Vitamin D3 receptor - Mus musculus (Mouse)

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Reviewed, UniProtKB/Swiss-Prot P48281 (VDR_MOUSE)

Last modified June 16, 2009. Version 77. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended 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

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

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Protein attributes

Sequence length	422 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

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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 By similarity.
Subcellular location	Nucleus By similarity.
Induction	By 1,25-dihydroxyvitamin D₃ in kidney. Ref.2
Domain	Composed of three domains: a modulating N-terminal domain, a DNA-binding domain and a C-terminal steroid-binding domain By similarity.
Sequence similarities	Belongs to the nuclear hormone receptor family. NR1 subfamily. Contains 1 nuclear receptor DNA-binding domain.

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Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Domain	Zinc-finger
Ligand	DNA-binding Metal-binding Zinc
Molecular function	Receptor
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	calcium ion transport Inferred from mutant phenotype. Source: MGI cellular calcium ion homeostasis Inferred from mutant phenotype. Source: MGI intestinal absorption Inferred from mutant phenotype. Source: MGI organ morphogenesis Inferred from mutant phenotype. Source: MGI regulation of calcidiol 1-monooxygenase activity Inferred from mutant phenotype. Source: UniProtKB regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW skeletal system development Inferred from mutant phenotype. Source: MGI transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	protein binding Inferred from physical interaction. Source: UniProtKB sequence-specific DNA binding Inferred from electronic annotation. Source: InterPro steroid hormone receptor activity Inferred from electronic annotation. Source: InterPro transcription factor activity Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 422

422

Vitamin D3 receptor

PRO_0000053543

Regions

DNA binding

21 – 96

Nuclear receptor

Zinc finger

24 – 44

NR C4-type

Zinc finger

60 – 84

NR C4-type

Region

97 – 186

Hinge

Region

187 – 422

236

Ligand-binding

Region

222 – 232

Vitamin D3 binding By similarity

Region

241 – 259

with Interaction with coactivator LXXLL motif By similarity

Region

266 – 273

Vitamin D3 binding By similarity

Sites

Binding site

143

Vitamin D3 By similarity

Binding site

300

Vitamin D3 By similarity

Binding site

392

Vitamin D3 By similarity

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Sequences

Sequence

Length

Mass (Da)

Tools

P48281-1 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: 4704CC8172445732
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FASTA

422

47,852

        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 NQSFTMDDMS 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

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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: 7835717] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"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: 14528024] [Abstract] Cited for: INDUCTION.
+	Additional computationally mapped references.

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Cross-references

Sequence databases
	D31969 mRNA. Translation: BAA06737.1.
IPI	IPI00311693.
PIR	PC4019.
UniGene	Mm.245084
3D structure databases
HSSP	HSSP built from PDB template 1KB2 based on UniProtKB P11473.
SMR	P48281. Positions 21-121, 165-418.
ModBase	Search...
Protein-protein interaction databases
IntAct	P48281. 1 interaction.
PTM databases
PhosphoSite	P48281.
Genome annotation databases
Ensembl	ENSMUSG00000022479. Mus musculus. [Contig view]
Organism-specific databases
MGI	MGI:103076. Vdr.
Phylogenomic databases
HOGENOM	P48281.
HOVERGEN	P48281.
Gene expression databases
ArrayExpress	P48281.
Bgee	P48281.
CleanEx	MM_VDR.
GermOnline	ENSMUSG00000022479. Mus musculus.
Family and domain databases
InterPro	IPR008946. 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]
Gene3D	G3DSA:1.10.565.10. Nucl_hrmn_rcpt_lig_bd. 1 hit. G3DSA:3.30.50.10. Znf_NHR/GATA. 1 hit.
Pfam	PF00104. Hormone_recep. 1 hit. PF00105. zf-C4. 1 hit. [Graphical view]
PRINTS	PR00398. STRDHORMONER. PR00047. STROIDFINGER. PR00350. VITAMINDR.
ProDom	PD000035. Znf_C4steroid. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00430. HOLI. 1 hit. SM00399. ZnF_C4. 1 hit. [Graphical view]
PROSITE	PS00031. NUCLEAR_REC_DBD_1. 1 hit. PS51030. NUCLEAR_REC_DBD_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
SOURCE	Search...

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Entry information

Entry name

VDR_MOUSE

Accession

Primary (citable) accession number: P48281

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	February 1, 1996
Last modified:	June 16, 2009
This is version 77 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents