ID   VDR_MOUSE               Reviewed;         422 AA.
AC   P48281; Q922X0;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   04-NOV-2026, entry version 204.
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   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=7835717; DOI=10.1016/0378-1119(94)00735-b;
RA   Kamei Y., Kawada T., Fukuwatari T., Ono T., Kato S., Sugimoto E.;
RT   "Cloning and sequencing of the gene encoding the mouse vitamin D
RT   receptor.";
RL   Gene 152:281-282(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Intestine;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
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   [5]
RP   FUNCTION.
RX   PubMed=12016314; DOI=10.1126/science.1070477;
RA   Makishima M., Lu T.T., Xie W., Whitfield G.K., Domoto H., Evans R.M.,
RA   Haussler M.R., Mangelsdorf D.J.;
RT   "Vitamin D receptor as an intestinal bile acid sensor.";
RL   Science 296:1313-1316(2002).
RN   [6]
RP   INDUCTION.
RX   PubMed=14528024; DOI=10.1210/me.2003-0048;
RA   Tsujikawa H., Kurotaki Y., Fujimori T., Fukuda K., Nabeshima Y.;
RT   "Klotho, a gene related to a syndrome resembling human premature aging,
RT   functions in a negative regulatory circuit of vitamin D endocrine system.";
RL   Mol. Endocrinol. 17:2393-2403(2003).
RN   [7]
RP   INTERACTION WITH CRY1 AND CRY2.
RX   PubMed=28751364; DOI=10.1073/pnas.1704955114;
RA   Kriebs A., Jordan S.D., Soto E., Henriksson E., Sandate C.R., Vaughan M.E.,
RA   Chan A.B., Duglan D., Papp S.J., Huber A.L., Afetian M.E., Yu R.T.,
RA   Zhao X., Downes M., Evans R.M., Lamia K.A.;
RT   "Circadian repressors CRY1 and CRY2 broadly interact with nuclear receptors
RT   and modulate transcriptional activity.";
RL   Proc. Natl. Acad. Sci. U.S.A. 114:8776-8781(2017).
RN   [8]
RP   FUNCTION.
RX   PubMed=32354638; DOI=10.1016/j.kint.2020.01.032;
RA   Hashimoto N., Matsui I., Ishizuka S., Inoue K., Matsumoto A., Shimada K.,
RA   Hori S., Lee D.G., Yasuda S., Katsuma Y., Kajimoto S., Doi Y.,
RA   Yamaguchi S., Kubota K., Oka T., Sakaguchi Y., Takabatake Y., Hamano T.,
RA   Isaka Y.;
RT   "Lithocholic acid increases intestinal phosphate and calcium absorption in
RT   a vitamin D receptor dependent but transcellular pathway independent
RT   manner.";
RL   Kidney Int. 97:1164-1180(2020).
CC   -!- FUNCTION: Nuclear receptor for calcitriol, the active form of vitamin
CC       D3 which mediates the action of this vitamin on cells (By similarity).
CC       Enters the nucleus upon vitamin D3 binding where it forms heterodimers
CC       with the retinoid X receptor/RXR (By similarity). The VDR-RXR
CC       heterodimers bind to specific response elements on DNA and activate the
CC       transcription of vitamin D3-responsive target genes (By similarity).
CC       Plays a central role in calcium homeostasis (PubMed:32354638). Also
CC       functions as a receptor for the secondary bile acid lithocholic acid
CC       (LCA) and its metabolites (PubMed:12016314, PubMed:32354638).
CC       {ECO:0000250|UniProtKB:P11473, ECO:0000250|UniProtKB:P13053,
CC       ECO:0000269|PubMed:12016314, ECO:0000269|PubMed:32354638}.
CC   -!- SUBUNIT: Homodimer in the absence of bound vitamin D3. Heterodimer with
CC       RXRA after vitamin D3 binding. Interacts with MED1, NCOA1, NCOA2, NCOA3
CC       and NCOA6 coactivators, leading to a strong increase of transcription
CC       of target genes. Interacts with the corepressor NCOR1. Interacts with
CC       SNW1. Interacts with IRX4, the interaction does not affect its
CC       transactivation activity (By similarity). Interacts with CRY1
CC       (PubMed:28751364). Interacts with CRY2 in a ligand-dependent manner
CC       (PubMed:28751364). {ECO:0000250|UniProtKB:P11473,
CC       ECO:0000269|PubMed:28751364}.
CC   -!- INTERACTION:
CC       P48281; Q925T6: Grip1; NbExp=2; IntAct=EBI-346797, EBI-537752;
CC       P48281; Q64337: Sqstm1; NbExp=3; IntAct=EBI-346797, EBI-645025;
CC       P48281; Q00403: GTF2B; Xeno; NbExp=2; IntAct=EBI-346797, EBI-389564;
CC       P48281; Q9Y6Q9: NCOA3; Xeno; NbExp=2; IntAct=EBI-346797, EBI-81196;
CC       P48281; Q13573: SNW1; Xeno; NbExp=2; IntAct=EBI-346797, EBI-632715;
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   -!- INDUCTION: By 1,25-dihydroxyvitamin D(3) in kidney.
CC       {ECO:0000269|PubMed:14528024}.
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   -!- PTM: Ubiquitinated by UBR5, leading to its degradation: UBR5
CC       specifically recognizes and binds ligand-bound VDR when it is not
CC       associated with coactivators (NCOAs). In presence of NCOAs, the UBR5-
CC       degron is not accessible, preventing its ubiquitination and
CC       degradation. {ECO:0000250|UniProtKB:P11473}.
CC   -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR1
CC       subfamily. {ECO:0000305}.
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DR   EMBL; D31969; BAA06737.1; -; mRNA.
DR   EMBL; AK030339; BAC26911.1; -; mRNA.
DR   EMBL; AK154647; BAE32738.1; -; mRNA.
DR   EMBL; CH466550; EDL04218.1; -; Genomic_DNA.
DR   EMBL; BC006716; AAH06716.1; -; mRNA.
DR   CCDS; CCDS27784.1; -.
DR   PIR; PC4019; PC4019.
DR   RefSeq; NP_033530.2; NM_009504.4.
DR   AlphaFoldDB; P48281; -.
DR   SMR; P48281; -.
DR   BioGRID; 204511; 7.
DR   ComplexPortal; CPX-673; RXRalpha-VDR nuclear hormone receptor complex.
DR   ComplexPortal; CPX-872; RXRbeta-VDR nuclear hormone receptor complex.
DR   CORUM; P48281; -.
DR   DIP; DIP-31478N; -.
DR   FunCoup; P48281; 846.
DR   IntAct; P48281; 12.
DR   STRING; 10090.ENSMUSP00000023119; -.
DR   BindingDB; P48281; -.
DR   ChEMBL; CHEMBL5601; -.
DR   DrugCentral; P48281; -.
DR   GlyGen; P48281; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P48281; -.
DR   PhosphoSitePlus; P48281; -.
DR   jPOST; P48281; -.
DR   PaxDb; 10090-ENSMUSP00000023119; -.
DR   PeptideAtlas; P48281; -.
DR   ProteomicsDB; 300197; -.
DR   Pumba; P48281; -.
DR   Antibodypedia; 3902; 921 antibodies from 47 providers.
DR   DNASU; 22337; -.
DR   Ensembl; ENSMPUT00000000424; ENSMPUP00000000416; ENSMPUG00000000419.
DR   Ensembl; ENSMUST00000023119.15; ENSMUSP00000023119.9; ENSMUSG00000022479.16.
DR   GeneID; 22337; -.
DR   KEGG; mmu:22337; -.
DR   UCSC; uc007xlk.1; mouse.
DR   AGR; MGI:103076; -.
DR   CTD; 7421; -.
DR   MGI; MGI:103076; Vdr.
DR   VEuPathDB; HostDB:ENSMUSG00000022479; -.
DR   eggNOG; KOG3575; Eukaryota.
DR   GeneTree; ENSGT00940000155473; -.
DR   HOGENOM; CLU_007368_12_0_1; -.
DR   InParanoid; P48281; -.
DR   OMA; AAQXRLS; -.
DR   OrthoDB; 6352325at2759; -.
DR   PhylomeDB; P48281; -.
DR   Reactome; R-MMU-196791; Vitamin D (calciferol) metabolism.
DR   Reactome; R-MMU-383280; Nuclear Receptor transcription pathway.
DR   Reactome; R-MMU-4090294; SUMOylation of intracellular receptors.
DR   BioGRID-ORCS; 22337; 3 hits in 80 CRISPR screens.
DR   PRO; PR:P48281; -.
DR   Proteomes; UP000000589; Chromosome 15.
DR   RNAct; P48281; protein.
DR   Bgee; ENSMUSG00000022479; Expressed in duodenum and 138 other cell types or tissues.
DR   ExpressionAtlas; P48281; baseline and differential.
DR   GO; GO:0005901; C:caveola; ISO:GO_Central.
DR   GO; GO:0000785; C:chromatin; ISO:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; ISO:GO_Central.
DR   GO; GO:0001651; C:dense fibrillar component; ISO:GO_Central.
DR   GO; GO:0000791; C:euchromatin; ISO:GO_Central.
DR   GO; GO:0000792; C:heterochromatin; ISO:GO_Central.
DR   GO; GO:0016363; C:nuclear matrix; ISO:GO_Central.
DR   GO; GO:0005654; C:nucleoplasm; ISO:GO_Central.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:GO_Central.
DR   GO; GO:0090575; C:RNA polymerase II transcription regulator complex; ISO:GO_Central.
DR   GO; GO:0043235; C:signaling receptor complex; ISO:GO_Central.
DR   GO; GO:0030315; C:T-tubule; ISO:GO_Central.
DR   GO; GO:0038186; F:bile acid nuclear receptor activity; ISO:GO_Central.
DR   GO; GO:1902098; F:calcitriol binding; ISO:GO_Central.
DR   GO; GO:0003677; F:DNA binding; IDA:MGI.
DR   GO; GO:1902121; F:lithocholic acid binding; ISO:GO_Central.
DR   GO; GO:0004879; F:nuclear receptor activity; IDA:MGI.
DR   GO; GO:0046965; F:nuclear retinoid X receptor binding; ISO:GO_Central.
DR   GO; GO:0003707; F:nuclear steroid receptor activity; ISO:GO_Central.
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; ISO:GO_Central.
DR   GO; GO:0005499; F:vitamin D binding; ISO:GO_Central.
DR   GO; GO:0070644; F:vitamin D response element binding; IEA:Ensembl.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0009887; P:animal organ morphogenesis; IMP:MGI.
DR   GO; GO:0097190; P:apoptotic signaling pathway; ISO:GO_Central.
DR   GO; GO:0006816; P:calcium ion transport; IMP:MGI.
DR   GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR   GO; GO:0000902; P:cell morphogenesis; ISO:GO_Central.
DR   GO; GO:0045217; P:cell-cell junction maintenance; ISO:GO_Central.
DR   GO; GO:0046697; P:decidualization; IEA:Ensembl.
DR   GO; GO:0050892; P:intestinal absorption; IMP:MGI.
DR   GO; GO:0006874; P:intracellular calcium ion homeostasis; IMP:MGI.
DR   GO; GO:0030522; P:intracellular receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0007595; P:lactation; IMP:MGI.
DR   GO; GO:0060745; P:mammary gland branching involved in pregnancy; IMP:MGI.
DR   GO; GO:0042789; P:mRNA transcription by RNA polymerase II; ISO:GO_Central.
DR   GO; GO:1900155; P:negative regulation of bone trabecula formation; ISO:GO_Central.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:GO_Central.
DR   GO; GO:0045892; P:negative regulation of DNA-templated transcription; ISO:MGI.
DR   GO; GO:0010839; P:negative regulation of keratinocyte proliferation; ISO:GO_Central.
DR   GO; GO:0030279; P:negative regulation of ossification; ISO:GO_Central.
DR   GO; GO:2000186; P:negative regulation of phosphate transmembrane transport; ISO:GO_Central.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:GO_Central.
DR   GO; GO:0038185; P:nuclear receptor-mediated bile acid signaling pathway; ISO:GO_Central.
DR   GO; GO:0035435; P:phosphate ion transmembrane transport; ISO:GO_Central.
DR   GO; GO:0060058; P:positive regulation of apoptotic process involved in mammary gland involution; IMP:MGI.
DR   GO; GO:0030501; P:positive regulation of bone mineralization; NAS:ComplexPortal.
DR   GO; GO:0010628; P:positive regulation of gene expression; ISO:GO_Central.
DR   GO; GO:0045618; P:positive regulation of keratinocyte differentiation; ISO:GO_Central.
DR   GO; GO:2000830; P:positive regulation of parathyroid hormone secretion; ISO:GO_Central.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:GO_Central.
DR   GO; GO:0070564; P:positive regulation of vitamin D receptor signaling pathway; ISO:GO_Central.
DR   GO; GO:0051924; P:regulation of calcium ion transport; ISO:GO_Central.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IDA:MGI.
DR   GO; GO:1903412; P:response to bile acid; ISO:GO_Central.
DR   GO; GO:0048384; P:retinoic acid receptor signaling pathway; ISO:GO_Central.
DR   GO; GO:0001501; P:skeletal system development; IMP:MGI.
DR   GO; GO:0070561; P:vitamin D receptor signaling pathway; IMP:BHF-UCL.
DR   CDD; cd06955; NR_DBD_VDR; 1.
DR   CDD; cd06933; NR_LBD_VDR; 1.
DR   FunFam; 3.30.50.10:FF:000023; Vitamin D3 receptor; 1.
DR   FunFam; 1.10.565.10:FF:000021; Vitamin D3 receptor B; 1.
DR   Gene3D; 3.30.50.10; Erythroid Transcription Factor GATA-1, subunit A; 1.
DR   Gene3D; 1.10.565.10; Retinoid X Receptor; 1.
DR   InterPro; IPR042153; DBD_VDR.
DR   InterPro; IPR035500; NHR-like_dom_sf.
DR   InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
DR   InterPro; IPR050234; Nuclear_hormone_rcpt_NR1.
DR   InterPro; IPR001723; Nuclear_hrmn_rcpt.
DR   InterPro; IPR000324; VitD_rcpt.
DR   InterPro; IPR001628; Znf_hrmn_rcpt.
DR   InterPro; IPR013088; Znf_NHR/GATA.
DR   PANTHER; PTHR24082; NUCLEAR HORMONE RECEPTOR; 1.
DR   PANTHER; PTHR24082:SF38; VITAMIN D3 RECEPTOR; 1.
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; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
DR   SUPFAM; SSF48508; Nuclear receptor ligand-binding domain; 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   Cytoplasm; DNA-binding; Metal-binding; Nucleus; Receptor;
KW   Reference proteome; Transcription; Transcription regulation;
KW   Ubl conjugation; Zinc; Zinc-finger.
FT   CHAIN           1..422
FT                   /note="Vitamin D3 receptor"
FT                   /id="PRO_0000053543"
FT   DOMAIN          127..418
FT                   /note="NR LBD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT   DNA_BIND        21..96
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          161..185
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          241..259
FT                   /note="Interaction with coactivator LXXLL motif"
FT                   /evidence="ECO:0000250|UniProtKB:P13053"
FT   MOTIF           411..419
FT                   /note="9aaTAD"
FT                   /evidence="ECO:0000250|UniProtKB:P11473"
FT   COMPBIAS        162..172
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        173..182
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         24
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P11473"
FT   BINDING         27
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P11473"
FT   BINDING         41
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P11473"
FT   BINDING         44
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P11473"
FT   BINDING         60
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P11473"
FT   BINDING         66
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P11473"
FT   BINDING         76
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P11473"
FT   BINDING         79
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P11473"
FT   BINDING         143
FT                   /ligand="calcitriol"
FT                   /ligand_id="ChEBI:CHEBI:17823"
FT                   /evidence="ECO:0000250|UniProtKB:P11473"
FT   BINDING         232
FT                   /ligand="calcitriol"
FT                   /ligand_id="ChEBI:CHEBI:17823"
FT                   /evidence="ECO:0000250|UniProtKB:P11473"
FT   BINDING         269
FT                   /ligand="calcitriol"
FT                   /ligand_id="ChEBI:CHEBI:17823"
FT                   /evidence="ECO:0000250|UniProtKB:P11473"
FT   BINDING         273
FT                   /ligand="calcitriol"
FT                   /ligand_id="ChEBI:CHEBI:17823"
FT                   /evidence="ECO:0000250|UniProtKB:P11473"
FT   BINDING         300
FT                   /ligand="calcitriol"
FT                   /ligand_id="ChEBI:CHEBI:17823"
FT                   /evidence="ECO:0000250|UniProtKB:P11473"
FT   BINDING         392
FT                   /ligand="calcitriol"
FT                   /ligand_id="ChEBI:CHEBI:17823"
FT                   /evidence="ECO:0000250|UniProtKB:P11473"
FT   CONFLICT        276
FT                   /note="L -> M (in Ref. 1; BAA06737)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   422 AA;  47834 MW;  4614DD4A129F2732 CRC64;
     MEAMAASTSL PDPGDFDRNV PRICGVCGDR ATGFHFNAMT CEGCKGFFRR SMKRKALFTC
     PFNGDCRITK DNRRHCQACR LKRCVDIGMM KEFILTDEEV QRKREMIMKR KEEEALKDSL
     RPKLSEEQQH IIAILLDAHH KTYDPTYADF RDFRPPIRAD VSTGSYSPRP TLSFSGDSSS
     NSDLYTPSLD MMEPASFSTM DLNEEGSDDP SVTLDLSPLS MLPHLADLVS YSIQKVIGFA
     KMIPGFRDLT SDDQIVLLKS SAIEVIMLRS NQSFTLDDMS WDCGSQDYKY DITDVSRAGH
     TLELIEPLIK FQVGLKKLNL HEEEHVLLMA ICIVSPDRPG VQDAKLVEAI QDRLSNTLQT
     YIRCRHPPPG SHQLYAKMIQ KLADLRSLNE EHSKQYRSLS FQPENSMKLT PLVLEVFGNE
     IS
//