VDR_RAT
ID VDR_RAT Reviewed; 423 AA.
AC P13053;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Vitamin D3 receptor;
DE Short=VDR;
DE AltName: Full=1,25-dihydroxyvitamin D3 receptor;
DE AltName: Full=Nuclear receptor subfamily 1 group I member 1;
GN Name=Vdr; Synonyms=Nr1i1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=2849110; DOI=10.1073/pnas.85.24.9499;
RA Burmester J.K., Wiese R.J., Maeda N., Deluca H.;
RT "Structure and regulation of the rat 1,25-dihydroxyvitamin D3 receptor.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:9499-9502(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 58-423.
RC TISSUE=Kidney;
RX PubMed=2829212; DOI=10.1073/pnas.85.4.1005;
RA Burmester J.K., Maeda N., Deluca H.F.;
RT "Isolation and expression of rat 1,25-dihydroxyvitamin D3 receptor cDNA.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:1005-1009(1988).
RN [3]
RP INTERACTION WITH NCOA6.
RX PubMed=10866662; DOI=10.1128/mcb.20.14.5048-5063.2000;
RA Mahajan M.A., Samuels H.H.;
RT "A new family of nuclear receptor coregulators that integrates nuclear
RT receptor signaling through CBP.";
RL Mol. Cell. Biol. 20:5048-5063(2000).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 116-423 IN COMPLEXES WITH VITAMIN
RP D3 ANALOGS AND MED1.
RX PubMed=15065852; DOI=10.1021/bi036056y;
RA Vanhooke J.L., Benning M.M., Bauer C.B., Pike J.W., DeLuca H.F.;
RT "Molecular structure of the rat vitamin D receptor ligand binding domain
RT complexed with 2-carbon-substituted vitamin D3 hormone analogues and a
RT LXXLL-containing coactivator peptide.";
RL Biochemistry 43:4101-4110(2004).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS) OF 116-423 IN COMPLEXES WITH VITAMIN
RP D3 ANALOGS AND MED1, AND FUNCTION.
RX PubMed=17227670; DOI=10.1016/j.abb.2006.11.029;
RA Vanhooke J.L., Tadi B.P., Benning M.M., Plum L.A., DeLuca H.F.;
RT "New analogs of 2-methylene-19-nor-(20S)-1,25-dihydroxyvitamin D3 with
RT conformationally restricted side chains: evaluation of biological activity
RT and structural determination of VDR-bound conformations.";
RL Arch. Biochem. Biophys. 460:161-165(2007).
CC -!- FUNCTION: Nuclear receptor for calcitriol, the active form of vitamin
CC D3 which mediates the action of this vitamin on cells
CC (PubMed:17227670). Enters the nucleus upon vitamin D3 binding where it
CC forms heterodimers with the retinoid X receptor/RXR (By similarity).
CC The VDR-RXR heterodimers bind to specific response elements on DNA and
CC activate the transcription of vitamin D3-responsive target genes (By
CC similarity). Plays a central role in calcium homeostasis
CC (PubMed:17227670). {ECO:0000250|UniProtKB:P11473,
CC ECO:0000269|PubMed:17227670}.
CC -!- SUBUNIT: Homodimer in the absence of bound vitamin D3 (By similarity).
CC Heterodimer with RXRA after vitamin D3 binding (By similarity).
CC Interacts with MED1 and NCOA6 (PubMed:10866662, PubMed:15065852,
CC PubMed:17227670). Interacts with MED1, NCOA1, NCOA2, NCOA3 and NCOA6
CC coactivators, leading to a strong increase of transcription of target
CC genes (By similarity). Interacts with the corepressor NCOR1 (By
CC similarity). Interacts with SNW1 (By similarity). Interacts with IRX4,
CC the interaction does not affect its transactivation activity (By
CC similarity). Interacts with CRY1 (By similarity). Interacts with CRY2
CC in a ligand-dependent manner (By similarity).
CC {ECO:0000250|UniProtKB:P11473, ECO:0000250|UniProtKB:P48281,
CC ECO:0000269|PubMed:10866662, ECO:0000269|PubMed:15065852,
CC ECO:0000269|PubMed:17227670}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P11473,
CC ECO:0000255|PROSITE-ProRule:PRU00407}. Cytoplasm
CC {ECO:0000250|UniProtKB:P11473}. Note=Localizes mainly to the nucleus.
CC Translocated into the nucleus via both ligand-dependent and ligand-
CC independent pathways; ligand-independent nuclear translocation is
CC mediated by IPO4. {ECO:0000250|UniProtKB:P11473}.
CC -!- TISSUE SPECIFICITY: Detected in intestine and kidney.
CC {ECO:0000269|PubMed:2849110}.
CC -!- DOMAIN: Composed of three domains: a modulating N-terminal domain, a
CC DNA-binding domain and a C-terminal ligand-binding domain.
CC {ECO:0000250|UniProtKB:P11473}.
CC -!- DOMAIN: The 9aaTAD motif is a transactivation domain present in a large
CC number of yeast and animal transcription factors.
CC {ECO:0000250|UniProtKB:P11473}.
CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR1
CC subfamily. {ECO:0000305}.
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DR EMBL; J04147; AAA41089.1; -; mRNA.
DR PIR; A31761; A31761.
DR RefSeq; NP_058754.1; NM_017058.1.
DR PDB; 1RJK; X-ray; 1.99 A; A=116-423.
DR PDB; 1RK3; X-ray; 2.20 A; A=116-423.
DR PDB; 1RKG; X-ray; 1.90 A; A=116-423.
DR PDB; 1RKH; X-ray; 2.28 A; A=116-423.
DR PDB; 2O4J; X-ray; 1.74 A; A=116-423.
DR PDB; 2O4R; X-ray; 1.98 A; A=116-423.
DR PDB; 2ZFX; X-ray; 1.99 A; A=116-423.
DR PDB; 2ZL9; X-ray; 1.90 A; A=116-423.
DR PDB; 2ZLA; X-ray; 2.00 A; A=116-423.
DR PDB; 2ZLC; X-ray; 2.00 A; A=116-423.
DR PDB; 2ZMH; X-ray; 2.10 A; A=116-423.
DR PDB; 2ZMI; X-ray; 1.70 A; A=116-423.
DR PDB; 2ZMJ; X-ray; 2.35 A; A=116-423.
DR PDB; 2ZXM; X-ray; 3.01 A; A=116-423.
DR PDB; 2ZXN; X-ray; 2.10 A; A=116-423.
DR PDB; 3A2H; X-ray; 2.50 A; A=116-423.
DR PDB; 3AFR; X-ray; 2.00 A; A=116-423.
DR PDB; 3AUN; X-ray; 1.81 A; A=116-423.
DR PDB; 3VJS; X-ray; 1.93 A; A=116-423.
DR PDB; 3VJT; X-ray; 2.00 A; A=116-423.
DR PDB; 3VRT; X-ray; 2.40 A; A=116-423.
DR PDB; 3VRU; X-ray; 2.00 A; A=116-423.
DR PDB; 3VRV; X-ray; 1.90 A; A=116-423.
DR PDB; 3VRW; X-ray; 2.40 A; A=116-423.
DR PDB; 3VT3; X-ray; 1.70 A; A=116-423.
DR PDB; 3VT4; X-ray; 1.90 A; A=116-423.
DR PDB; 3VT5; X-ray; 2.11 A; A=116-423.
DR PDB; 3VT6; X-ray; 2.30 A; A=116-423.
DR PDB; 3VT7; X-ray; 1.65 A; A=116-423.
DR PDB; 3VT8; X-ray; 2.10 A; A=116-423.
DR PDB; 3VT9; X-ray; 2.35 A; A=116-423.
DR PDB; 3VTB; X-ray; 2.00 A; A=116-423.
DR PDB; 3VTC; X-ray; 1.50 A; A=116-423.
DR PDB; 3VTD; X-ray; 2.70 A; A=116-423.
DR PDB; 3W0G; X-ray; 1.94 A; A=121-420.
DR PDB; 3W0H; X-ray; 1.80 A; A=118-420.
DR PDB; 3W0I; X-ray; 1.90 A; A=121-420.
DR PDB; 3W0J; X-ray; 1.84 A; A=121-420.
DR PDB; 3W5P; X-ray; 1.90 A; A=116-423.
DR PDB; 3W5Q; X-ray; 1.90 A; A=116-423.
DR PDB; 3W5R; X-ray; 2.20 A; A=116-423.
DR PDB; 3W5T; X-ray; 2.29 A; A=116-423.
DR PDB; 3WT5; X-ray; 1.90 A; A=116-423.
DR PDB; 3WT6; X-ray; 2.00 A; A=116-423.
DR PDB; 3WT7; X-ray; 2.40 A; A=116-423.
DR PDB; 3WTQ; X-ray; 2.10 A; A=116-423.
DR PDB; 4YNK; X-ray; 2.30 A; A=116-423.
DR PDB; 5AWJ; X-ray; 2.20 A; A=116-423.
DR PDB; 5AWK; X-ray; 2.90 A; A=116-423.
DR PDB; 5B41; X-ray; 1.89 A; A=116-423.
DR PDB; 5B5B; X-ray; 2.00 A; A/D=116-423.
DR PDB; 5GIC; X-ray; 2.35 A; A=124-420.
DR PDB; 5GID; X-ray; 2.15 A; A=124-419.
DR PDB; 5GIE; X-ray; 2.39 A; A/D=117-419.
DR PDB; 5H1E; X-ray; 2.60 A; A=116-423.
DR PDB; 5XPL; X-ray; 2.05 A; A=116-423.
DR PDB; 5XPM; X-ray; 2.20 A; A=116-423.
DR PDB; 5XPN; X-ray; 1.96 A; A=116-423.
DR PDB; 5XPO; X-ray; 2.28 A; A=116-423.
DR PDB; 5XPP; X-ray; 2.85 A; A=116-423.
DR PDB; 5XUQ; X-ray; 2.80 A; A=116-423.
DR PDB; 5XZF; X-ray; 2.10 A; A=116-423.
DR PDB; 5XZH; X-ray; 2.00 A; A=116-423.
DR PDB; 5ZWE; X-ray; 2.72 A; A=116-423.
DR PDB; 5ZWF; X-ray; 2.10 A; A=116-423.
DR PDB; 5ZWH; X-ray; 2.38 A; A=116-423.
DR PDB; 5ZWI; X-ray; 2.40 A; A=116-423.
DR PDB; 6JEZ; X-ray; 2.30 A; A=116-163, A=213-423.
DR PDB; 6K5O; X-ray; 1.80 A; A=116-419.
DR PDB; 7C7V; X-ray; 2.00 A; A=116-423.
DR PDB; 7C7W; X-ray; 1.90 A; A=116-423.
DR PDBsum; 1RJK; -.
DR PDBsum; 1RK3; -.
DR PDBsum; 1RKG; -.
DR PDBsum; 1RKH; -.
DR PDBsum; 2O4J; -.
DR PDBsum; 2O4R; -.
DR PDBsum; 2ZFX; -.
DR PDBsum; 2ZL9; -.
DR PDBsum; 2ZLA; -.
DR PDBsum; 2ZLC; -.
DR PDBsum; 2ZMH; -.
DR PDBsum; 2ZMI; -.
DR PDBsum; 2ZMJ; -.
DR PDBsum; 2ZXM; -.
DR PDBsum; 2ZXN; -.
DR PDBsum; 3A2H; -.
DR PDBsum; 3AFR; -.
DR PDBsum; 3AUN; -.
DR PDBsum; 3VJS; -.
DR PDBsum; 3VJT; -.
DR PDBsum; 3VRT; -.
DR PDBsum; 3VRU; -.
DR PDBsum; 3VRV; -.
DR PDBsum; 3VRW; -.
DR PDBsum; 3VT3; -.
DR PDBsum; 3VT4; -.
DR PDBsum; 3VT5; -.
DR PDBsum; 3VT6; -.
DR PDBsum; 3VT7; -.
DR PDBsum; 3VT8; -.
DR PDBsum; 3VT9; -.
DR PDBsum; 3VTB; -.
DR PDBsum; 3VTC; -.
DR PDBsum; 3VTD; -.
DR PDBsum; 3W0G; -.
DR PDBsum; 3W0H; -.
DR PDBsum; 3W0I; -.
DR PDBsum; 3W0J; -.
DR PDBsum; 3W5P; -.
DR PDBsum; 3W5Q; -.
DR PDBsum; 3W5R; -.
DR PDBsum; 3W5T; -.
DR PDBsum; 3WT5; -.
DR PDBsum; 3WT6; -.
DR PDBsum; 3WT7; -.
DR PDBsum; 3WTQ; -.
DR PDBsum; 4YNK; -.
DR PDBsum; 5AWJ; -.
DR PDBsum; 5AWK; -.
DR PDBsum; 5B41; -.
DR PDBsum; 5B5B; -.
DR PDBsum; 5GIC; -.
DR PDBsum; 5GID; -.
DR PDBsum; 5GIE; -.
DR PDBsum; 5H1E; -.
DR PDBsum; 5XPL; -.
DR PDBsum; 5XPM; -.
DR PDBsum; 5XPN; -.
DR PDBsum; 5XPO; -.
DR PDBsum; 5XPP; -.
DR PDBsum; 5XUQ; -.
DR PDBsum; 5XZF; -.
DR PDBsum; 5XZH; -.
DR PDBsum; 5ZWE; -.
DR PDBsum; 5ZWF; -.
DR PDBsum; 5ZWH; -.
DR PDBsum; 5ZWI; -.
DR PDBsum; 6JEZ; -.
DR PDBsum; 6K5O; -.
DR PDBsum; 7C7V; -.
DR PDBsum; 7C7W; -.
DR AlphaFoldDB; P13053; -.
DR SMR; P13053; -.
DR BioGRID; 246986; 5.
DR MINT; P13053; -.
DR STRING; 10116.ENSRNOP00000011601; -.
DR BindingDB; P13053; -.
DR ChEMBL; CHEMBL3150; -.
DR DrugCentral; P13053; -.
DR GuidetoPHARMACOLOGY; 605; -.
DR PhosphoSitePlus; P13053; -.
DR PaxDb; P13053; -.
DR GeneID; 24873; -.
DR KEGG; rno:24873; -.
DR UCSC; RGD:3959; rat.
DR CTD; 7421; -.
DR RGD; 3959; Vdr.
DR eggNOG; KOG3575; Eukaryota.
DR InParanoid; P13053; -.
DR OrthoDB; 297114at2759; -.
DR PhylomeDB; P13053; -.
DR Reactome; R-RNO-196791; Vitamin D (calciferol) metabolism.
DR Reactome; R-RNO-383280; Nuclear Receptor transcription pathway.
DR Reactome; R-RNO-4090294; SUMOylation of intracellular receptors.
DR EvolutionaryTrace; P13053; -.
DR PRO; PR:P13053; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0001651; C:dense fibrillar component; IDA:RGD.
DR GO; GO:0000791; C:euchromatin; IDA:RGD.
DR GO; GO:0000792; C:heterochromatin; IDA:RGD.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
DR GO; GO:0016363; C:nuclear matrix; IDA:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR GO; GO:0043235; C:receptor complex; ISO:RGD.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; ISO:RGD.
DR GO; GO:0030315; C:T-tubule; IDA:RGD.
DR GO; GO:1902098; F:calcitriol binding; IDA:RGD.
DR GO; GO:0003677; F:DNA binding; ISO:RGD.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; TAS:RGD.
DR GO; GO:1902121; F:lithocholic acid binding; ISO:RGD.
DR GO; GO:0038186; F:lithocholic acid receptor activity; ISO:RGD.
DR GO; GO:0004879; F:nuclear receptor activity; IDA:RGD.
DR GO; GO:0046965; F:nuclear retinoid X receptor binding; ISO:RGD.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:RGD.
DR GO; GO:0005499; F:vitamin D binding; IDA:RGD.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0009887; P:animal organ morphogenesis; ISO:RGD.
DR GO; GO:0097190; P:apoptotic signaling pathway; IDA:RGD.
DR GO; GO:0038183; P:bile acid signaling pathway; ISO:RGD.
DR GO; GO:0006816; P:calcium ion transport; ISO:RGD.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0000902; P:cell morphogenesis; ISO:RGD.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; ISO:RGD.
DR GO; GO:1904646; P:cellular response to amyloid-beta; IEP:RGD.
DR GO; GO:0071305; P:cellular response to vitamin D; IEP:RGD.
DR GO; GO:0046697; P:decidualization; ISO:RGD.
DR GO; GO:0007507; P:heart development; IEP:RGD.
DR GO; GO:0050892; P:intestinal absorption; ISO:RGD.
DR GO; GO:0007595; P:lactation; ISO:RGD.
DR GO; GO:0060745; P:mammary gland branching involved in pregnancy; ISO:RGD.
DR GO; GO:0042789; P:mRNA transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:1900155; P:negative regulation of bone trabecula formation; IMP:RGD.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:RGD.
DR GO; GO:0010839; P:negative regulation of keratinocyte proliferation; ISO:RGD.
DR GO; GO:0030279; P:negative regulation of ossification; IMP:RGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0060058; P:positive regulation of apoptotic process involved in mammary gland involution; ISO:RGD.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR GO; GO:0045618; P:positive regulation of keratinocyte differentiation; ISO:RGD.
DR GO; GO:2000830; P:positive regulation of parathyroid hormone secretion; IMP:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0010980; P:positive regulation of vitamin D 24-hydroxylase activity; ISO:RGD.
DR GO; GO:0070564; P:positive regulation of vitamin D receptor signaling pathway; ISO:RGD.
DR GO; GO:0060558; P:regulation of calcidiol 1-monooxygenase activity; ISO:RGD.
DR GO; GO:0051924; P:regulation of calcium ion transport; IDA:RGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; TAS:RGD.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0051592; P:response to calcium ion; IEP:RGD.
DR GO; GO:0032355; P:response to estradiol; IEP:RGD.
DR GO; GO:0001501; P:skeletal system development; ISO:RGD.
DR GO; GO:0070561; P:vitamin D receptor signaling pathway; ISO:RGD.
DR CDD; cd06955; NR_DBD_VDR; 1.
DR Gene3D; 1.10.565.10; -; 1.
DR Gene3D; 3.30.50.10; -; 1.
DR IDEAL; IID50032; -.
DR InterPro; IPR042153; DBD_VDR.
DR InterPro; IPR035500; NHR-like_dom_sf.
DR InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
DR InterPro; IPR001723; Nuclear_hrmn_rcpt.
DR InterPro; IPR000324; VitD_rcpt.
DR InterPro; IPR001628; Znf_hrmn_rcpt.
DR InterPro; IPR013088; Znf_NHR/GATA.
DR Pfam; PF00104; Hormone_recep; 1.
DR Pfam; PF00105; zf-C4; 1.
DR PRINTS; PR00398; STRDHORMONER.
DR PRINTS; PR00047; STROIDFINGER.
DR PRINTS; PR00350; VITAMINDR.
DR SMART; SM00430; HOLI; 1.
DR SMART; SM00399; ZnF_C4; 1.
DR SUPFAM; SSF48508; SSF48508; 1.
DR PROSITE; PS51843; NR_LBD; 1.
DR PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
DR PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; DNA-binding; Metal-binding; Nucleus; Receptor;
KW Reference proteome; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..423
FT /note="Vitamin D3 receptor"
FT /id="PRO_0000053544"
FT DOMAIN 127..419
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT DNA_BIND 24..89
FT /note="Nuclear receptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 24..44
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 60..84
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT REGION 97..126
FT /note="Hinge"
FT /evidence="ECO:0000250|UniProtKB:P11473"
FT REGION 159..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 242..260
FT /note="Interaction with coactivator LXXLL motif"
FT /evidence="ECO:0000269|PubMed:15065852"
FT MOTIF 412..420
FT /note="9aaTAD"
FT /evidence="ECO:0000250|UniProtKB:P11473"
FT COMPBIAS 164..180
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 143
FT /ligand="calciol"
FT /ligand_id="ChEBI:CHEBI:28940"
FT /evidence="ECO:0000269|PubMed:15065852,
FT ECO:0000269|PubMed:17227670"
FT BINDING 223..233
FT /ligand="calciol"
FT /ligand_id="ChEBI:CHEBI:28940"
FT /evidence="ECO:0000269|PubMed:15065852,
FT ECO:0000269|PubMed:17227670"
FT BINDING 267..274
FT /ligand="calciol"
FT /ligand_id="ChEBI:CHEBI:28940"
FT /evidence="ECO:0000269|PubMed:15065852,
FT ECO:0000269|PubMed:17227670"
FT BINDING 301
FT /ligand="calciol"
FT /ligand_id="ChEBI:CHEBI:28940"
FT /evidence="ECO:0000269|PubMed:15065852,
FT ECO:0000269|PubMed:17227670"
FT BINDING 393
FT /ligand="calciol"
FT /ligand_id="ChEBI:CHEBI:28940"
FT /evidence="ECO:0000269|PubMed:15065852,
FT ECO:0000269|PubMed:17227670"
FT HELIX 116..119
FT /evidence="ECO:0007829|PDB:3VT3"
FT HELIX 126..142
FT /evidence="ECO:0007829|PDB:3VTC"
FT HELIX 148..152
FT /evidence="ECO:0007829|PDB:3VTC"
FT TURN 219..222
FT /evidence="ECO:0007829|PDB:3VT3"
FT HELIX 223..241
FT /evidence="ECO:0007829|PDB:3VTC"
FT HELIX 247..249
FT /evidence="ECO:0007829|PDB:3VTC"
FT HELIX 252..270
FT /evidence="ECO:0007829|PDB:3VTC"
FT HELIX 271..273
FT /evidence="ECO:0007829|PDB:3VTC"
FT STRAND 274..276
FT /evidence="ECO:0007829|PDB:3VTD"
FT TURN 277..280
FT /evidence="ECO:0007829|PDB:3VTC"
FT STRAND 281..283
FT /evidence="ECO:0007829|PDB:3VTC"
FT HELIX 287..289
FT /evidence="ECO:0007829|PDB:3VTC"
FT STRAND 290..292
FT /evidence="ECO:0007829|PDB:3VTD"
FT HELIX 293..297
FT /evidence="ECO:0007829|PDB:3VTC"
FT TURN 298..300
FT /evidence="ECO:0007829|PDB:3VTC"
FT HELIX 303..317
FT /evidence="ECO:0007829|PDB:3VTC"
FT HELIX 323..334
FT /evidence="ECO:0007829|PDB:3VTC"
FT STRAND 337..339
FT /evidence="ECO:0007829|PDB:5H1E"
FT HELIX 345..366
FT /evidence="ECO:0007829|PDB:3VTC"
FT TURN 369..374
FT /evidence="ECO:0007829|PDB:3VTC"
FT HELIX 375..401
FT /evidence="ECO:0007829|PDB:3VTC"
FT HELIX 404..407
FT /evidence="ECO:0007829|PDB:3VTC"
FT HELIX 412..418
FT /evidence="ECO:0007829|PDB:3VTC"
SQ SEQUENCE 423 AA; 47814 MW; 1A0E519A9DCCE990 CRC64;
MEATAASTSL PDPGDFDRNV PRICGVCGDR ATGFHFNAMT CEGCKGFFRR SMKRKALFTC
PFNGDCRITK DNRRHCQACR LKRCVDIGMM KEFILTDEEV QRKREMIMKR KEEEALKDSL
RPKLSEEQQH IIAILLDAHH KTYDPTYADF RDFRPPVRMD GSTGSYSPRP TLSFSGNSSS
SSSDLYTTSL DMMEPSGFSN LDLNGEDSDD PSVTLDLSPL SMLPHLADLV SYSIQKVIGF
AKMIPGFRDL TSDDQIVLLK SSAIEVIMLR SNQSFTMDDM SWDCGSQDYK YDVTDVSKAG
HTLELIEPLI KFQVGLKKLN LHEEEHVLLM AICIVSPDRP GVQDAKLVEA IQDRLSNTLQ
TYIRCRHPPP GSHQLYAKMI QKLADLRSLN EEHSKQYRSL SFQPENSMKL TPLVLEVFGN
EIS
