ID   Q59GD8_HUMAN            Unreviewed;      1854 AA.
AC   Q59GD8;
DT   26-APR-2005, integrated into UniProtKB/TrEMBL.
DT   26-APR-2005, sequence version 1.
DT   02-SEP-2026, entry version 159.
DE   RecName: Full=Voltage-dependent L-type calcium channel subunit alpha-1D {ECO:0000256|ARBA:ARBA00015724};
DE   AltName: Full=Voltage-gated calcium channel subunit alpha Cav1.3 {ECO:0000256|ARBA:ARBA00030573};
DE   Flags: Fragment;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606 {ECO:0000313|EMBL:BAD92408.1};
RN   [1] {ECO:0000313|EMBL:BAD92408.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Brain {ECO:0000313|EMBL:BAD92408.1};
RA   Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA   Ohara O., Nagase T., Kikuno R.F.;
RT   "Homo sapiens protein coding cDNA.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Voltage-sensitive calcium channels (VSCC) mediate the entry
CC       of calcium ions into excitable cells and are also involved in a variety
CC       of calcium-dependent processes, including muscle contraction, hormone
CC       or neurotransmitter release, gene expression, cell motility, cell
CC       division and cell death. The isoform alpha-1D gives rise to L-type
CC       calcium currents. Long-lasting (L-type) calcium channels belong to the
CC       'high-voltage activated' (HVA) group. They are blocked by
CC       dihydropyridines (DHP), phenylalkylamines, and by benzothiazepines.
CC       {ECO:0000256|ARBA:ARBA00057257}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Ca(2+)(in) = Ca(2+)(out); Xref=Rhea:RHEA:29671,
CC         ChEBI:CHEBI:29108; Evidence={ECO:0000256|ARBA:ARBA00036634};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC       ECO:0000256|RuleBase:RU003808}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU003808}.
CC   -!- SIMILARITY: Belongs to the calcium channel alpha-1 subunit
CC       (TC 1.A.1.11) family. CACNA1D subfamily.
CC       {ECO:0000256|ARBA:ARBA00010354}.
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DR   EMBL; AB209171; BAD92408.1; -; mRNA.
DR   RefSeq; NP_000711.1; NM_000720.4.
DR   RefSeq; NP_001122312.1; NM_001128840.3.
DR   SMR; Q59GD8; -.
DR   MassIVE; Q59GD8; -.
DR   PeptideAtlas; Q59GD8; -.
DR   ProteomicsDB; 62658; -.
DR   Antibodypedia; 4062; 300 antibodies from 33 providers.
DR   DNASU; 776; -.
DR   GeneID; 776; -.
DR   KEGG; hsa:776; -.
DR   UCSC; uc062ksr.1; human.
DR   ClinPGx; PA84; -.
DR   CTD; 776; -.
DR   DisGeNET; 776; -.
DR   VEuPathDB; HostDB:ENSG00000157388; -.
DR   OrthoDB; 431720at2759; -.
DR   BioGRID-ORCS; 776; 14 hits in 1163 CRISPR screens.
DR   ChiTaRS; CACNA1D; human.
DR   Bgee; ENSG00000157388; Expressed in buccal mucosa cell and 149 other cell types or tissues.
DR   GO; GO:0030315; C:T-tubule; IEA:UniProtKB-ARBA.
DR   GO; GO:0005891; C:voltage-gated calcium channel complex; IEA:InterPro.
DR   GO; GO:0008092; F:cytoskeletal protein binding; IEA:UniProtKB-ARBA.
DR   GO; GO:0086007; F:voltage-gated calcium channel activity involved in cardiac muscle cell action potential; IEA:UniProtKB-ARBA.
DR   GO; GO:0007154; P:cell communication; IEA:UniProtKB-ARBA.
DR   GO; GO:0006936; P:muscle contraction; IEA:UniProtKB-ARBA.
DR   GO; GO:0050877; P:nervous system process; IEA:UniProtKB-ARBA.
DR   GO; GO:0051050; P:positive regulation of transport; IEA:UniProtKB-ARBA.
DR   GO; GO:0010959; P:regulation of metal ion transport; IEA:UniProtKB-ARBA.
DR   GO; GO:0023052; P:signaling; IEA:UniProtKB-ARBA.
DR   FunFam; 1.10.287.70:FF:000007; Voltage-dependent L-type calcium channel subunit alpha; 1.
DR   FunFam; 1.10.287.70:FF:000009; Voltage-dependent L-type calcium channel subunit alpha; 1.
DR   FunFam; 1.10.287.70:FF:000021; Voltage-dependent L-type calcium channel subunit alpha; 1.
DR   FunFam; 1.20.120.350:FF:000001; Voltage-dependent L-type calcium channel subunit alpha; 1.
DR   FunFam; 1.20.120.350:FF:000006; Voltage-dependent L-type calcium channel subunit alpha; 1.
DR   FunFam; 1.20.120.350:FF:000027; Voltage-dependent L-type calcium channel subunit alpha; 1.
DR   FunFam; 1.10.238.10:FF:000063; Voltage-dependent N-type calcium channel subunit alpha; 1.
DR   Gene3D; 1.10.287.70; -; 4.
DR   Gene3D; 6.10.250.2180; -; 1.
DR   Gene3D; 6.10.250.2500; -; 1.
DR   Gene3D; 1.20.120.350; Voltage-gated potassium channels. Chain C; 3.
DR   InterPro; IPR031688; CAC1F_C.
DR   InterPro; IPR031649; GPHH_dom.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR005452; LVDCC_a1dsu.
DR   InterPro; IPR014873; VDCC_a1su_IQ.
DR   InterPro; IPR050599; VDCC_alpha-1_subunit.
DR   InterPro; IPR002077; VDCCAlpha1.
DR   InterPro; IPR027359; Volt_channel_dom_sf.
DR   PANTHER; PTHR45628; VOLTAGE-DEPENDENT CALCIUM CHANNEL TYPE A SUBUNIT ALPHA-1; 1.
DR   PANTHER; PTHR45628:SF11; VOLTAGE-DEPENDENT L-TYPE CALCIUM CHANNEL SUBUNIT ALPHA-1D; 1.
DR   Pfam; PF08763; Ca_chan_IQ; 1.
DR   Pfam; PF16885; CAC1F_C; 1.
DR   Pfam; PF16905; GPHH; 1.
DR   Pfam; PF00520; Ion_trans; 4.
DR   PRINTS; PR00167; CACHANNEL.
DR   PRINTS; PR01636; LVDCCALPHA1D.
DR   SMART; SM01062; Ca_chan_IQ; 1.
DR   SUPFAM; SSF81324; Voltage-gated potassium channels; 4.
PE   2: Evidence at transcript level;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PIRSR:PIRSR602077-1};
KW   Calcium channel {ECO:0000256|ARBA:ARBA00022673,
KW   ECO:0000256|RuleBase:RU003808};
KW   Calcium transport {ECO:0000256|ARBA:ARBA00022568,
KW   ECO:0000256|RuleBase:RU003808};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycoprotein {ECO:0000256|PIRSR:PIRSR602077-3};
KW   Ion channel {ECO:0000256|ARBA:ARBA00023303};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR602077-1};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448};
KW   Voltage-gated channel {ECO:0000256|ARBA:ARBA00022882,
KW   ECO:0000256|RuleBase:RU003808}.
FT   TRANSMEM        56..78
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        216..234
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        254..277
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        346..365
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        418..445
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        580..598
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        618..638
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        650..676
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        696..726
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        823..848
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        902..920
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        932..952
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1042..1060
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1134..1157
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1291..1325
FT                   /note="Voltage-dependent calcium channel alpha-1 subunit
FT                   IQ"
FT                   /evidence="ECO:0000259|SMART:SM01062"
FT   REGION          122..153
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          459..543
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1352..1371
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1377..1497
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1565..1612
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1801..1845
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        136..152
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        459..483
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        484..495
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        518..531
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1438..1456
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1472..1490
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1831..1845
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         37
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT   BINDING         398
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT   BINDING         794
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT   CARBOHYD        2
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602077-3"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:BAD92408.1"
SQ   SEQUENCE   1854 AA;  211464 MW;  73DE6B07DF531A39 CRC64;
     ANGTECRSGW VGPNGGITNF DNFAFAMLTV FQCITMEGWT DVLYWMNDAM GFELPWVYFV
     SLVIFGSFFV LNLVLGVLSG EFSKEREKAK ARGDFQKLRE KQQLEEDLKG YLDWITQAED
     IDPENEEEGG EEGKRNTSMP TSETESVNTE NVSGEGENRG CCGSLWCWWR RRGAAKAGPS
     GCRRWGQAIS KSKLSRRWRR WNRFNRRRCR AAVKSVTFYW LVIVLVFLNT LTISSEHYNQ
     PDWLTQIQDI ANKVLLALFT CEMLVKMYSL GLQAYFVSLF NRFDCFVVCG GITETILVEL
     EIMSPLGISV FRCVRLLRIF KVTRHWTSLS NLVASLLNSM KSIASLLLLL FLFIIIFSLL
     GMQLFGGKFN FDETQTKRST FDNFPQALLT VFQILTGEDW NAVMYDGIMA YGGPSSSGMI
     VCIYFIILFI CGNYILLNVF LAIAVDNLAD AESLNTAQKE EAEEKERKKI ARKESLENKK
     NNKPEVNQIA NSDNKVTIDD YREEDEDKDP YPPCDVPVGE EEEEEEEDEP EVPAGPRPRR
     ISELNMKEKI APIPEGSAFF ILSKTNPIRV GCHKLINHHI FTNLILVFIM LSSAALAAED
     PIRSHSFRNT ILGYFDYAFT AIFTVEILLK MTTFGAFLHK GAFCRNYFNL LDMLVVGVSL
     VSFGIQSSAI SVVKILRVLR VLRPLRAINR AKGLKHVVQC VFVAIRTIGN IMIVTTLLQF
     MFACIGVQLF KGKFYRCTDE AKSNPEECRG LFILYKDGDV DSPVVRERIW QNSDFNFDNV
     LSAMMALFTV STFEGWPALL YKAIDSNGEN IGPIYNHRVE ISIFFIIYII IVAFFMMNIF
     VGFVIVTFQE QGEKEYKNCE LDKNQRQCVE YALKARPLRR YIPKNPYQYK FWYVVNSSPF
     EYMMFVLIML NTLCLAMQHY EQSKMFNDAM DILNMVFTGV FTVEMVLKVI AFKPKHYFTD
     AWNTFDALIV VGSVVDIAIT EVNPTESENV PVPTATPGNS EESNRISITF FRLFRVMRLV
     KLLSRGEGIR TLLWTFIKSF QALPYVALLI AMLFFIYAVI GMQMFGKVAM RDNNQINRNN
     NFQTFPQAVL LLFRCATGEA WQEIMLACLP GKLCDPESDY NPGEEYTCGS NFAIVYFISF
     YMLCAFLIIN LFVAVIMDNF DYLTRDWSIL GPHHLDEFKR IWSEYDPEAK GRIKHLDVVT
     LLRRIQPPLG FGKLCPHRVA CKRLVAMNMP LNSDGTVMFN ATLFALVRTA LKIKTEGNLE
     QANEELRAVI KKIWKKTSMK LLDQVVPPAG DDEVTVGKFY ATFLIQDYFR KFKKRKEQGL
     VGKYPAKNTT IALQAGLRTL HDIGPEIRRA ISCDLQDDEP EETKREEEDD VFKRNGALLG
     NHVNHVNSDR RDSLQQTNTT HRPLHVQRPS IPPASDTEKP LFPPAGNSVC HNHHNHNSIG
     KQVPTSTNAN LNNANMSKAA HGKRPSIGNL EHVSENGHHS SHKHDREPQR RSSVKRTRYY
     ETYIRSDSGD EQLPTICRED PEIHGYFRDP HCLGEQEYFS SEECYEDDSS PTWSRQNYGY
     YSRYPGRNID SERPRGYHHP QGFLEDDDSP VCYDSRRSPR RRLLPPTPAS HRRSSFNFEC
     LRRQSSQEEV PSSPIFPHRT ALPLHLMQQQ IMAVAGLDSS KAQKYSPSHS TRSWATPPAT
     PPYRDWTPCY TPLIQVEQSE ALDQVNGSLP SLHRSSWYTD EPDISYRTFT PASLTVPSSF
     RNKNSDKQRS ADSLVEAVLI SEGLGRYARD PKFVSATKHE IADACDLTID EMESAASTLL
     NGNVRPRANG DVGPLSHRQD YELQDFGPGY SDEEPDPGRD EEDLADEMIC ITTL
//