VDR_XENLA
ID VDR_XENLA Reviewed; 422 AA.
AC O13124;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 131.
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 Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Kidney;
RX PubMed=9165021; DOI=10.1210/endo.138.6.5210;
RA Li Y.C., Bergwitz C., Jueppner H., Demay M.B.;
RT "Cloning and characterization of the vitamin D receptor from Xenopus
RT laevis.";
RL Endocrinology 138:2347-2353(1997).
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 -!- TISSUE SPECIFICITY: Detected in all tissues examined. Highest level in
CC small intestine and skin. {ECO:0000269|PubMed:9165021}.
CC -!- DEVELOPMENTAL STAGE: First detected at stage 13. Increases gradually
CC and peaks at stage 57-61 then decreases to the level seen in adult.
CC {ECO:0000269|PubMed:9165021}.
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; U91846; AAB58585.1; -; mRNA.
DR RefSeq; NP_001079288.1; NM_001085819.2.
DR AlphaFoldDB; O13124; -.
DR SMR; O13124; -.
DR GeneID; 378575; -.
DR KEGG; xla:378575; -.
DR CTD; 378575; -.
DR Xenbase; XB-GENE-864847; vdr.S.
DR OrthoDB; 297114at2759; -.
DR Proteomes; UP000186698; Chromosome 2S.
DR Bgee; 378575; Expressed in zone of skin and 9 other tissues.
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 Cytoplasm; DNA-binding; Metal-binding; Nucleus; Receptor;
KW Reference proteome; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..422
FT /note="Vitamin D3 receptor"
FT /id="PRO_0000053546"
FT DOMAIN 128..418
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT DNA_BIND 22..90
FT /note="Nuclear receptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 25..45
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 61..85
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT REGION 98..127
FT /note="Hinge"
FT /evidence="ECO:0000250|UniProtKB:P11473"
FT REGION 170..191
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 BINDING 222..232
FT /ligand="calciol"
FT /ligand_id="ChEBI:CHEBI:28940"
FT /evidence="ECO:0000250|UniProtKB:P11473"
FT BINDING 266..273
FT /ligand="calciol"
FT /ligand_id="ChEBI:CHEBI:28940"
FT /evidence="ECO:0000250|UniProtKB:P11473"
FT BINDING 300
FT /ligand="calciol"
FT /ligand_id="ChEBI:CHEBI:28940"
FT /evidence="ECO:0000250|UniProtKB:P11473"
FT BINDING 392
FT /ligand="calciol"
FT /ligand_id="ChEBI:CHEBI:28940"
FT /evidence="ECO:0000250|UniProtKB:P11473"
SQ SEQUENCE 422 AA; 48188 MW; C8A9F25414FEE9D5 CRC64;
MEFMAATTSI ADTDMEFDKN VPRICGVCGD KATGFHFNAM TCEGCKGFFR RSMKRKAMFT
CPFNGDCRIT KDNRRHCQSC RLKRCVDIGM MKEFILTDEE VQRKRQMINK RKSEEALKES
MRPKISDEQQ KMIDILLEAH RKTFDTTYSD FNKFRPPVRE NVDPFRRITR SSSVHTQGSP
SEDSDVFTSS PDSSEHGFFS ASLFGQFEYS SMGGKSGELS MLPHIADLVS YSIQKIIGFA
KMIPGFRDLI AEDQIALLKS SVIEVIMLRS NQSFSLDDMS WTCGSEDFKY KVDDVTQAGH
NMELLEPLVK FQVGLKKLDL HEEEHVLLMA ICILSPDRPG LQDKALVESI QDRLSSTLQT
YILCKHPPPG SRLLYAKMIQ KLADLRSLNE EHSKQYRSIS FLPEHSMKLT PLMLEVFSDE
IP
