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A3RGC1 (VDR_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 53. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·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
OrganismSus scrofa (Pig) [Reference proteome]
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus

Protein attributes

Sequence length427 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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.

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 electronic annotation. Source: Ensembl

cell morphogenesis

Inferred from electronic annotation. Source: Ensembl

cellular calcium ion homeostasis

Inferred from electronic annotation. Source: Ensembl

decidualization

Inferred from electronic annotation. Source: Ensembl

intestinal absorption

Inferred from electronic annotation. Source: Ensembl

lactation

Inferred from electronic annotation. Source: Ensembl

mammary gland branching involved in pregnancy

Inferred from electronic annotation. Source: Ensembl

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

organ morphogenesis

Inferred from electronic annotation. Source: Ensembl

positive regulation of apoptotic process involved in mammary gland involution

Inferred from electronic annotation. Source: Ensembl

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 electronic annotation. Source: Ensembl

skeletal system development

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentnucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncalcitriol binding

Inferred from electronic annotation. Source: Ensembl

calcitriol receptor activity

Inferred from electronic annotation. Source: InterPro

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...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 427427Vitamin D3 receptor
PRO_0000337877

Regions

DNA binding21 – 9676Nuclear receptor
Zinc finger24 – 4421NR C4-type
Zinc finger60 – 7920NR C4-type
Region97 – 19195Hinge
Region192 – 427236Ligand-binding
Region227 – 23711Vitamin D3 binding By similarity
Region246 – 26419Interaction with coactivator LXXLL motif By similarity
Region271 – 2788Vitamin D3 binding By similarity
Compositional bias168 – 22558Ser-rich

Sites

Binding site1431Vitamin D3 By similarity
Binding site3051Vitamin D3 By similarity
Binding site3971Vitamin D3 By similarity

Sequences

Sequence LengthMass (Da)Tools
A3RGC1 [UniParc].

Last modified April 3, 2007. Version 1.
Checksum: 79670A39FE013858

FASTA42748,128
        10         20         30         40         50         60 
MEATAASTSL PDPGDFDRNV PRICGVCGDR ATGFHFNAMT CEGCKGFFRR SMKRKALFTC 

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

       130        140        150        160        170        180 
RPKLSEEQQR IIAILLDAHH KTYDPTYADF GQFRPPVRGD EEEGTLPSRS SSAHAPSFSG 

       190        200        210        220        230        240 
SSSSSCSDQY TSSPDTMEPA SFSHLDLSEE DSDDPSVTLD LSQLSMLPHL ADLVSYSIQK 

       250        260        270        280        290        300 
VIGFAKMIPG FRDLTAEDQI VLLKSSAIEV IMLRSNQSFT MDDMSWTCGS RDYKYQVSDV 

       310        320        330        340        350        360 
AKAGHSLELI EPLIKFQVGL KKLNLHEEEH VLLMAICIVS PDRPGVQDPT LIEAIQDRLS 

       370        380        390        400        410        420 
NTLQTYIRCR HPPPGSHLLY AKMIQKLADL RSLNEEHSKQ YRCLSFQPEC SMKLTPLVLE 


VFGNEIS 

« Hide

References

[1]"Vitamin D receptor characterization."
Fernandez A.I., Silio L., Rodriguez C., Ovilo C.
Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
EF405627 mRNA. Translation: ABN80095.1.
RefSeqNP_001090883.1. NM_001097414.1.
UniGeneSsc.51953.

3D structure databases

ProteinModelPortalA3RGC1.
SMRA3RGC1. Positions 21-423.
ModBaseSearch...
MobiDBSearch...

Chemistry

ChEMBLCHEMBL5304.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSSSCT00000032274; ENSSSCP00000019810; ENSSSCG00000020864.
GeneID396628.
KEGGssc:396628.

Organism-specific databases

CTD7421.

Phylogenomic databases

GeneTreeENSGT00720000108423.
HOVERGENHBG108655.
KOK08539.
OMAFCQFRPP.
OrthoDBEOG79KPF8.
TreeFamTF316304.

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...

Entry information

Entry nameVDR_PIG
AccessionPrimary (citable) accession number: A3RGC1
Entry history
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: April 3, 2007
Last modified: April 16, 2014
This is version 53 of the entry and version 1 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