P11473 (VDR_HUMAN) Reviewed, UniProtKB/Swiss-Prot

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

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	427 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Ref.14 Ref.15 Ref.20 Ref.21
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. Ref.11 Ref.12 Ref.13 Ref.14 Ref.17 Ref.19 Ref.20
Subcellular location	Nucleus.
Domain	Composed of three domains: a modulating N-terminal domain, a DNA-binding domain and a C-terminal ligand-binding domain.
Polymorphism	Genetic variations in VDR may determine Mycobacterium tuberculosis susceptibility [MIM:607948].
Involvement in disease	Rickets vitamin D-dependent 2A (VDDR2A) [MIM:277440]: A disorder of vitamin D metabolism resulting in severe rickets, hypocalcemia and secondary hyperparathyroidism. Most patients have total alopecia in addition to rickets. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.22 Ref.23 Ref.24 Ref.25 Ref.26 Ref.27 Ref.28 Ref.29 Ref.30 Ref.31
Sequence similarities	Belongs to the nuclear hormone receptor family. NR1 subfamily. Contains 1 nuclear receptor DNA-binding domain.
Caution	It is uncertain whether Met-1 or Met-4 is the initiator.
Sequence caution	The sequence AAP88938.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Polymorphism
Disease	Disease mutation
Domain	Zinc-finger
Ligand	DNA-binding Metal-binding Zinc
Molecular function	Receptor
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell morphogenesis Inferred from mutant phenotype PubMed 17223341. Source: UniProtKB decidualization Inferred from expression pattern PubMed 16720713. Source: BHF-UCL negative regulation of keratinocyte proliferation Inferred from mutant phenotype PubMed 17223341. Source: UniProtKB negative regulation of transcription from RNA polymerase II promoter Inferred from direct assay PubMed 17426122. Source: BHF-UCL positive regulation of keratinocyte differentiation Inferred from mutant phenotype PubMed 17082781. Source: UniProtKB positive regulation of transcription from RNA polymerase II promoter Inferred from mutant phenotype PubMed 17082781PubMed 17254542. Source: UniProtKB positive regulation of vitamin D 24-hydroxylase activity Inferred from direct assay PubMed 16549446. Source: BHF-UCL regulation of calcidiol 1-monooxygenase activity Inferred from sequence or structural similarity. Source: BHF-UCL transcription initiation from RNA polymerase II promoter Traceable author statement. Source: Reactome
Cellular_component	nucleoplasm Traceable author statement. Source: Reactome
Molecular_function	DNA binding Inferred from direct assay PubMed 11891224. Source: MGI sequence-specific DNA binding Inferred from electronic annotation. Source: InterPro steroid hormone receptor activity Inferred from electronic annotation. Source: InterPro vitamin D3 receptor activity Inferred from direct assay PubMed 17082781. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Ncoa6	Q9JLI4	2	EBI-286357,EBI-286271	From a different organism.
PTPN3	P26045	4	EBI-286357,EBI-1047946
SNW1	Q13573	5	EBI-286357,EBI-632715
TP53	P04637	6	EBI-286357,EBI-366083

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 427

427

Vitamin D3 receptor

PRO_0000053542

Regions

DNA binding

21 – 96

76

Nuclear receptor

Zinc finger

24 – 44

21

NR C4-type

Zinc finger

60 – 84

25

NR C4-type

Region

97 – 191

95

Hinge

Region

192 – 427

236

Ligand-binding

Region

227 – 237

11

Vitamin D3 binding

Region

271 – 278

8

Vitamin D3 binding

Sites

Binding site

143

1

Vitamin D3

Binding site

305

1

Vitamin D3

Binding site

397

1

Vitamin D3

Natural variations

Natural variant

33

1

G → D in VDDR2A. Ref.22

VAR_004656

Natural variant

35

1

H → Q in VDDR2A. Ref.23

VAR_004657

Natural variant

45

1

K → E in VDDR2A. Ref.28

VAR_004658

Natural variant

46

1

G → D in VDDR2A. Ref.29

VAR_004659

Natural variant

47

1

F → I in VDDR2A. Ref.28

VAR_004660

Natural variant

50

1

R → Q in VDDR2A. Ref.24

VAR_004661

Natural variant

73

1

R → Q in VDDR2A. Ref.22

VAR_004662

Natural variant

80

1

R → Q in VDDR2A. Ref.25 Ref.26

VAR_004663

Natural variant

230

1

L → V. Ref.5
Corresponds to variant rs11574090 [ dbSNP | Ensembl ].

VAR_029309

Natural variant

274

1

R → L in VDDR2A; decreases affinity for ligand by a factor of 1000. Ref.27

VAR_004664

Natural variant

305

1

H → Q in VDDR2A. Ref.31

VAR_004665

Natural variant

314

1

I → S in VDDR2A. Ref.30

VAR_004666

Natural variant

362

1

T → I. Ref.5
Corresponds to variant rs11574115 [ dbSNP | Ensembl ].

VAR_029310

Natural variant

391

1

R → C in VDDR2A. Ref.30

VAR_004667

Experimental info

Mutagenesis

61 – 62

2

PF → AA: Promotes heterodimerization with RXRA; when associated with A-75.

Mutagenesis

75

1

H → A: Promotes heterodimerization with RXRA; when associated with A-61 and A-62. Ref.17

Secondary structure

1

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427

Helix Strand Turn

Details...

Turn

25 – 27

3

Beta strand

33 – 35

3

Beta strand

38 – 40

3

Helix

42 – 53

12

Beta strand

61 – 64

4

Turn

70 – 75

6

Helix

77 – 86

10

Helix

91 – 93

3

Helix

97 – 107

11

Beta strand

108 – 110

3

Turn

111 – 113

3

Helix

126 – 142

17

Helix

150 – 152

3

Helix

217 – 223

7

Helix

227 – 247

21

Helix

251 – 253

3

Helix

256 – 274

19

Helix

275 – 277

3

Turn

281 – 284

4

Beta strand

285 – 287

3

Helix

291 – 293

3

Helix

297 – 301

5

Turn

302 – 304

3

Helix

307 – 321

15

Turn

322 – 324

3

Helix

327 – 338

12

Beta strand

341 – 343

3

Helix

349 – 370

22

Turn

373 – 378

6

Helix

379 – 404

26

Helix

410 – 413

4

Helix

416 – 422

7

Sequences

	Sequence		Length	Mass (Da)
	P11473 [UniParc]. Last modified October 1, 1989. Version 1. Checksum: F95F300D042C4CB7	FASTA	427	48,289
	10 20 30 40 50 60 MEAMAASTSL 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 KTYDPTYSDF CQFRPPVRVN DGGGSHPSRP NSRHTPSFSG 190 200 210 220 230 240 DSSSSCSDHC ITSSDMMDSS SFSNLDLSEE DSDDPSVTLE LSQLSMLPHL ADLVSYSIQK 250 260 270 280 290 300 VIGFAKMIPG FRDLTSEDQI VLLKSSAIEV IMLRSNESFT MDDMSWTCGN QDYKYRVSDV 310 320 330 340 350 360 TKAGHSLELI EPLIKFQVGL KKLNLHEEEH VLLMAICIVS PDRPGVQDAA LIEAIQDRLS 370 380 390 400 410 420 NTLQTYIRCR HPPPGSHLLY AKMIQKLADL RSLNEEHSKQ YRCLSFQPEC SMKLTPLVLE VFGNEIS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and expression of full-length cDNA encoding human vitamin D receptor." Baker A.R., McDonnell D.P., Hughes M., Crisp T.M., Mangelsdorf D.J., Haussler M.R., Pike J.W., Shine J., O'Malley B.W. Proc. Natl. Acad. Sci. U.S.A. 85:3294-3298(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"A single receptor identical with that from intestine/T47D cells mediates the action of 1,25-dihydroxyvitamin D-3 in HL-60 cells." Goto H., Chen K.S., Prahl J.M., Deluca H.F. Biochim. Biophys. Acta 1132:103-108(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	Rae J.L., Shepard A.R. Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Lens epithelium.
[4]	"Structural organization of the human vitamin D receptor chromosomal gene and its promoter." Miyamoto K., Kesterson R.A., Yamamoto H., Taketani Y., Nishiwaki E., Tatsumi S., Inoue Y., Morita K., Takeda E., Pike J.W. Mol. Endocrinol. 11:1165-1179(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]	NIEHS SNPs program Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS VAL-230 AND ILE-362.
[6]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[7]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	"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]. Tissue: Placenta.
[9]	"Vitamin D receptor expression in human lymphocytes. Signal requirements and characterization by western blots and DNA sequencing." Yu X.-P., Mocharla H., Hustmyer F.G., Manolagas S.C. J. Biol. Chem. 266:7588-7595(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 24-90. Tissue: Peripheral blood.
[10]	"Promoter and 3'-untranslated-region haplotypes in the vitamin D receptor gene predispose to osteoporotic fracture: the Rotterdam study." Fang Y., van Meurs J.B., d'Alesio A., Jhamai M., Zhao H., Rivadeneira F., Hofman A., van Leeuwen J.P., Jehan F., Pols H.A., Uitterlinden A.G. Am. J. Hum. Genet. 77:807-823(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 343-427.
[11]	"Nuclear receptor coactivator ACTR is a novel histone acetyltransferase and forms a multimeric activation complex with P/CAF and CBP/p300." Chen H., Lin R.J., Schiltz R.L., Chakravarti D., Nash A., Nagy L., Privalsky M.L., Nakatani Y., Evans R.M. Cell 90:569-580(1997) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH NCOA3.
[12]	"Isolation and characterization of a novel coactivator protein, NCoA-62, involved in vitamin D-mediated transcription." Baudino T.A., Kraichely D.M., Jefcoat S.C. Jr., Winchester S.K., Partridge N.C., Macdonald P.N. J. Biol. Chem. 273:16434-16441(1998) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SNW1.
[13]	"A new family of nuclear receptor coregulators that integrates nuclear receptor signaling through CBP." Mahajan M.A., Samuels H.H. Mol. Cell. Biol. 20:5048-5063(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH NCOA6.
[14]	"Ligand-induced transrepression by VDR through association of WSTF with acetylated histones." Fujiki R., Kim M.-S., Sasaki Y., Yoshimura K., Kitagawa H., Kato S. EMBO J. 24:3881-3894(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH BAZ1B.
[15]	"The crystal structure of the nuclear receptor for vitamin D bound to its natural ligand." Rochel N., Wurtz J.-M., Mitschler A., Klaholz B., Moras D. Mol. Cell 5:173-179(2000) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 118-427 IN COMPLEX WITH DIHYDROXYVITAMIN D3, MASS SPECTROMETRY, FUNCTION.
[16]	"Crystal structures of the vitamin D receptor complexed to superagonist 20-epi ligands." Tocchini-Valentini G., Rochel N., Wurtz J.-M., Mitschler A., Moras D. Proc. Natl. Acad. Sci. U.S.A. 98:5491-5496(2001) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 118-427 IN COMPLEXES WITH VITAMIN D3 AND VITAMIN D3 ANALOGS.
[17]	"Structural basis of VDR-DNA interactions on direct repeat response elements." Shaffer P.L., Gewirth D.T. EMBO J. 21:2242-2252(2002) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 16-125 IN COMPLEX WITH DNA, MUTAGENESIS OF 61-PRO-PHE-62 AND HIS-75, SUBUNIT.
[18]	"Crystal structures of the vitamin D nuclear receptor liganded with the vitamin D side chain analogues calcipotriol and seocalcitol, receptor agonists of clinical importance. Insights into a structural basis for the switching of calcipotriol to a receptor antagonist by further side chain modification." Tocchini-Valentini G., Rochel N., Wurtz J.-M., Moras D. J. Med. Chem. 47:1956-1961(2004) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 188-427 IN COMPLEXES WITH VITAMIN D3 ANALOGS.
[19]	"Structural analysis of RXR-VDR interactions on DR3 DNA." Shaffer P.L., Gewirth D.T. J. Steroid Biochem. Mol. Biol. 89:215-219(2004) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 16-125 OF MUTANT ALA-61/ALA-62/ALA-75 IN COMPLEX WITH RXRA AND DNA, SUBUNIT.
[20]	"Superagonistic action of 14-epi-analogs of 1,25-dihydroxyvitamin D explained by vitamin D receptor-coactivator interaction." Eelen G., Verlinden L., Rochel N., Claessens F., De Clercq P., Vandewalle M., Tocchini-Valentini G., Moras D., Bouillon R., Verstuyf A. Mol. Pharmacol. 67:1566-1573(2005) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 188-427 IN COMPLEX WITH VITAMIN D3 ANALOG, MASS SPECTROMETRY, FUNCTION, INTERACTION WITH NCOA1; NCOA2 AND MED1.
[21]	"Probing a water channel near the A-ring of receptor-bound 1 alpha,25-dihydroxyvitamin D3 with selected 2 alpha-substituted analogues." Hourai S., Fujishima T., Kittaka A., Suhara Y., Takayama H., Rochel N., Moras D. J. Med. Chem. 49:5199-5205(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 188-427 IN COMPLEXES WITH DIHYDROXYVITAMIN D3 AND VITAMIN D3 ANALOGS, FUNCTION.
[22]	"Point mutations in the human vitamin D receptor gene associated with hypocalcemic rickets." Hughes M.R., Malloy P.J., Kieback D.G., Kesterson R.A., Pike J.W., Feldman D., O'Malley B.W. Science 242:1702-1705(1988) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS VDDR2A ASP-33 AND GLN-73.
[23]	"A new point mutation in the deoxyribonucleic acid-binding domain of the vitamin D receptor in a kindred with hereditary 1,25-dihydroxyvitamin D-resistant rickets." Yagi H., Ozono K., Miyake H., Nagashima K., Kuroume T., Pike J.W. J. Clin. Endocrinol. Metab. 76:509-512(1993) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT VDDR2A GLN-35.
[24]	"A unique mutation in the vitamin D receptor gene in three Japanese patients with vitamin D-dependent rickets type II: utility of single-strand conformation polymorphism analysis for heterozygous carrier detection." Saijo T., Ito M., Takeda E., Mahbubul Huq A.H.M., Naito E., Yokota I., Sone T., Pike J.W., Kuroda Y. Am. J. Hum. Genet. 49:668-673(1991) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT VDDR2A GLN-50.
[25]	"A unique point mutation in the human vitamin D receptor chromosomal gene confers hereditary resistance to 1,25-dihydroxyvitamin D3." Sone T., Marx S.J., Liberman U.A., Pike J.W. Mol. Endocrinol. 4:623-631(1990) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT VDDR2A GLN-80.
[26]	"Hereditary 1 alpha,25-dihydroxyvitamin D-resistant rickets resulting from a mutation in the vitamin D receptor deoxyribonucleic acid-binding domain." Malloy P.J., Weisman Y., Feldman D. J. Clin. Endocrinol. Metab. 78:313-316(1994) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT VDDR2A GLN-80.
[27]	"Two mutations in the hormone binding domain of the vitamin D receptor cause tissue resistance to 1,25 dihydroxyvitamin D3." Kristjansson K., Rut A.R., Hewison M., O'Riordan J.L.H., Hughes M.R. J. Clin. Invest. 92:12-16(1993) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT VDDR2A LEU-274.
[28]	"Two mutations causing vitamin D resistant rickets: modelling on the basis of steroid hormone receptor DNA-binding domain crystal structures." Rut A.R., Hewison M., Kristjansson K., Luisi B., Hughes M.R., O'Riordan J.L.H. Clin. Endocrinol. (Oxf.) 41:581-590(1994) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS VDDR2A GLU-45 AND ILE-47.
[29]	"A novel mutation in the deoxyribonucleic acid-binding domain of the vitamin D receptor causes hereditary 1,25-dihydroxyvitamin D-resistant rickets." Lin U.-T., Malloy P.J., Sakati N., Al-Ashwal A., Feldman D. J. Clin. Endocrinol. Metab. 81:2564-2569(1996) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT VDDR2A ASP-46.
[30]	"Vitamin D receptors from patients with resistance to 1,25-dihydroxyvitamin D(3): point mutations confer reduced transactivation in response to ligand and impaired interaction with the retinoid X receptor heterodimeric partner." Whitfield G.K., Selznick S.H., Haussler C.A., Hsieh J.-C., Galligan M.A., Jurutka P.W., Thompson P.D., Lee S.M., Zerwekh J.E., Haussler M.R. Mol. Endocrinol. 10:1617-1631(1996) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS VDDR2A SER-314 AND CYS-391.
[31]	"Hereditary vitamin D resistant rickets caused by a novel mutation in the vitamin D receptor that results in decreased affinity for hormone and cellular hyporesponsiveness." Malloy P.J., Eccleshall T.R., Gross C., van Maldergem L., Bouillon R., Feldman D. J. Clin. Invest. 99:297-304(1997) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT VDDR2A GLN-305.
[32]	"Vitamin D receptor gene variants of BsmI, ApaI, TaqI, and FokI polymorphisms in spinal tuberculosis." Selvaraj P., Kurian S.M., Chandra G., Reetha A.M., Charles N., Narayanan P.R. Clin. Genet. 65:73-76(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN MYCOBACTERIUM TUBERCULOSIS SUSCEPTIBILITY.
+	Additional computationally mapped references.

Web resources

GeneReviews

NIEHS-SNPs

SHMPD

The Singapore human mutation and polymorphism database

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

J03258 mRNA. Translation: AAA61273.1.
X67482 mRNA. Translation: CAA47824.1.
AF026260 mRNA. Translation: AAB95155.1.
AB002168 Genomic DNA. Translation: BAA83389.1.
AY342401 Genomic DNA. Translation: AAP88938.1. Sequence problems.
AK312267 mRNA. Translation: BAG35198.1.
CH471111 Genomic DNA. Translation: EAW57961.1.
BC060832 mRNA. Translation: AAH60832.1.
M65208 mRNA. Translation: AAA61274.1.
AY827087 Genomic DNA. Translation: AAV85448.1.

IPI

IPI00005716.

PIR

A28200.

RefSeq

NP_000367.1. NM_000376.2.
NP_001017535.1. NM_001017535.1.
NP_001017536.1. NM_001017536.1.

UniGene

Hs.524368.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1DB1	X-ray	1.80	A	118-427	[»]
1IE8	X-ray	1.52	A	118-427	[»]
1IE9	X-ray	1.40	A	118-427	[»]
1KB2	X-ray	2.70	A/B	16-125	[»]
1KB4	X-ray	2.80	A/B	16-125	[»]
1KB6	X-ray	2.70	A/B	16-125	[»]
1S0Z	X-ray	2.50	A	118-427	[»]
1S19	X-ray	2.10	A	118-427	[»]
1TXI	X-ray	1.90	A	118-427	[»]
1YNW	X-ray	3.00	A	16-125	[»]
2HAM	X-ray	1.90	A	118-427	[»]
2HAR	X-ray	1.90	A	118-427	[»]
2HAS	X-ray	1.96	A	118-427	[»]
2HB7	X-ray	1.80	A	118-427	[»]
2HB8	X-ray	2.00	A	118-427	[»]
3A2I	X-ray	3.27	A	118-427	[»]
3A2J	X-ray	2.70	A	118-427	[»]
3A3Z	X-ray	1.72	X	118-427	[»]
3A40	X-ray	1.45	X	118-427	[»]
3A78	X-ray	1.90	A	118-427	[»]
3AUQ	X-ray	2.64	A	118-427	[»]
3AUR	X-ray	2.21	A	118-427	[»]
3AX8	X-ray	2.60	A	118-427	[»]
3AZ1	X-ray	1.50	A	120-423	[»]
3AZ2	X-ray	1.69	A	120-423	[»]
3AZ3	X-ray	1.36	A	120-423	[»]
3B0T	X-ray	1.30	A	120-423	[»]
3CS4	X-ray	2.00	A	118-427	[»]
3CS6	X-ray	1.80	A	118-427	[»]
3M7R	X-ray	1.80	A	120-423	[»]
3OGT	X-ray	1.75	A	118-427	[»]
3P8X	X-ray	1.70	A	118-427	[»]
3TKC	X-ray	1.75	A	118-427	[»]
3VHW	X-ray	2.43	A	118-427	[»]
4G2I	X-ray	1.80	A	118-427	[»]

DisProt

DP00184.

ProteinModelPortal

P11473.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-32624N.

IntAct

P11473. 17 interactions.

MINT

MINT-236408.

STRING

9606.ENSP00000229022.

PTM databases

PhosphoSite

P11473.

Polymorphism databases

DMDM

137617.

Proteomic databases

PaxDb

P11473.

PRIDE

P11473.

Protocols and materials databases

DNASU

7421.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000229022; ENSP00000229022; ENSG00000111424.
ENST00000395324; ENSP00000378734; ENSG00000111424.
ENST00000549336; ENSP00000449573; ENSG00000111424.

GeneID

7421.

KEGG

hsa:7421.

UCSC

uc001rql.3. human.

Organism-specific databases

CTD

7421.

GeneCards

GC12M048247.

HGNC

HGNC:12679. VDR.

MIM

277440. phenotype.
601769. gene.
607948. phenotype.

neXtProt

NX_P11473.

Orphanet

93160. Hypocalcemic vitamin D resistant rickets.

PharmGKB

PA37301.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG283526.

HOGENOM

HOG000220844.

HOVERGEN

HBG108655.

InParanoid

P11473.

KO

K08539.

OrthoDB

EOG4J6RR1.

PhylomeDB

P11473.

Enzyme and pathway databases

Pathway_Interaction_DB

smad2_3nuclearpathway. Regulation of nuclear SMAD2/3 signaling.
retinoic_acid_pathway. Retinoic acid receptors-mediated signaling.
rxr_vdr_pathway. RXR and RAR hetrodimerization with other nuclear receptor.

Reactome

REACT_71. Gene Expression.

SignaLink

P11473.

Gene expression databases

ArrayExpress

P11473.

Bgee

P11473.

CleanEx

HS_VDR.

Genevestigator

P11473.

GermOnline

ENSG00000111424. Homo sapiens.

Family and domain databases

Gene3D

1.10.565.10. 2 hits.
3.30.50.10. 1 hit.

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]

Pfam

PF00104. Hormone_recep. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view]

PRINTS

PR00398. STRDHORMONER.
PR00047. STROIDFINGER.
PR00350. VITAMINDR.

SMART

SM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view]

SUPFAM

SSF48508. Str_ncl_receptor. 1 hit.

PROSITE

PS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P11473.

ChEMBL

CHEMBL1977.

ChiTaRS

VDR. human.

DrugBank

DB00146. Calcidiol.
DB02300. Calcipotriol.
DB00136. Calcitriol.
DB01070. Dihydrotachysterol.
DB00153. Ergocalciferol.
DB00910. Paricalcitol.

EvolutionaryTrace

P11473.

GenomeRNAi

7421.

NextBio

29054.

SOURCE

Search...

Entry information

Entry name

VDR_HUMAN

Accession

Primary (citable) accession number: P11473
Secondary accession number(s): B2R5Q1, Q5PSV3

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1989
Last sequence update:	October 1, 1989
Last modified:	May 29, 2013
This is version 168 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.