VDR_CHICK
ID VDR_CHICK Reviewed; 451 AA.
AC O42392;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 139.
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 Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B).
RC STRAIN=Leghorn; TISSUE=Kidney;
RX PubMed=9056239; DOI=10.1006/abbi.1996.9864;
RA Lu Z., Hanson K., Deluca H.F.;
RT "Cloning and origin of the two forms of chicken vitamin D receptor.";
RL Arch. Biochem. Biophys. 339:99-106(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 45-114.
RX PubMed=3029866; DOI=10.1126/science.3029866;
RA McDonnell D.P., Mangelsdorf D.J., Pike J.W., Haussler M.R., O'Malley B.W.;
RT "Molecular cloning of complementary DNA encoding the avian receptor for
RT vitamin D.";
RL Science 235:1214-1217(1987).
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=O42392-1; Sequence=Displayed;
CC Name=B;
CC IsoId=O42392-2; Sequence=VSP_018771;
CC -!- TISSUE SPECIFICITY: Expressed in kidney and intestine.
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; AF011356; AAB62579.1; -; mRNA.
DR PIR; A60912; A60912.
DR RefSeq; NP_990429.1; NM_205098.1. [O42392-1]
DR AlphaFoldDB; O42392; -.
DR SMR; O42392; -.
DR BioGRID; 676260; 1.
DR STRING; 9031.ENSGALP00000043420; -.
DR BindingDB; O42392; -.
DR ChEMBL; CHEMBL2353; -.
DR DrugCentral; O42392; -.
DR GeneID; 395988; -.
DR KEGG; gga:395988; -.
DR CTD; 7421; -.
DR VEuPathDB; HostDB:geneid_395988; -.
DR eggNOG; KOG3575; Eukaryota.
DR InParanoid; O42392; -.
DR OrthoDB; 297114at2759; -.
DR PhylomeDB; O42392; -.
DR PRO; PR:O42392; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005901; C:caveola; IDA:AgBase.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:AgBase.
DR GO; GO:0005886; C:plasma membrane; TAS:AgBase.
DR GO; GO:0004879; F:nuclear receptor activity; ISS:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0005499; F:vitamin D binding; IDA:AgBase.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006816; P:calcium ion transport; TAS:AgBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0033280; P:response to vitamin D; TAS:AgBase.
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..451
FT /note="Vitamin D3 receptor"
FT /id="PRO_0000019933"
FT DOMAIN 150..447
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT DNA_BIND 44..112
FT /note="Nuclear receptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 47..67
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 83..107
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT REGION 113..149
FT /note="Hinge"
FT /evidence="ECO:0000250|UniProtKB:P11473"
FT REGION 120..149
FT /note="Hinge"
FT /evidence="ECO:0000250|UniProtKB:P11473"
FT REGION 270..288
FT /note="Interaction with coactivator LXXLL motif"
FT /evidence="ECO:0000250|UniProtKB:P13053"
FT MOTIF 440..448
FT /note="9aaTAD"
FT /evidence="ECO:0000250|UniProtKB:P11473"
FT BINDING 251..261
FT /ligand="calciol"
FT /ligand_id="ChEBI:CHEBI:28940"
FT /evidence="ECO:0000250|UniProtKB:P11473"
FT BINDING 295..302
FT /ligand="calciol"
FT /ligand_id="ChEBI:CHEBI:28940"
FT /evidence="ECO:0000250|UniProtKB:P11473"
FT BINDING 329
FT /ligand="calciol"
FT /ligand_id="ChEBI:CHEBI:28940"
FT /evidence="ECO:0000250|UniProtKB:P11473"
FT BINDING 421
FT /ligand="calciol"
FT /ligand_id="ChEBI:CHEBI:28940"
FT /evidence="ECO:0000250|UniProtKB:P11473"
FT VAR_SEQ 14
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000303|PubMed:9056239"
FT /id="VSP_018771"
SQ SEQUENCE 451 AA; 51300 MW; 2078B6A6C8D8E5FC CRC64;
MSELRGSWDE QQQSMAYLPD ADMDTVAAST SLPDPAGDFD RNVPRICGVC GDRATGFHFN
AMTCEGCKGF FRRSMKRKAM FTCPFNGDCK ITKDNRRHCQ ACRLKRCVDI GMMKEFILTD
EEVQRKREMI LKRKEEEALK ESLKPKLSEE QQKVIDTLLE AHHKTFDTTY SDFNKFRPPV
RSKFSSRMAT HSSSVVSQDF SSEDSNDVFG SDAFAAFPEP MEPQMFSNLD LSEESDESPS
MNIELPHLPM LPHLADLVSY SIQKVIGFAK MIPGFRDLTA EDQIALLKSS AIEVIMLRSN
QSFTMEDMSW TCGSNDFKYK VSDVTQAGHS MDLLEPLVKF QVGLKKLNLH EEEHVLLMAI
CILSPDRPGV QDTSLVESIQ DRLSDILQTY IRCRHPPPGS RLLYAKMIQK LADLRSLNEE
HSKQYRCLSF QPEHSMQLTP LVLEVFGNEI S
