ID   VDR_SAGOE               Reviewed;         427 AA.
AC   Q95MH5;
DT   21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 101.
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   Saguinus oedipus (Cotton-top tamarin).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC   Callitrichinae; Saguinus.
OX   NCBI_TaxID=9490;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=11376448; DOI=10.1002/ajp.1016;
RA   Chun R.F., Chen H., Boldrick L., Sweet C., Adams J.S.;
RT   "Cloning, sequencing, and functional characterization of the vitamin D
RT   receptor in vitamin D-resistant New World primates.";
RL   Am. J. Primatol. 54:107-118(2001).
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 (By similarity).
CC       {ECO:0000250|UniProtKB:P11473, ECO:0000250|UniProtKB:P13053}.
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. {ECO:0000250|UniProtKB:P11473}.
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   -!- 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; AF354232; AAK48863.1; -; mRNA.
DR   AlphaFoldDB; Q95MH5; -.
DR   SMR; Q95MH5; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005654; C:nucleoplasm; IEA:UniProt.
DR   GO; GO:0004879; F:nuclear receptor activity; ISS:UniProtKB.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0070561; P:vitamin D receptor signaling pathway; ISS:UniProtKB.
DR   CDD; cd06955; NR_DBD_VDR; 1.
DR   Gene3D; 1.10.565.10; -; 1.
DR   Gene3D; 3.30.50.10; -; 1.
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   2: Evidence at transcript level;
KW   Cytoplasm; DNA-binding; Metal-binding; Nucleus; Receptor; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..427
FT                   /note="Vitamin D3 receptor"
FT                   /id="PRO_0000053545"
FT   DOMAIN          127..423
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          158..183
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          246..264
FT                   /note="Interaction with coactivator LXXLL motif"
FT                   /evidence="ECO:0000250|UniProtKB:P13053"
FT   MOTIF           416..424
FT                   /note="9aaTAD"
FT                   /evidence="ECO:0000250|UniProtKB:P11473"
FT   COMPBIAS        165..183
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:0000250|UniProtKB:P11473"
FT   BINDING         227..237
FT                   /ligand="calciol"
FT                   /ligand_id="ChEBI:CHEBI:28940"
FT                   /evidence="ECO:0000250|UniProtKB:P11473"
FT   BINDING         271..278
FT                   /ligand="calciol"
FT                   /ligand_id="ChEBI:CHEBI:28940"
FT                   /evidence="ECO:0000250|UniProtKB:P11473"
FT   BINDING         305
FT                   /ligand="calciol"
FT                   /ligand_id="ChEBI:CHEBI:28940"
FT                   /evidence="ECO:0000250|UniProtKB:P11473"
FT   BINDING         397
FT                   /ligand="calciol"
FT                   /ligand_id="ChEBI:CHEBI:28940"
FT                   /evidence="ECO:0000250|UniProtKB:P11473"
SQ   SEQUENCE   427 AA;  48383 MW;  5B933C4F023B5199 CRC64;
     MEAMAASTSL PDPGDFDRNV PRICGVCGDR ATGFHFNAMT CEGCKGFFRR SMKRKALFTC
     PFNGDCRITK DNRRHCQACR LKRCVDIGMM KEFILTDEEV QRKREMILKR KEEEALKDSL
     RPKLSEEQQR IIAILLDAHH KTYDPTYSDF CQFRPPVRVN DGGGSHPSRP NSRHTPSFSG
     DSSSCCSDHY ITSPDMMDSS SFSNLDLSEE DSDDPSLTLE LSQLSMLPHL ADLVSYSIQK
     VIGFAKMIPG FRDLTSEDQI VLLKSSAIEV IMLRSNESFT MDDMSWTCGN PDYKYRISDV
     TKAGHNLELI EPLIKFQVGL KKLNLHEEEH VLLMAICIVS PDRPGVQDAA LIEAIQDRLS
     NTLQTYIRCR HPPPGSHLLY AKMIQKLADL RSLNEEHSKQ YRCLSFQPES SMKLTPLVLE
     VFGNEIS