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Q01668 (CAC1D_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 148. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:CACNA1D
Synonyms:CACH3, CACN4, CACNL1A2, CCHL1A2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length2161 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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-1Dgives 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). Ref.4

Subunit structure

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. Ref.4

Subcellular location

Membrane; Multi-pass membrane protein Ref.4.

Tissue specificity

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. Ref.7

Domain

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.

Polymorphism

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).

Involvement in disease

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.9

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.10

Sequence similarities

Belongs to the calcium channel alpha-1 subunit (TC 1.A.1.11) family. CACNA1D subfamily. [View classification]

Ontologies

Keywords
   Biological processCalcium transport
Ion transport
Transport
   Cellular componentMembrane
   Coding sequence diversityAlternative splicing
Polymorphism
Triplet repeat expansion
   DiseaseDeafness
Disease mutation
Epilepsy
   DomainRepeat
Transmembrane
Transmembrane helix
   LigandCalcium
Metal-binding
   Molecular functionCalcium channel
Ion channel
Voltage-gated channel
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processadenylate cyclase-modulating G-protein coupled receptor signaling pathway

Inferred from sequence or structural similarity. Source: BHF-UCL

axon guidance

Traceable author statement. Source: Reactome

calcium ion import

Inferred from direct assay Ref.1. Source: BHF-UCL

calcium ion transmembrane transport

Inferred from sequence or structural similarity. Source: BHF-UCL

calcium ion transport

Inferred from direct assay PubMed 11160515. Source: UniProtKB

energy reserve metabolic process

Traceable author statement. Source: Reactome

membrane depolarization during action potential

Inferred from Biological aspect of Ancestor. Source: RefGenome

membrane depolarization during cardiac muscle cell action potential

Inferred by curator PubMed 21859974. Source: BHF-UCL

membrane repolarization during SA node cell action potential

Inferred from mutant phenotype Ref.9. Source: BHF-UCL

positive regulation of calcium ion transport

Inferred from direct assay Ref.1. Source: BHF-UCL

regulation of atrial cardiac muscle cell membrane repolarization

Inferred from sequence or structural similarity. Source: BHF-UCL

regulation of heart rate by cardiac conduction

Inferred from mutant phenotype Ref.9. Source: BHF-UCL

regulation of insulin secretion

Traceable author statement. Source: Reactome

regulation of potassium ion transmembrane transport

Inferred from sequence or structural similarity. Source: BHF-UCL

regulation of potassium ion transmembrane transporter activity

Inferred from sequence or structural similarity. Source: BHF-UCL

sensory perception of sound

Inferred from mutant phenotype Ref.9. Source: BHF-UCL

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentZ disc

Inferred from sequence or structural similarity. Source: BHF-UCL

plasma membrane

Inferred from sequence or structural similarity PubMed 21859974. Source: BHF-UCL

voltage-gated calcium channel complex

Inferred from direct assay PubMed 11160515. Source: UniProtKB

   Molecular_functionalpha-actinin binding

Inferred from physical interaction PubMed 17110593. Source: BHF-UCL

ankyrin binding

Inferred from sequence or structural similarity PubMed 21859974. Source: BHF-UCL

high voltage-gated calcium channel activity

Inferred from electronic annotation. Source: Ensembl

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

voltage-gated calcium channel activity

Inferred from direct assay PubMed 11160515. Source: UniProtKB

voltage-gated calcium channel activity involved SA node cell action potential

Inferred from mutant phenotype Ref.9. Source: BHF-UCL

voltage-gated calcium channel activity involved in cardiac muscle cell action potential

Inferred by curator PubMed 21859974. Source: BHF-UCL

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform Neuronal-type (identifier: Q01668-1)

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.
Isoform Beta-cell-type (identifier: Q01668-2)

The sequence of this isoform differs from the canonical sequence as follows:
     373-392: MNDAMGFELPWVYFVSLVIF → VNDAIGWEWPWVYFVSLIIL
     493-493: C → WCWWRRRGAAKAGPSGCRRWG
Isoform 4 (identifier: Q01668-4)

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.
Isoform 3 (identifier: Q01668-3)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 21612161Voltage-dependent L-type calcium channel subunit alpha-1D
PRO_0000053933

Regions

Topological domain1 – 126126Cytoplasmic Potential
Transmembrane127 – 14519Helical; Name=S1 of repeat I; Potential
Topological domain146 – 16318Extracellular Potential
Transmembrane164 – 18320Helical; Name=S2 of repeat I; Potential
Topological domain184 – 19512Cytoplasmic Potential
Transmembrane196 – 21419Helical; Name=S3 of repeat I; Potential
Topological domain215 – 23521Extracellular Potential
Transmembrane236 – 25419Helical; Name=S4 of repeat I; Potential
Topological domain255 – 27319Cytoplasmic Potential
Transmembrane274 – 29320Helical; Name=S5 of repeat I; Potential
Topological domain294 – 38188Extracellular Potential
Transmembrane382 – 40625Helical; Name=S6 of repeat I; Potential
Topological domain407 – 523117Cytoplasmic Potential
Transmembrane524 – 54320Helical; Name=S1 of repeat II; Potential
Topological domain544 – 55815Extracellular Potential
Transmembrane559 – 57719Helical; Name=S2 of repeat II; Potential
Topological domain578 – 5858Cytoplasmic Potential
Transmembrane586 – 60419Helical; Name=S3 of repeat II; Potential
Topological domain605 – 61410Extracellular Potential
Transmembrane615 – 63319Helical; Name=S4 of repeat II; Potential
Topological domain634 – 65219Cytoplasmic Potential
Transmembrane653 – 67321Helical; Name=S5 of repeat II; Potential
Topological domain674 – 72754Extracellular Potential
Transmembrane728 – 75225Helical; Name=S6 of repeat II; Potential
Topological domain753 – 886134Cytoplasmic Potential
Transmembrane887 – 90519Helical; Name=S1 of repeat III; Potential
Topological domain906 – 92116Extracellular Potential
Transmembrane922 – 94120Helical; Name=S2 of repeat III; Potential
Topological domain942 – 95312Cytoplasmic Potential
Transmembrane954 – 97219Helical; Name=S3 of repeat III; Potential
Topological domain973 – 9786Extracellular Potential
Transmembrane979 – 99820Helical; Name=S4 of repeat III; Potential
Topological domain999 – 101719Cytoplasmic Potential
Transmembrane1018 – 103720Helical; Name=S5 of repeat III; Potential
Topological domain1038 – 112790Extracellular Potential
Transmembrane1128 – 114821Helical; Name=S6 of repeat III; Potential
Topological domain1149 – 120557Cytoplasmic Potential
Transmembrane1206 – 122419Helical; Name=S1 of repeat IV; Potential
Topological domain1225 – 123915Extracellular Potential
Transmembrane1240 – 125920Helical; Name=S2 of repeat IV; Potential
Topological domain1260 – 12667Cytoplasmic Potential
Transmembrane1267 – 128822Helical; Name=S3 of repeat IV; Potential
Topological domain1289 – 131325Extracellular Potential
Transmembrane1314 – 133320Helical; Name=S4 of repeat IV; Potential
Topological domain1334 – 135219Cytoplasmic Potential
Transmembrane1353 – 137220Helical; Name=S5 of repeat IV; Potential
Topological domain1373 – 143967Extracellular Potential
Transmembrane1440 – 146425Helical; Name=S6 of repeat IV; Potential
Topological domain1465 – 2161697Cytoplasmic Potential
Repeat113 – 409297I
Repeat509 – 755247II
Repeat873 – 1155283III
Repeat1192 – 1467276IV
Calcium binding1493 – 150412 By similarity
Region429 – 44618Binding to the beta subunit By similarity
Region1075 – 116591Dihydropyridine binding By similarity
Region1420 – 148667Dihydropyridine binding By similarity
Region1432 – 147544Phenylalkylamine binding By similarity
Compositional bias1 – 77Poly-Met
Compositional bias653 – 6597Poly-Leu
Compositional bias827 – 83812Poly-Glu

Sites

Site3641Calcium ion selectivity and permeability By similarity
Site7051Calcium ion selectivity and permeability By similarity
Site11011Calcium ion selectivity and permeability By similarity
Site14061Calcium ion selectivity and permeability By similarity

Amino acid modifications

Modified residue14751Phosphoserine; by PKA Potential
Glycosylation1551N-linked (GlcNAc...) Potential
Glycosylation2251N-linked (GlcNAc...) Potential
Glycosylation3291N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence373 – 39220MNDAM…SLVIF → VNDAIGWEWPWVYFVSLIIL in isoform Beta-cell-type.
VSP_000913
Alternative sequence4931C → WCWWRRRGAAKAGPSGCRRW G in isoform Beta-cell-type.
VSP_000914
Alternative sequence1291 – 130515Missing in isoform 3.
VSP_046743
Alternative sequence1642 – 16476AGLRTL → MLERML in isoform 4.
VSP_047921
Alternative sequence1648 – 2161514Missing in isoform 4.
VSP_047922
Alternative sequence1803 – 18119Missing in isoform 3.
VSP_046744
Natural variant11M → MM in a NIDDM patient. Ref.3
VAR_001497
Natural variant4031G → D in PASNA; the mutant channel is activated at less depolarized potentials; results in increased current density and impaired channel inactivation. Ref.10
VAR_070868
Natural variant4031G → GG in SANDD; the mutant channels are unable to conduct calcium ions currents and have abnormal voltage-dependent gating. Ref.9
VAR_069170
Natural variant7501I → M in PASNA; the mutant channel is activated at less depolarized potentials; results in increased current density. Ref.10
VAR_070869
Natural variant20971D → N.
Corresponds to variant rs41276455 [ dbSNP | Ensembl ].
VAR_061103

Experimental info

Sequence conflict5761S → T in BAA07804. Ref.3
Sequence conflict6371S → C in AAA58402. Ref.1
Sequence conflict6501I → S in AAA58402. Ref.1
Sequence conflict9181I → T in BAA07804. Ref.3
Sequence conflict9601M → I in BAA07804. Ref.3
Sequence conflict1289 – 12902Missing in BAA07804. Ref.3
Sequence conflict13461S → F in AAA58402. Ref.1
Sequence conflict14331Y → H in AAA58402. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform Neuronal-type [UniParc].

Last modified October 17, 2006. Version 2.
Checksum: 31B0ADFCDB30B575

FASTA2,161245,141
        10         20         30         40         50         60 
MMMMMMMKKM QHQRQQQADH ANEANYARGT RLPLSGEGPT SQPNSSKQTV LSWQAAIDAA 

        70         80         90        100        110        120 
RQAKAAQTMS TSAPPPVGSL SQRKRQQYAK SKKQGNSSNS RPARALFCLS LNNPIRRACI 

       130        140        150        160        170        180 
SIVEWKPFDI FILLAIFANC VALAIYIPFP EDDSNSTNHN LEKVEYAFLI IFTVETFLKI 

       190        200        210        220        230        240 
IAYGLLLHPN AYVRNGWNLL DFVIVIVGLF SVILEQLTKE TEGGNHSSGK SGGFDVKALR 

       250        260        270        280        290        300 
AFRVLRPLRL VSGVPSLQVV LNSIIKAMVP LLHIALLVLF VIIIYAIIGL ELFIGKMHKT 

       310        320        330        340        350        360 
CFFADSDIVA EEDPAPCAFS GNGRQCTANG TECRSGWVGP NGGITNFDNF AFAMLTVFQC 

       370        380        390        400        410        420 
ITMEGWTDVL YWMNDAMGFE LPWVYFVSLV IFGSFFVLNL VLGVLSGEFS KEREKAKARG 

       430        440        450        460        470        480 
DFQKLREKQQ LEEDLKGYLD WITQAEDIDP ENEEEGGEEG KRNTSMPTSE TESVNTENVS 

       490        500        510        520        530        540 
GEGENRGCCG SLCQAISKSK LSRRWRRWNR FNRRRCRAAV KSVTFYWLVI VLVFLNTLTI 

       550        560        570        580        590        600 
SSEHYNQPDW LTQIQDIANK VLLALFTCEM LVKMYSLGLQ AYFVSLFNRF DCFVVCGGIT 

       610        620        630        640        650        660 
ETILVELEIM SPLGISVFRC VRLLRIFKVT RHWTSLSNLV ASLLNSMKSI ASLLLLLFLF 

       670        680        690        700        710        720 
IIIFSLLGMQ LFGGKFNFDE TQTKRSTFDN FPQALLTVFQ ILTGEDWNAV MYDGIMAYGG 

       730        740        750        760        770        780 
PSSSGMIVCI YFIILFICGN YILLNVFLAI AVDNLADAES LNTAQKEEAE EKERKKIARK 

       790        800        810        820        830        840 
ESLENKKNNK PEVNQIANSD NKVTIDDYRE EDEDKDPYPP CDVPVGEEEE EEEEDEPEVP 

       850        860        870        880        890        900 
AGPRPRRISE LNMKEKIAPI PEGSAFFILS KTNPIRVGCH KLINHHIFTN LILVFIMLSS 

       910        920        930        940        950        960 
AALAAEDPIR SHSFRNTILG YFDYAFTAIF TVEILLKMTT FGAFLHKGAF CRNYFNLLDM 

       970        980        990       1000       1010       1020 
LVVGVSLVSF GIQSSAISVV KILRVLRVLR PLRAINRAKG LKHVVQCVFV AIRTIGNIMI 

      1030       1040       1050       1060       1070       1080 
VTTLLQFMFA CIGVQLFKGK FYRCTDEAKS NPEECRGLFI LYKDGDVDSP VVRERIWQNS 

      1090       1100       1110       1120       1130       1140 
DFNFDNVLSA MMALFTVSTF EGWPALLYKA IDSNGENIGP IYNHRVEISI FFIIYIIIVA 

      1150       1160       1170       1180       1190       1200 
FFMMNIFVGF VIVTFQEQGE KEYKNCELDK NQRQCVEYAL KARPLRRYIP KNPYQYKFWY 

      1210       1220       1230       1240       1250       1260 
VVNSSPFEYM MFVLIMLNTL CLAMQHYEQS KMFNDAMDIL NMVFTGVFTV EMVLKVIAFK 

      1270       1280       1290       1300       1310       1320 
PKGYFSDAWN TFDSLIVIGS IIDVALSEAD PTESENVPVP TATPGNSEES NRISITFFRL 

      1330       1340       1350       1360       1370       1380 
FRVMRLVKLL SRGEGIRTLL WTFIKSFQAL PYVALLIAML FFIYAVIGMQ MFGKVAMRDN 

      1390       1400       1410       1420       1430       1440 
NQINRNNNFQ TFPQAVLLLF RCATGEAWQE IMLACLPGKL CDPESDYNPG EEYTCGSNFA 

      1450       1460       1470       1480       1490       1500 
IVYFISFYML CAFLIINLFV AVIMDNFDYL TRDWSILGPH HLDEFKRIWS EYDPEAKGRI 

      1510       1520       1530       1540       1550       1560 
KHLDVVTLLR RIQPPLGFGK LCPHRVACKR LVAMNMPLNS DGTVMFNATL FALVRTALKI 

      1570       1580       1590       1600       1610       1620 
KTEGNLEQAN EELRAVIKKI WKKTSMKLLD QVVPPAGDDE VTVGKFYATF LIQDYFRKFK 

      1630       1640       1650       1660       1670       1680 
KRKEQGLVGK YPAKNTTIAL QAGLRTLHDI GPEIRRAISC DLQDDEPEET KREEEDDVFK 

      1690       1700       1710       1720       1730       1740 
RNGALLGNHV NHVNSDRRDS LQQTNTTHRP LHVQRPSIPP ASDTEKPLFP PAGNSVCHNH 

      1750       1760       1770       1780       1790       1800 
HNHNSIGKQV PTSTNANLNN ANMSKAAHGK RPSIGNLEHV SENGHHSSHK HDREPQRRSS 

      1810       1820       1830       1840       1850       1860 
VKRTRYYETY IRSDSGDEQL PTICREDPEI HGYFRDPHCL GEQEYFSSEE CYEDDSSPTW 

      1870       1880       1890       1900       1910       1920 
SRQNYGYYSR YPGRNIDSER PRGYHHPQGF LEDDDSPVCY DSRRSPRRRL LPPTPASHRR 

      1930       1940       1950       1960       1970       1980 
SSFNFECLRR QSSQEEVPSS PIFPHRTALP LHLMQQQIMA VAGLDSSKAQ KYSPSHSTRS 

      1990       2000       2010       2020       2030       2040 
WATPPATPPY RDWTPCYTPL IQVEQSEALD QVNGSLPSLH RSSWYTDEPD ISYRTFTPAS 

      2050       2060       2070       2080       2090       2100 
LTVPSSFRNK NSDKQRSADS LVEAVLISEG LGRYARDPKF VSATKHEIAD ACDLTIDEME 

      2110       2120       2130       2140       2150       2160 
SAASTLLNGN VRPRANGDVG PLSHRQDYEL QDFGPGYSDE EPDPGRDEED LADEMICITT 


L 

« Hide

Isoform Beta-cell-type [UniParc].

Checksum: 93C3A848E89B5A76
Show »

FASTA2,181247,566
Isoform 4 (Ca(V)1.3(42A)) [UniParc].

Checksum: D90F644342325721
Show »

FASTA1,647187,035
Isoform 3 [UniParc].

Checksum: 0247ED997C1E6128
Show »

FASTA2,137242,417

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Loss of Ca(v)1.3 (CACNA1D) function in a human channelopathy with bradycardia and congenital deafness."
Baig S.M., Koschak A., Lieb A., Gebhart M., Dafinger C., Nurnberg G., Ali A., Ahmad I., Sinnegger-Brauns M.J., Brandt N., Engel J., Mangoni M.E., Farooq M., Khan H.U., Nurnberg P., Striessnig J., Bolz H.J.
Nat. Neurosci. 14:77-84(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SANDD GLY-403 INS, CHARACTERIZATION OF VARIANT SANDD GLY-403 INS.
[10]"Somatic and germline CACNA1D calcium channel mutations in aldosterone-producing adenomas and primary aldosteronism."
Scholl U.I., Goh G., Stoelting G., de Oliveira R.C., Choi M., Overton J.D., Fonseca A.L., Korah R., Starker L.F., Kunstman J.W., Prasad M.L., Hartung E.A., Mauras N., Benson M.R., Brady T., Shapiro J.R., Loring E., Nelson-Williams C. expand/collapse author list , Libutti S.K., Mane S., Hellman P., Westin G., Aakerstroem G., Bjoerklund P., Carling T., Fahlke C., Hidalgo P., Lifton R.P.
Nat. Genet. 45:1050-1054(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PASNA ASP-403 AND MET-750, CHARACTERIZATION OF VARIANTS PASNA ASP-403 AND MET-750.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS2872.1. [Q01668-2]
CCDS46848.1. [Q01668-1]
CCDS46849.1. [Q01668-3]
PIRJH0564.
RefSeqNP_000711.1. NM_000720.3. [Q01668-2]
NP_001122311.1. NM_001128839.2. [Q01668-3]
NP_001122312.1. NM_001128840.2. [Q01668-1]
UniGeneHs.476358.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3LV3X-ray1.94C502-510[»]
ProteinModelPortalQ01668.
SMRQ01668. Positions 120-405, 420-448, 519-753, 882-1152, 1201-1465, 1548-1628.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107230. 1 interaction.
DIPDIP-48998N.
IntActQ01668. 1 interaction.
STRING9606.ENSP00000288139.

Chemistry

BindingDBQ01668.
ChEMBLCHEMBL2095229.
DrugBankDB00661. Verapamil.
GuidetoPHARMACOLOGY530.

PTM databases

PhosphoSiteQ01668.

Polymorphism databases

DMDM116241275.

Proteomic databases

PaxDbQ01668.
PRIDEQ01668.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000288139; ENSP00000288139; ENSG00000157388. [Q01668-2]
ENST00000350061; ENSP00000288133; ENSG00000157388. [Q01668-1]
ENST00000422281; ENSP00000409174; ENSG00000157388. [Q01668-3]
GeneID776.
KEGGhsa:776.
UCSCuc003dgu.5. human. [Q01668-2]
uc003dgv.5. human. [Q01668-1]

Organism-specific databases

CTD776.
GeneCardsGC03P053504.
HGNCHGNC:1391. CACNA1D.
HPAHPA020215.
MIM114206. gene.
614896. phenotype.
615474. phenotype.
neXtProtNX_Q01668.
Orphanet85142. Aldosterone-producing adenoma.
369929. Aldosterone-producing adenoma with seizures and neurological abnormalities.
324321. Sinoatrial node dysfunction and deafness.
PharmGKBPA84.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1226.
HOGENOMHOG000231529.
HOVERGENHBG050763.
KOK04851.
OMAFSDAWNT.
OrthoDBEOG7T1RBQ.
PhylomeDBQ01668.
TreeFamTF312805.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
REACT_111217. Metabolism.

Gene expression databases

ArrayExpressQ01668.
BgeeQ01668.
CleanExHS_CACNA1D.
GenevestigatorQ01668.

Family and domain databases

Gene3D1.20.120.350. 5 hits.
InterProIPR027359. Channel_four-helix_dom.
IPR005821. Ion_trans_dom.
IPR005452. LVDCC_a1dsu.
IPR014873. VDCC_a1su_IQ.
IPR005446. VDCC_L_a1su.
IPR002077. VDCCAlpha1.
[Graphical view]
PfamPF08763. Ca_chan_IQ. 1 hit.
PF00520. Ion_trans. 4 hits.
[Graphical view]
PRINTSPR00167. CACHANNEL.
PR01630. LVDCCALPHA1.
PR01636. LVDCCALPHA1D.
SMARTSM01062. Ca_chan_IQ. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiCav1.3.
GenomeRNAi776.
NextBio3136.
PROQ01668.
SOURCESearch...

Entry information

Entry nameCAC1D_HUMAN
AccessionPrimary (citable) accession number: Q01668
Secondary accession number(s): B0FYA3 expand/collapse secondary AC list , Q13916, Q13931, Q71UT1, Q9UDC3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: October 17, 2006
Last modified: July 9, 2014
This is version 148 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM