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Vitamin D3 receptor (VDR) (1,25-dihydroxyvitamin D3 receptor) (Nuclear receptor subfamily 1 group I member 1)

 VDR_RAT                 Reviewed;         423 AA.
P13053;
01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
01-JAN-1990, sequence version 1.
31-JAN-2018, entry version 161.
RecName: Full=Vitamin D3 receptor;
Short=VDR;
AltName: Full=1,25-dihydroxyvitamin D3 receptor;
AltName: Full=Nuclear receptor subfamily 1 group I member 1;
Name=Vdr; Synonyms=Nr1i1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
PubMed=2849110; DOI=10.1073/pnas.85.24.9499;
Burmester J.K., Wiese R.J., Maeda N., Deluca H.;
"Structure and regulation of the rat 1,25-dihydroxyvitamin D3
receptor.";
Proc. Natl. Acad. Sci. U.S.A. 85:9499-9502(1988).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 58-423.
TISSUE=Kidney;
PubMed=2829212; DOI=10.1073/pnas.85.4.1005;
Burmester J.K., Maeda N., Deluca H.F.;
"Isolation and expression of rat 1,25-dihydroxyvitamin D3 receptor
cDNA.";
Proc. Natl. Acad. Sci. U.S.A. 85:1005-1009(1988).
[3]
INTERACTION WITH NCOA6.
PubMed=10866662; DOI=10.1128/MCB.20.14.5048-5063.2000;
Mahajan M.A., Samuels H.H.;
"A new family of nuclear receptor coregulators that integrates nuclear
receptor signaling through CBP.";
Mol. Cell. Biol. 20:5048-5063(2000).
[4]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 116-423 IN COMPLEXES WITH
VITAMIN D3 ANALOGS AND MED1.
PubMed=15065852; DOI=10.1021/bi036056y;
Vanhooke J.L., Benning M.M., Bauer C.B., Pike J.W., DeLuca H.F.;
"Molecular structure of the rat vitamin D receptor ligand binding
domain complexed with 2-carbon-substituted vitamin D3 hormone
analogues and a LXXLL-containing coactivator peptide.";
Biochemistry 43:4101-4110(2004).
[5]
X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS) OF 116-423 IN COMPLEXES WITH
VITAMIN D3 ANALOGS AND MED1, AND FUNCTION.
PubMed=17227670; DOI=10.1016/j.abb.2006.11.029;
Vanhooke J.L., Tadi B.P., Benning M.M., Plum L.A., DeLuca H.F.;
"New analogs of 2-methylene-19-nor-(20S)-1,25-dihydroxyvitamin D3 with
conformationally restricted side chains: evaluation of biological
activity and structural determination of VDR-bound conformations.";
Arch. Biochem. Biophys. 460:161-165(2007).
-!- FUNCTION: Nuclear receptor for calcitriol, the active form of
vitamin D3 which mediates the action of this vitamin on cells.
Enters the nucleus upon vitamin D3 binding where it forms
heterodimers with the retinoid X receptor/RXR. The VDR-RXR
heterodimers bind to specific response elements on DNA and
activate the transcription of vitamin D3-responsive target genes.
Recruited to promoters via its interaction with BAZ1B/WSTF which
mediates the interaction with acetylated histones, an essential
step for VDR-promoter association. Plays a central role in calcium
homeostasis. {ECO:0000250|UniProtKB:P11473}.
-!- SUBUNIT: Homodimer in the absence of bound vitamin D3. Heterodimer
with RXRA after vitamin D3 binding. Interacts with SMAD3.
Interacts with MED1, NCOA1, NCOA2, NCOA3 and NCOA6 coactivators,
leading to a strong increase of transcription of target genes.
Interacts with the corepressor NCOR1. Interacts (in a ligand-
dependent manner) with BAZ1B/WSTF. Interacts with SNW1. Interacts
with IRX4, the interaction doesn't affect its transactivation
activity. {ECO:0000250|UniProtKB:P11473}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
ProRule:PRU00407}. Cytoplasm {ECO:0000250|UniProtKB:P11473}.
Note=Localizes mainly to the nucleus. Localization to the nucleus
is enhanced by vitamin D3. {ECO:0000250|UniProtKB:P11473}.
-!- TISSUE SPECIFICITY: Detected in intestine and kidney.
{ECO:0000269|PubMed:2849110}.
-!- DOMAIN: Composed of three domains: a modulating N-terminal domain,
a DNA-binding domain and a C-terminal ligand-binding domain.
-!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR1
subfamily. {ECO:0000305}.
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EMBL; J04147; AAA41089.1; -; mRNA.
PIR; A31761; A31761.
RefSeq; NP_058754.1; NM_017058.1.
UniGene; Rn.10911; -.
PDB; 1RJK; X-ray; 1.99 A; A=116-423.
PDB; 1RK3; X-ray; 2.20 A; A=116-423.
PDB; 1RKG; X-ray; 1.90 A; A=116-423.
PDB; 1RKH; X-ray; 2.28 A; A=116-423.
PDB; 2O4J; X-ray; 1.74 A; A=116-423.
PDB; 2O4R; X-ray; 1.98 A; A=116-423.
PDB; 2ZFX; X-ray; 1.99 A; A=116-423.
PDB; 2ZL9; X-ray; 1.90 A; A=116-423.
PDB; 2ZLA; X-ray; 2.00 A; A=116-423.
PDB; 2ZLC; X-ray; 2.00 A; A=116-423.
PDB; 2ZMH; X-ray; 2.10 A; A=116-423.
PDB; 2ZMI; X-ray; 1.70 A; A=116-423.
PDB; 2ZMJ; X-ray; 2.35 A; A=116-423.
PDB; 2ZXM; X-ray; 3.01 A; A=116-423.
PDB; 2ZXN; X-ray; 2.10 A; A=116-423.
PDB; 3A2H; X-ray; 2.50 A; A=116-423.
PDB; 3AFR; X-ray; 2.00 A; A=116-423.
PDB; 3AUN; X-ray; 1.81 A; A=116-423.
PDB; 3VJS; X-ray; 1.93 A; A=116-423.
PDB; 3VJT; X-ray; 2.00 A; A=116-423.
PDB; 3VRT; X-ray; 2.40 A; A=116-423.
PDB; 3VRU; X-ray; 2.00 A; A=116-423.
PDB; 3VRV; X-ray; 1.90 A; A=116-423.
PDB; 3VRW; X-ray; 2.40 A; A=116-423.
PDB; 3VT3; X-ray; 1.70 A; A=116-423.
PDB; 3VT4; X-ray; 1.90 A; A=116-423.
PDB; 3VT5; X-ray; 2.11 A; A=116-423.
PDB; 3VT6; X-ray; 2.30 A; A=116-423.
PDB; 3VT7; X-ray; 1.65 A; A=116-423.
PDB; 3VT8; X-ray; 2.10 A; A=116-423.
PDB; 3VT9; X-ray; 2.35 A; A=116-423.
PDB; 3VTB; X-ray; 2.00 A; A=116-423.
PDB; 3VTC; X-ray; 1.50 A; A=116-423.
PDB; 3VTD; X-ray; 2.70 A; A=116-423.
PDB; 3W0G; X-ray; 1.94 A; A=121-420.
PDB; 3W0H; X-ray; 1.80 A; A=118-420.
PDB; 3W0I; X-ray; 1.90 A; A=121-420.
PDB; 3W0J; X-ray; 1.84 A; A=121-420.
PDB; 3W5P; X-ray; 1.90 A; A=116-423.
PDB; 3W5Q; X-ray; 1.90 A; A=116-423.
PDB; 3W5R; X-ray; 2.20 A; A=116-423.
PDB; 3W5T; X-ray; 2.29 A; A=116-423.
PDB; 3WT5; X-ray; 1.90 A; A=116-423.
PDB; 3WT6; X-ray; 2.00 A; A=116-423.
PDB; 3WT7; X-ray; 2.40 A; A=116-423.
PDB; 3WTQ; X-ray; 2.10 A; A=116-423.
PDB; 4YNK; X-ray; 2.30 A; A=116-423.
PDB; 5AWJ; X-ray; 2.20 A; A=116-423.
PDB; 5AWK; X-ray; 2.90 A; A=116-423.
PDB; 5B41; X-ray; 1.89 A; A=116-423.
PDB; 5B5B; X-ray; 2.00 A; A/D=116-423.
PDB; 5GIC; X-ray; 2.35 A; A=124-420.
PDB; 5GID; X-ray; 2.15 A; A=124-419.
PDB; 5GIE; X-ray; 2.39 A; A/D=117-419.
PDB; 5H1E; X-ray; 2.60 A; A=116-423.
PDBsum; 1RJK; -.
PDBsum; 1RK3; -.
PDBsum; 1RKG; -.
PDBsum; 1RKH; -.
PDBsum; 2O4J; -.
PDBsum; 2O4R; -.
PDBsum; 2ZFX; -.
PDBsum; 2ZL9; -.
PDBsum; 2ZLA; -.
PDBsum; 2ZLC; -.
PDBsum; 2ZMH; -.
PDBsum; 2ZMI; -.
PDBsum; 2ZMJ; -.
PDBsum; 2ZXM; -.
PDBsum; 2ZXN; -.
PDBsum; 3A2H; -.
PDBsum; 3AFR; -.
PDBsum; 3AUN; -.
PDBsum; 3VJS; -.
PDBsum; 3VJT; -.
PDBsum; 3VRT; -.
PDBsum; 3VRU; -.
PDBsum; 3VRV; -.
PDBsum; 3VRW; -.
PDBsum; 3VT3; -.
PDBsum; 3VT4; -.
PDBsum; 3VT5; -.
PDBsum; 3VT6; -.
PDBsum; 3VT7; -.
PDBsum; 3VT8; -.
PDBsum; 3VT9; -.
PDBsum; 3VTB; -.
PDBsum; 3VTC; -.
PDBsum; 3VTD; -.
PDBsum; 3W0G; -.
PDBsum; 3W0H; -.
PDBsum; 3W0I; -.
PDBsum; 3W0J; -.
PDBsum; 3W5P; -.
PDBsum; 3W5Q; -.
PDBsum; 3W5R; -.
PDBsum; 3W5T; -.
PDBsum; 3WT5; -.
PDBsum; 3WT6; -.
PDBsum; 3WT7; -.
PDBsum; 3WTQ; -.
PDBsum; 4YNK; -.
PDBsum; 5AWJ; -.
PDBsum; 5AWK; -.
PDBsum; 5B41; -.
PDBsum; 5B5B; -.
PDBsum; 5GIC; -.
PDBsum; 5GID; -.
PDBsum; 5GIE; -.
PDBsum; 5H1E; -.
ProteinModelPortal; P13053; -.
SMR; P13053; -.
BioGrid; 246986; 5.
MINT; MINT-236433; -.
STRING; 10116.ENSRNOP00000011601; -.
BindingDB; P13053; -.
ChEMBL; CHEMBL3150; -.
GuidetoPHARMACOLOGY; 605; -.
PhosphoSitePlus; P13053; -.
PaxDb; P13053; -.
GeneID; 24873; -.
KEGG; rno:24873; -.
UCSC; RGD:3959; rat.
CTD; 7421; -.
RGD; 3959; Vdr.
eggNOG; KOG3575; Eukaryota.
eggNOG; ENOG410XRZC; LUCA.
HOGENOM; HOG000220844; -.
HOVERGEN; HBG108655; -.
InParanoid; P13053; -.
KO; K08539; -.
PhylomeDB; P13053; -.
EvolutionaryTrace; P13053; -.
PRO; PR:P13053; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005829; C:cytosol; IDA:RGD.
GO; GO:0001651; C:dense fibrillar component; IDA:RGD.
GO; GO:0000791; C:euchromatin; IDA:RGD.
GO; GO:0000792; C:heterochromatin; IDA:RGD.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
GO; GO:0005720; C:nuclear heterochromatin; IDA:RGD.
GO; GO:0016363; C:nuclear matrix; IDA:RGD.
GO; GO:0005634; C:nucleus; ISO:RGD.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
GO; GO:0043235; C:receptor complex; ISO:RGD.
GO; GO:0090575; C:RNA polymerase II transcription factor complex; ISO:RGD.
GO; GO:0030315; C:T-tubule; IDA:RGD.
GO; GO:1902098; F:calcitriol binding; IDA:RGD.
GO; GO:0008434; F:calcitriol receptor activity; IDA:RGD.
GO; GO:0003677; F:DNA binding; ISO:RGD.
GO; GO:0003700; F:DNA binding transcription factor activity; TAS:RGD.
GO; GO:1902121; F:lithocholic acid binding; ISO:RGD.
GO; GO:0038186; F:lithocholic acid receptor activity; ISO:RGD.
GO; GO:0004879; F:nuclear receptor activity; ISO:RGD.
GO; GO:0046965; F:retinoid X receptor binding; ISO:RGD.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:RGD.
GO; GO:0003707; F:steroid hormone receptor activity; IEA:InterPro.
GO; GO:0005499; F:vitamin D binding; IDA:RGD.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0007568; P:aging; IEP:RGD.
GO; GO:0009887; P:animal organ morphogenesis; ISO:RGD.
GO; GO:0097190; P:apoptotic signaling pathway; IDA:RGD.
GO; GO:0038183; P:bile acid signaling pathway; ISO:RGD.
GO; GO:0006816; P:calcium ion transport; ISO:RGD.
GO; GO:0000902; P:cell morphogenesis; ISO:RGD.
GO; GO:0006874; P:cellular calcium ion homeostasis; ISO:RGD.
GO; GO:1904646; P:cellular response to amyloid-beta; IEP:RGD.
GO; GO:0071305; P:cellular response to vitamin D; IEP:RGD.
GO; GO:0046697; P:decidualization; ISO:RGD.
GO; GO:0007507; P:heart development; IEP:RGD.
GO; GO:0050892; P:intestinal absorption; ISO:RGD.
GO; GO:0007595; P:lactation; ISO:RGD.
GO; GO:0060745; P:mammary gland branching involved in pregnancy; ISO:RGD.
GO; GO:0007275; P:multicellular organism development; ISO:RGD.
GO; GO:0008285; P:negative regulation of cell proliferation; ISO:RGD.
GO; GO:0010839; P:negative regulation of keratinocyte proliferation; ISO:RGD.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; ISO:RGD.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:RGD.
GO; GO:0060058; P:positive regulation of apoptotic process involved in mammary gland involution; ISO:RGD.
GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
GO; GO:0045618; P:positive regulation of keratinocyte differentiation; ISO:RGD.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; ISO:RGD.
GO; GO:0010980; P:positive regulation of vitamin D 24-hydroxylase activity; ISO:RGD.
GO; GO:0060558; P:regulation of calcidiol 1-monooxygenase activity; ISO:RGD.
GO; GO:0051924; P:regulation of calcium ion transport; IDA:RGD.
GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; TAS:RGD.
GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:RGD.
GO; GO:0051592; P:response to calcium ion; IEP:RGD.
GO; GO:0032355; P:response to estradiol; IEP:RGD.
GO; GO:0001501; P:skeletal system development; ISO:RGD.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0070561; P:vitamin D receptor signaling pathway; ISO:RGD.
Gene3D; 1.10.565.10; -; 1.
Gene3D; 3.30.50.10; -; 1.
InterPro; IPR035500; NHR_like_dom_sf.
InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
InterPro; IPR001723; Nuclear_hrmn_rcpt.
InterPro; IPR000324; VitD_rcpt.
InterPro; IPR001628; Znf_hrmn_rcpt.
InterPro; IPR013088; Znf_NHR/GATA.
Pfam; PF00104; Hormone_recep; 1.
Pfam; PF00105; zf-C4; 1.
PRINTS; PR00398; STRDHORMONER.
PRINTS; PR00047; STROIDFINGER.
PRINTS; PR00350; VITAMINDR.
SMART; SM00430; HOLI; 1.
SMART; SM00399; ZnF_C4; 1.
SUPFAM; SSF48508; SSF48508; 1.
PROSITE; PS51843; NR_LBD; 1.
PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytoplasm; DNA-binding;
Metal-binding; Nucleus; Receptor; Reference proteome; Transcription;
Transcription regulation; Zinc; Zinc-finger.
CHAIN 1 423 Vitamin D3 receptor.
/FTId=PRO_0000053544.
DOMAIN 127 419 NR LBD. {ECO:0000255|PROSITE-
ProRule:PRU01189}.
DNA_BIND 24 89 Nuclear receptor. {ECO:0000255|PROSITE-
ProRule:PRU00407}.
ZN_FING 24 44 NR C4-type. {ECO:0000255|PROSITE-
ProRule:PRU00407}.
ZN_FING 60 84 NR C4-type. {ECO:0000255|PROSITE-
ProRule:PRU00407}.
REGION 90 126 Hinge.
REGION 223 233 Vitamin D3 binding.
REGION 242 260 Interaction with coactivator LXXLL motif.
REGION 267 274 Vitamin D3 binding.
BINDING 143 143 Vitamin D3.
BINDING 301 301 Vitamin D3.
BINDING 393 393 Vitamin D3.
HELIX 116 119 {ECO:0000244|PDB:3VT3}.
HELIX 126 142 {ECO:0000244|PDB:3VTC}.
HELIX 148 152 {ECO:0000244|PDB:3VTC}.
TURN 219 222 {ECO:0000244|PDB:3VT3}.
HELIX 223 241 {ECO:0000244|PDB:3VTC}.
HELIX 247 249 {ECO:0000244|PDB:3VTC}.
HELIX 252 270 {ECO:0000244|PDB:3VTC}.
HELIX 271 273 {ECO:0000244|PDB:3VTC}.
STRAND 274 276 {ECO:0000244|PDB:3VTD}.
TURN 277 280 {ECO:0000244|PDB:3VTC}.
STRAND 281 283 {ECO:0000244|PDB:3VTC}.
HELIX 287 289 {ECO:0000244|PDB:3VTC}.
STRAND 290 292 {ECO:0000244|PDB:3VTD}.
HELIX 293 297 {ECO:0000244|PDB:3VTC}.
TURN 298 300 {ECO:0000244|PDB:3VTC}.
HELIX 303 317 {ECO:0000244|PDB:3VTC}.
HELIX 323 334 {ECO:0000244|PDB:3VTC}.
STRAND 337 339 {ECO:0000244|PDB:5H1E}.
HELIX 345 366 {ECO:0000244|PDB:3VTC}.
TURN 369 374 {ECO:0000244|PDB:3VTC}.
HELIX 375 401 {ECO:0000244|PDB:3VTC}.
HELIX 404 407 {ECO:0000244|PDB:3VTC}.
HELIX 412 418 {ECO:0000244|PDB:3VTC}.
SEQUENCE 423 AA; 47814 MW; 1A0E519A9DCCE990 CRC64;
MEATAASTSL PDPGDFDRNV PRICGVCGDR ATGFHFNAMT CEGCKGFFRR SMKRKALFTC
PFNGDCRITK DNRRHCQACR LKRCVDIGMM KEFILTDEEV QRKREMIMKR KEEEALKDSL
RPKLSEEQQH IIAILLDAHH KTYDPTYADF RDFRPPVRMD GSTGSYSPRP TLSFSGNSSS
SSSDLYTTSL DMMEPSGFSN LDLNGEDSDD PSVTLDLSPL SMLPHLADLV SYSIQKVIGF
AKMIPGFRDL TSDDQIVLLK SSAIEVIMLR SNQSFTMDDM SWDCGSQDYK YDVTDVSKAG
HTLELIEPLI KFQVGLKKLN LHEEEHVLLM AICIVSPDRP GVQDAKLVEA IQDRLSNTLQ
TYIRCRHPPP GSHQLYAKMI QKLADLRSLN EEHSKQYRSL SFQPENSMKL TPLVLEVFGN
EIS


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E2042r ELISA kit Bar,Bile acid receptor,Farnesoid X-activated receptor,Farnesol receptor HRR-1,Fxr,Nr1h4,Nuclear receptor subfamily 1 group H member 4,Rat,Rattus norvegicus,Retinoid X receptor-interacting p 96T


 

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