti918 – 9181I → T in BAA07804. (PubMed:7557998)Curated
Sequence conflicti960 – 9601M → I in BAA07804. (PubMed:7557998)Curated
Sequence conflicti1289 – 12902Missing in BAA07804. (PubMed:7557998)Curated
Sequence conflicti1346 – 13461S → F in AAA58402. (PubMed:1309651)Curated
Sequence conflicti1433 – 14331Y → H in AAA58402. (PubMed:1309651)Curated

Polymorphismi

A change from seven to eight ATG trinucleotide repeats, resulting in an additional N-terminal methionine, has been found in a patient with non-insulin-dependent diabetes mellitus (NIDDM).

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti1 – 11M → MM in a NIDDM patient. 1 Publication
VAR_001497
Natural varianti403 – 4031G → D in PASNA; the mutant channel is activated at less depolarized potentials; results in increased current density and impaired channel inactivation. 1 Publication
VAR_070868
Natural varianti403 – 4031G → GG in SANDD; the mutant channels are unable to conduct calcium ions currents and have abnormal voltage-dependent gating. 1 Publication
VAR_069170
Natural varianti750 – 7501I → M in PASNA; the mutant channel is activated at less depolarized potentials; results in increased current density. 1 Publication
VAR_070869
Natural varianti2097 – 20971D → N.
Corresponds to variant rs41276455 [ dbSNP | Ensembl ].
VAR_061103

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei373 – 39220MNDAM…SLVIF → VNDAIGWEWPWVYFVSLIIL in isoform Beta-cell-type. 1 PublicationVSP_000913Add
BLAST
Alternative sequencei493 – 4931C → WCWWRRRGAAKAGPSGCRRW G in isoform Beta-cell-type. 1 PublicationVSP_000914
Alternative sequencei1291 – 130515Missing in isoform 3. 1 PublicationVSP_046743Add
BLAST
Alternative sequencei1642 – 16476AGLRTL → MLERML in isoform 4. CuratedVSP_047921
Alternative sequencei1648 – 2161514Missing in isoform 4. CuratedVSP_047922Add
BLAST
Alternative sequencei1803 – 18119Missing in isoform 3. 1 PublicationVSP_046744

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M76558 mRNA. Translation: AAA58402.1.
M83566 mRNA. Translation: AAA35629.1.
D43747 Genomic DNA. Translation: BAA07804.1.
EU363339 mRNA. Translation: ABY66526.1.
AC005905 Genomic DNA. No translation available.
AC012467 Genomic DNA. No translation available.
AC024149 Genomic DNA. No translation available.
AC132810 Genomic DNA. No translation available.
AF055575 Genomic DNA. Translation: AAD08651.1.
CCDSiCCDS2872.1. [Q01668-2]
CCDS46848.1. [Q01668-1]
CCDS46849.1. [Q01668-3]
PIRiJH0564.
RefSeqiNP_000711.1. NM_000720.3. [Q01668-2]
NP_001122311.1. NM_001128839.2. [Q01668-3]
NP_001122312.1. NM_001128840.2. [Q01668-1]
UniGeneiHs.476358.

Genome annotation databases

EnsembliENST00000288139; ENSP00000288139; ENSG00000157388. [Q01668-2]
ENST00000350061; ENSP00000288133; ENSG00000157388. [Q01668-1]
ENST00000422281; ENSP00000409174; ENSG00000157388. [Q01668-3]
GeneIDi776.
KEGGihsa:776.
UCSCiuc003dgu.5. human. [Q01668-2]
uc003dgv.5. human. [Q01668-1]
uc003dgy.5. human.

Polymorphism databases

DMDMi116241275.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism, Triplet repeat expansion

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M76558 mRNA. Translation: AAA58402.1 .
M83566 mRNA. Translation: AAA35629.1 .
D43747 Genomic DNA. Translation: BAA07804.1 .
EU363339 mRNA. Translation: ABY66526.1 .
AC005905 Genomic DNA. No translation available.
AC012467 Genomic DNA. No translation available.
AC024149 Genomic DNA. No translation available.
AC132810 Genomic DNA. No translation available.
AF055575 Genomic DNA. Translation: AAD08651.1 .
CCDSi CCDS2872.1. [Q01668-2 ]
CCDS46848.1. [Q01668-1 ]
CCDS46849.1. [Q01668-3 ]
PIRi JH0564.
RefSeqi NP_000711.1. NM_000720.3. [Q01668-2 ]
NP_001122311.1. NM_001128839.2. [Q01668-3 ]
NP_001122312.1. NM_001128840.2. [Q01668-1 ]
UniGenei Hs.476358.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3LV3 X-ray 1.94 C 502-510 [» ]
ProteinModelPortali Q01668.
SMRi Q01668. Positions 164-405, 420-448, 519-753, 882-1152, 1201-1465, 1548-1628.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107230. 1 interaction.
DIPi DIP-48998N.
IntActi Q01668. 1 interaction.
STRINGi 9606.ENSP00000288139.

Chemistry

BindingDBi Q01668.
ChEMBLi CHEMBL4138.
DrugBanki DB00381. Amlodipine.
DB00568. Cinnarizine.
DB04920. Clevidipine.
DB04855. Dronedarone.
DB01023. Felodipine.
DB00270. Isradipine.
DB00622. Nicardipine.
DB01115. Nifedipine.
DB06712. Nilvadipine.
DB00393. Nimodipine.
DB00401. Nisoldipine.
DB01054. Nitrendipine.
DB00421. Spironolactone.
DB00661. Verapamil.
GuidetoPHARMACOLOGYi 530.

PTM databases

PhosphoSitei Q01668.

Polymorphism databases

DMDMi 116241275.

Proteomic databases

PaxDbi Q01668.
PRIDEi Q01668.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000288139 ; ENSP00000288139 ; ENSG00000157388 . [Q01668-2 ]
ENST00000350061 ; ENSP00000288133 ; ENSG00000157388 . [Q01668-1 ]
ENST00000422281 ; ENSP00000409174 ; ENSG00000157388 . [Q01668-3 ]
GeneIDi 776.
KEGGi hsa:776.
UCSCi uc003dgu.5. human. [Q01668-2 ]
uc003dgv.5. human. [Q01668-1 ]
uc003dgy.5. human.

Organism-specific databases

CTDi 776.
GeneCardsi GC03P053504.
HGNCi HGNC:1391. CACNA1D.
HPAi HPA020215.
MIMi 114206. gene.
614896. phenotype.
615474. phenotype.
neXtProti NX_Q01668.
Orphaneti 85142. Aldosterone-producing adenoma.
369929. Aldosterone-producing adenoma with seizures and neurological abnormalities.
324321. Sinoatrial node dysfunction and deafness.
PharmGKBi PA84.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1226.
GeneTreei ENSGT00760000118827.
HOGENOMi HOG000231529.
HOVERGENi HBG050763.
InParanoidi Q01668.
KOi K04851.
OMAi FSDAWNT.
OrthoDBi EOG7T1RBQ.
PhylomeDBi Q01668.
TreeFami TF312805.

Enzyme and pathway databases

Reactomei REACT_18312. NCAM1 interactions.
REACT_18325. Regulation of insulin secretion.
REACT_18339. Adrenaline,noradrenaline inhibits insulin secretion.

Miscellaneous databases

ChiTaRSi CACNA1D. human.
GeneWikii Cav1.3.
GenomeRNAii 776.
NextBioi 3136.
PROi Q01668.
SOURCEi Search...

Gene expression databases

Bgeei Q01668.
CleanExi HS_CACNA1D.
ExpressionAtlasi Q01668. baseline and differential.
Genevestigatori Q01668.

Family and domain databases

Gene3Di 1.20.120.350. 5 hits.
InterProi IPR027359. Channel_four-helix_dom.
IPR005821. Ion_trans_dom.
IPR005452. LVDCC_a1dsu.
IPR014873. VDCC_a1su_IQ.
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.
PR01636. LVDCCALPHA1D.
SMARTi SM01062. Ca_chan_IQ. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Structure and functional expression of alpha 1, alpha 2, and beta subunits of a novel human neuronal calcium channel subtype."
    Williams M.E., Feldman D.H., McCue A.F., Brenner R., Velicelebi G., Ellis S.B., Harpold M.M.
    Neuron 8:71-84(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM NEURONAL-TYPE).
    Tissue: Neuroblastoma.
  2. "Cloning of the alpha 1 subunit of a voltage-dependent calcium channel expressed in pancreatic beta cells."
    Seino S., Chen L., Seino M., Blondel O., Takeda J., Johnson J.H., Bell G.I.
    Proc. Natl. Acad. Sci. U.S.A. 89:584-588(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA-CELL-TYPE).
    Tissue: Pancreatic islet.
  3. "The structures of the human calcium channel alpha 1 subunit (CACNL1A2) and beta subunit (CACNLB3) genes."
    Yamada Y., Masuda K., Li Q., Ihara Y., Kubota A., Miura T., Nakamura K., Fujii Y., Seino S., Seino Y.
    Genomics 27:312-319(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM BETA-CELL-TYPE), VARIANT MET-1 INS.
  4. "Modulation of voltage- and Ca2+-dependent gating of CaV1.3 L-type calcium channels by alternative splicing of a C-terminal regulatory domain."
    Singh A., Gebhart M., Fritsch R., Sinnegger-Brauns M.J., Poggiani C., Hoda J.C., Engel J., Romanin C., Striessnig J., Koschak A.
    J. Biol. Chem. 283:20733-20744(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, ALTERNATIVE SPLICING (ISOFORM 4).
    Tissue: Pancreas.
  5. "The DNA sequence, annotation and analysis of human chromosome 3."
    Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
    , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
    Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "Genomic structure of the regulatory region of the voltage-gated calcium channel alpha 1D."
    Kim H.-L., Chang Y.J., Lee S.M., Hong Y.-S.
    Exp. Mol. Med. 30:246-251(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-125.
  7. "Molecular diversity of neuronal-type calcium channels identified in small cell lung carcinoma."
    Oguro-Okano M., Griesmann G.E., Wieben E.D., Slaymaker S.J., Snutch T.P., Lennon V.A.
    Mayo Clin. Proc. 67:1150-1159(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 747-1039, TISSUE SPECIFICITY.
    Tissue: Lung carcinoma.
  8. "Loss of recognition by cross-reactive T cells and its relation to a C-terminus-induced conformational reorientation of an HLA-B*2705-bound peptide."
    Loll B., Ruckert C., Hee C.S., Saenger W., Uchanska-Ziegler B., Ziegler A.
    Protein Sci. 20:278-290(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS) OF 502-510 IN COMPLEX WITH HLA.
  9. Cited for: VARIANT SANDD GLY-403 INS, CHARACTERIZATION OF VARIANT SANDD GLY-403 INS.
  10. Cited for: VARIANTS PASNA ASP-403 AND MET-750, CHARACTERIZATION OF VARIANTS PASNA ASP-403 AND MET-750.

Entry informationi

Entry nameiCAC1D_HUMAN
AccessioniPrimary (citable) accession number: Q01668
Secondary accession number(s): B0FYA3
, Q13916, Q13931, Q71UT1, Q9UDC3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: October 17, 2006
Last modified: November 26, 2014
This is version 152 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3