ID   CA2D1_HUMAN             Reviewed;        1103 AA.
AC   P54289; Q17R45; Q9UD80; Q9UD81; Q9UD82;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   03-NOV-2009, sequence version 3.
DT   27-MAR-2024, entry version 212.
DE   RecName: Full=Voltage-dependent calcium channel subunit alpha-2/delta-1;
DE   AltName: Full=Voltage-gated calcium channel subunit alpha-2/delta-1;
DE   Contains:
DE     RecName: Full=Voltage-dependent calcium channel subunit alpha-2-1;
DE   Contains:
DE     RecName: Full=Voltage-dependent calcium channel subunit delta-1;
DE   Flags: Precursor;
GN   Name=CACNA2D1; Synonyms=CACNL2A, CCHL2A, MHS3;
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
RX   PubMed=1309651; DOI=10.1016/0896-6273(92)90109-q;
RA   Williams M.E., Feldman D.H., McCue A.F., Brenner R., Velicelebi G.,
RA   Ellis S.B., Harpold M.M.;
RT   "Structure and functional expression of alpha 1, alpha 2, and beta subunits
RT   of a novel human neuronal calcium channel subtype.";
RL   Neuron 8:71-84(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Cerebellum;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 528-648 (ISOFORMS 1; 2; 3; 4 AND 5), TISSUE
RP   SPECIFICITY, AND ALTERNATIVE SPLICING.
RC   TISSUE=Neuroblastoma;
RX   PubMed=8107964; DOI=10.1016/0028-3908(93)90004-m;
RA   Brust P.F., Simerson S., McCue A.F., Deal C.R., Schoonmaker S.,
RA   Williams M.E., Velicelebi G., Johnson E.C., Harpold M.M., Ellis S.B.;
RT   "Human neuronal voltage-dependent calcium channels: studies on subunit
RT   structure and role in channel assembly.";
RL   Neuropharmacology 32:1089-1102(1993).
RN   [5]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-136; ASN-324 AND ASN-675.
RC   TISSUE=Plasma;
RX   PubMed=16335952; DOI=10.1021/pr0502065;
RA   Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA   Smith R.D.;
RT   "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT   hydrazide chemistry, and mass spectrometry.";
RL   J. Proteome Res. 4:2070-2080(2005).
RN   [6]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-348; ASN-475 AND ASN-824.
RC   TISSUE=Liver;
RX   PubMed=19159218; DOI=10.1021/pr8008012;
RA   Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT   "Glycoproteomics analysis of human liver tissue by combination of multiple
RT   enzyme digestion and hydrazide chemistry.";
RL   J. Proteome Res. 8:651-661(2009).
RN   [7]
RP   INTERCHAIN DISULFIDE BOND, AND SUBUNIT.
RX   PubMed=22054663; DOI=10.1016/j.ceca.2011.10.002;
RA   Calderon-Rivera A., Andrade A., Hernandez-Hernandez O.,
RA   Gonzalez-Ramirez R., Sandoval A., Rivera M., Gomora J.C., Felix R.;
RT   "Identification of a disulfide bridge essential for structure and function
RT   of the voltage-gated Ca(2+) channel alpha(2)delta-1 auxiliary subunit.";
RL   Cell Calcium 51:22-30(2012).
RN   [8]
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.0 ANGSTROMS) OF 38-361 IN COMPLEX WITH
RP   HUMAN CAV2.2/CACNA1B AND BETA-3 SUBUNIT IN PRESENCE AND ABSENCE OF THE
RP   OMEGA-CONOTOXIN MVIIA, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-92;
RP   ASN-184; ASN-348; ASN-468; ASN-613; ASN-781 AND ASN-895.
RX   PubMed=34234349; DOI=10.1038/s41586-021-03699-6;
RA   Gao S., Yao X., Yan N.;
RT   "Structure of human Cav2.2 channel blocked by the painkiller ziconotide.";
RL   Nature 596:143-147(2021).
RN   [9]
RP   VARIANT DEE110 ASP-209, CHARACTERIZATION OF VARIANT DEE110 ASP-209,
RP   FUNCTION, SUBCELLULAR LOCATION, AND INVOLVEMENT IN DEE110.
RX   PubMed=35293990; DOI=10.1093/brain/awac081;
RA   Dahimene S., von Elsner L., Holling T., Mattas L.S., Pickard J., Lessel D.,
RA   Pilch K.S., Kadurin I., Pratt W.S., Zhulin I.B., Dai H., Hempel M.,
RA   Ruzhnikov M.R.Z., Kutsche K., Dolphin A.C.;
RT   "Biallelic CACNA2D1 loss-of-function variants cause early-onset
RT   developmental epileptic encephalopathy.";
RL   Brain 145:2721-2729(2022).
CC   -!- FUNCTION: The alpha-2/delta subunit of voltage-dependent calcium
CC       channels regulates calcium current density and activation/inactivation
CC       kinetics of the calcium channel (PubMed:35293990). Plays an important
CC       role in excitation-contraction coupling (By similarity). {ECO:0000250,
CC       ECO:0000269|PubMed:35293990}.
CC   -!- SUBUNIT: Dimer formed of alpha-2-1 and delta-1 chains; disulfide-
CC       linked. Voltage-dependent calcium channels are multisubunit complexes,
CC       consisting of alpha-1 (CACNA1), alpha-2 (CACNA2D), beta (CACNB) and
CC       delta (CACNA2D) subunits in a 1:1:1:1 ratio (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC       membrane protein {ECO:0000305}. Cell membrane
CC       {ECO:0000269|PubMed:35293990}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=1; Synonyms=Alpha-2a;
CC         IsoId=P54289-1; Sequence=Displayed;
CC       Name=2; Synonyms=Alpha-2b;
CC         IsoId=P54289-2; Sequence=VSP_038348, VSP_038350;
CC       Name=3; Synonyms=Alpha-2c;
CC         IsoId=P54289-3; Sequence=VSP_038349, VSP_038350;
CC       Name=4; Synonyms=Alpha-2d;
CC         IsoId=P54289-4; Sequence=VSP_038349;
CC       Name=5; Synonyms=Alpha-2e;
CC         IsoId=P54289-5; Sequence=VSP_038348;
CC   -!- TISSUE SPECIFICITY: Isoform 1 is expressed in skeletal muscle. Isoform
CC       2 is expressed in the central nervous system. Isoform 2, isoform 4 and
CC       isoform 5 are expressed in neuroblastoma cells. Isoform 3, isoform 4
CC       and isoform 5 are expressed in the aorta. {ECO:0000269|PubMed:1309651,
CC       ECO:0000269|PubMed:8107964}.
CC   -!- DOMAIN: The MIDAS-like motif in the VWFA domain binds divalent metal
CC       cations and is required to promote trafficking of the alpha-1 (CACNA1)
CC       subunit to the plasma membrane by an integrin-like switch.
CC       {ECO:0000250}.
CC   -!- PTM: Proteolytically processed into subunits alpha-2-1 and delta-1 that
CC       are disulfide-linked. {ECO:0000250}.
CC   -!- DISEASE: Developmental and epileptic encephalopathy 110 (DEE110)
CC       [MIM:620149]: A form of epileptic encephalopathy, a heterogeneous group
CC       of early-onset epilepsies characterized by refractory seizures,
CC       neurodevelopmental impairment, and poor prognosis. Development is
CC       normal prior to seizure onset, after which cognitive and motor delays
CC       become apparent. DEE110 is an autosomal recessive form characterized by
CC       profound global developmental delay and hypotonia apparent in infancy
CC       followed by onset of seizures in the first months or years of life.
CC       {ECO:0000269|PubMed:35293990}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- MISCELLANEOUS: Binds gabapentin, an antiepileptic drug.
CC   -!- SIMILARITY: Belongs to the calcium channel subunit alpha-2/delta
CC       family. {ECO:0000305}.
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DR   EMBL; M76559; AAA51903.1; -; mRNA.
DR   EMBL; CH471091; EAW76990.1; -; Genomic_DNA.
DR   EMBL; BC117468; AAI17469.1; -; mRNA.
DR   EMBL; BC117470; AAI17471.1; -; mRNA.
DR   CCDS; CCDS5598.1; -. [P54289-2]
DR   CCDS; CCDS94135.1; -. [P54289-1]
DR   PIR; JH0565; JH0565.
DR   RefSeq; NP_000713.2; NM_000722.3. [P54289-2]
DR   RefSeq; XP_005250627.1; XM_005250570.2.
DR   RefSeq; XP_005250629.1; XM_005250572.2. [P54289-3]
DR   RefSeq; XP_005250630.1; XM_005250573.2. [P54289-5]
DR   RefSeq; XP_005250631.1; XM_005250574.2. [P54289-4]
DR   PDB; 7MIX; EM; 3.00 A; D=1-1103.
DR   PDB; 7MIY; EM; 3.10 A; D=1-1103.
DR   PDB; 7UHF; EM; 3.10 A; D=1-1103.
DR   PDB; 7UHG; EM; 3.00 A; D=1-1103.
DR   PDB; 7VFS; EM; 2.80 A; B=1-1103.
DR   PDB; 7VFU; EM; 3.00 A; B=1-1103.
DR   PDB; 7VFV; EM; 3.00 A; B=1-1103.
DR   PDB; 7VFW; EM; 3.30 A; B=1-1103.
DR   PDB; 7XLQ; EM; 3.10 A; D=27-1103.
DR   PDB; 7YG5; EM; 3.00 A; D=1-1103.
DR   PDB; 8E59; EM; 3.10 A; D=1-1103.
DR   PDB; 8E5A; EM; 3.30 A; D=1-1103.
DR   PDB; 8E5B; EM; 3.30 A; D=1-1103.
DR   PDB; 8EPL; EM; 3.10 A; C=1-1103.
DR   PDB; 8EPM; EM; 3.10 A; C=1-1103.
DR   PDB; 8IF3; EM; 3.20 A; A=1-1103.
DR   PDB; 8IF4; EM; 3.20 A; A=1-1103.
DR   PDB; 8WE6; EM; 2.90 A; D=1-1103.
DR   PDB; 8WE7; EM; 3.20 A; D=1-1103.
DR   PDB; 8WE8; EM; 2.90 A; D=1-1103.
DR   PDB; 8WE9; EM; 3.00 A; D=1-1103.
DR   PDB; 8WEA; EM; 3.20 A; D=1-1103.
DR   PDBsum; 7MIX; -.
DR   PDBsum; 7MIY; -.
DR   PDBsum; 7UHF; -.
DR   PDBsum; 7UHG; -.
DR   PDBsum; 7VFS; -.
DR   PDBsum; 7VFU; -.
DR   PDBsum; 7VFV; -.
DR   PDBsum; 7VFW; -.
DR   PDBsum; 7XLQ; -.
DR   PDBsum; 7YG5; -.
DR   PDBsum; 8E59; -.
DR   PDBsum; 8E5A; -.
DR   PDBsum; 8E5B; -.
DR   PDBsum; 8EPL; -.
DR   PDBsum; 8EPM; -.
DR   PDBsum; 8IF3; -.
DR   PDBsum; 8IF4; -.
DR   PDBsum; 8WE6; -.
DR   PDBsum; 8WE7; -.
DR   PDBsum; 8WE8; -.
DR   PDBsum; 8WE9; -.
DR   PDBsum; 8WEA; -.
DR   AlphaFoldDB; P54289; -.
DR   EMDB; EMD-23867; -.
DR   EMDB; EMD-23868; -.
DR   EMDB; EMD-26513; -.
DR   EMDB; EMD-26514; -.
DR   EMDB; EMD-27907; -.
DR   EMDB; EMD-27908; -.
DR   EMDB; EMD-27909; -.
DR   EMDB; EMD-28529; -.
DR   EMDB; EMD-28530; -.
DR   EMDB; EMD-31958; -.
DR   EMDB; EMD-31959; -.
DR   EMDB; EMD-31960; -.
DR   EMDB; EMD-31961; -.
DR   EMDB; EMD-33285; -.
DR   EMDB; EMD-33808; -.
DR   EMDB; EMD-35399; -.
DR   EMDB; EMD-35400; -.
DR   SMR; P54289; -.
DR   BioGRID; 107235; 83.
DR   ComplexPortal; CPX-3192; Skeletal muscle VGCC complex.
DR   ComplexPortal; CPX-3195; Cardiac muscle voltage-gated calcium channel complex.
DR   CORUM; P54289; -.
DR   IntAct; P54289; 36.
DR   STRING; 9606.ENSP00000349320; -.
DR   BindingDB; P54289; -.
DR   ChEMBL; CHEMBL1919; -.
DR   DrugBank; DB13746; Bioallethrin.
DR   DrugBank; DB11148; Butamben.
DR   DrugBank; DB04838; Cyclandelate.
DR   DrugBank; DB09235; Efonidipine.
DR   DrugBank; DB00228; Enflurane.
DR   DrugBank; DB00153; Ergocalciferol.
DR   DrugBank; DB01023; Felodipine.
DR   DrugBank; DB00996; Gabapentin.
DR   DrugBank; DB08872; Gabapentin enacarbil.
DR   DrugBank; DB00308; Ibutilide.
DR   DrugBank; DB00270; Isradipine.
DR   DrugBank; DB00622; Nicardipine.
DR   DrugBank; DB06712; Nilvadipine.
DR   DrugBank; DB00401; Nisoldipine.
DR   DrugBank; DB01054; Nitrendipine.
DR   DrugBank; DB00230; Pregabalin.
DR   DrugBank; DB00421; Spironolactone.
DR   DrugBank; DB00661; Verapamil.
DR   DrugCentral; P54289; -.
DR   TCDB; 8.A.18.1.1; the ca(2+) channel auxiliary subunit Alpha2Delta types 1-4 (cca-Alpha2Delta) family.
DR   GlyConnect; 1895; 24 N-Linked glycans (7 sites).
DR   GlyCosmos; P54289; 17 sites, 25 glycans.
DR   GlyGen; P54289; 17 sites, 25 N-linked glycans (7 sites).
DR   iPTMnet; P54289; -.
DR   PhosphoSitePlus; P54289; -.
DR   SwissPalm; P54289; -.
DR   BioMuta; CACNA2D1; -.
DR   DMDM; 262527579; -.
DR   EPD; P54289; -.
DR   jPOST; P54289; -.
DR   MassIVE; P54289; -.
DR   MaxQB; P54289; -.
DR   PaxDb; 9606-ENSP00000349320; -.
DR   PeptideAtlas; P54289; -.
DR   ProteomicsDB; 56675; -. [P54289-1]
DR   ProteomicsDB; 56676; -. [P54289-2]
DR   ProteomicsDB; 56677; -. [P54289-3]
DR   ProteomicsDB; 56678; -. [P54289-4]
DR   ProteomicsDB; 56679; -. [P54289-5]
DR   Pumba; P54289; -.
DR   Antibodypedia; 2200; 308 antibodies from 35 providers.
DR   DNASU; 781; -.
DR   Ensembl; ENST00000356860.8; ENSP00000349320.3; ENSG00000153956.17. [P54289-2]
DR   Ensembl; ENST00000443883.2; ENSP00000409374.2; ENSG00000153956.17. [P54289-1]
DR   GeneID; 781; -.
DR   KEGG; hsa:781; -.
DR   MANE-Select; ENST00000356860.8; ENSP00000349320.3; NM_000722.4; NP_000713.2. [P54289-2]
DR   UCSC; uc003uhr.2; human. [P54289-1]
DR   AGR; HGNC:1399; -.
DR   CTD; 781; -.
DR   DisGeNET; 781; -.
DR   GeneCards; CACNA2D1; -.
DR   GeneReviews; CACNA2D1; -.
DR   HGNC; HGNC:1399; CACNA2D1.
DR   HPA; ENSG00000153956; Tissue enhanced (skeletal muscle, tongue).
DR   MalaCards; CACNA2D1; -.
DR   MIM; 114204; gene.
DR   MIM; 620149; phenotype.
DR   neXtProt; NX_P54289; -.
DR   OpenTargets; ENSG00000153956; -.
DR   Orphanet; 130; Brugada syndrome.
DR   Orphanet; 51083; Familial short QT syndrome.
DR   Orphanet; 442835; Non-specific early-onset epileptic encephalopathy.
DR   PharmGKB; PA86; -.
DR   VEuPathDB; HostDB:ENSG00000153956; -.
DR   eggNOG; KOG2353; Eukaryota.
DR   GeneTree; ENSGT00940000155209; -.
DR   HOGENOM; CLU_004660_0_0_1; -.
DR   InParanoid; P54289; -.
DR   OMA; CLWPMLG; -.
DR   OrthoDB; 2971287at2759; -.
DR   PhylomeDB; P54289; -.
DR   TreeFam; TF315824; -.
DR   PathwayCommons; P54289; -.
DR   SignaLink; P54289; -.
DR   BioGRID-ORCS; 781; 9 hits in 1156 CRISPR screens.
DR   ChiTaRS; CACNA2D1; human.
DR   GeneWiki; CACNA2D1; -.
DR   GenomeRNAi; 781; -.
DR   Pharos; P54289; Tclin.
DR   PRO; PR:P54289; -.
DR   Proteomes; UP000005640; Chromosome 7.
DR   RNAct; P54289; Protein.
DR   Bgee; ENSG00000153956; Expressed in biceps brachii and 186 other cell types or tissues.
DR   ExpressionAtlas; P54289; baseline and differential.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:1990454; C:L-type voltage-gated calcium channel complex; IDA:BHF-UCL.
DR   GO; GO:0098992; C:neuronal dense core vesicle; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0016529; C:sarcoplasmic reticulum; IEA:Ensembl.
DR   GO; GO:0005891; C:voltage-gated calcium channel complex; IDA:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005245; F:voltage-gated calcium channel activity; IDA:BHF-UCL.
DR   GO; GO:0098703; P:calcium ion import across plasma membrane; ISS:BHF-UCL.
DR   GO; GO:0061577; P:calcium ion transmembrane transport via high voltage-gated calcium channel; ISS:BHF-UCL.
DR   GO; GO:0006816; P:calcium ion transport; IDA:UniProtKB.
DR   GO; GO:0060402; P:calcium ion transport into cytosol; ISS:BHF-UCL.
DR   GO; GO:0086002; P:cardiac muscle cell action potential involved in contraction; IMP:BHF-UCL.
DR   GO; GO:1904646; P:cellular response to amyloid-beta; IGI:ARUK-UCL.
DR   GO; GO:0086048; P:membrane depolarization during bundle of His cell action potential; IMP:BHF-UCL.
DR   GO; GO:1901843; P:positive regulation of high voltage-gated calcium channel activity; ISS:BHF-UCL.
DR   GO; GO:1902514; P:regulation of calcium ion transmembrane transport via high voltage-gated calcium channel; IGI:ARUK-UCL.
DR   GO; GO:0051924; P:regulation of calcium ion transport; IDA:BHF-UCL.
DR   GO; GO:0086091; P:regulation of heart rate by cardiac conduction; IMP:BHF-UCL.
DR   GO; GO:0098903; P:regulation of membrane repolarization during action potential; ISS:BHF-UCL.
DR   GO; GO:0060307; P:regulation of ventricular cardiac muscle cell membrane repolarization; IMP:BHF-UCL.
DR   CDD; cd18774; PDC2_HK_sensor; 1.
DR   CDD; cd01463; vWA_VGCC_like; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 1.
DR   Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 1.
DR   InterPro; IPR013680; VDCC_a2/dsu.
DR   InterPro; IPR013608; VWA_N.
DR   InterPro; IPR002035; VWF_A.
DR   InterPro; IPR036465; vWFA_dom_sf.
DR   PANTHER; PTHR10166; VOLTAGE-DEPENDENT CALCIUM CHANNEL SUBUNIT ALPHA-2/DELTA-RELATED; 1.
DR   PANTHER; PTHR10166:SF6; VOLTAGE-DEPENDENT CALCIUM CHANNEL SUBUNIT ALPHA-2_DELTA-1; 1.
DR   Pfam; PF08473; VGCC_alpha2; 1.
DR   Pfam; PF00092; VWA; 1.
DR   Pfam; PF08399; VWA_N; 1.
DR   SMART; SM00327; VWA; 1.
DR   SUPFAM; SSF53300; vWA-like; 1.
DR   PROSITE; PS50234; VWFA; 1.
DR   Genevisible; P54289; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Calcium; Calcium channel;
KW   Calcium transport; Cell membrane; Disease variant; Disulfide bond;
KW   Epilepsy; Glycoprotein; Intellectual disability; Ion channel;
KW   Ion transport; Membrane; Metal-binding; Phosphoprotein; Reference proteome;
KW   Signal; Transmembrane; Transmembrane helix; Transport;
KW   Voltage-gated channel.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..1103
FT                   /note="Voltage-dependent calcium channel subunit alpha-
FT                   2/delta-1"
FT                   /id="PRO_0000304633"
FT   CHAIN           25..956
FT                   /note="Voltage-dependent calcium channel subunit alpha-2-1"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000005001"
FT   CHAIN           957..1103
FT                   /note="Voltage-dependent calcium channel subunit delta-1"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000005002"
FT   TOPO_DOM        25..1073
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1074..1094
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1095..1103
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          253..430
FT                   /note="VWFA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT   DOMAIN          446..556
FT                   /note="Cache"
FT   MOTIF           259..263
FT                   /note="MIDAS-like motif"
FT   BINDING         259
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250"
FT   BINDING         261
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250"
FT   BINDING         263
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         119
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P54290"
FT   CARBOHYD        92
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:34234349,
FT                   ECO:0007744|PDB:7MIX, ECO:0007744|PDB:7MIY"
FT   CARBOHYD        136
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        184
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:34234349,
FT                   ECO:0007744|PDB:7MIX, ECO:0007744|PDB:7MIY"
FT   CARBOHYD        324
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        348
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:34234349,
FT                   ECO:0007744|PDB:7MIX, ECO:0007744|PDB:7MIY"
FT   CARBOHYD        468
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:34234349,
FT                   ECO:0007744|PDB:7MIX, ECO:0007744|PDB:7MIY"
FT   CARBOHYD        475
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        604
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        613
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:34234349,
FT                   ECO:0007744|PDB:7MIX, ECO:0007744|PDB:7MIY"
FT   CARBOHYD        675
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        781
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:34234349,
FT                   ECO:0007744|PDB:7MIX, ECO:0007744|PDB:7MIY"
FT   CARBOHYD        824
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        888
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        895
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:34234349,
FT                   ECO:0007744|PDB:7MIX, ECO:0007744|PDB:7MIY"
FT   CARBOHYD        985
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        998
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        404..1059
FT                   /note="Interchain (between alpha-2-1 and delta-1 chains)"
FT   VAR_SEQ         531..554
FT                   /note="Missing (in isoform 3 and isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:8107964"
FT                   /id="VSP_038349"
FT   VAR_SEQ         531..549
FT                   /note="Missing (in isoform 2 and isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:1309651,
FT                   ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:8107964"
FT                   /id="VSP_038348"
FT   VAR_SEQ         644
FT                   /note="Y -> SKKGKMKD (in isoform 2 and isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:1309651,
FT                   ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:8107964"
FT                   /id="VSP_038350"
FT   VARIANT         209
FT                   /note="G -> D (in DEE110; does not promote calcium currents
FT                   in transfected cells indicating loss of function in the
FT                   positive regulation of voltage-gated calcium channel
FT                   activity; severely decreased localization at the cell
FT                   membrane; undergoes limited proteolytic cleavage)"
FT                   /evidence="ECO:0000269|PubMed:35293990"
FT                   /id="VAR_087875"
FT   VARIANT         1019
FT                   /note="E -> D (in dbSNP:rs9886043)"
FT                   /id="VAR_053960"
FT   VARIANT         1057
FT                   /note="D -> A (in dbSNP:rs35131433)"
FT                   /id="VAR_035047"
FT   CONFLICT        99
FT                   /note="R -> S (in Ref. 1; AAA51903)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        386
FT                   /note="T -> R (in Ref. 1; AAA51903)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        395
FT                   /note="D -> E (in Ref. 1; AAA51903)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        635
FT                   /note="L -> I (in Ref. 4; no nucleotide entry)"
FT                   /evidence="ECO:0000305"
FT   HELIX           30..52
FT                   /evidence="ECO:0007829|PDB:7VFS"
FT   HELIX           54..63
FT                   /evidence="ECO:0007829|PDB:7VFS"
FT   TURN            64..66
FT                   /evidence="ECO:0007829|PDB:7VFS"
FT   STRAND          67..72
FT                   /evidence="ECO:0007829|PDB:7VFS"
FT   HELIX           75..109
FT                   /evidence="ECO:0007829|PDB:7VFS"
FT   STRAND          118..120
FT                   /evidence="ECO:0007829|PDB:7VFS"
FT   STRAND          122..126
FT                   /evidence="ECO:0007829|PDB:7VFS"
FT   HELIX           135..137
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   STRAND          142..144
FT                   /evidence="ECO:0007829|PDB:7VFS"
FT   STRAND          150..152
FT                   /evidence="ECO:0007829|PDB:7VFS"
FT   TURN            153..156
FT                   /evidence="ECO:0007829|PDB:7VFS"
FT   STRAND          157..163
FT                   /evidence="ECO:0007829|PDB:7VFS"
FT   STRAND          165..167
FT                   /evidence="ECO:0007829|PDB:7VFS"
FT   STRAND          170..172
FT                   /evidence="ECO:0007829|PDB:8IF4"
FT   STRAND          174..176
FT                   /evidence="ECO:0007829|PDB:8IF3"
FT   HELIX           177..185
FT                   /evidence="ECO:0007829|PDB:7VFS"
FT   HELIX           187..198
FT                   /evidence="ECO:0007829|PDB:7VFS"
FT   STRAND          206..210
FT                   /evidence="ECO:0007829|PDB:7VFS"
FT   STRAND          215..220
FT                   /evidence="ECO:0007829|PDB:7VFS"
FT   STRAND          227..229
FT                   /evidence="ECO:0007829|PDB:7VFS"
FT   HELIX           238..240
FT                   /evidence="ECO:0007829|PDB:7VFS"
FT   HELIX           242..247
FT                   /evidence="ECO:0007829|PDB:7VFS"
FT   STRAND          253..258
FT                   /evidence="ECO:0007829|PDB:7VFS"
FT   HELIX           262..264
FT                   /evidence="ECO:0007829|PDB:7VFS"
FT   HELIX           267..280
FT                   /evidence="ECO:0007829|PDB:7VFS"
FT   STRAND          288..303
FT                   /evidence="ECO:0007829|PDB:7VFS"
FT   HELIX           312..323
FT                   /evidence="ECO:0007829|PDB:7VFS"
FT   HELIX           333..344
FT                   /evidence="ECO:0007829|PDB:7VFS"
FT   STRAND          356..362
FT                   /evidence="ECO:0007829|PDB:7VFS"
FT   HELIX           370..376
FT                   /evidence="ECO:0007829|PDB:7VFS"
FT   STRAND          377..379
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   STRAND          382..391
FT                   /evidence="ECO:0007829|PDB:7VFS"
FT   HELIX           397..404
FT                   /evidence="ECO:0007829|PDB:7VFS"
FT   TURN            405..407
FT                   /evidence="ECO:0007829|PDB:7VFS"
FT   STRAND          409..413
FT                   /evidence="ECO:0007829|PDB:7VFS"
FT   HELIX           416..418
FT                   /evidence="ECO:0007829|PDB:7MIX"
FT   HELIX           419..430
FT                   /evidence="ECO:0007829|PDB:7VFS"
FT   HELIX           432..436
FT                   /evidence="ECO:0007829|PDB:7VFS"
FT   TURN            438..440
FT                   /evidence="ECO:0007829|PDB:7VFS"
FT   STRAND          453..455
FT                   /evidence="ECO:0007829|PDB:7VFS"
FT   STRAND          457..467
FT                   /evidence="ECO:0007829|PDB:7VFS"
FT   STRAND          470..474
FT                   /evidence="ECO:0007829|PDB:7VFS"
FT   HELIX           480..482
FT                   /evidence="ECO:0007829|PDB:8IF4"
FT   STRAND          483..493
FT                   /evidence="ECO:0007829|PDB:7VFS"
FT   HELIX           494..498
FT                   /evidence="ECO:0007829|PDB:7VFS"
FT   STRAND          504..506
FT                   /evidence="ECO:0007829|PDB:7UHF"
FT   STRAND          511..515
FT                   /evidence="ECO:0007829|PDB:7VFS"
FT   STRAND          517..520
FT                   /evidence="ECO:0007829|PDB:7VFS"
FT   HELIX           561..564
FT                   /evidence="ECO:0007829|PDB:7VFS"
FT   HELIX           570..579
FT                   /evidence="ECO:0007829|PDB:7VFS"
FT   STRAND          584..593
FT                   /evidence="ECO:0007829|PDB:7VFS"
FT   STRAND          600..611
FT                   /evidence="ECO:0007829|PDB:7VFS"
FT   STRAND          613..616
FT                   /evidence="ECO:0007829|PDB:7MIX"
FT   STRAND          618..624
FT                   /evidence="ECO:0007829|PDB:7VFS"
FT   HELIX           625..627
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   STRAND          628..633
FT                   /evidence="ECO:0007829|PDB:7VFS"
FT   STRAND          637..639
FT                   /evidence="ECO:0007829|PDB:7VFS"
FT   HELIX           640..646
FT                   /evidence="ECO:0007829|PDB:7VFS"
FT   HELIX           650..652
FT                   /evidence="ECO:0007829|PDB:7MIX"
FT   TURN            653..655
FT                   /evidence="ECO:0007829|PDB:7VFS"
FT   STRAND          658..661
FT                   /evidence="ECO:0007829|PDB:7MIX"
FT   STRAND          667..670
FT                   /evidence="ECO:0007829|PDB:7MIX"
FT   HELIX           676..688
FT                   /evidence="ECO:0007829|PDB:7VFS"
FT   TURN            694..696
FT                   /evidence="ECO:0007829|PDB:7VFS"
FT   HELIX           699..716
FT                   /evidence="ECO:0007829|PDB:7VFS"
FT   TURN            717..723
FT                   /evidence="ECO:0007829|PDB:7VFS"
FT   STRAND          727..736
FT                   /evidence="ECO:0007829|PDB:7VFS"
FT   STRAND          739..741
FT                   /evidence="ECO:0007829|PDB:8IF4"
FT   STRAND          743..748
FT                   /evidence="ECO:0007829|PDB:7VFS"
FT   TURN            749..751
FT                   /evidence="ECO:0007829|PDB:7VFS"
FT   HELIX           758..760
FT                   /evidence="ECO:0007829|PDB:7VFS"
FT   HELIX           762..769
FT                   /evidence="ECO:0007829|PDB:7VFS"
FT   STRAND          771..776
FT                   /evidence="ECO:0007829|PDB:7VFS"
FT   STRAND          780..785
FT                   /evidence="ECO:0007829|PDB:7MIX"
FT   TURN            788..790
FT                   /evidence="ECO:0007829|PDB:7VFS"
FT   STRAND          792..797
FT                   /evidence="ECO:0007829|PDB:7VFS"
FT   STRAND          800..804
FT                   /evidence="ECO:0007829|PDB:7MIX"
FT   STRAND          805..807
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   STRAND          810..816
FT                   /evidence="ECO:0007829|PDB:7VFS"
FT   HELIX           818..827
FT                   /evidence="ECO:0007829|PDB:7VFS"
FT   HELIX           828..830
FT                   /evidence="ECO:0007829|PDB:7VFS"
FT   STRAND          851..853
FT                   /evidence="ECO:0007829|PDB:7VFS"
FT   HELIX           855..857
FT                   /evidence="ECO:0007829|PDB:7VFS"
FT   STRAND          858..866
FT                   /evidence="ECO:0007829|PDB:7VFS"
FT   HELIX           868..870
FT                   /evidence="ECO:0007829|PDB:7VFS"
FT   HELIX           875..878
FT                   /evidence="ECO:0007829|PDB:7VFS"
FT   HELIX           880..888
FT                   /evidence="ECO:0007829|PDB:7VFS"
FT   STRAND          891..904
FT                   /evidence="ECO:0007829|PDB:7VFS"
FT   STRAND          972..983
FT                   /evidence="ECO:0007829|PDB:7VFS"
FT   STRAND          989..994
FT                   /evidence="ECO:0007829|PDB:7VFS"
FT   STRAND          997..999
FT                   /evidence="ECO:0007829|PDB:7UHG"
FT   STRAND          1001..1007
FT                   /evidence="ECO:0007829|PDB:7VFS"
FT   STRAND          1014..1016
FT                   /evidence="ECO:0007829|PDB:7VFS"
FT   TURN            1021..1023
FT                   /evidence="ECO:0007829|PDB:7MIX"
FT   STRAND          1036..1038
FT                   /evidence="ECO:0007829|PDB:7MIX"
FT   HELIX           1043..1046
FT                   /evidence="ECO:0007829|PDB:7VFS"
FT   STRAND          1047..1049
FT                   /evidence="ECO:0007829|PDB:7VFS"
FT   TURN            1072..1074
FT                   /evidence="ECO:0007829|PDB:7MIX"
SQ   SEQUENCE   1103 AA;  124568 MW;  0749685DE9DB0700 CRC64;
     MAAGCLLALT LTLFQSLLIG PSSEEPFPSA VTIKSWVDKM QEDLVTLAKT ASGVNQLVDI
     YEKYQDLYTV EPNNARQLVE IAARDIEKLL SNRSKALVRL ALEAEKVQAA HQWREDFASN
     EVVYYNAKDD LDPEKNDSEP GSQRIKPVFI EDANFGRQIS YQHAAVHIPT DIYEGSTIVL
     NELNWTSALD EVFKKNREED PSLLWQVFGS ATGLARYYPA SPWVDNSRTP NKIDLYDVRR
     RPWYIQGAAS PKDMLILVDV SGSVSGLTLK LIRTSVSEML ETLSDDDFVN VASFNSNAQD
     VSCFQHLVQA NVRNKKVLKD AVNNITAKGI TDYKKGFSFA FEQLLNYNVS RANCNKIIML
     FTDGGEERAQ EIFNKYNKDK KVRVFTFSVG QHNYDRGPIQ WMACENKGYY YEIPSIGAIR
     INTQEYLDVL GRPMVLAGDK AKQVQWTNVY LDALELGLVI TGTLPVFNIT GQFENKTNLK
     NQLILGVMGV DVSLEDIKRL TPRFTLCPNG YYFAIDPNGY VLLHPNLQPK PIGVGIPTIN
     LRKRRPNIQN PKSQEPVTLD FLDAELENDI KVEIRNKMID GESGEKTFRT LVKSQDERYI
     DKGNRTYTWT PVNGTDYSLA LVLPTYSFYY IKAKLEETIT QARYSETLKP DNFEESGYTF
     IAPRDYCNDL KISDNNTEFL LNFNEFIDRK TPNNPSCNAD LINRVLLDAG FTNELVQNYW
     SKQKNIKGVK ARFVVTDGGI TRVYPKEAGE NWQENPETYE DSFYKRSLDN DNYVFTAPYF
     NKSGPGAYES GIMVSKAVEI YIQGKLLKPA VVGIKIDVNS WIENFTKTSI RDPCAGPVCD
     CKRNSDVMDC VILDDGGFLL MANHDDYTNQ IGRFFGEIDP SLMRHLVNIS VYAFNKSYDY
     QSVCEPGAAP KQGAGHRSAY VPSVADILQI GWWATAAAWS ILQQFLLSLT FPRLLEAVEM
     EDDDFTASLS KQSCITEQTQ YFFDNDSKSF SGVLDCGNCS RIFHGEKLMN TNLIFIMVES
     KGTCPCDTRL LIQAEQTSDG PNPCDMVKQP RYRKGPDVCF DNNVLEDYTD CGGVSGLNPS
     LWYIIGIQFL LLWLVSGSTH RLL
//