Swiss-Prot entry
ID VDR_RAT STANDARD; PRT; 423 AA.
AC P13053;
DT 01-JAN-1990 (Rel. 13, Created)
DT 01-JAN-1990 (Rel. 13, Last sequence update)
DT 01-MAY-2005 (Rel. 47, Last annotation update)
DE Vitamin D3 receptor (VDR) (1,25-dihydroxyvitamin D3 receptor).
GN Name=Vdr; Synonyms=Nr1i1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC Muridae; Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RX MEDLINE=89071726; PubMed=2849110 [NCBI, ExPASy, EBI, Israel, Japan];
RA Burmester J.K., Wiese R.J., Maeda N., Deluca H.;
RT "Structure and regulation of the rat 1,25-dihydroxyvitamin D3
RT receptor.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:9499-9502(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE OF 58-423.
RX MEDLINE=88124963; PubMed=2829212 [NCBI, ExPASy, EBI, Israel, Japan];
RA Burmester J.K., Maeda N., Deluca H.F.;
RT "Isolation and expression of rat 1,25-dihydroxyvitamin D3 receptor
RT cDNA.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:1005-1009(1988).
RN [3]
RP INTERACTION WITH NCOA6.
RX MEDLINE=20325329; PubMed=10866662 [NCBI, ExPASy, EBI, Israel, Japan];
RX DOI=10.1128/MCB.20.14.5048-5063.2000;
RA Mahajan M.A., Samuels H.H.;
RT "A new family of nuclear receptor coregulators that integrates nuclear
RT receptor signaling through CBP.";
RL Mol. Cell. Biol. 20:5048-5063(2000).
CC -!- FUNCTION: Nuclear hormone receptor. VDR mediates the action of
CC vitamin D3 by controlling the expression of hormone sensitive
CC genes.
CC -!- SUBUNIT: Interacts with NCOA3 and NCOA6 coactivators, leading to a
CC strong increase of transcription of target genes.
CC -!- SUBCELLULAR LOCATION: Nuclear.
CC -!- DOMAIN: Composed of three domains: a modulating N-terminal domain,
CC a DNA-binding domain and a C-terminal steroid-binding domain.
CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR1
CC subfamily.
CC -!- SIMILARITY: Contains 1 nuclear receptor DNA-binding domain.
CC --------------------------------------------------------------------------
CC This Swiss-Prot entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use as long as its content is in no way modified and this statement is not
CC removed.
CC --------------------------------------------------------------------------
DR EMBL; J04147; AAA41089.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR PIR; A31761; A31761.
DR HSSP; P11473; 1KB2. [HSSP ENTRY / SWISS-3DIMAGE / PDB]
DR SMR; P13053; 21-121.
DR TRANSFAC; T00882; -.
DR Ensembl; ENSRNOG00000008574; Rattus_norvegicus
DR RGD; 3959; Vdr.
DR GO; GO:0000228; C:nuclear chromosome; TAS.
DR GO; GO:0003700; F:transcription factor activity; TAS.
DR GO; GO:0005499; F:vitamin D binding; IMP.
DR GO; GO:0008434; F:vitamin D3 receptor activity; TAS.
DR GO; GO:0008628; P:induction of apoptosis by hormones; IDA.
DR GO; GO:0006357; P:regulation of transcription from Pol II pro...; TAS.
DR InterPro; IPR000536; Hrmon_recept_lig.
DR InterPro; IPR001723; Stdhrmn_receptor.
DR InterPro; IPR008946; Str_ncl_receptor.
DR InterPro; IPR000324; VitD_receptor.
DR InterPro; IPR001628; Znf_C4steroid.
DR InterPro; Graphical view of domain structure.
DR Pfam; PF00104; Hormone_recep; 1.
DR Pfam; PF00105; zf-C4; 1.
DR Pfam; Graphical view of domain structure.
DR PRINTS; PR00398; STRDHORMONER.
DR PRINTS; PR00047; STROIDFINGER.
DR PRINTS; PR00350; VITAMINDR.
DR ProDom; PD000035; Znf_C4steroid; 1.
DR ProDom [Domain structure / List of seq. sharing at least 1 domain ]
DR SMART; SM00430; HOLI; 1.
DR SMART; SM00399; ZnF_C4; 1.
DR PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
DR PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
DR CMR; P13053.
DR HOVERGEN [Family / Alignment / Tree]
DR BLOCKS; P13053.
DR ProtoNet; P13053.
DR ProtoMap; P13053.
DR PRESAGE; P13053.
DR DIP; P13053.
DR ModBase; P13053.
DR SWISS-2DPAGE; GET REGION ON 2D PAGE.
KW DNA-binding; Nuclear protein; Phosphorylation; Receptor;
KW Transcription; Transcription regulation; Zinc-finger.
FT DNA_BIND 24 89 Nuclear receptor-type.
FT ZN_FING 24 44 C4-type.
FT ZN_FING 60 84 C4-type.
FT DOMAIN 90 187 Hinge.
FT DOMAIN 188 423 Ligand-binding.
SQ 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
//