VDR_COTJA
ID VDR_COTJA Reviewed; 448 AA.
AC P49701;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 128.
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 Coturnix japonica (Japanese quail) (Coturnix coturnix japonica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Perdicinae; Coturnix.
OX NCBI_TaxID=93934;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B).
RC TISSUE=Chorioallantoic membrane;
RX PubMed=7972109; DOI=10.1073/pnas.91.24.11596;
RA Elaroussi M.A., Prahl J.M., Deluca H.F.;
RT "The avian vitamin D receptors: primary structures and their origins.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:11596-11600(1994).
CC -!- FUNCTION: Nuclear receptor for calcitriol, the active form of vitamin
CC D3 which mediates the action of this vitamin on cells. Enters the
CC nucleus upon vitamin D3 binding where it forms heterodimers with the
CC retinoid X receptor/RXR. The VDR-RXR heterodimers bind to specific
CC response elements on DNA and activate the transcription of vitamin D3-
CC responsive target genes. Recruited to promoters via its interaction
CC with BAZ1B/WSTF which mediates the interaction with acetylated
CC histones, an essential step for VDR-promoter association. Plays a
CC central role in calcium homeostasis. {ECO:0000250|UniProtKB:P11473}.
CC -!- SUBUNIT: Homodimer in the absence of bound vitamin D3. Heterodimer with
CC RXRA after vitamin D3 binding. {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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=A;
CC IsoId=P49701-1; Sequence=Displayed;
CC Name=B;
CC IsoId=P49701-2; Sequence=VSP_018772;
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U12641; AAA56725.1; -; mRNA.
DR PIR; I50451; I50451.
DR RefSeq; NP_001310170.1; NM_001323241.1. [P49701-1]
DR AlphaFoldDB; P49701; -.
DR SMR; P49701; -.
DR GeneID; 107306955; -.
DR KEGG; cjo:107306955; -.
DR CTD; 7421; -.
DR Proteomes; UP000694412; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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 Alternative initiation; Cytoplasm; DNA-binding; Metal-binding; Nucleus;
KW Receptor; Reference proteome; Transcription; Transcription regulation;
KW Zinc; Zinc-finger.
FT CHAIN 1..448
FT /note="Vitamin D3 receptor"
FT /id="PRO_0000019935"
FT DOMAIN 147..444
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT DNA_BIND 41..116
FT /note="Nuclear receptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 44..64
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 80..104
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT REGION 117..146
FT /note="Hinge"
FT /evidence="ECO:0000250|UniProtKB:P11473"
FT REGION 267..285
FT /note="Interaction with coactivator LXXLL motif"
FT /evidence="ECO:0000250|UniProtKB:P13053"
FT MOTIF 437..445
FT /note="9aaTAD"
FT /evidence="ECO:0000250|UniProtKB:P11473"
FT BINDING 248..258
FT /ligand="calciol"
FT /ligand_id="ChEBI:CHEBI:28940"
FT /evidence="ECO:0000250|UniProtKB:P11473"
FT BINDING 292..299
FT /ligand="calciol"
FT /ligand_id="ChEBI:CHEBI:28940"
FT /evidence="ECO:0000250|UniProtKB:P11473"
FT BINDING 326
FT /ligand="calciol"
FT /ligand_id="ChEBI:CHEBI:28940"
FT /evidence="ECO:0000250|UniProtKB:P11473"
FT BINDING 418
FT /ligand="calciol"
FT /ligand_id="ChEBI:CHEBI:28940"
FT /evidence="ECO:0000250|UniProtKB:P11473"
FT VAR_SEQ 1..25
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000303|PubMed:7972109"
FT /id="VSP_018772"
SQ SEQUENCE 448 AA; 50668 MW; FCF1FC3DEAEEAF3E CRC64;
MVSISASGGY AMPCCCESQE LQSSDMETPA VGTPEFDRNV PRICGVCGDR ATGFHFNAMT
CEGCKGFFRR SMKRKAMFTC PFSGDCKITK DNRRHCQACR LKRCVDIGMM KEFILTDEEV
QRKREMILKR KEEEALKESL KPKLSEEQQK VINILLEAHH KTFDTTYSDF NKFRPPVRSK
FSSSTATHSS SVVSQDFSSE DSNDVFGSDA FGAFPEPMEP QMFSNLDLSE ESDESPSMNI
ELPHLPMLPH LADLVSYSIQ KVIGFAKMIP GFRDLTAEDQ IALLKSSAIE VIMLRSNQSF
TMEDMSWTCG SNDFKYKVSD VTQAGHSMDL LEPLVKFQVG LKKLNLHEEE HVLLMAICIL
SPDRPGVQDT SLVESIQDRL SDTLQTYIRC RHPPPGSRLL YAKMIQKLAD LRSLNEEHSK
QYRCLSFQPE HSMQLTPLVL EVFGNEIS