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Protein

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

Gene

CACNA1D

Organism
Homo sapiens (Human)
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-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)DescriptionActionsGraphical viewLength
Sitei364Calcium ion selectivity and permeabilityBy similarity1
Sitei705Calcium ion selectivity and permeabilityBy similarity1
Sitei1101Calcium ion selectivity and permeabilityBy similarity1
Sitei1406Calcium ion selectivity and permeabilityBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Calcium bindingi1493 – 1504By similarityAdd BLAST12

GO - Molecular functioni

  • alpha-actinin binding Source: BHF-UCL
  • ankyrin binding Source: BHF-UCL
  • high voltage-gated calcium channel activity Source: Ensembl
  • metal ion binding Source: UniProtKB-KW
  • voltage-gated calcium channel activity Source: UniProtKB
  • voltage-gated calcium channel activity involved in cardiac muscle cell action potential Source: BHF-UCL
  • voltage-gated calcium channel activity involved SA node cell action potential Source: BHF-UCL

GO - Biological processi

  • adenylate cyclase-modulating G-protein coupled receptor signaling pathway Source: BHF-UCL
  • calcium ion import Source: BHF-UCL
  • calcium ion transmembrane transport Source: BHF-UCL
  • calcium ion transport Source: UniProtKB
  • cardiac conduction Source: Reactome
  • membrane depolarization during cardiac muscle cell action potential Source: BHF-UCL
  • membrane depolarization during SA node cell action potential Source: BHF-UCL
  • positive regulation of calcium ion transport Source: BHF-UCL
  • regulation of atrial cardiac muscle cell membrane repolarization Source: BHF-UCL
  • regulation of heart rate by cardiac conduction Source: BHF-UCL
  • regulation of insulin secretion Source: Reactome
  • regulation of potassium ion transmembrane transport Source: BHF-UCL
  • regulation of potassium ion transmembrane transporter activity Source: BHF-UCL
  • sensory perception of sound 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

Enzyme and pathway databases

BioCyciZFISH:ENSG00000157388-MONOMER.
ReactomeiR-HSA-400042. Adrenaline,noradrenaline inhibits insulin secretion.
R-HSA-419037. NCAM1 interactions.
R-HSA-422356. Regulation of insulin secretion.
R-HSA-5576892. Phase 0 - rapid depolarisation.
R-HSA-5576893. Phase 2 - plateau phase.
R-HSA-5576894. Phase 1 - inactivation of fast Na+ channels.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:1391. CACNA1D.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 126CytoplasmicSequence analysisAdd BLAST126
Transmembranei127 – 145Helical; Name=S1 of repeat ISequence analysisAdd BLAST19
Topological domaini146 – 163ExtracellularSequence analysisAdd BLAST18
Transmembranei164 – 183Helical; Name=S2 of repeat ISequence analysisAdd BLAST20
Topological domaini184 – 195CytoplasmicSequence analysisAdd BLAST12
Transmembranei196 – 214Helical; Name=S3 of repeat ISequence analysisAdd BLAST19
Topological domaini215 – 235ExtracellularSequence analysisAdd BLAST21
Transmembranei236 – 254Helical; Name=S4 of repeat ISequence analysisAdd BLAST19
Topological domaini255 – 273CytoplasmicSequence analysisAdd BLAST19
Transmembranei274 – 293Helical; Name=S5 of repeat ISequence analysisAdd BLAST20
Topological domaini294 – 381ExtracellularSequence analysisAdd BLAST88
Transmembranei382 – 406Helical; Name=S6 of repeat ISequence analysisAdd BLAST25
Topological domaini407 – 523CytoplasmicSequence analysisAdd BLAST117
Transmembranei524 – 543Helical; Name=S1 of repeat IISequence analysisAdd BLAST20
Topological domaini544 – 558ExtracellularSequence analysisAdd BLAST15
Transmembranei559 – 577Helical; Name=S2 of repeat IISequence analysisAdd BLAST19
Topological domaini578 – 585CytoplasmicSequence analysis8
Transmembranei586 – 604Helical; Name=S3 of repeat IISequence analysisAdd BLAST19
Topological domaini605 – 614ExtracellularSequence analysis10
Transmembranei615 – 633Helical; Name=S4 of repeat IISequence analysisAdd BLAST19
Topological domaini634 – 652CytoplasmicSequence analysisAdd BLAST19
Transmembranei653 – 673Helical; Name=S5 of repeat IISequence analysisAdd BLAST21
Topological domaini674 – 727ExtracellularSequence analysisAdd BLAST54
Transmembranei728 – 752Helical; Name=S6 of repeat IISequence analysisAdd BLAST25
Topological domaini753 – 886CytoplasmicSequence analysisAdd BLAST134
Transmembranei887 – 905Helical; Name=S1 of repeat IIISequence analysisAdd BLAST19
Topological domaini906 – 921ExtracellularSequence analysisAdd BLAST16
Transmembranei922 – 941Helical; Name=S2 of repeat IIISequence analysisAdd BLAST20
Topological domaini942 – 953CytoplasmicSequence analysisAdd BLAST12
Transmembranei954 – 972Helical; Name=S3 of repeat IIISequence analysisAdd BLAST19
Topological domaini973 – 978ExtracellularSequence analysis6
Transmembranei979 – 998Helical; Name=S4 of repeat IIISequence analysisAdd BLAST20
Topological domaini999 – 1017CytoplasmicSequence analysisAdd BLAST19
Transmembranei1018 – 1037Helical; Name=S5 of repeat IIISequence analysisAdd BLAST20
Topological domaini1038 – 1127ExtracellularSequence analysisAdd BLAST90
Transmembranei1128 – 1148Helical; Name=S6 of repeat IIISequence analysisAdd BLAST21
Topological domaini1149 – 1205CytoplasmicSequence analysisAdd BLAST57
Transmembranei1206 – 1224Helical; Name=S1 of repeat IVSequence analysisAdd BLAST19
Topological domaini1225 – 1239ExtracellularSequence analysisAdd BLAST15
Transmembranei1240 – 1259Helical; Name=S2 of repeat IVSequence analysisAdd BLAST20
Topological domaini1260 – 1266CytoplasmicSequence analysis7
Transmembranei1267 – 1288Helical; Name=S3 of repeat IVSequence analysisAdd BLAST22
Topological domaini1289 – 1313ExtracellularSequence analysisAdd BLAST25
Transmembranei1314 – 1333Helical; Name=S4 of repeat IVSequence analysisAdd BLAST20
Topological domaini1334 – 1352CytoplasmicSequence analysisAdd BLAST19
Transmembranei1353 – 1372Helical; Name=S5 of repeat IVSequence analysisAdd BLAST20
Topological domaini1373 – 1439ExtracellularSequence analysisAdd BLAST67
Transmembranei1440 – 1464Helical; Name=S6 of repeat IVSequence analysisAdd BLAST25
Topological domaini1465 – 2161CytoplasmicSequence analysisAdd BLAST697

GO - Cellular componenti

  • L-type voltage-gated calcium channel complex Source: BHF-UCL
  • plasma membrane Source: BHF-UCL
  • voltage-gated calcium channel complex Source: UniProtKB
  • Z disc Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Involvement in diseasei

Sinoatrial node dysfunction and deafness (SANDD)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disease characterized by congenital severe to profound deafness without vestibular dysfunction, associated with episodic syncope due to intermittent pronounced bradycardia.
See also OMIM:614896
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_069170403G → GG in SANDD; the mutant channels are unable to conduct calcium ions currents and have abnormal voltage-dependent gating. 1 Publication1
Primary aldosteronism, seizures, and neurologic abnormalities (PASNA)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:615474
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_070868403G → D in PASNA; the mutant channel is activated at less depolarized potentials; results in increased current density and impaired channel inactivation. 1 Publication1
Natural variantiVAR_070869750I → M in PASNA; the mutant channel is activated at less depolarized potentials; results in increased current density. 1 PublicationCorresponds to variant rs41276445dbSNPEnsembl.1

Keywords - Diseasei

Deafness, Disease mutation, Epilepsy

Organism-specific databases

DisGeNETi776.
MalaCardsiCACNA1D.
MIMi614896. phenotype.
615474. phenotype.
OpenTargetsiENSG00000157388.
Orphaneti85142. Aldosterone-producing adenoma.
369929. Aldosterone-producing adenoma with seizures and neurological abnormalities.
324321. Sinoatrial node dysfunction and deafness.
PharmGKBiPA84.

Chemistry databases

ChEMBLiCHEMBL4138.
DrugBankiDB00381. Amlodipine.
DB00568. Cinnarizine.
DB04920. Clevidipine.
DB04855. Dronedarone.
DB00898. Ethanol.
DB01023. Felodipine.
DB00270. Isradipine.
DB00622. Nicardipine.
DB01115. Nifedipine.
DB06712. Nilvadipine.
DB00393. Nimodipine.
DB00401. Nisoldipine.
DB01054. Nitrendipine.
DB00421. Spironolactone.
DB00661. Verapamil.
GuidetoPHARMACOLOGYi530.

Polymorphism and mutation databases

DMDMi116241275.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000539331 – 2161Voltage-dependent L-type calcium channel subunit alpha-1DAdd BLAST2161

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi155N-linked (GlcNAc...)Sequence analysis1
Glycosylationi225N-linked (GlcNAc...)Sequence analysis1
Glycosylationi329N-linked (GlcNAc...)Sequence analysis1
Modified residuei469PhosphoserineBy similarity1
Modified residuei473PhosphoserineBy similarity1
Modified residuei1475Phosphoserine; by PKASequence analysis1
Modified residuei1700PhosphoserineBy similarity1

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiQ01668.
PeptideAtlasiQ01668.
PRIDEiQ01668.

PTM databases

iPTMnetiQ01668.
PhosphoSitePlusiQ01668.

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

BgeeiENSG00000157388.
CleanExiHS_CACNA1D.
ExpressionAtlasiQ01668. baseline and differential.
GenevisibleiQ01668. HS.

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

GO - Molecular functioni

  • alpha-actinin binding Source: BHF-UCL
  • ankyrin binding Source: BHF-UCL

Protein-protein interaction databases

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

Chemistry databases

BindingDBiQ01668.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3LV3X-ray1.94C502-510[»]
ProteinModelPortaliQ01668.
SMRiQ01668.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati113 – 409IAdd BLAST297
Repeati509 – 755IIAdd BLAST247
Repeati873 – 1155IIIAdd BLAST283
Repeati1192 – 1467IVAdd BLAST276

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni429 – 446Binding to the beta subunitBy similarityAdd BLAST18
Regioni1075 – 1165Dihydropyridine bindingBy similarityAdd BLAST91
Regioni1420 – 1486Dihydropyridine bindingBy similarityAdd BLAST67
Regioni1432 – 1475Phenylalkylamine bindingBy similarityAdd BLAST44

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi1 – 7Poly-Met7
Compositional biasi653 – 659Poly-Leu7
Compositional biasi827 – 838Poly-GluAdd BLAST12

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

eggNOGiKOG2301. Eukaryota.
ENOG410XNP6. LUCA.
GeneTreeiENSGT00830000128247.
HOGENOMiHOG000231529.
HOVERGENiHBG050763.
InParanoidiQ01668.
KOiK04851.
OMAiIQVERPE.
OrthoDBiEOG091G0TKO.
PhylomeDBiQ01668.
TreeFamiTF312805.

Family and domain databases

Gene3Di1.20.120.350. 5 hits.
InterProiIPR031688. CAC1F_C.
IPR027359. Channel_four-helix_dom.
IPR031649. GPHH_dom.
IPR005821. Ion_trans_dom.
IPR005452. LVDCC_a1dsu.
IPR014873. VDCC_a1su_IQ.
IPR005446. VDCC_L_a1su.
IPR002077. VDCCAlpha1.
[Graphical view]
PANTHERiPTHR10037:SF139. PTHR10037:SF139. 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.
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. AlignAdd to basket

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)DescriptionActionsGraphical viewLength
Sequence conflicti576S → T in BAA07804 (PubMed:7557998).Curated1
Sequence conflicti637S → C in AAA58402 (PubMed:1309651).Curated1
Sequence conflicti650I → S in AAA58402 (PubMed:1309651).Curated1
Sequence conflicti918I → T in BAA07804 (PubMed:7557998).Curated1
Sequence conflicti960M → I in BAA07804 (PubMed:7557998).Curated1
Sequence conflicti1289 – 1290Missing in BAA07804 (PubMed:7557998).Curated2
Sequence conflicti1346S → F in AAA58402 (PubMed:1309651).Curated1
Sequence conflicti1433Y → H in AAA58402 (PubMed:1309651).Curated1

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).1 Publication

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0014971M → MM in a NIDDM patient. 1 Publication1
Natural variantiVAR_070868403G → D in PASNA; the mutant channel is activated at less depolarized potentials; results in increased current density and impaired channel inactivation. 1 Publication1
Natural variantiVAR_069170403G → GG in SANDD; the mutant channels are unable to conduct calcium ions currents and have abnormal voltage-dependent gating. 1 Publication1
Natural variantiVAR_070869750I → M in PASNA; the mutant channel is activated at less depolarized potentials; results in increased current density. 1 PublicationCorresponds to variant rs41276445dbSNPEnsembl.1
Natural variantiVAR_0611032097D → N.Corresponds to variant rs41276455dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_000913373 – 392MNDAM…SLVIF → VNDAIGWEWPWVYFVSLIIL in isoform Beta-cell-type. 1 PublicationAdd BLAST20
Alternative sequenceiVSP_000914493C → WCWWRRRGAAKAGPSGCRRW G in isoform Beta-cell-type. 1 Publication1
Alternative sequenceiVSP_0467431291 – 1305Missing in isoform 3. 1 PublicationAdd BLAST15
Alternative sequenceiVSP_0479211642 – 1647AGLRTL → MLERML in isoform 4. Curated6
Alternative sequenceiVSP_0479221648 – 2161Missing in isoform 4. CuratedAdd BLAST514
Alternative sequenceiVSP_0467441803 – 1811Missing in isoform 3. 1 Publication9

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.6. human. [Q01668-1]

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.
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3LV3X-ray1.94C502-510[»]
ProteinModelPortaliQ01668.
SMRiQ01668.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Chemistry databases

BindingDBiQ01668.
ChEMBLiCHEMBL4138.
DrugBankiDB00381. Amlodipine.
DB00568. Cinnarizine.
DB04920. Clevidipine.
DB04855. Dronedarone.
DB00898. Ethanol.
DB01023. Felodipine.
DB00270. Isradipine.
DB00622. Nicardipine.
DB01115. Nifedipine.
DB06712. Nilvadipine.
DB00393. Nimodipine.
DB00401. Nisoldipine.
DB01054. Nitrendipine.
DB00421. Spironolactone.
DB00661. Verapamil.
GuidetoPHARMACOLOGYi530.

PTM databases

iPTMnetiQ01668.
PhosphoSitePlusiQ01668.

Polymorphism and mutation databases

DMDMi116241275.

Proteomic databases

PaxDbiQ01668.
PeptideAtlasiQ01668.
PRIDEiQ01668.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000288139; ENSP00000288139; ENSG00000157388. [Q01668-2]
ENST00000350061; ENSP00000288133; ENSG00000157388. [Q01668-1]
ENST00000422281; ENSP00000409174; ENSG00000157388. [Q01668-3]
GeneIDi776.
KEGGihsa:776.
UCSCiuc003dgu.6. human. [Q01668-1]

Organism-specific databases

CTDi776.
DisGeNETi776.
GeneCardsiCACNA1D.
HGNCiHGNC:1391. CACNA1D.
HPAiHPA020215.
MalaCardsiCACNA1D.
MIMi114206. gene.
614896. phenotype.
615474. phenotype.
neXtProtiNX_Q01668.
OpenTargetsiENSG00000157388.
Orphaneti85142. Aldosterone-producing adenoma.
369929. Aldosterone-producing adenoma with seizures and neurological abnormalities.
324321. Sinoatrial node dysfunction and deafness.
PharmGKBiPA84.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2301. Eukaryota.
ENOG410XNP6. LUCA.
GeneTreeiENSGT00830000128247.
HOGENOMiHOG000231529.
HOVERGENiHBG050763.
InParanoidiQ01668.
KOiK04851.
OMAiIQVERPE.
OrthoDBiEOG091G0TKO.
PhylomeDBiQ01668.
TreeFamiTF312805.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000157388-MONOMER.
ReactomeiR-HSA-400042. Adrenaline,noradrenaline inhibits insulin secretion.
R-HSA-419037. NCAM1 interactions.
R-HSA-422356. Regulation of insulin secretion.
R-HSA-5576892. Phase 0 - rapid depolarisation.
R-HSA-5576893. Phase 2 - plateau phase.
R-HSA-5576894. Phase 1 - inactivation of fast Na+ channels.

Miscellaneous databases

ChiTaRSiCACNA1D. human.
GeneWikiiCav1.3.
GenomeRNAii776.
PROiQ01668.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000157388.
CleanExiHS_CACNA1D.
ExpressionAtlasiQ01668. baseline and differential.
GenevisibleiQ01668. HS.

Family and domain databases

Gene3Di1.20.120.350. 5 hits.
InterProiIPR031688. CAC1F_C.
IPR027359. Channel_four-helix_dom.
IPR031649. GPHH_dom.
IPR005821. Ion_trans_dom.
IPR005452. LVDCC_a1dsu.
IPR014873. VDCC_a1su_IQ.
IPR005446. VDCC_L_a1su.
IPR002077. VDCCAlpha1.
[Graphical view]
PANTHERiPTHR10037:SF139. PTHR10037:SF139. 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.
PR01636. LVDCCALPHA1D.
SMARTiSM01062. Ca_chan_IQ. 1 hit.
[Graphical view]
ProtoNetiSearch...

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 2, 2016
This is version 172 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

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.