ID   CAC1E_HUMAN             Reviewed;        2313 AA.
AC   Q15878; B1AM12; B1AM13; B1AM14; Q14580; Q14581;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 3.
DT   27-MAR-2024, entry version 209.
DE   RecName: Full=Voltage-dependent R-type calcium channel subunit alpha-1E;
DE   AltName: Full=Brain calcium channel II;
DE            Short=BII;
DE   AltName: Full=Calcium channel, L type, alpha-1 polypeptide, isoform 6;
DE   AltName: Full=Voltage-gated calcium channel subunit alpha Cav2.3;
GN   Name=CACNA1E; Synonyms=CACH6, CACNL1A6;
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 1), AND VARIANT THR-1955.
RC   TISSUE=Brain;
RX   PubMed=7536609;
RA   Schneider T., Wei X., Olcese R., Costantin J.L., Neely A., Palade P.,
RA   Perez-Reyes E., Qin N., Zhou J., Crawford G.D., Smith R.G., Appel S.H.,
RA   Stefani E., Birnbaumer M.;
RT   "Molecular analysis and functional expression of the human type E neuronal
RT   Ca2+ channel alpha 1 subunit.";
RL   Recept. Channels 2:255-270(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3).
RC   TISSUE=Hippocampus;
RX   PubMed=8071363; DOI=10.1016/s0021-9258(17)31796-9;
RA   Williams M.E., Marubio L.M., Deal C.R., Hans M., Brust P.F.,
RA   Philipson L.H., Miller R.J., Johnson E.C., Harpold M.M., Ellis S.B.;
RT   "Structure and functional characterization of neuronal alpha 1E calcium
RT   channel subtypes.";
RL   J. Biol. Chem. 269:22347-22357(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [4]
RP   INTERACTION WITH EFHC1.
RX   PubMed=15258581; DOI=10.1038/ng1393;
RA   Suzuki T., Delgado-Escueta A.V., Aguan K., Alonso M.E., Shi J., Hara Y.,
RA   Nishida M., Numata T., Medina M.T., Takeuchi T., Morita R., Bai D.,
RA   Ganesh S., Sugimoto Y., Inazawa J., Bailey J.N., Ochoa A., Jara-Prado A.,
RA   Rasmussen A., Ramos-Peek J., Cordova S., Rubio-Donnadieu F., Inoue Y.,
RA   Osawa M., Kaneko S., Oguni H., Mori Y., Yamakawa K.;
RT   "Mutations in EFHC1 cause juvenile myoclonic epilepsy.";
RL   Nat. Genet. 36:842-849(2004).
RN   [5]
RP   FUNCTION, INVOLVEMENT IN DEE69, VARIANTS DEE69 PRO-228; ARG-348; ARG-352;
RP   LEU-603; ASP-690; SER-698; THR-700; VAL-701; PRO-702; THR-702;
RP   829-ARG--CYS-2313 DEL; 1389-ARG--CYS-2313 DEL; PHE-1422; ASN-1425; ARG-1430
RP   AND GLY-1720, AND CHARACTERIZATION OF VARIANTS DEE69 LEU-603; SER-698;
RP   VAL-701 AND THR-702.
RX   PubMed=30343943; DOI=10.1016/j.ajhg.2018.09.006;
RG   Task Force for Neonatal Genomics;
RG   Deciphering Developmental Disorders Study;
RA   Helbig K.L., Lauerer R.J., Bahr J.C., Souza I.A., Myers C.T., Uysal B.,
RA   Schwarz N., Gandini M.A., Huang S., Keren B., Mignot C., Afenjar A.,
RA   Billette de Villemeur T., Heron D., Nava C., Valence S., Buratti J.,
RA   Fagerberg C.R., Soerensen K.P., Kibaek M., Kamsteeg E.J., Koolen D.A.,
RA   Gunning B., Schelhaas H.J., Kruer M.C., Fox J., Bakhtiari S., Jarrar R.,
RA   Padilla-Lopez S., Lindstrom K., Jin S.C., Zeng X., Bilguvar K.,
RA   Papavasileiou A., Xing Q., Zhu C., Boysen K., Vairo F., Lanpher B.C.,
RA   Klee E.W., Tillema J.M., Payne E.T., Cousin M.A., Kruisselbrink T.M.,
RA   Wick M.J., Baker J., Haan E., Smith N., Sadeghpour A., Davis E.E.,
RA   Katsanis N., Corbett M.A., MacLennan A.H., Gecz J., Biskup S., Goldmann E.,
RA   Rodan L.H., Kichula E., Segal E., Jackson K.E., Asamoah A., Dimmock D.,
RA   McCarrier J., Botto L.D., Filloux F., Tvrdik T., Cascino G.D.,
RA   Klingerman S., Neumann C., Wang R., Jacobsen J.C., Nolan M.A., Snell R.G.,
RA   Lehnert K., Sadleir L.G., Anderlid B.M., Kvarnung M., Guerrini R.,
RA   Friez M.J., Lyons M.J., Leonhard J., Kringlen G., Casas K., El Achkar C.M.,
RA   Smith L.A., Rotenberg A., Poduri A., Sanchis-Juan A., Carss K.J.,
RA   Rankin J., Zeman A., Raymond F.L., Blyth M., Kerr B., Ruiz K., Urquhart J.,
RA   Hughes I., Banka S., Hedrich U.B.S., Scheffer I.E., Helbig I.,
RA   Zamponi G.W., Lerche H., Mefford H.C.;
RT   "De novo pathogenic variants in CACNA1E cause developmental and epileptic
RT   encephalopathy with contractures, macrocephaly, and dyskinesias.";
RL   Am. J. Hum. Genet. 103:666-678(2018).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1867-1885.
RX   PubMed=18400181; DOI=10.1016/j.str.2008.01.011;
RA   Mori M.X., Vander Kooi C.W., Leahy D.J., Yue D.T.;
RT   "Crystal structure of the CaV2 IQ domain in complex with Ca2+/calmodulin:
RT   high-resolution mechanistic implications for channel regulation by Ca2+.";
RL   Structure 16:607-620(2008).
CC   -!- FUNCTION: Voltage-sensitive calcium channels (VSCC) mediate the entry
CC       of calcium ions into excitable cells (PubMed:30343943). They are also
CC       involved in a variety of calcium-dependent processes, including muscle
CC       contraction, hormone or neurotransmitter release, gene expression, cell
CC       motility, cell division and cell death. The isoform alpha-1E gives rise
CC       to R-type calcium currents. R-type calcium channels belong to the
CC       'high-voltage activated' (HVA) group and are blocked by nickel. They
CC       are however insensitive to dihydropyridines (DHP). Calcium channels
CC       containing alpha-1E subunit could be involved in the modulation of
CC       firing patterns of neurons which is important for information
CC       processing. {ECO:0000269|PubMed:30343943}.
CC   -!- SUBUNIT: Interacts with EFHC1. Voltage-dependent calcium channels are
CC       multisubunit complexes, consisting of alpha-1, alpha-2, beta and delta
CC       subunits in a 1:1:1:1 ratio. The channel activity is directed by the
CC       pore-forming and voltage-sensitive alpha-1 subunit. In many cases, this
CC       subunit is sufficient to generate voltage-sensitive calcium channel
CC       activity. The auxiliary subunits beta and alpha-2/delta linked by a
CC       disulfide bridge regulate the channel activity.
CC       {ECO:0000269|PubMed:15258581}.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1; Synonyms=Alpha-1E;
CC         IsoId=Q15878-1; Sequence=Displayed;
CC       Name=2; Synonyms=Alpha-1E-1;
CC         IsoId=Q15878-2; Sequence=VSP_000937, VSP_024817;
CC       Name=3; Synonyms=Alpha-1E-3;
CC         IsoId=Q15878-3; Sequence=VSP_024817;
CC   -!- TISSUE SPECIFICITY: Expressed in neuronal tissues and in kidney.
CC   -!- DOMAIN: Each of the four internal repeats contains five hydrophobic
CC       transmembrane segments (S1, S2, S3, S5, S6) and one positively charged
CC       transmembrane segment (S4). S4 segments probably represent the voltage-
CC       sensor and are characterized by a series of positively charged amino
CC       acids at every third position.
CC   -!- DISEASE: Developmental and epileptic encephalopathy 69 (DEE69)
CC       [MIM:618285]: A form of epileptic encephalopathy, a heterogeneous group
CC       of severe 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. DEE69 is an autosomal dominant form characterized by
CC       refractory seizures, hypotonia, and profoundly impaired development
CC       often associated with macrocephaly, hyperkinetic movements, and
CC       contractures. The disorder can sometimes result in early death. Some
CC       patients may have a favorable seizure response to topiramate
CC       medication. {ECO:0000269|PubMed:30343943}. Note=The disease is caused
CC       by variants affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the calcium channel alpha-1 subunit
CC       (TC 1.A.1.11) family. CACNA1E subfamily. {ECO:0000305}.
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DR   EMBL; L27745; AAA72125.1; -; mRNA.
DR   EMBL; L29384; AAA59204.1; -; mRNA.
DR   EMBL; L29385; AAA59205.1; -; mRNA.
DR   EMBL; AL161734; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL359270; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL160059; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL590998; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS53443.1; -. [Q15878-3]
DR   CCDS; CCDS55664.1; -. [Q15878-1]
DR   CCDS; CCDS55665.1; -. [Q15878-2]
DR   PIR; A54972; A54972.
DR   PIR; B54972; B54972.
DR   RefSeq; NP_000712.2; NM_000721.3. [Q15878-3]
DR   RefSeq; NP_001192222.1; NM_001205293.1. [Q15878-1]
DR   RefSeq; NP_001192223.1; NM_001205294.1. [Q15878-2]
DR   PDB; 3BXL; X-ray; 2.30 A; B=1867-1887.
DR   PDB; 7XLQ; EM; 3.10 A; A=1-2313.
DR   PDB; 7YG5; EM; 3.00 A; A=1-2313.
DR   PDB; 8EPL; EM; 3.10 A; A=1-2313.
DR   PDB; 8EPM; EM; 3.10 A; A=1-2313.
DR   PDBsum; 3BXL; -.
DR   PDBsum; 7XLQ; -.
DR   PDBsum; 7YG5; -.
DR   PDBsum; 8EPL; -.
DR   PDBsum; 8EPM; -.
DR   AlphaFoldDB; Q15878; -.
DR   EMDB; EMD-28529; -.
DR   EMDB; EMD-28530; -.
DR   EMDB; EMD-33285; -.
DR   EMDB; EMD-33808; -.
DR   SMR; Q15878; -.
DR   BioGRID; 107231; 4.
DR   IntAct; Q15878; 1.
DR   STRING; 9606.ENSP00000356545; -.
DR   BindingDB; Q15878; -.
DR   ChEMBL; CHEMBL1687682; -.
DR   DrugBank; DB13746; Bioallethrin.
DR   DrugBank; DB11148; Butamben.
DR   DrugBank; DB11093; Calcium citrate.
DR   DrugBank; DB11348; Calcium Phosphate.
DR   DrugBank; DB14481; Calcium phosphate dihydrate.
DR   DrugBank; DB09235; Efonidipine.
DR   DrugBank; DB00228; Enflurane.
DR   DrugBank; DB00153; Ergocalciferol.
DR   DrugBank; DB00555; Lamotrigine.
DR   DrugBank; DB00622; Nicardipine.
DR   DrugBank; DB00421; Spironolactone.
DR   DrugBank; DB00273; Topiramate.
DR   DrugBank; DB00661; Verapamil.
DR   GuidetoPHARMACOLOGY; 534; -.
DR   GlyCosmos; Q15878; 3 sites, No reported glycans.
DR   GlyGen; Q15878; 3 sites.
DR   iPTMnet; Q15878; -.
DR   PhosphoSitePlus; Q15878; -.
DR   BioMuta; CACNA1E; -.
DR   DMDM; 209572758; -.
DR   EPD; Q15878; -.
DR   jPOST; Q15878; -.
DR   MassIVE; Q15878; -.
DR   MaxQB; Q15878; -.
DR   PaxDb; 9606-ENSP00000356545; -.
DR   PeptideAtlas; Q15878; -.
DR   ProteomicsDB; 60800; -. [Q15878-1]
DR   ProteomicsDB; 60801; -. [Q15878-2]
DR   ProteomicsDB; 60802; -. [Q15878-3]
DR   Antibodypedia; 34433; 143 antibodies from 20 providers.
DR   DNASU; 777; -.
DR   Ensembl; ENST00000367570.6; ENSP00000356542.1; ENSG00000198216.14. [Q15878-3]
DR   Ensembl; ENST00000367573.7; ENSP00000356545.2; ENSG00000198216.14. [Q15878-1]
DR   Ensembl; ENST00000621791.4; ENSP00000481619.1; ENSG00000198216.14. [Q15878-2]
DR   GeneID; 777; -.
DR   KEGG; hsa:777; -.
DR   MANE-Select; ENST00000367573.7; ENSP00000356545.2; NM_001205293.3; NP_001192222.1.
DR   UCSC; uc001gow.5; human. [Q15878-1]
DR   AGR; HGNC:1392; -.
DR   CTD; 777; -.
DR   DisGeNET; 777; -.
DR   GeneCards; CACNA1E; -.
DR   HGNC; HGNC:1392; CACNA1E.
DR   HPA; ENSG00000198216; Tissue enriched (brain).
DR   MalaCards; CACNA1E; -.
DR   MIM; 601013; gene.
DR   MIM; 618285; phenotype.
DR   neXtProt; NX_Q15878; -.
DR   OpenTargets; ENSG00000198216; -.
DR   PharmGKB; PA26009; -.
DR   VEuPathDB; HostDB:ENSG00000198216; -.
DR   eggNOG; KOG2301; Eukaryota.
DR   GeneTree; ENSGT00940000155601; -.
DR   HOGENOM; CLU_000540_1_0_1; -.
DR   InParanoid; Q15878; -.
DR   OMA; XRERRRR; -.
DR   OrthoDB; 1110761at2759; -.
DR   PhylomeDB; Q15878; -.
DR   TreeFam; TF312805; -.
DR   PathwayCommons; Q15878; -.
DR   Reactome; R-HSA-112308; Presynaptic depolarization and calcium channel opening.
DR   Reactome; R-HSA-422356; Regulation of insulin secretion.
DR   SignaLink; Q15878; -.
DR   SIGNOR; Q15878; -.
DR   BioGRID-ORCS; 777; 11 hits in 1138 CRISPR screens.
DR   ChiTaRS; CACNA1E; human.
DR   EvolutionaryTrace; Q15878; -.
DR   GeneWiki; R-type_calcium_channel; -.
DR   GenomeRNAi; 777; -.
DR   Pharos; Q15878; Tchem.
DR   PRO; PR:Q15878; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; Q15878; Protein.
DR   Bgee; ENSG00000198216; Expressed in middle temporal gyrus and 119 other cell types or tissues.
DR   ExpressionAtlas; Q15878; baseline and differential.
DR   GO; GO:0043025; C:neuronal cell body; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0045202; C:synapse; IEA:GOC.
DR   GO; GO:0005891; C:voltage-gated calcium channel complex; IBA:GO_Central.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0008331; F:high voltage-gated calcium channel activity; IBA:GO_Central.
DR   GO; GO:0005245; F:voltage-gated calcium channel activity; IDA:MGI.
DR   GO; GO:0022843; F:voltage-gated monoatomic cation channel activity; IDA:UniProtKB.
DR   GO; GO:0098703; P:calcium ion import across plasma membrane; IBA:GO_Central.
DR   GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
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; 4.
DR   InterPro; IPR002048; EF_hand_dom.
DR   InterPro; IPR031649; GPHH_dom.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR014873; VDCC_a1su_IQ.
DR   InterPro; IPR005449; VDCC_R_a1su.
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:SF5; VOLTAGE-DEPENDENT R-TYPE CALCIUM CHANNEL SUBUNIT ALPHA-1E; 1.
DR   Pfam; PF08763; Ca_chan_IQ; 1.
DR   Pfam; PF16905; GPHH; 1.
DR   Pfam; PF00520; Ion_trans; 4.
DR   PRINTS; PR00167; CACHANNEL.
DR   PRINTS; PR01633; RVDCCALPHA1.
DR   SMART; SM01062; Ca_chan_IQ; 1.
DR   SUPFAM; SSF81324; Voltage-gated potassium channels; 4.
DR   PROSITE; PS50222; EF_HAND_2; 1.
DR   Genevisible; Q15878; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Calcium; Calcium channel;
KW   Calcium transport; Disease variant; Disulfide bond; Epilepsy; Glycoprotein;
KW   Ion channel; Ion transport; Membrane; Metal-binding; Phosphoprotein;
KW   Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport;
KW   Voltage-gated channel.
FT   CHAIN           1..2313
FT                   /note="Voltage-dependent R-type calcium channel subunit
FT                   alpha-1E"
FT                   /id="PRO_0000053938"
FT   TOPO_DOM        1..89
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        90..108
FT                   /note="Helical; Name=S1 of repeat I"
FT   TOPO_DOM        109..127
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        128..146
FT                   /note="Helical; Name=S2 of repeat I"
FT   TOPO_DOM        147..158
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        159..173
FT                   /note="Helical; Name=S3 of repeat I"
FT   TOPO_DOM        174..185
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        186..205
FT                   /note="Helical; Name=S4 of repeat I"
FT   TOPO_DOM        206..223
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        224..244
FT                   /note="Helical; Name=S5 of repeat I"
FT   TOPO_DOM        245..326
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        327..350
FT                   /note="Helical; Name=S6 of repeat I"
FT   TOPO_DOM        351..476
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        477..496
FT                   /note="Helical; Name=S1 of repeat II"
FT   TOPO_DOM        497..509
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        510..529
FT                   /note="Helical; Name=S2 of repeat II"
FT   TOPO_DOM        530..538
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        539..557
FT                   /note="Helical; Name=S3 of repeat II"
FT   TOPO_DOM        558..567
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        568..586
FT                   /note="Helical; Name=S4 of repeat II"
FT   TOPO_DOM        587..605
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        606..625
FT                   /note="Helical; Name=S5 of repeat II"
FT   TOPO_DOM        626..678
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        679..703
FT                   /note="Helical; Name=S6 of repeat II"
FT   TOPO_DOM        704..1148
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1149..1165
FT                   /note="Helical; Name=S1 of repeat III"
FT   TOPO_DOM        1166..1189
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1190..1209
FT                   /note="Helical; Name=S2 of repeat III"
FT   TOPO_DOM        1210..1217
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1218..1240
FT                   /note="Helical; Name=S3 of repeat III"
FT   TOPO_DOM        1241..1254
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1255..1272
FT                   /note="Helical; Name=S4 of repeat III"
FT   TOPO_DOM        1273..1291
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1292..1311
FT                   /note="Helical; Name=S5 of repeat III"
FT   TOPO_DOM        1312..1398
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1399..1422
FT                   /note="Helical; Name=S6 of repeat III"
FT   TOPO_DOM        1423..1479
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1480..1498
FT                   /note="Helical; Name=S1 of repeat IV"
FT   TOPO_DOM        1499..1513
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1514..1533
FT                   /note="Helical; Name=S2 of repeat IV"
FT   TOPO_DOM        1534..1541
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1542..1560
FT                   /note="Helical; Name=S3 of repeat IV"
FT   TOPO_DOM        1561..1571
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1572..1590
FT                   /note="Helical; Name=S4 of repeat IV"
FT   TOPO_DOM        1591..1609
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1610..1629
FT                   /note="Helical; Name=S5 of repeat IV"
FT   TOPO_DOM        1630..1698
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1699..1724
FT                   /note="Helical; Name=S6 of repeat IV"
FT   TOPO_DOM        1725..2313
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REPEAT          76..354
FT                   /note="I"
FT   REPEAT          462..706
FT                   /note="II"
FT   REPEAT          1140..1426
FT                   /note="III"
FT   REPEAT          1463..1726
FT                   /note="IV"
FT   DOMAIN          1739..1774
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   REGION          1..38
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          374..391
FT                   /note="Binding to the beta subunit"
FT                   /evidence="ECO:0000250"
FT   REGION          729..774
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          851..984
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1103..1125
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1970..2170
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2206..2225
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2263..2295
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        17..31
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        745..765
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        950..982
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1970..1996
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2005..2019
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2020..2034
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2065..2122
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2123..2156
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         426
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000305"
FT   BINDING         428
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000305"
FT   BINDING         430
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000305"
FT   BINDING         432
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000305"
FT   BINDING         1752
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000305"
FT   BINDING         1758
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000305"
FT   BINDING         1763
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000305"
FT   SITE            309
FT                   /note="Calcium ion selectivity and permeability"
FT                   /evidence="ECO:0000250"
FT   SITE            657
FT                   /note="Calcium ion selectivity and permeability"
FT                   /evidence="ECO:0000250"
FT   SITE            1372
FT                   /note="Calcium ion selectivity and permeability"
FT                   /evidence="ECO:0000250"
FT   SITE            1663
FT                   /note="Calcium ion selectivity and permeability"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         14
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q61290"
FT   MOD_RES         19
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q61290"
FT   MOD_RES         427
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q61290"
FT   MOD_RES         440
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q61290"
FT   MOD_RES         736
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q07652"
FT   MOD_RES         745
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q61290"
FT   MOD_RES         793
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q07652"
FT   MOD_RES         815
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q61290"
FT   MOD_RES         855
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q61290"
FT   MOD_RES         947
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q07652"
FT   MOD_RES         1097
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q07652"
FT   MOD_RES         2094
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q61290"
FT   MOD_RES         2113
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q07652"
FT   CARBOHYD        254
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1566
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1571
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         748..766
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:8071363"
FT                   /id="VSP_000937"
FT   VAR_SEQ         1967..2009
FT                   /note="Missing (in isoform 2 and isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:8071363"
FT                   /id="VSP_024817"
FT   VARIANT         228
FT                   /note="L -> P (in DEE69; dbSNP:rs1553286282)"
FT                   /evidence="ECO:0000269|PubMed:30343943"
FT                   /id="VAR_081838"
FT   VARIANT         348
FT                   /note="G -> R (in DEE69)"
FT                   /evidence="ECO:0000269|PubMed:30343943"
FT                   /id="VAR_081839"
FT   VARIANT         352
FT                   /note="G -> R (in DEE69; dbSNP:rs886039323)"
FT                   /evidence="ECO:0000269|PubMed:30343943"
FT                   /id="VAR_081840"
FT   VARIANT         603
FT                   /note="I -> L (in DEE69; gain-of-function variant affecting
FT                   channel activity; results in hyperpolarizing shift in half
FT                   activation voltage; dbSNP:rs778291283)"
FT                   /evidence="ECO:0000269|PubMed:30343943"
FT                   /id="VAR_081841"
FT   VARIANT         690
FT                   /note="G -> D (in DEE69; dbSNP:rs1361083258)"
FT                   /evidence="ECO:0000269|PubMed:30343943"
FT                   /id="VAR_081842"
FT   VARIANT         698
FT                   /note="F -> S (in DEE69; gain-of-function variant affecting
FT                   channel activity; shifts the voltage dependence of
FT                   activation toward more negative potentials and slows the
FT                   fast inactivation time course; dbSNP:rs869312920)"
FT                   /evidence="ECO:0000269|PubMed:30343943"
FT                   /id="VAR_081843"
FT   VARIANT         700
FT                   /note="A -> T (in DEE69)"
FT                   /evidence="ECO:0000269|PubMed:30343943"
FT                   /id="VAR_081844"
FT   VARIANT         701
FT                   /note="I -> V (in DEE69; gain-of-function variant affecting
FT                   channel activity; shifts the voltage dependence of
FT                   activation toward more negative potentials and slows the
FT                   fast inactivation time course; dbSNP:rs1558308998)"
FT                   /evidence="ECO:0000269|PubMed:30343943"
FT                   /id="VAR_081845"
FT   VARIANT         702
FT                   /note="A -> P (in DEE69; dbSNP:rs12131800)"
FT                   /evidence="ECO:0000269|PubMed:30343943"
FT                   /id="VAR_081846"
FT   VARIANT         702
FT                   /note="A -> T (in DEE69; gain-of-function variant affecting
FT                   channel activity; shifts the voltage dependence of
FT                   activation toward more negative potentials and slows the
FT                   fast inactivation time course; dbSNP:rs12131800)"
FT                   /evidence="ECO:0000269|PubMed:30343943"
FT                   /id="VAR_081847"
FT   VARIANT         829..2313
FT                   /note="Missing (in DEE69; uncertain significance)"
FT                   /evidence="ECO:0000269|PubMed:30343943"
FT                   /id="VAR_081848"
FT   VARIANT         859
FT                   /note="D -> E (in dbSNP:rs35737760)"
FT                   /id="VAR_031912"
FT   VARIANT         1389..2313
FT                   /note="Missing (in DEE69; uncertain significance)"
FT                   /evidence="ECO:0000269|PubMed:30343943"
FT                   /id="VAR_081849"
FT   VARIANT         1422
FT                   /note="I -> F (in DEE69)"
FT                   /evidence="ECO:0000269|PubMed:30343943"
FT                   /id="VAR_081850"
FT   VARIANT         1425
FT                   /note="T -> N (in DEE69)"
FT                   /evidence="ECO:0000269|PubMed:30343943"
FT                   /id="VAR_081851"
FT   VARIANT         1430
FT                   /note="G -> R (in DEE69; dbSNP:rs1553345844)"
FT                   /evidence="ECO:0000269|PubMed:30343943"
FT                   /id="VAR_081852"
FT   VARIANT         1720
FT                   /note="A -> G (in DEE69)"
FT                   /evidence="ECO:0000269|PubMed:30343943"
FT                   /id="VAR_081853"
FT   VARIANT         1955
FT                   /note="A -> T (in dbSNP:rs704326)"
FT                   /evidence="ECO:0000269|PubMed:7536609"
FT                   /id="VAR_046996"
FT   CONFLICT        648
FT                   /note="M -> I (in Ref. 1; AAA72125)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        836..838
FT                   /note="LAL -> WP (in Ref. 1; AAA72125)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2077
FT                   /note="R -> P (in Ref. 2; AAA59204/AAA59205)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2084
FT                   /note="G -> R (in Ref. 2; AAA59204/AAA59205)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2206
FT                   /note="C -> W (in Ref. 2; AAA59204/AAA59205)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2219
FT                   /note="S -> R (in Ref. 2; AAA59204/AAA59205)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2245
FT                   /note="G -> V (in Ref. 2; AAA59204/AAA59205)"
FT                   /evidence="ECO:0000305"
FT   HELIX           84..86
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   HELIX           89..92
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   HELIX           95..108
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   STRAND          113..115
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   HELIX           119..124
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   HELIX           128..145
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   STRAND          146..151
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   HELIX           155..157
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   HELIX           159..174
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   TURN            177..182
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   STRAND          187..190
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   HELIX           193..195
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   HELIX           196..198
FT                   /evidence="ECO:0007829|PDB:8EPM"
FT   HELIX           199..203
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   HELIX           205..217
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   TURN            219..223
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   HELIX           224..243
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   STRAND          249..254
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   STRAND          256..258
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   STRAND          269..271
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   STRAND          274..281
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   TURN            285..288
FT                   /evidence="ECO:0007829|PDB:8EPM"
FT   STRAND          293..295
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   HELIX           298..306
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   HELIX           311..320
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   TURN            324..327
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   HELIX           328..338
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   HELIX           340..358
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   HELIX           361..385
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   HELIX           461..472
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   HELIX           476..482
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   TURN            483..488
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   HELIX           489..492
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   HELIX           502..525
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   TURN            526..530
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   STRAND          536..538
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   HELIX           539..559
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   HELIX           570..582
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   HELIX           586..598
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   TURN            601..603
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   HELIX           604..607
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   TURN            608..611
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   HELIX           612..625
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   STRAND          640..642
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   HELIX           643..654
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   TURN            655..658
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   HELIX           659..668
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   STRAND          671..674
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   HELIX           678..680
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   HELIX           682..688
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   TURN            689..692
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   HELIX           693..711
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   HELIX           714..720
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   TURN            721..723
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   HELIX           724..727
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   HELIX           777..784
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   HELIX           1145..1147
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   HELIX           1148..1151
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   HELIX           1155..1166
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   HELIX           1168..1171
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   STRAND          1178..1180
FT                   /evidence="ECO:0007829|PDB:8EPL"
FT   HELIX           1181..1206
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   HELIX           1223..1242
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   HELIX           1251..1257
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   HELIX           1258..1267
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   HELIX           1268..1271
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   TURN            1273..1275
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   HELIX           1276..1286
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   TURN            1287..1290
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   HELIX           1295..1306
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   HELIX           1308..1311
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   TURN            1312..1314
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   STRAND          1316..1320
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   TURN            1326..1328
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   STRAND          1331..1335
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   HELIX           1337..1339
FT                   /evidence="ECO:0007829|PDB:8EPL"
FT   STRAND          1342..1345
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   STRAND          1348..1350
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   HELIX           1358..1369
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   HELIX           1375..1382
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   TURN            1393..1396
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   HELIX           1397..1400
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   HELIX           1402..1409
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   TURN            1410..1412
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   HELIX           1413..1424
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   HELIX           1434..1437
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   HELIX           1442..1446
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   HELIX           1468..1475
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   STRAND          1476..1484
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   HELIX           1487..1490
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   TURN            1491..1496
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   HELIX           1506..1525
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   TURN            1526..1528
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   HELIX           1529..1532
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   HELIX           1534..1537
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   STRAND          1540..1543
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   HELIX           1544..1559
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   STRAND          1561..1564
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   STRAND          1568..1570
FT                   /evidence="ECO:0007829|PDB:8EPL"
FT   HELIX           1572..1575
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   HELIX           1576..1579
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   TURN            1580..1583
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   HELIX           1584..1589
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   HELIX           1593..1602
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   TURN            1603..1605
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   HELIX           1610..1629
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   STRAND          1638..1640
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   STRAND          1642..1644
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   STRAND          1646..1648
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   HELIX           1649..1660
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   HELIX           1667..1670
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   STRAND          1673..1675
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   STRAND          1682..1684
FT                   /evidence="ECO:0007829|PDB:8EPL"
FT   STRAND          1688..1690
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   HELIX           1699..1722
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   TURN            1723..1725
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   HELIX           1726..1729
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   STRAND          1733..1735
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   HELIX           1738..1740
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   HELIX           1742..1752
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   TURN            1753..1755
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   HELIX           1763..1770
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   TURN            1773..1775
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   HELIX           1784..1792
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   HELIX           1796..1798
FT                   /evidence="ECO:0007829|PDB:8EPL"
FT   HELIX           1805..1816
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   STRAND          1823..1825
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   HELIX           1826..1842
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   HELIX           1848..1854
FT                   /evidence="ECO:0007829|PDB:7XLQ"
FT   HELIX           1868..1882
FT                   /evidence="ECO:0007829|PDB:3BXL"
SQ   SEQUENCE   2313 AA;  261731 MW;  CCC7F309C27C42F1 CRC64;
     MARFGEAVVA RPGSGDGDSD QSRNRQGTPV PASGQAAAYK QTKAQRARTM ALYNPIPVRQ
     NCFTVNRSLF IFGEDNIVRK YAKKLIDWPP FEYMILATII ANCIVLALEQ HLPEDDKTPM
     SRRLEKTEPY FIGIFCFEAG IKIVALGFIF HKGSYLRNGW NVMDFIVVLS GILATAGTHF
     NTHVDLRTLR AVRVLRPLKL VSGIPSLQIV LKSIMKAMVP LLQIGLLLFF AILMFAIIGL
     EFYSGKLHRA CFMNNSGILE GFDPPHPCGV QGCPAGYECK DWIGPNDGIT QFDNILFAVL
     TVFQCITMEG WTTVLYNTND ALGATWNWLY FIPLIIIGSF FVLNLVLGVL SGEFAKERER
     VENRRAFMKL RRQQQIEREL NGYRAWIDKA EEVMLAEENK NAGTSALEVL RRATIKRSRT
     EAMTRDSSDE HCVDISSVGT PLARASIKSA KVDGVSYFRH KERLLRISIR HMVKSQVFYW
     IVLSLVALNT ACVAIVHHNQ PQWLTHLLYY AEFLFLGLFL LEMSLKMYGM GPRLYFHSSF
     NCFDFGVTVG SIFEVVWAIF RPGTSFGISV LRALRLLRIF KITKYWASLR NLVVSLMSSM
     KSIISLLFLL FLFIVVFALL GMQLFGGRFN FNDGTPSANF DTFPAAIMTV FQILTGEDWN
     EVMYNGIRSQ GGVSSGMWSA IYFIVLTLFG NYTLLNVFLA IAVDNLANAQ ELTKDEQEEE
     EAFNQKHALQ KAKEVSPMSA PNMPSIERDR RRRHHMSMWE PRSSHLRERR RRHHMSVWEQ
     RTSQLRKHMQ MSSQEALNRE EAPTMNPLNP LNPLSSLNPL NAHPSLYRRP RAIEGLALGL
     ALEKFEEERI SRGGSLKGDG GDRSSALDNQ RTPLSLGQRE PPWLARPCHG NCDPTQQEAG
     GGEAVVTFED RARHRQSQRR SRHRRVRTEG KESSSASRSR SASQERSLDE AMPTEGEKDH
     ELRGNHGAKE PTIQEERAQD LRRTNSLMVS RGSGLAGGLD EADTPLVLPH PELEVGKHVV
     LTEQEPEGSS EQALLGNVQL DMGRVISQSE PDLSCITANT DKATTESTSV TVAIPDVDPL
     VDSTVVHISN KTDGEASPLK EAEIREDEEE VEKKKQKKEK RETGKAMVPH SSMFIFSTTN
     PIRRACHYIV NLRYFEMCIL LVIAASSIAL AAEDPVLTNS ERNKVLRYFD YVFTGVFTFE
     MVIKMIDQGL ILQDGSYFRD LWNILDFVVV VGALVAFALA NALGTNKGRD IKTIKSLRVL
     RVLRPLKTIK RLPKLKAVFD CVVTSLKNVF NILIVYKLFM FIFAVIAVQL FKGKFFYCTD
     SSKDTEKECI GNYVDHEKNK MEVKGREWKR HEFHYDNIIW ALLTLFTVST GEGWPQVLQH
     SVDVTEEDRG PSRSNRMEMS IFYVVYFVVF PFFFVNIFVA LIIITFQEQG DKMMEECSLE
     KNERACIDFA ISAKPLTRYM PQNRHTFQYR VWHFVVSPSF EYTIMAMIAL NTVVLMMKYY
     SAPCTYELAL KYLNIAFTMV FSLECVLKVI AFGFLNYFRD TWNIFDFITV IGSITEIILT
     DSKLVNTSGF NMSFLKLFRA ARLIKLLRQG YTIRILLWTF VQSFKALPYV CLLIAMLFFI
     YAIIGMQVFG NIKLDEESHI NRHNNFRSFF GSLMLLFRSA TGEAWQEIML SCLGEKGCEP
     DTTAPSGQNE NERCGTDLAY VYFVSFIFFC SFLMLNLFVA VIMDNFEYLT RDSSILGPHH
     LDEFVRVWAE YDRAACGRIH YTEMYEMLTL MSPPLGLGKR CPSKVAYKRL VLMNMPVAED
     MTVHFTSTLM ALIRTALDIK IAKGGADRQQ LDSELQKETL AIWPHLSQKM LDLLVPMPKA
     SDLTVGKIYA AMMIMDYYKQ SKVKKQRQQL EEQKNAPMFQ RMEPSSLPQE IIANAKALPY
     LQQDPVSGLS GRSGYPSMSP LSPQDIFQLA CMDPADDGQF QERQSLEPEV SELKSVQPSN
     HGIYLPSDTQ EHAGSGRASS MPRLTVDPQV VTDPSSMRRS FSTIRDKRSN SSWLEEFSME
     RSSENTYKSR RRSYHSSLRL SAHRLNSDSG HKSDTHRSGG RERGRSKERK HLLSPDVSRC
     NSEERGTQAD WESPERRQSR SPSEGRSQTP NRQGTGSLSE SSIPSVSDTS TPRRSRRQLP
     PVPPKPRPLL SYSSLIRHAG SISPPADGSE EGSPLTSQAL ESNNACLTES SNSPHPQQSQ
     HASPQRYISE PYLALHEDSH ASDCGEEETL TFEAAVATSL GRSNTIGSAP PLRHSWQMPN
     GHYRRRRRGG PGPGMMCGAV NNLLSDTEED DKC
//