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P48281 (VDR_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Vitamin D3 receptor

Short name=VDR
Alternative name(s):
1,25-dihydroxyvitamin D3 receptor
Nuclear receptor subfamily 1 group I member 1
Gene names
Name:Vdr
Synonyms:Nr1i1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length422 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Nuclear hormone receptor. Transcription factor that mediates the action of vitamin D3 by controlling the expression of hormone sensitive genes. Regulates transcription of hormone sensitive genes via its association with the WINAC complex, a chromatin-remodeling complex. Recruited to promoters via its interaction with the WINAC complex subunit BAZ1B/WSTF, which mediates the interaction with acetylated histones, an essential step for VDR-promoter association. Plays a central role in calcium homeostasis By similarity.

Subunit structure

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 (in a ligand-dependent manner) with BAZ1B/WSTF. Interacts with SNW1. Interacts with IRX4, the interaction doesn't affect its transactivation activity By similarity.

Subcellular location

Nucleus By similarity.

Induction

By 1,25-dihydroxyvitamin D3 in kidney. Ref.5

Domain

Composed of three domains: a modulating N-terminal domain, a DNA-binding domain and a C-terminal ligand-binding domain By similarity.

Sequence similarities

Belongs to the nuclear hormone receptor family. NR1 subfamily.

Contains 1 nuclear receptor DNA-binding domain.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   DomainZinc-finger
   LigandDNA-binding
Metal-binding
Zinc
   Molecular functionReceptor
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcalcium ion transport

Inferred from mutant phenotype PubMed 11687634. Source: MGI

cell morphogenesis

Inferred from electronic annotation. Source: Ensembl

cellular calcium ion homeostasis

Inferred from mutant phenotype PubMed 9241280. Source: MGI

decidualization

Inferred from electronic annotation. Source: Ensembl

intestinal absorption

Inferred from mutant phenotype PubMed 11687634. Source: MGI

lactation

Inferred from mutant phenotype PubMed 15178742. Source: MGI

mammary gland branching involved in pregnancy

Inferred from mutant phenotype PubMed 15178742. Source: MGI

multicellular organismal development

Inferred from mutant phenotype PubMed 9241280. Source: MGI

negative regulation of keratinocyte proliferation

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription, DNA-templated

Inferred from sequence orthology PubMed 11891224. Source: MGI

organ morphogenesis

Inferred from mutant phenotype PubMed 9241280. Source: MGI

positive regulation of apoptotic process involved in mammary gland involution

Inferred from mutant phenotype PubMed 15178742. Source: MGI

positive regulation of keratinocyte differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

positive regulation of vitamin D 24-hydroxylase activity

Inferred from electronic annotation. Source: Ensembl

regulation of calcidiol 1-monooxygenase activity

Inferred from mutant phenotype PubMed 9295274. Source: BHF-UCL

regulation of transcription, DNA-templated

Inferred from direct assay PubMed 15322135. Source: MGI

skeletal system development

Inferred from mutant phenotype PubMed 9241280. Source: MGI

   Cellular_componentnucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionDNA binding

Inferred from direct assay PubMed 15601870. Source: MGI

calcitriol binding

Inferred from electronic annotation. Source: Ensembl

calcitriol receptor activity

Inferred from electronic annotation. Source: InterPro

ligand-activated sequence-specific DNA binding RNA polymerase II transcription factor activity

Inferred from direct assay PubMed 15322135. Source: MGI

lithocholic acid binding

Inferred from electronic annotation. Source: Ensembl

lithocholic acid receptor activity

Inferred from electronic annotation. Source: Ensembl

sequence-specific DNA binding

Inferred from electronic annotation. Source: InterPro

steroid hormone receptor activity

Inferred from electronic annotation. Source: InterPro

vitamin D response element binding

Inferred from electronic annotation. Source: Ensembl

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Grip1Q925T62EBI-346797,EBI-537752
GTF2BQ004032EBI-346797,EBI-389564From a different organism.
NCOA3Q9Y6Q92EBI-346797,EBI-81196From a different organism.
SNW1Q135732EBI-346797,EBI-632715From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 422422Vitamin D3 receptor
PRO_0000053543

Regions

DNA binding21 – 9676Nuclear receptor
Zinc finger24 – 4421NR C4-type
Zinc finger60 – 8425NR C4-type
Region97 – 18690Hinge
Region187 – 422236Ligand-binding
Region222 – 23211Vitamin D3 binding By similarity
Region241 – 25919Interaction with coactivator LXXLL motif By similarity
Region266 – 2738Vitamin D3 binding By similarity

Sites

Binding site1431Vitamin D3 By similarity
Binding site3001Vitamin D3 By similarity
Binding site3921Vitamin D3 By similarity

Experimental info

Sequence conflict2761L → M in BAA06737. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P48281 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 4614DD4A129F2732

FASTA42247,834
        10         20         30         40         50         60 
MEAMAASTSL PDPGDFDRNV PRICGVCGDR ATGFHFNAMT CEGCKGFFRR SMKRKALFTC 

        70         80         90        100        110        120 
PFNGDCRITK DNRRHCQACR LKRCVDIGMM KEFILTDEEV QRKREMIMKR KEEEALKDSL 

       130        140        150        160        170        180 
RPKLSEEQQH IIAILLDAHH KTYDPTYADF RDFRPPIRAD VSTGSYSPRP TLSFSGDSSS 

       190        200        210        220        230        240 
NSDLYTPSLD MMEPASFSTM DLNEEGSDDP SVTLDLSPLS MLPHLADLVS YSIQKVIGFA 

       250        260        270        280        290        300 
KMIPGFRDLT SDDQIVLLKS SAIEVIMLRS NQSFTLDDMS WDCGSQDYKY DITDVSRAGH 

       310        320        330        340        350        360 
TLELIEPLIK FQVGLKKLNL HEEEHVLLMA ICIVSPDRPG VQDAKLVEAI QDRLSNTLQT 

       370        380        390        400        410        420 
YIRCRHPPPG SHQLYAKMIQ KLADLRSLNE EHSKQYRSLS FQPENSMKLT PLVLEVFGNE 


IS 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and sequencing of the gene encoding the mouse vitamin D receptor."
Kamei Y., Kawada T., Fukuwatari T., Ono T., Kato S., Sugimoto E.
Gene 152:281-282(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J and NOD.
Tissue: Intestine.
[3]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Mammary tumor.
[5]"Klotho, a gene related to a syndrome resembling human premature aging, functions in a negative regulatory circuit of vitamin D endocrine system."
Tsujikawa H., Kurotaki Y., Fujimori T., Fukuda K., Nabeshima Y.
Mol. Endocrinol. 17:2393-2403(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D31969 mRNA. Translation: BAA06737.1.
AK030339 mRNA. Translation: BAC26911.1.
AK154647 mRNA. Translation: BAE32738.1.
CH466550 Genomic DNA. Translation: EDL04218.1.
BC006716 mRNA. Translation: AAH06716.1.
PIRPC4019.
RefSeqNP_033530.2. NM_009504.4.
UniGeneMm.245084.

3D structure databases

ProteinModelPortalP48281.
SMRP48281. Positions 22-106, 124-421.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid204511. 4 interactions.
DIPDIP-31478N.
IntActP48281. 8 interactions.
STRING10090.ENSMUSP00000023119.

Chemistry

BindingDBP48281.
ChEMBLCHEMBL5601.
GuidetoPHARMACOLOGY605.

PTM databases

PhosphoSiteP48281.

Proteomic databases

PRIDEP48281.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000023119; ENSMUSP00000023119; ENSMUSG00000022479.
GeneID22337.
KEGGmmu:22337.
UCSCuc007xlk.1. mouse.

Organism-specific databases

CTD7421.
MGIMGI:103076. Vdr.

Phylogenomic databases

eggNOGNOG283526.
GeneTreeENSGT00720000108423.
HOGENOMHOG000220844.
HOVERGENHBG108655.
InParanoidQ922X0.
KOK08539.
OMAFCQFRPP.
OrthoDBEOG79KPF8.
TreeFamTF316304.

Gene expression databases

ArrayExpressP48281.
BgeeP48281.
CleanExMM_VDR.
GenevestigatorP48281.

Family and domain databases

Gene3D1.10.565.10. 2 hits.
3.30.50.10. 1 hit.
InterProIPR008946. Nucl_hormone_rcpt_ligand-bd.
IPR000536. Nucl_hrmn_rcpt_lig-bd_core.
IPR001723. Str_hrmn_rcpt.
IPR000324. VitD_rcpt.
IPR001628. Znf_hrmn_rcpt.
IPR013088. Znf_NHR/GATA.
[Graphical view]
PfamPF00104. Hormone_recep. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view]
PRINTSPR00398. STRDHORMONER.
PR00047. STROIDFINGER.
PR00350. VITAMINDR.
SMARTSM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view]
SUPFAMSSF48508. SSF48508. 1 hit.
PROSITEPS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSVDR. mouse.
NextBio302589.
PROP48281.
SOURCESearch...

Entry information

Entry nameVDR_MOUSE
AccessionPrimary (citable) accession number: P48281
Secondary accession number(s): Q922X0
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: July 27, 2011
Last modified: April 16, 2014
This is version 123 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot