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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}.
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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
 
 
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